part of
PSI-MI
'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
contains
The inverse relationship to "part of".
PSI-MOD
'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
derives from
PSI-MOD
'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
has functional parent
This relationship indicates that the formula and mass of the child are not inherited from the mass of the parent.
PSI-MOD
'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
molecular interaction
PSI-MI
Controlled vocabularies originally created for protein protein interactions, extended to other molecules interactions.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mi
interaction detection method
PSI-MI
Method to determine the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interaction detect
participant identification method
PSI-MI
Method to determine the molecules involved in the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
participant detection
participant ident
feature detection method
PSI-MI
Method to determine the features of the proteins involved in the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
feature detection
affinity chromatography technology
PSI-MI
affinity chrom
This class of approaches is characterised by the use of affinity resins as tools to purify molecule of interest (baits) and their binding partners. The baits can be captured by a variety of high affinity ligands linked to a resin - for example, antibodies specific for the bait itself, antibodies for specific tags engineered to be expressed as part of the bait or other high affinity binders such as glutathione resins for GST fusion proteins, metal resins for histidine-tagged proteins.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
Affinity purification
alanine scanning
PSI-MI
This approach is used to identify the residues that are involved in an interaction. Several variants of the native protein are prepared by sequentially mutating each residue of interest to an alanine. The mutated proteins are expressed and probed in the binding assay.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
anti bait coimmunoprecipitation
PSI-MI
A specific antibody for the molecule of interest (bait) is available, this is used to generate a high affinity resin to capture the endogenous bait present in a sample.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
anti bait coip
anti tag coimmunoprecipitation
PSI-MI
A specific antibody for the molecule of interest is not available, therefore the bait protein is expressed as a hybrid protein fused to a tag peptide/protein for which efficient and specific antibodies or a specific ligand are available.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
anti tag coip
array technology
PSI-MI
In this class of methodologies, the molecules to be tested are presented ordered in an array format (typically at high density) on planar supports. The characteristics and chemical nature of the planar support can vary. This format permits the simultaneous assay, in controlled conditions, of several thousand proteins/peptides/nucleic acids for different functions, for instance their ability to bind any given molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bacterial display
PSI-MI
The protein of interest is presented on the outer membrane of Gram negative bacteria by expressing it as a fusion partner to peptide signals that direct heterologous proteins to the cell surface. For instance, a single chain Fv (scFv) antibody fragment, consisting of the variable heavy and variable light domains from two separate anti-digoxin monoclonal antibodies, was displayed on the outer membrane of Escherichia coli by fusing it to an Lpp-OmpA. Similar systems have also been developed for gram positive bacteria. Fluorescence-activated cell sorting (FACS), is used to specifically select clones displaying a protein binding to scFv-producing cells.
PMID:8248129
http://purl.org/obo/owl/PMID#PMID_8248129
PMID:10436088
http://purl.org/obo/owl/PMID#PMID_10436088
beta galactosidase complementation
PSI-MI
Beta-galactosidase activity can be used to monitor the interaction of chimeric proteins. Pairs of inactive beta gal deletion mutants are capable of complementing to restore activity when fused to interacting protein partners. Critical to the success of this system is the choice of two poorly complementing mutant moieties, since strongly complementing mutants spontaneously assemble and produce functional beta-gal activity detectable in absence of any fused protein fragment.
PMID:12042868
http://purl.org/obo/owl/PMID#PMID_12042868
PMID:9237989
http://purl.org/obo/owl/PMID#PMID_9237989
beta galactosidase
beta lactamase complementation
PSI-MI
This strategy is based on a protein fragment complementation assay (PCA) of the enzyme TEM-1 beta-lactamase. The approach includes a simple colorimetric in vitro assays using the cephalosporin nitrocefin and assays in intact cells using the fluorescent substrate CCF2/AM. The combination of in vitro colorimetric and in vivo fluorescence assays of beta-lactamase in mammalian cells permits a variety of sensitive and high-throughput large-scale applications.
PMID:12042868
http://purl.org/obo/owl/PMID#PMID_12042868
beta lactamase
bioluminescence resonance energy transfer
PSI-MI
bret
BRET
LRET
In this variation of the FRET assay the donor fluorophore is replaced by a luciferase (typically Renilla luciferase). In the presence of its substrate, the luciferase catalyses a bioluminescent reaction that excites the acceptor fluorophore through a resonance energy transfer mechanism. As with FRET the energy transfer occurs only if the protein fused to the luciferase and the one fused to the acceptor fluorophore are in close proximity (10-100 Angstrom).
PMID:9874787
http://purl.org/obo/owl/PMID#PMID_9874787
PMID_for_application_instance:10725388
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_10725388
biophysical
PSI-MI
The application of physical principles and methods to biological experiments.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
adenylate cyclase complementation
PSI-MI
bacterial two-hybrid
adenylate cyclase
Adenylate cyclase is encoded by the cyaA gene and contains a catalytic domain which can be proteolytically cleaved into two complementary fragments, T25 and T18, which remain associated in the presence of calmodulin in a fully active ternary complex. In the absence of calmodulin, the mixture of the two fragments does not exhibit detectable activity, suggesting that the two fragments do not associate. When expressed in an adenylate cyclase-deficient E. coli strain (E. coli lacks calmodulin or calmodulin-related proteins), the T25 and T18 fragments fused to putative interacting proteins are brought into close association which result in cAMP synthesis. The level of reconstructed adenylate cyclase can be estimated by monitoring the expression of a cAMP dependent reporter gene.
PMID:9576956
http://purl.org/obo/owl/PMID#PMID_9576956
circular dichroism
PSI-MI
Circular dichroism (CD) is observed when optically active molecules absorb left and right hand circularly polarized light slightly differently. Linearly polarized light can be viewed as a superposition of two components of circularly polarized light of equal amplitude and phase but opposite handness. When this light passes through an optically active sample the two polarized components are absorbed differently. The difference in left and right handed absorbance A(l)- A(r) is the signal registered in CD spectra. This signal displays distinct features corresponding to different secondary structures present in peptides, proteins and nucleic acids. The analysis of CD spectra can therefore yield valuable information about the secondary structure of biological macromolecules and the interactions among molecules that influence their structure.
PMID:11578931
http://purl.org/obo/owl/PMID#PMID_11578931
CD
cd
classical fluorescence spectroscopy
PSI-MI
fluorescence spectr
Proteins contain endogenous fluorophores such as tryptophan residue and heme or flavins groups. Protein folding and protein-protein interaction can be studied by monitoring changes in the tryptophan environment detected by changes in its intrinsic fluorescence. Changes in the fluorescence emission spectrum on complex formation can occur either due to a shift in the wavelength of maximum fluorescence emission or by a shift in fluorescence intensity caused by the mixing of two proteins. The interaction of two proteins causes a shift in the fluorescence emission spectrum relative to the sum of the individual fluorescence spectra, resulting in a difference spectrum [F (complex)-2 F (sum)], which is a measurable effect of the interaction. Loss of fluorescence signal from a substrate can be used to measure protein cleavage.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
two hybrid
PSI-MI
classical two hybrid
Gal4 transcription regeneration
two-hybrid
2h
Y2H
2H
2-hybrid
2 hybrid
yeast two hybrid
The classical two-hybrid system is a method that uses transcriptional activity as a measure of protein-protein interaction. It relies on the modular nature of many site-specific transcriptional activators (GAL 4) , which consist of a DNA-binding domain and a transcriptional activation domain. The DNA-binding domain serves to target the activator to the specific genes that will be expressed, and the activation domain contacts other proteins of the transcriptional machinery to enable transcription to occur. The two-hybrid system is based on the observation that the two domains of the activator need to be non-covalently brought together by the interaction of any two proteins. The application of this system requires the expression of two hybrid. Generally this assay is performed in yeast cell, but it can also be carried out in other organism. The bait protein is fused to the DNA binding molecule, the prey to the transcriptional activator.
PMID:12634794
http://purl.org/obo/owl/PMID#PMID_12634794
PMID:1946372
http://purl.org/obo/owl/PMID#PMID_1946372
PMID:10967325
http://purl.org/obo/owl/PMID#PMID_10967325
coimmunoprecipitation
PSI-MI
immunoprecipitation
coip
In this approach an antibody, specific for the molecule of interest (bait) or any tag expressed within a fusion protein, is used to separate the bait from a molecular mixture or a cell lysate and to capture its ligand simultaneously. The partners that bind to the bait molecule retained by the resin can then be eluted and identified. The antibody may be free or bound to a matrix during this process.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
co-immunoprecipitation
CoIp
Co-IP
transmission electron microscopy
PSI-MI
tem
During the treatment for microscope analysis a tissue section is incubated with high-specificity antibodies coupled to heavy metals (gold). Any tissue section can then be analysed by electron microscopy to localise the target proteins within the cell. This method supports very high resolution colocalisation of different molecules in a cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
colocalization by fluorescent probes cloning
PSI-MI
coloc fluoresc probe
Two proteins can be localised to cell compartments, in the same experiment, if they are expressed as chimeric proteins fused to distinct proteins fluorescing at different wavelengths (Green Fluorescent Protein and Red Fluorescent Protein for example). Using a confocal microscope the two proteins can be visualized in living cells and it can be determined whether they have the same subcellular location. Fluorescence microscopy of cells expressing a GFP fusion protein can also demonstrate dynamic processes such as its translocation from one subcellular compartment to another.nOBSOLETE: use imaging technique (MI:0428) and specific probe as feature of each interacting protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
colocalization by immunostaining
PSI-MI
The subcellular location of a protein can be demonstrated by treating cells fixed on a microscope slide with an antibody specific for the protein of interest. A secondary antibody conjugated with a reactive enzyme (e.g. horseradish peroxidase) is then added. Following a washing step to remove the unbound secondary ligand, a chromogenic substrate (e.g. 3,3', 5,5' tetramethyl benzidine chromogen [TMB]) is converted to a soluble coloured product by the conjugated enzyme and can then be visualised by standard microscopic techniques.nOBSOLETE since combination of Interaction Detection Method and Interaction Type.Consider using the Interaction Detection Method imaging techniques (MI:0428) coupled with Interaction Type colocalisation (MI:0403) and Participant detection immunostaining (MI:0422) instead.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Immunofluorescence Staining
coloc immunostaining
Immunostaining
colocalization/visualisation technologies
PSI-MI
coloc visual technol
Techniques enabling the identification of the subcellular localisation of a protein or complex. Two different proteins show a similar distribution in the cell are said to co-localise. Obsolete since combination of Interaction Detection Method and Interaction Type.nOBSOLETE. Consider using imaging techniques (MI:0428) as interaction detection method coupled with colocalisation (MI:0401) as interaction type and predetermined (MI:0396) as participant detection.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
confirmational text mining
PSI-MI
Text mining is used to support interactions which have been determined by other methods.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
conformational tm
copurification
PSI-MI
Approaches designed to separate cell components on the basis of their physicochemical properties. The observation that two or more proteins copurify in one or several conditions is taken as an indication that they form a molecular complex.nOBSOLETE since too non-specific. Consider use of cosedimentation (MI:0027) or comigration in non denaturing gel electrophoresis (MI:0404) or affinity chromatography technologies (MI:0004) or molecular sieving (MI:0071) or for unspecific cases biochemical (MI:0401).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
correlated mutations
PSI-MI
Pairs of multiple alignments of orthologous sequences are used to identify potential interacting partners as proteins that show covariation of their residue identities between different species. Proteins displaying inter-protein correlated mutations during evolution are likely to be interacting proteins due to co-adapted evolution of their protein interacting interfaces.
PMID:11933068
http://purl.org/obo/owl/PMID#PMID_11933068
cosedimentation
PSI-MI
Separation of a mixture of molecules under the influence of a force such as artificial gravity. Molecules sedimenting together are assumed to interact.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cosedimentation in solution
PSI-MI
The ultracentrifuge can be used to characterise and/or purify macromolecules in solution according to their mass and hydrodynamic properties. Sedimentation studies provide information about the molecular weight and shape of a molecule. It is also possible to measure the association state of the sample. Both the mass of a molecule and its shape, that influences the friction forces and diffusion that counterbalances gravity, determine the sedimentation speed.
PMID:10410796
http://purl.org/obo/owl/PMID#PMID_10410796
solution sedimentati
cosedimentation through density gradient
PSI-MI
Sedimentation through a density gradient measures the sedimentation rate of a mixture of proteins through either a glycerol or sucrose gradient. Two interacting proteins will sediment mostly as a complex at concentrations above the binding constant. By varying the concentration of one or both of the complex constituents and taking into account the dilution of the species during sedimentation, one can reasonably accurately estimate the binding constant.
PMID:10410796
http://purl.org/obo/owl/PMID#PMID_10410796
density sedimentatio
cross-linking study
PSI-MI
Analysis of complexes obtained by chemical treatments that promote the formation of covalent bonds among molecules in close proximity.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
crosslink
protein cross-linking with a bifunctional reagent
PSI-MI
A cross-linker is a bifunctional molecule having two reactive ends linked by a spacer, often containing a disulfide bond. Cross-linkers induce the formation of covalent bonds among proteins that are neighbours. When a reducing agent is added the disulfide bridge is cleaved, the cross-linked pairs are released and can be identified. There are various classes of cross-linkers, the most common are those having photoreactive groups that become reactive fluorophores when activated by UV light thereby resulting in photolabeling the cross-linked moieties.
PMID:10679368
http://purl.org/obo/owl/PMID#PMID_10679368
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
protein crosslink
Label transfer techniques
Photoaffinity labelling
de novo protein sequencing by mass spectrometry
PSI-MI
The strategy to determine the complete amino acid sequence of a protein by mass spectrometry relies on the generation of a nested set of fragments differing by one amino acid. This reveals the identity of the residue that has been removed at each degradation step by measuring the mass difference of fragments differing of one residue. Peptide fragments can be obtained by protease treatment combined with the fragmentation promoted by collision (or other methods) within a tandem mass spectrometer. This approach can be carried out with LC MS/MS (Liquid Chromatography Tandem Mass Spectrometry), nanoESI MS/MS (nanoElectrospray Ionisation tandem mass spectrometry), or FTMS (Fourier Transform mass spectrometry) instruments.
PMID:10984529
http://purl.org/obo/owl/PMID#PMID_10984529
MS/MS
de novo protein sequence
deletion analysis
PSI-MI
In this approach, once a molecule is demonstrated to participate in an interaction, several deletion derivatives are produced and tested in the binding assay to identify the minimal fragment (domain) that can still support the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
display technology
PSI-MI
All the methods that permit the physical linking of a protein/peptide to its coding sequence. As a consequence affinity purification of the displayed peptide results in the genetic enrichment of its coding sequence. By these technologies genes encoding a peptide with desired binding properties can be selected over an excess of up to 1012 unrelated molecules.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
docking
PSI-MI
Predicts the structure of a molecular complex from the unbound structures of its components. The initial approach in the majority of docking procedures is based largely on the 'rigid-body' assumption, whereby the proteins are treated as solid objects. Initial scoring of a complex is based on geometric fit or surface complementarity. This generally requires some knowledge of the binding site to limit the number of solutions.
PMID:9631301
http://purl.org/obo/owl/PMID#PMID_9631301
PMID_for_application_instance:11478868
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_11478868
domain fusion
PSI-MI
Rosetta Stone
The rosetta stone, or domain fusion procedure, is based on the assumption that proteins whose homologues in other organisms happen to be fused into a single protein chain are likely to interact or to be functionally related.
PMID:10573422
http://purl.org/obo/owl/PMID#PMID_10573422
domain profile pairs
PSI-MI
This approach uses a protein interaction network of a given organism to infer interaction in another organism using information about the interacting region. The regions or domains involved in interactions are clustered if they share sequence similarity and have common interacting partners. The resulting domain profiles are then used to screen the proteome of another organism and domain-domain interactions are inferred. Ultimately, an inferred protein interaction map is built in this second organism.
PMID:11473021
http://purl.org/obo/owl/PMID#PMID_11473021
dynamic light scattering
PSI-MI
In dynamic light scattering, particle diffusion in solution gives rise to fluctuations in the intensity of the scattered light on the microsecond scale. The hydrodynamic radius of the particles can be easily calculated.
PMID:9013660
http://purl.org/obo/owl/PMID#PMID_9013660
dls
edman degradation
PSI-MI
In this procedure the N-terminus amino acid is cleaved from a polypeptide and identified by high-pressure liquid chromatography. The cycle is repeated on the ever-shortening polypeptide until all the residues are identified. On average only 20-30 consecutive cycles can be performed and lead to amino acid identification. Longer polypeptides or full length proteins must be cleaved by specific protease before Edman degradation and their sequences built by fragment overlapping.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
electron microscopy
PSI-MI
Electron crystallography
Electron cryomicroscopy
Electron microscopy methods provide insights into the structure of biological macromolecules and their supramolecular assemblies. Resolution is on average around 10 Angstroms but can reach the atomic level when the samples analysed are 2D crystals. Different types of samples can be analysed by electron microscopy: crystals, single particles like viruses, macromolecular complexes or entire cells and tissue sections. Samples can be chemically fixed or vitrified by rapid freezing in liquid ethane, and then transferred into the electron microscope. Data collection consists of the recording of electron diffraction data (2D crystals) and images. Depending on the type of sample, different approaches are used to analyse and merge images and electron diffraction data.
PMID:11785754
http://purl.org/obo/owl/PMID#PMID_11785754
electron nuclear double resonance
PSI-MI
A combination of NMR and EPR. The lines in the EPR spectrum that are caused by coupling of an unpaired electron nearby nuclei change in intensity when these nuclei are excited at their NMR frequency.
PMID:11988476
http://purl.org/obo/owl/PMID#PMID_11988476
PMID_for_application_instance:12186859
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_12186859
PMID:11817959
http://purl.org/obo/owl/PMID#PMID_11817959
ENDOR
endor
electron paramagnetic resonance
PSI-MI
EPR (also called ESR, Electron Spin Resonance) spectroscopy is analogous to NMR, but is based on the excitation of unpaired electrons instead of nuclei. Unpaired (single) electrons are only found in radicals and some metal ions (paramagnetic species); the EPR spectrum provides information about the environment and mobility of the paramagnetic species. The magnetic interaction of two paramagnetic centres in a protein can be used to calculate the distance between them; this allows studies of the movements and interactions of protein segments. In proteins without any intrinsic unpaired electrons it is possible to attach a radical probe (spin label). Stable nitroxide radicals can be bound to amino acid residues, in analogy with fluorescent probes. In combination with site directed mutagenesis this method is used in particular to study structure and assembly of membrane proteins, by measuring with EPR whether an amino acid is in a polar or non polar environment.
PMID:11817959
http://purl.org/obo/owl/PMID#PMID_11817959
ESR
EPR
epr
electron resonance
PSI-MI
A form of spectroscopy in which the absorption of microwave by a sample in a strong magnetic field is used to study atoms or molecules with unpaired electrons.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental interaction detection
PSI-MI
Methods based on laboratory experiments to determine an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental interac
experimental knowledge based
PSI-MI
experimental info
Predictive algorithms that rely on the information obtained by experimental results.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
far western blotting
PSI-MI
Affinity blotting
Proteins are fractionated by PAGE (SDS-polyacrylamide gel electrophoresis), transferred to a nitrocellulose membrane and tested for the ability to bind to a protein, a peptide, or any other ligand. Cell lysates can also be fractionated before gel electrophoresis to increase the sensitivity of the method for detecting interactions with rare proteins. Denaturants are removed during the blotting procedure, which allows many proteins to recover (or partially recover) activity. However, if biological activity is not recoverable, the proteins can be fractionated by a non denaturing gel system. This variation of the method eliminates the problem of activity regeneration and allows the detection of binding when the presence of a protein complex is required for binding. The protein probe can be prepared by any one of several procedures, while fusion affinity tags greatly facilitate purification. Synthesis in E. coli with a GST fusion, epitope tag, or other affinity tag is most commonly used. The protein of interest can then be radioactively labelled, biotinylated, or used in the blotting procedure as an unlabeled probe that is detected by a specific antibody.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
filamentous phage display
PSI-MI
filamentous phage
Filamentous phages (M13, f1, fd) have been extensively used to develop and implement the technology of phage display. Repertoires of relatively short peptides of random amino acid sequences or cDNA libraries have been constructed and searched successfully. Most experiments have taken advantage of the ability to assemble phages decorated with hybrid versions of the receptor protein pIII or of the major coat protein pVIII. Both systems allow the display of foreign peptides by fusion to the amino-terminus of the capsid protein but differ in the number of peptide copies that can be displayed on each phage particle. Display libraries of very diverse protein fragments have been constructed by fusing either genomic or cDNA fragments to gene III or gene VIII.
PMID:7682645
http://purl.org/obo/owl/PMID#PMID_7682645
filter binding
PSI-MI
Filter overlay assay
dot blot
A method in which separation depends upon the ability of one participant to bind to a filter or membrane which the other participants do not. Molecules interacting with the bound molecule will also be retain on the filter. For example, proteins expressed by different clones of an expression library are bound to a nitrocellulose membrane, by colony (bacterial library) or plaque (phage library) blotting. A labelled protein can then be used as a probe to identify clones expressing proteins that interact with the probe. Interactions occur on the nitrocellulose filters. The method is highly general and therefore widely applicable. A variety of approaches can be used to label the ligand, alternatively the ligand can be detected by a specific antibody.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
flag tag coimmunoprecipitation
PSI-MI
flag tag coip
The protein of interest is expressed as a fusion to the peptide DYKDDDDKV for which antibodies are commercially available. Sometimes multiple copies of the peptide are fused in tandem.nOBSOLETE redundant term. Map to feature type: flag-tagged (MI:0518) and Interaction detection method: anti tag coimmunoprecipitation (MI:0007).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence technology
PSI-MI
Techniques based upon the measurement of the emission of one or more photons by a molecule activated by the absorption of a quantum of electro-magnetic radiation. Typically the emission, which is characterised by a wavelength that is longer than the one of excitatory radiation, occurs within 10-8 seconds.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence
fluorescence correlation spectroscopy
PSI-MI
FCS monitors the random motion of fluorescently labelled molecules inside a defined volume irradiated by a focused laser beam. These fluctuations provide information on the rate of diffusion or diffusion time of a particle and this is directly dependent on the particle mass. As a consequence, any increase in the mass of a biomolecule, e.g. as a result of an interaction with a second molecule, is readily detected as an increase in the diffusion time of the particle. From these results the concentration of the different molecules can be calculated as well as their binding constant.
PMID:10733953
http://purl.org/obo/owl/PMID#PMID_10733953
fluctuation correlation specctrometry
fcs
FCS
fluorescence polarization spectroscopy
PSI-MI
fps
FPS
Fluorescence anisotropy
Because of the long lifetimes of excited fluorescent molecules (nanoseconds), fluorescence can be used to monitor the rotational motion of molecules, which occurs on this timescale. This is accomplished experimentally by excitation with plane-polarized light, followed by measurement of the emission at parallel and perpendicular planes. Since rotational correlation times depend on the size of the molecule, this method can be used to measure the binding of two proteins because the observed polarization increase when a larger complex is formed. A fluorescence anisotropy experiment is normally carried out with a protein bearing a covalently added fluorescent group, which increases both the observed fluorescence lifetime of the excited state and the intensity of the fluorescent signal. Residue modification can be assessed by addition of an antibody which binds to the modified residue and alters the molecular weight of the complex. A variation of this technique has been used to show interaction of a DNA binding protein with another protein. In this case the DNA rather than protein is fluorescently labelled.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
PMID:12805227
http://purl.org/obo/owl/PMID#PMID_12805227
fluorescence-activated cell sorting
PSI-MI
facs
Flow cytometry
Cells in suspension flow through a laser beam, the scattered light or emitted fluorescence is measured, filtered and converted to digital values. Cells can be sorted according to their properties. Using flow cytometry, any fluorescent or light scattering experiment can be carried out on entire cells. With this instrument, interactions occurring either on cell surfaces or in any other subcellular location can be studied by using suitable fluorescent labels.
PMID:11988464
http://purl.org/obo/owl/PMID#PMID_11988464
FACS
fluorescent resonance energy transfer
PSI-MI
RET
FRET is a quantum mechanical process involving the radiationless transfer of energy from a donor fluorophore to an appropriately positioned acceptor fluorophore. The fluorophores are genetically fused to the protein in analysis and cotransfected. Three basic conditions must be fulfilled for FRET to occur between a donor molecule and acceptor molecule. First, the donor emission spectrum must significantly overlap the absorption spectrum of the acceptor. Second, the distance between the donor and acceptor fluorophores must fall within the range 20 to 100 Angstrom. Third, the donor and acceptor fluorophores must be in favourable orientations.
PMID:11558993
http://purl.org/obo/owl/PMID#PMID_11558993
FRET analysis
fret
FRET
full identification by DNA sequencing
PSI-MI
Sequencing occurs during the course of the experiment. DNA sequencing is the process of determining the nucleotide order of a given DNA fragment. Thus far, most DNA sequencing has been performed using the chain termination method developed by Frederick Sanger. This technique uses sequence-specific termination of a DNA synthesis reaction using modified nucleotide substrates. However, new sequencing technologies such as Pyrosequencing are generating the majority of data.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
full dna sequence
gene neighbourhood
PSI-MI
Gene pairs that show a conserved topological neighbourhood in many prokaryotic genomes are considered by this approach to encode interacting or functionally related proteins. By measuring the physical distance of any given gene pair in different genomes, interacting partners are inferred.
PMID:9787636
http://purl.org/obo/owl/PMID#PMID_9787636
genome based prediction
PSI-MI
Methods that require fully sequenced genomes either because they are based on the comparison of genome topology or on the identification of orthologous sequences in different genomes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genome prediction
gst pull down
PSI-MI
The bait protein is expressed and purified as a fusion to the glutathione S-tranferase protein. The bait protein is normally attached to a glutathione sepharose resin or alternatively to a support containing an anti-GST antibody.nOBSOLETE redundant term. Map to feature type : gst-tagged (MI:0519) and Interaction detection method: pull down (MI:0096).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ha tag coimmunoprecipitation
PSI-MI
The protein of interest is expressed as a fusion to the peptide YPYDVPDYA (a fragment of the influenza hemaglutinin protein) for which antibodies are commercially available.nOBSOLETE redundant term. Map to feature type : ha-tagged (MI:0520) and Interaction detection method: anti tag coimmunoprecipitation (MI:0007).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ha tag coip
his pull down
PSI-MI
The bait protein is expressed and purified fused to an amino or carboxyterminal tail containing a variable number of histidines. The bait protein is normally attached to a metal (usually nickel) resin.nOBSOLETE redundant term. Map to feature type : his-tagged (MI:0521) and Interaction detection method: pull down (MI:0096).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
his tag coimmunoprecipitation
PSI-MI
The protein of interest is expressed as a fusion to a poly-His tail. This permits purification by chromatography over a metal column or by binding to commercially available anti poly-His antibodies.nOBSOLETE redundant term. Map to feature type: his-tagged (MI:0521) and Interaction detection method: anti tag coimmunoprecipitation (MI:0007).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
his tag coip
interaction prediction
PSI-MI
Computational methods to predict an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
in silico methods
predicted interac
interologs mapping
PSI-MI
Protein interactions, experimentally detected in an organism, are extended to a second organism assuming that homologue proteins, in different organisms, maintain their interaction properties.
PMID:11731503
http://purl.org/obo/owl/PMID#PMID_11731503
Homology based interaction prediction
isothermal titration calorimetry
PSI-MI
Isothermal titration calorimetry (ITC) measures directly the energy associated with a chemical reaction triggered by the mixing of two components. A typical ITC experiment is carried out by the stepwise addition of one of the reactants (~10-6 L per injection) into the reaction cell (~1mL) containing the second reactant. The chemical reaction occurring after each injection either releases or absorbs heat (qi) proportional to the amount of ligand that binds to the protein with a characteristic binding enthalpy (DH). As modern ITC instruments operate on the heat compensation principle, the instrumental response (measured signal) is the amount of power (microcalories per second) necessary to maintain constant the temperature difference between the reaction and the reference cells. Because the amount of uncomplexed protein available progressively decreases after each successive injection, the magnitude of the peaks becomes progressively smaller until complete saturation is achieved. The difference between the concentration of bound ligand in the ith and (i-1)th injections depends on the binding constant Ka and the total ligand injected. The calculations depend on the binding model (number of substrates). Analysis of the data yields DH and DG = -RTlnKa. The entropy change is obtained by using the standard thermodynamic expression DG = DH-TDS.
PMID:11785756
http://purl.org/obo/owl/PMID#PMID_11785756
itc
ITC
lambda phage display
PSI-MI
lambda phage
Morphologically classified as one of the siphoviridae, lambda is a temperate bacteriophage of E.coli, with a double-stranded DNA genome. It has an icosahedral head attached to a flexible helical tail. Both the tail protein pV and the head protein pD have been used for displaying (C or N terminally) foreign peptides on the viral capsid.
PMID:7682645
http://purl.org/obo/owl/PMID#PMID_7682645
light scattering
PSI-MI
Dynamic and static laser light scattering probes the size, shape, and structure of biological macromolecules or of their assemblies. A beam is focused on an optically clear cylindrical cell containing the sample. Most of the light passes directly through the sample. A small portion of the light is scattered; the scattered light intensity containing information about the scattering particle is detected at an angle (typically in the range 15-180degrees) from the direction of the incident beam.
PMID:9013660
http://purl.org/obo/owl/PMID#PMID_9013660
mass detection of residue modification
PSI-MI
Mass spectrometry can be used to characterise chemical modifications within peptides. One approach consists in the observation of a mass difference when a sample is treated with an enzyme that can specifically remove a peptide modification, for instance a phosphatase. The mass difference corresponds to the mass of the chemical group covalently linked to a residue. Such experiments carried out with a MALDI-TOF (Matrix-assisted laser desorption ionization time-of-flight ) do not allow the mapping of the modification site within the sequence, whereas any tandem mass spectrometer (LC MS/MS Liquid Chromatography Tandem Mass Spectrometry, nanoESI MS/MS nanoElectrospray Ionisation tandem mass spectrometry, FTMS Fourier Transform mass spectrometry) provide such information. A second approach consists of the direct mass measurement of the ionized chemical group dissociated from the residue within a tandem mass spectrometer. Both approaches need a prior enrichment of the modified peptide population in the samples with IMAC (Immobilized Metal Affinity Chromatography)or specific anti-modification antibodies.
PMID_for_application_instance:11875433
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_11875433
PMID:11395414
http://purl.org/obo/owl/PMID#PMID_11395414
modified residue ms
mass spectrometry studies of complexes
PSI-MI
ms of complexes
Mass spectrometric approaches to the study of protein in complexes permits the identification of subunit stoichiometry and transient associations. By preserving complexes intact in the mass spectrometer, mass measurement can be used for monitoring changes in different experimental conditions, or to investigate how variations of collision energy affect their dissociation.
PMID_for_application_instance:12057199
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_12057199
PMID:12504676
http://purl.org/obo/owl/PMID#PMID_12504676
mobility shift
PSI-MI
Protein modifications can be identified by gel electrophoresis since any change in the mass and/or the charge of the protein can alter its mobility in PAGE. Although this method does not allow the unequivocal identification of the type of modification that has caused the shift, it is possible, by combining this approach with more direct methods, to correlate the extent of the shift to a specific modification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molecular sieving
PSI-MI
Siezing column
Size Exclusion Chromatography
Gel Filtration
In sizing columns (gel filtration), the elution position of a protein or of a complex depends on its Stokes radius. Molecules with a radius that is smaller than the bead size are retained and retarded by the interaction with the matrix. The observation that two proteins, loaded on a sieving column, elute in a fraction(s) corresponding to a MW that is larger than the MW of either protein may be taken as an indication that the two proteins interact. Furthermore this technique provides a conceptually simple method for evaluating the affinity of the interaction.
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
monoclonal antibody western blot
PSI-MI
Western blot assay carried out using monospecific antibodies produced in the supernatant of a cell line obtained by fusing a lymphocyte B to a myeloma cell line or selected by phage display technology.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
monoclonal western
mrna display
PSI-MI
This method relies on the covalent coupling of mRNA to the nascent polypeptide. The mRNA (natural or artificial) is first covalently linked to a short DNA linker carrying a puromycin moiety. The mRNA mixture is then translated in vitro. When the ribosome reaches the RNA-DNA junction the ribosome stalls and the puromycin moiety enters the peptidyltransferase site of the ribosome and forms a covalent linkage to the nascent polypeptide. As a result the protein and the mRNA are covalently joined and can be isolated from the ribosome and purified. In the current protocol, a cDNA strand is then synthesised to form a less sticky RNA-DNA hybrid and these complexes are finally used for affinity selection. As in most display approaches, several selections cycles (3-6) are sufficient to enrich for mRNAs encoding ligand proteins.
PMID:11551470
http://purl.org/obo/owl/PMID#PMID_11551470
mutation analysis
PSI-MI
Mutant molecules are produced by random or directed techniques and assayed for their ability to support binding.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
myc tag coimmunoprecipitation
PSI-MI
The protein of interest is expressed as a fusion to the peptide EUKLISEED (a fragment of the Myc oncogene protein) for which antibodies are commercially available. Sometimes multiple copies of the peptide are fused in tandem.nOBSOLETE redundant term. Map to feature type: myc-tagged (MI:0522) and Interaction detection method: anti tag coimmunoprecipitation (MI:0007).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
myc tag coip
neural network on interface properties
PSI-MI
interface predictor
Neural networks are trained on the properties of residues belonging to a cluster of residues that are neighbours in space on protein surface. The predictor permits the inference of the residues that are likely to be on an interaction interface.
PMID:11874449
http://purl.org/obo/owl/PMID#PMID_11874449
PMID:11455607
http://purl.org/obo/owl/PMID#PMID_11455607
nuclear magnetic resonance
PSI-MI
NMR
nmr
Nuclear magnetic resonance (NMR) is an effect whereby magnetic nuclei in a magnetic field absorb and re-emit electromagnetic (EM) energy. Certain atomic nuclei, and in particular hydrogen, have a magnetic moment or spin; i.e., they have an intrinsic magnetisation, like a bar magnet. The spin aligns along the strong magnetic field, but can be changed to a misaligned excited state in response to applied radio frequency (RF) pulses of electromagnetic radiation. When the excited hydrogen nuclei relax to their aligned state, they emit RF radiation, which can be measured and displayed as a spectrum. The nature of the emitted radiation depends on the environment of each hydrogen nucleus, and if one nucleus is excited, it will influence the absorption and emission of radiation by other nuclei that lie close to it. It is consequently possible, by an ingenious elaboration of the basic NMR technique known as two-dimensional NMR, to distinguish the signals from hydrogen nuclei in different amino acid residues and to identify and measure the small shifts in these signals that occur when these hydrogen nuclei lie close enough to interact: the size of such a shift reveals the distance between the interacting pair of hydrogen atoms. In this way NMR can give information about the distances between the parts of the interacting molecule. NMR provides information about interacting atoms thereby permitting to obtain information about macromolecular structure and molecular interactions.
PMID_for_application_instance:12062432
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_12062432
PMID:12120505
http://purl.org/obo/owl/PMID#PMID_12120505
nucleotide sequence identification
PSI-MI
Identification of a nucleotide sequence. Depending on the experimental design, nucleotide sequence can be determined before the interaction detection while building a collection of clones or after the selection of randomly generated clones.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleotide sequence
sequence cloning
other biochemical technologies
PSI-MI
Experimental methods that could not be assigned to the other large group of technologies.nOBSOLETE use biochemical (MI:0401) instead.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
other biochemic tech
partial DNA sequence identification by hybridization
PSI-MI
partial dna sequence
Genes are recognised by hybridization of a probe with a fragment of the gene sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
peptide array
PSI-MI
The peptide synthesis methods offer numerous opportunities to synthesise and subsequently screen large arrays of synthetic peptides on planar cellulose supports. Discrete spots are arranged as arrays on membrane sheets where each spot is individually accessed by manual or automated delivery of the appropriate reagent solutions. Over the past few years protein-protein recognition, peptide-metal ion interactions, peptide-nucleic acid binding, enzymatic modification of peptides experiments, have been explored using synthetic peptide arrays on planar support.
PMID:11167074
http://purl.org/obo/owl/PMID#PMID_11167074
peptide massfingerprinting
PSI-MI
fingerprinting
This approach leads to protein identification by matching peptide masses, as measured by mass spectrometry, to the ones calculated from in silico fragmentation of a protein sequence database. A peptide mixture from a tryptic digest is analysed by MALDI-MS (Matrix-assisted laser desorption ionization mass spectrometry). The list of peptide masses obtained by MALDI MS is automatically compared to the calculated masses of the predicted peptide fragments for each entry in the database. High mass accuracy is very important in order to obtain a statistically significant and unambiguous match This method is best applied to completely sequenced genomes and well characterised proteomes. However, depending on the data quality, proteins that are highly homologous to already characterised proteins (greater than 80 to 90% sequence identity) can also be identified. The retrieved sequence are evaluated by mass accuracy of the peptides, matching of additional peptide masses in the MALDI spectrum after accounting for common modifications such as oxidation, acrylamidation of cysteine and missed cleavages and the use of secondary information (apparent isoelectric point and molecular weight). If any ambiguity about the identification by MALDI-MS still exists, the results must verified by an other identification method. Peptide mass fingerprint is generally carried out with a MALDI-TOF (Matrix-assisted laser desorption ionization time-of-flight ) instrument but can also be achieved ESI-TOF (Electrospray Ionisation time-of-flight) or LC-MS (Liquid Chromatography-Mass Spectrometry) mass spectrometer.
PMID:10967324
http://purl.org/obo/owl/PMID#PMID_10967324
PMID:11752590
http://purl.org/obo/owl/PMID#PMID_11752590
PMID_for_application_instance:11805826
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_11805826
peptide synthesis
PSI-MI
When one of the partners participates in the interaction with a relatively short peptide fragment, it is often convenient to precisely identify the minimal region that supports the interaction by synthesising a series of overlapping peptides and by testing them in the binding assay. Synthetic peptides that are identical with peptides synthesised in vivo are useful experimental tools for such studies. Peptides are routinely synthesised in a test tube from monomeric amino acids by condensation reactions that form peptide bonds. Peptides are constructed sequentially by coupling the C-terminus of a monomeric amino acid to the N-terminus of the growing peptide. To prevent unwanted reactions involving the amino groups and carboxyl groups of the side chains during the coupling steps, a protecting (blocking) group is attached to the side chains. Without these protecting groups, branched peptides would be generated. In the last steps of synthesis, the side chain-protecting groups are removed and the peptide is cleaved from the resin on which synthesis occurs.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phage display
PSI-MI
Peptide sequences or entire proteins can be displayed on phage capsids by fusion to coat proteins to generate a library of fusion phages each displaying a different peptide. Such a library can then be exploited to identify specific phages that display peptides that bind to any given bait molecule for instance an antibody. The selection is performed by a series of cycles of affinity purification known as panning. The bait protein, immobilized on a solid support (plastic, agarose, sepharose, magnetic beads and others) is soaked in the phage mixture and that phage that remains attached to the bait is amplified and carried through a further affinity purification step. Each cycle results in an approximately 1,000-fold enrichment of specific phage and after a few selection rounds (2-4), DNA sequencing of the tight-binding phage reveals only a small number of sequences. Phage display panning experiments can be carried out either on libraries of peptides of random amino acid sequence or on libraries of displaying natural peptides obtained by inserting cDNA fragments into the phage vector (cDNA libraries). Libraries have been assembled on several different phages (Fd, Lambda or T7).
PMID:7708014
http://purl.org/obo/owl/PMID#PMID_7708014
PMID:10975452
http://purl.org/obo/owl/PMID#PMID_10975452
phylogenetic profile
PSI-MI
The phylogenetic profile of a protein stores information about the presence and the absence of that protein in a set of genomes. By clustering identical or similar profiles, proteins with similar functions and potentially interacting are identified.
PMID:10200254
http://purl.org/obo/owl/PMID#PMID_10200254
polyclonal antibody western blot
PSI-MI
Western blot assay carried out using a mixture of different antibodies that represent the immune response, normally in an experimental animal, to the protein of interest.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
polyclonal western
predictive text mining
PSI-MI
predictive tm
Methods based on natural language processing to detect possible interactions between proteins (direct physical interactions or indirect genetic interactions). This includes the detection of non ambiguous protein or gene names and analysis of the relation expressed in a sentence among them.
PMID:11791231
http://purl.org/obo/owl/PMID#PMID_11791231
primer specific pcr
PSI-MI
Sequences can be identified in a DNA mixture by launching a PCR (Polymerase Chain Reaction) controlled by sequence specific primers. Such reaction starts only when the hybridization of the primer with a complementary sequence occurs.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein array
PSI-MI
The protein array technology allows the screening of biochemical activities or binding abilities of hundreds or thousands of protein samples in parallel. After synthesis and purification by high-throughput methodologies, the proteins are printed onto the chip by using an instrument (micro-arrayer) that is capable of spotting liquid samples in a reproducible manner onto a planar support. The ordered protein array can then be probed with labelled molecules to identify proteins that bind to the bait.
PMID:10976071
http://purl.org/obo/owl/PMID#PMID_10976071
PMID:12067604
http://purl.org/obo/owl/PMID#PMID_12067604
protein complementation assay
PSI-MI
complementation
PCA
In the protein-fragment complementation assay, the proteins of interest ("Bait" and "Prey") are covalently linked at the genetic level to incomplete fragments of a third protein (known as the "reporter") and are expressed in vivo, Interaction between the "bait" and the "prey" proteins brings the fragments of the "reporter" protein in close enough proximity to allow them to reform and become the functional reporter protein. Typically enzymes which confer resistance to antibiotics, such as Dihydrofolate reductase or Beta-lactamase, or proteins that give colorimetric or fluorescent signals are used. The Bait protein is generally the protein under study and the methods are readily adaptable to highthroughput mode.
PMID:11495741
http://purl.org/obo/owl/PMID#PMID_11495741
chromatography technology
PSI-MI
Used to separate and/or analyse complex mixtures. The components to be separated are distributed between two phases: a stationary phase (bed) and a mobile phase which percolates through the stationary bed. The nature of the two phases determines the separation criteria exploited by the column such as affinity, ionic charges, size or hydrophobicity of the molecules under analysis. Each type of column can be implemented with the mobile phase under atmospheric or high pressure condition. In this later case columns are designated as High Pressure Liquid Chromatography (HPLC).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
column chromatography
chromatography
protein in situ array
PSI-MI
pisa
Protein In Situ Array is a method by which protein arrays are rapidly generated in one step directly from DNA, by cell-free protein expression and simultaneous in situ immobilisation at a surface. Individual genes or fragments are produce by PCR or RT-PCR depending on the source of genetic material using properly designed primers. The PISA is generated by cell-free protein synthesis using coupled transcription and translation to produce a double HexaHis-tagged protein, the reaction being carried out on a surface to which the protein adheres as soon as it is synthesised.
PMID:11470888
http://purl.org/obo/owl/PMID#PMID_11470888
PISA
protein sequence identification
PSI-MI
Single amino acid identification along a protein sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein sequence
protein staining
PSI-MI
A wide range of dyes have been used over the years to visualise proteins in polyacrylamide gels - Coomasie Blue and silver-staining being two classical methods. Fluorescent dyes such as Nile Red and SYPRO Orange are now increasingly used due to their superior dynamic range. Use of non-denaturing gels can allow visualisation of protein protein interactions. Several dyes can be used to specifically indicate residue modification, however this methodology will give no information as the number of residues modified or their position within the protein sequence. Examples include the use of acid fuscian or the fluorescent dansyl hydrazine to show protein glycosylation.
PMID:12015990
http://purl.org/obo/owl/PMID#PMID_12015990
proteinchip(r) on a surface-enhanced laser desorption/ionization
PSI-MI
SELDI ProteinChip
seldi chip
ProteinChip(r) Array technology is a surface-enhanced laser desorption/ionization (SELDI) approach (Ciphergen Biosystems Inc. Fremont, CA, USA) for sample fractionation accomplished by retentate chromatography. Retentate chromatography is performed on ProteinChip Arrays with varying chromatographic properties (e.g. anion exchange, cation exchange, metal affinity and reverse phase). By utilising arrays with differing surface chemistries in parallel and in series, a complex mixture of proteins, as from cells or body fluids, can be resolved into subsets of proteins with common properties. Specific analytes can also be examined by using preactivated arrays to which a bait molecule (such as an antibody or biotinylated DNA) is immobilized and a solution containing the binding partner(s) is presented to the array. This array-based immunoprecipitation or protein-binding experiment has been used with good success to study DNA-binding proteins, receptor-ligand interactions, and protein complexes. Any ligand retained on a SELDI chip can directly be identified by mass spectrometry.
PMID:11827829
http://purl.org/obo/owl/PMID#PMID_11827829
pull down
PSI-MI
A specific affinity chromatography method where a molecule of interest (bait) is expressed as a fusion to an affinity tag (GST, HIS tag and others) and binds to a support that has affinity for the tag. The molecule may be expressed or synthesised and purified first, often in an heterologous system, bound to the matrix at high concentration and then challenged with a solution or cellular extract containing the candidate partner molecules. Alternatively, a multi-molecular complex may be adsorbed to the resin and the retained binding molecules subsequently identified.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
reverse ras recruitment system
PSI-MI
In this complementation approach the bait can be any membrane protein (for example a receptor or a channel protein), the prey is cloned as a fusion protein of any cDNA from a library and the coding sequence of cytoplasmic RAS (cdc25 in yeast). If the bait and the prey interact, RAS is recruited close to the membrane and can activate cell growth. This procedure must take place in cells having a mutated RAS (Cdc25-2 yeast strain having a temperature sensitive mutation of RAS) to avoid constitutive growth activation.
PMID:11160938
http://purl.org/obo/owl/PMID#PMID_11160938
reverse RRS
reverse rrs
ribosome display
PSI-MI
This method permits the coupling of phenotype to genotype via the formation of a non-covalent ternary complex between mRNAs and their encoded polypeptides while they are translated in an in vitro system. As a first step a cDNA library is constructed that encodes chimeric proteins in which the natural proteins or protein domains are fused to a C-terminal tether. As a consequence when the mRNA is translated in vitro the domain can fold while the tether is still in the ribosomal tunnel. Furthermore this chimeric mRNAs lack a stop codon, thus preventing release of the mRNA and the polypeptide from the ribosome. High concentrations of magnesium and low temperature further stabilise the ternary complex. Similarly to phage display, these complexes can be used directly to select for nucleic acids encoding proteins with desired properties.
PMID_for_application_instance:12167034
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_12167034
PMID:11551470
http://purl.org/obo/owl/PMID#PMID_11551470
scintillation proximity assay
PSI-MI
SPA relies upon the fact that a beta particle emitted from a radioisotope decay can excite a fluorophore only when it is at a very short distance in water solution (few micrometers). The ligand is labelled with a radioactive atom and its potential partner is fixed to fluorophore containing beads, the emitted fluorescence proving their interaction can be measured in a scintillation counter. The scintillator measures only the amount of bound radiolabelled ligand. Competition experiment with cold competitor can be done to estimate the binding affinities (50% inhibitory concentration [IC50], cold ligand versus labelled ligand). Loss of signal can also be used to measure substrate cleavage by an enzyme, and labelled antibodies used to titrate the degree of modified residue present.
PMID:3866247
http://purl.org/obo/owl/PMID#PMID_3866247
spa
SPA
RIA Radio Immuno Assay
sequence based phylogenetic profile
PSI-MI
sequence phylogeny
Multiple alignments of orthologous sequences in the same species and their corresponding phylogenetic trees are built. Every phylogenetic tree is computed as a matrix of distances between all possible interacting pairs. The covariation of the distance matrices reveals interacting pairs.
PMID:11707606
http://purl.org/obo/owl/PMID#PMID_11707606
sequence based prediction
PSI-MI
predict from sequenc
Computational methods based on evolutionary hypothesis, used as criteria to browse sequences and predict interacting pairs.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
sequence tag identification
PSI-MI
This approach leads to protein identification by combining mass measurement and short amino acid sequence information obtained by tandem mass spectrometry. This information is then used to automatically find the best match in a sequence database. A mixture of peptides derived from a protease digestion is analysed by nanoelectrospray LC-MS/MS (Liquid Chromatography Tandem Mass Spectrometer or nanoESI MS/MS) mass spectrometry. Electrospray mass spectrometry cannot be applied to dilute samples and is affected by high salt. As a consequence peptides, normally extracted from acrylamide gels by in situ proteolysis, are desalted and concentrated on a microcolumn followed by elution into a capillary used for nanoelectrospray tandem mass spectrometry. A first mass spectrum (Normal mass spectrum or Q1 mass spectrum) gives information about the masses of all the peptides. Peptides observed in the normal mass spectrum are isolated in turn and dissociated into fragments by collision with gas molecules within the mass spectrometer. Some of the fragments obtained from a peptide constitute a nested set, differing by one amino acid, and the mass difference between them allows assignment of a partial sequence. The masses of the fragments define the position of the partial sequence in the peptide. Together with the cleavage specificity of the protease used to cleave the protein, and mass information such sequence tag provides much higher search specificity to match the a database entry. The procedure is repeated with several peptides from the digest, resulting in multiple identifications of the same protein or identification of several proteins from the peptide mixture. Unknown proteins can easily be identified by using the high specificity of the peptide sequence tag for searches in most sequence databases including EST or genome databases.
PMID:10967324
http://purl.org/obo/owl/PMID#PMID_10967324
PMID:11752590
http://purl.org/obo/owl/PMID#PMID_11752590
PMID_for_application_instance:11805837
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_11805837
MS/MS
sequence tag
southern blot
PSI-MI
A standard procedure to identify DNA fragments containing specific gene sequences. In this procedure i) a genome is fragmented using a restriction enzyme ii) the generated fragments are separated by electrophoresis iii) the fragments are transferred to a membrane iv)the membrane is incubated with a radio labelled probe that hybridises any complementary subsequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
static light scattering
PSI-MI
sls
In static light scattering, the average intensity of scattered light at multiple angles is measured. The data yield information on particle molecular weight, particle size and shape, and particle-particle interactions.
PMID:9013660
http://purl.org/obo/owl/PMID#PMID_9013660
structure based prediction
PSI-MI
predict from struct
Methods based on 3D structure information.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
surface patches
PSI-MI
Surface patches are built using 6 criteria: solvation potential, residue interface propensity, hydrophobicity, planarity, protrusion and accessible surface area. Protein structures having similar patches are likely to have the same interactions.
PMID:9299343
http://purl.org/obo/owl/PMID#PMID_9299343
surface plasmon resonance
PSI-MI
This method measures formation of complex by monitoring changes in the resonance angle of light impinging on a gold surface as a result of changes in the refractive index of the surface. A ligand of interest (small molecule, peptide, protein, sugar, lipid, nucleic acid) is immobilized on a gold surface, and the interacting partner is injected in buffer flow over it. Biomolecules that interact with the immobilized ligand are retained on the surface, and alter the resonance angle of impinging light as a result of the change in refractive index brought about by the increased biomolecule mass retained on the surface. Since all the biomolecules belonging to the same class have the same refractive index and since there is a linear correlation between resonance angle shift and biomolecule concentration near the surface, this allows one to measure changes in concentration at the surface as a consequence of interaction. Furthermore, this is done in real time, allowing direct measurement of both the on-rate and the off-rate and of the affinity constant of complex formation.
PMID:11896282
http://purl.org/obo/owl/PMID#PMID_11896282
PMID:16338355
http://purl.org/obo/owl/PMID#PMID_16338355
PMID:12120258
http://purl.org/obo/owl/PMID#PMID_12120258
Optical biosensor
BIAcore(r)
spr
t7 phage display
Reference not index in medline: Rosenberg, A, Griffin, K, Studier, WS, McCormick, M, Berg, J, Novy, R, Mierendorf, R inNovations, 1996, 6, 1.
PSI-MI
T7 is a double stranded DNA bacteriophage with a thin-walled icosahedral capsid, ~550 Angstrom in diameter, which is decorated by 415 copies of the capsid protein, the product of gene 10. gp10 can tolerate insertions at the carboxyterminus without loosing its ability to be inserted into functional phage capsids. Both low density and high density display (albeit only with short peptides) can be achieved.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
t7 phage
tap tag coimmunoprecipitation
PSI-MI
The TAP method involves the fusion of the TAP tag (encoding a calmodulin binding peptide, a TEV cleavage site, and the Staphylococcus aureus Protein A) to the target protein and the introduction of the construct into the host cell or organism, maintaining the expression of the fusion protein at, or close to, its natural level. The fusion protein and associated components are recovered from cell extracts by affinity selection on an IgG matrix. After washing, the TEV protease is added to release the bound material. The eluate is incubated with calmodulin-coated beads in the presence of calcium. This second affinity step is required to remove the TEV protease as well as traces of contaminants remaining after the first affinity selection. After washing, the bound material is released with EGTA. This two steps purification steps ensures a highly selective complex purification of the tapped protein (first round of selection on the protein A, a high affinity tag) under mild condition (non denaturant pH or conditions required to remove the tag).nOBSOLETE redundant term. Map to feature type: tap tagged (MI:0524) and as interaction detection method tandem affinity purification (MI:0676).
PMID:10504710
http://purl.org/obo/owl/PMID#PMID_10504710
tap tag coip
text mining
PSI-MI
Text mining methods can be used to predict or confirm interactions by automated processing of scientific literature. Co-occurrence in the same sentence of an abstract of gene products labels are analysed to evaluate whether it represents a valid evidence of an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dihydrofolate reductase reconstruction
PSI-MI
dhfr reconstruction
The gene for DHFR is rationally dissected into two fragments called F[1,2] and F[3]. Two proteins or protein domains that are thought to bind to each other can then be fused to either of the two DHFR fragments. Reconstitution of enzyme activity can be monitored in vivo by cell survival in DHFR-negative cells grown in the absence of nucleotides. A fluorescence assay can also be carried out taking advantage of fMTX binding to reconstituted DHFR. The basis of this assay is that complementary fragments of DHFR, when expressed and reassembled in cells, will bind with high affinity (Kd 5 540 pM) to fMTX in a 1:1 complex. fMTX is retained in cells by this complex, whereas the unbound fMTX is actively and rapidly transported out of the cells. Survival depends only on the number of molecules of DHFR reassembled.
PMID:10318894
http://purl.org/obo/owl/PMID#PMID_10318894
ubiquitin reconstruction
PSI-MI
ub reconstruction
In this method the two proteins, whose interaction is under investigation, (in this case mostly membrane proteins) are fused to an terminal fragment (Nub) and to a C-terminal fragment of ubiquitin (Cub). The two fragments do not associate to form a functional ubiquitin unless the two fused membrane proteins form a complex. The association is monitored by an ingenious trick. The C-term fragment of ubiquitin is expressed as a fusion to a transcription factor that being linked to a membrane protein cannot perform its function unless it is released form the ubiquitin fusion by a specific protease. This achieved through the activity of UBP (an ubiquitin specific protease) that cleaves off the reporter protein only when a functional ubiquitin is reconstituted.
PMID:9560251
http://purl.org/obo/owl/PMID#PMID_9560251
western blot
PSI-MI
Western blot is a procedure to identify and quantify proteins. A mixture of protein is first submitted to an electrophoresis in denaturing condition and then electro-transferred from the gel to a membrane. The membrane is then incubated with a primary antibody specific for a given protein or a specific residue modification in the sample under analysis. A secondary antibody, radiolabelled or fused to fluorophore or to a chromogenic enzyme, targets the first antibody and allows the visualisation of the protein band on the membrane.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Immuno blot
x-ray crystallography
PSI-MI
Analysis of a diffraction pattern generated by a single crystal. X-rays have a wavelength, typically around 1 Angstrom (the diameter of a hydrogen atom). If a narrow parallel beam of X-rays is directed at a sample of a pure protein, most of the X-rays will pass straight through it. A small fraction, however, will be scattered by the atoms in the sample. If the sample is a well-ordered crystal, the scattered waves will reinforce one another at certain points and will appear as diffraction spots when the X-rays are recorded by a suitable detector. The position and intensity of each spot in the X-ray diffraction pattern contain information about the position and nature of the atoms in the crystal. The three-dimensional structure of a large molecule can be deduced from the electron-density map of its crystal. In recent years X-ray diffraction analysis has become increasingly automated, and now the slowest step is likely to be the production of suitable macromolecule crystals. This requires high concentration of very pure macromolecule and empirical searching for the proper crystallisation conditions.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
x-ray diffraction
X-ray
yeast display
PSI-MI
The proteins are displayed on the surface of the yeast S. cerevisiae by fusion to signal sequences for protein secretion. This method is limited by the low efficiency of the yeast display system but can take full advantage of exploiting cell sorting methods (FACS) to isolate cells that display molecules with desired binding properties.
PMID:9181578
http://purl.org/obo/owl/PMID#PMID_9181578
feature type
PSI-MI
Property of a subsequence that may interfere with the binding of a molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
binding-associated region
PSI-MI
A region of a molecule identified as being involved in an interaction. This may or may not be a region of the protein in direct contact with the interacting partner.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
binding site
binding region
mutation
PSI-MI
Sequence variation due to insertion, deletion or substitution event.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation decreasing interaction
PSI-MI
Region of a molecule whose mutation or deletion decreases significantly interaction strength or rate (in the case of interactions inferred from enzymatic reaction).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation decreasing
hotspot
post translation modification
PSI-MI
Residue covalent modifications occurring in the specific protein form involved in an interaction.nOBSOLETE remap to MOD:00000.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ptm
acetylated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00394.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n-acetyl-alanine
PSI-MI
AAC
acetylalanine
(S)-2-(acetylamino)propanoic acid
[A:ac]
Residue modification.nOBSOLETE remap to MOD:00050.
RESID:AA0041
http://purl.org/obo/owl/RESID#RESID_AA0041
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
acetylalanine
N-acetyl-L-alanine
n2-acetyl-arginine
PSI-MI
[R:ac]
N2-acetyl-L-arginine
alpha-acetylamino-delta-guanidinovaleric acid
acetylarginine
acetylarginine
RAC
Residue modification.nOBSOLETE remap to MOD:00359.
RESID:AA0354
http://purl.org/obo/owl/RESID#RESID_AA0354
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n-acetyl-asparagine
PSI-MI
[N:ac]
acetylasparagine
Residue modification.nOBSOLETE remap to MOD:00780.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
NAC
N-acetyl-L-asparagine
n-acetyl-aspartic acid
PSI-MI
DAC
acetylaspartic acid
acetylaspartate
[D:ac]
(S)-2-(acetylamino)butanedioic acid
Residue modification.nOBSOLETE remap to MOD:00051.
RESID:AA0042
http://purl.org/obo/owl/RESID#RESID_AA0042
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N-acetyl-L-aspartic acid
n-acetyl-cysteine
PSI-MI
(R)-2-acetylamino-3-sulfanylpropanoic acid
2-acetylamino-3-mercaptopropanoic acid
[C:ac]
acetylcysteine
CAC
N-acetyl-L-cysteine
N-acetylcysteine
Residue modification.nOBSOLETE remap to MOD:00052.
RESID:AA0043
http://purl.org/obo/owl/RESID#RESID_AA0043
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n-acetyl-glutamine
PSI-MI
QAC
N-acetyl-L-glutamine
Residue modification.nOBSOLETE remap to MOD:00054.
RESID:AA0045
http://purl.org/obo/owl/RESID#RESID_AA0045
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[Q:ac]
(S)-2-acetylamino-5-pentanediamic acid
acetylglutamine
acetylglutamine
n-acetyl-glutamic acid
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00053.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0044
http://purl.org/obo/owl/RESID#RESID_AA0044
(S)-2-(acetylamino)pentanedioic acid
EAC
acetylglutamic acid
acetylglutamate
[E:ac]
N-acetyl-L-glutamic acid
n-acetylglycine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00055.
RESID:AA0046
http://purl.org/obo/owl/RESID#RESID_AA0046
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[G:ac]
2-(acetylamino)ethanoic acid
N-acetylglycine
GAC
acetylglycine
aceturic acid
n-acetyl-histidine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00781.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
acetylhistidine
HAC
[H:ac]
N-acetyl-L-histidine
n-acetyl-isoleucine
PSI-MI
(2S,3S)-2-acetylamino-3-methylpentanoic acid
acetylisoleucine
[I:ac]
Residue modification.nOBSOLETE remap to MOD:00056.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0047
http://purl.org/obo/owl/RESID#RESID_AA0047
acetylisoleucine
IAC
N-acetyl-L-isoleucine
n-acetyl-leucine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00782.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[L:ac]
acetylleucine
LAC
N-acetyl-L-leucine
n2-acetyl-lysine
PSI-MI
(S)-2-acetylamino-6-aminohexanoic acid
n2-acetyllysine
Residue modification.nOBSOLETE remap to MOD:00057.
RESID:AA0048
http://purl.org/obo/owl/RESID#RESID_AA0048
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[K:ac]
KAC
N2-acetyl-L-lysine
N2-acetyllysine
n6-acetyl-lysine
PSI-MI
N(zeta)-acetyllysine
N6-acetyl-L-lysine
epsilon-acetyllysine
KA6
n6-acetyllysine
Residue modification.nOBSOLETE remap to MOD:00064.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0055
http://purl.org/obo/owl/RESID#RESID_AA0055
[K:N6ac]
(S)-2-amino-6-(acetylamino)hexanoic acid
n-acetyl-methionine
PSI-MI
[M:ac]
acetylmethionine
acetylmethionine
MAC
methionamine
N-acetyl-L-methionine
(S)-2-acetylamino-4-(methylsulfanyl)butanoic acid
2-acetylamino-4-(methylthio)butanoic acid
Residue modification.nOBSOLETE remap to MOD:00058.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0049
http://purl.org/obo/owl/RESID#RESID_AA0049
n-acetyl-phenylalanine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00784.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N-acetyl-L-phenylalanine
FAC
acetylphenylalanine
[F:ac]
n-acetyl-proline
PSI-MI
[P:ac]
(2S)-1-acetyl-2-pyrrolidinecarboxylic acid
PAC
acetylproline
Residue modification.nOBSOLETE remap to MOD:00059.
RESID:AA0050
http://purl.org/obo/owl/RESID#RESID_AA0050
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N-acetyl-L-proline
acetylproline
n-acetyl-serine
PSI-MI
SAC
N-acetylserine
N-acetyl-L-serine
Residue modification.nOBSOLETE remap to MOD:00060.
RESID:AA0051
http://purl.org/obo/owl/RESID#RESID_AA0051
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(S)-2-acetylamino-3-hydroxypropanoic acid
[S:ac]
acetylserine
n-acetyl-threonine
PSI-MI
(2S,3R)-2-acetylamino-3-hydroxybutanoic acid
[T:ac]
acetylthreonine
N-acetyl-L-threonine
Residue modification.nOBSOLETE remap to MOD:00061.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0052
http://purl.org/obo/owl/RESID#RESID_AA0052
TAC
N-acetylthreonine
n-acetyl-tryptophan
PSI-MI
N-acetyl-L-tryptophan
acetyltryptophan
WAC
Residue modification.nOBSOLETE remap to MOD:00785.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[W:ac]
n-acetyl-tyrosine
PSI-MI
N-acetyl-L-tyrosine
acetyltyrosine
[Y:ac]
(S)-2-acetylamino-3-(4-hydoxyphenyl)propanoic acid
Residue modification.nOBSOLETE remap to MOD:00062.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0053
http://purl.org/obo/owl/RESID#RESID_AA0053
YAC
N-acetyltyrosine
n-acetyl-valine
PSI-MI
(S)-2-acetylamino-3-methylbutanoic acid
N-acetyl-L-valine
Residue modification.nOBSOLETE remap to MOD:00063.
RESID:AA0054
http://purl.org/obo/owl/RESID#RESID_AA0054
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N-acetylvaline
[V:ac]
acetylvaline
VAC
amidated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00674.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
alanine amide
PSI-MI
L-alanine amide
alanineamide
(S)-2-aminopropanamide
[A:am]
AAM
alaninamide
Residue modification.nOBSOLETE remap to MOD:00090.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
arginine amide
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00091.
RESID:AA0082
http://purl.org/obo/owl/RESID#RESID_AA0082
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(S)-2-amino-5-guanidinopentanamide
arginineamide
argininamide
RAM
L-arginine amide
[R:am]
formylated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00493.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n-formyl-methionine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00030.
RESID:AA0021
http://purl.org/obo/owl/RESID#RESID_AA0021
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N-formyl-L-methionine
MFM
2-formylamino-4-(methylthio)butanoic acid
(S)-2-formylamino-4-(methylsulfanyl)butanoic acid
formylmethionine
[M:form]
hydroxylated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00428.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
4-hydroxy-proline
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00039.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0030
http://purl.org/obo/owl/RESID#RESID_AA0030
4-hydroxy-L-proline
4hydroxyproline
[P:hy_g]
HYP
lipid modification
PSI-MI
Residue modification.nOBSOLETE remap to MOD:01155.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
s-farnesyl-cysteine
PSI-MI
(R,E,E)-2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylsulfanyl)propanoic acid
farnesylcysteine
CFN
Residue modification.nOBSOLETE remap to MOD:00111.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0102
http://purl.org/obo/owl/RESID#RESID_AA0102
[C:farn]
2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid
S-farnesyl-L-cysteine
s-geranylgeranyl-cysteine
PSI-MI
2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid
Residue modification.nOBSOLETE remap to MOD:00113.
RESID:AA0104
http://purl.org/obo/owl/RESID#RESID_AA0104
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(R,E,E,E)-2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylsulfanyl)propanoic acid
[C:ger]
CGR
geranylgeranylcys
S-geranylgeranyl-L-cysteine
n-palmitoyl-cysteine
PSI-MI
[C:palm_n]
n-palmitoylcysteine
N-palmitoyl-L-cysteine
N-(1-oxahexadecyl)-L-cysteine
CPN
(R)-2-hexadecanoylamino-3-sulfanylpropanoic acid
2-hexadecanoylamino-3-mercaptopropanoic acid
Residue modification.nOBSOLETE remap to MOD:00069.
RESID:AA0060
http://purl.org/obo/owl/RESID#RESID_AA0060
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
s-palmitoyl-cysteine
PSI-MI
2-amino-3-(hexadecanoylthio)propanoic acid
(R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid
s-palmitoylcysteine
cysteine palmitate thioester
S-palmitoyl-L-cysteine
CPS
cysteine hexadecanoate thioester
Residue modification.nOBSOLETE remap to MOD:00115.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0106
http://purl.org/obo/owl/RESID#RESID_AA0106
[C:palm_s]
n-myristoyl-glycine
PSI-MI
myristoylglycine
N-myristoyl-glycine
Residue modification.nOBSOLETE remap to MOD:00068.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0059
http://purl.org/obo/owl/RESID#RESID_AA0059
[G:myr]
GMY
n6-myristoyl-lysine
PSI-MI
KMY
epsilon-myristoyllysine
myristoyllysine
Residue modification.nOBSOLETE remap to MOD:00087.
RESID:AA0078
http://purl.org/obo/owl/RESID#RESID_AA0078
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(S)-2-amino-6-(tetradecanoylamino)hexanoic acid
[K:myr]
N(zeta)-myristoyllysine
N6-(1-oxotetradecyl)-L-lysine
N6-myristoyl-L-lysine
methylated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00427.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n-methyl-alanine
PSI-MI
(S)-2-methylaminopropanoic acid
Residue modification.nOBSOLETE remap to MOD:00070.
RESID:AA0061
http://purl.org/obo/owl/RESID#RESID_AA0061
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[A:meth_n]
AMT
methylalanine
N-methyl-L-alanine
N-methylalanine
n,n,n-trimethyl-alanine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00071.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0062
http://purl.org/obo/owl/RESID#RESID_AA0062
[A:meth_n3]
AM3
N,N,N-trimethyl-L-alanine
(S)-2-(trimethylammonio)propanoic acid
trimethylalanine
(S)-1-carboxy-N,N,N-trimethylethanaminium
omega-n,omega-n-dimethyl-arginine
PSI-MI
NG,NG-dimethylarginine
dimethylarginine
RM2
omega-N,omega-N-dimethyl-L-arginine
asymmetric dimethylarginine
(S)-2-amino-5-[((dimethylamino)iminomethyl)amino]pentanoic acid
[R:meth_n7]
Residue modification.nOBSOLETE remap to MOD:00077.
RESID:AA0068
http://purl.org/obo/owl/RESID#RESID_AA0068
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
beta-methylthioaspartic acid
PSI-MI
3-carboxy-S-methyl-cysteine
(2R,3Xi)-2-amino-3-methylsulfanylbutanedioic acid
3-methylthio-aspartic acid
Residue modification.nOBSOLETE remap to MOD:00237.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0232
http://purl.org/obo/owl/RESID#RESID_AA0232
[D:meth_b]
beta-methylthio-aspartic acid
DM2
L-beta-methylthioaspartic acid
methylthioaspartate
n5-methyl-glutamine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00080.
RESID:AA0071
http://purl.org/obo/owl/RESID#RESID_AA0071
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
[Q:meth_n5]
(S)-2-amino-N5-methylpentanediamic acid
QM5
N5-methyl-L-glutamine
methylglutamine
gamma-methylglutamine
N-methylglutamine
N(delta)-methylglutamine
glutamic acid 5-methyl ester
PSI-MI
glutamic acid gamma-methyl ester
L-glutamic acid 5-methyl ester
EM5
Residue modification.nOBSOLETE remap to MOD:00081.
RESID:AA0072
http://purl.org/obo/owl/RESID#RESID_AA0072
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
glutamatemethylester
5-methyl-L-glutamate
[E:meth_o5]
(S)-2-aminopentanedioic acid 5-methyl ester
3'-methyl-histidine
PSI-MI
methylhistidine
[H:meth_n4]
3'-methyl-L-histidine
1-methylhistidine [misnomer]
pros-methylhistidine
pi-methylhistidine
N(delta)-methylhistidine
MHS
Residue modification.nOBSOLETE remap to MOD:00082.
RESID:AA0073
http://purl.org/obo/owl/RESID#RESID_AA0073
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid
n6-methyl-lysine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00085.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N6-methyl-L-lysine
N(zeta)-methyllysine
MLZ
methyllysine
epsilon-methyllysine
[K:meth_1]
(S)-2-amino-6-methylaminohexanoic acid
n6,n6-dimethyl-lysine
PSI-MI
[K:meth_2]
(S)-2-amino-6-dimethylaminohexanoic acid
epsilon-dimethyllysine
dimethyllysine
MLY
lysine derivative Lys(y)
N6,N6-dimethyl-L-lysine
N(zeta)-dimethyllysine
Residue modification.nOBSOLETE remap to MOD:00084.
RESID:AA0075
http://purl.org/obo/owl/RESID#RESID_AA0075
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n6,n6,n6-trimethyl-lysine
PSI-MI
trimethyllysine
[K:meth_3]
(S)-5-amino-5-carboxy-N,N,N-trimethylpentanaminium
(S)-2-amino-6-(trimethylammonio)hexanoic acid
N6,N6,N6-trimethyl-L-lysine
N(zeta)-trimethyllysine
Residue modification.nOBSOLETE remap to MOD:00083.
RESID:AA0074
http://purl.org/obo/owl/RESID#RESID_AA0074
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
M3L
epsilon-trimethyllysine
n-methyl-methionine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00073.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0064
http://purl.org/obo/owl/RESID#RESID_AA0064
N-methylmethionine
MMT
N-methyl-L-methionine
[M:meth]
methylmethionine
(S)-2-methylamino-4-(methylsulfanyl)butanoic acid
2-methylamino-4-(methylthio)butanoic acid
n-methyl-phenylalanine
PSI-MI
N-methylphenylalanine
N-methyl-L-phenylalanine
methylphenylalanine
FMT
[F:meth]
(S)-2-methylamino-3-phenylpropanoic acid
Residue modification.nOBSOLETE remap to MOD:00074.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphorylated residue
PSI-MI
phosphorylated
Residue modification.nOBSOLETE remap to MOD:00696.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
omega-n-phospho-arginine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00227.
RESID:AA0222
http://purl.org/obo/owl/RESID#RESID_AA0222
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RPO
phosphoarginine
omega-N-phospho-L-arginine
N5-[imino(phosphonoamino)methyl]-L-ornithine
alpha-amino-delta-phosphonoguanidinovaleric acid
[R:po]
(S)-2-amino-5-[imino(phosphonoamino)methyl]aminopentanoic acid
aspartic 4-phosphoric anhydride
PSI-MI
L-aspartic 4-phosphoric anhydride
phosphoaspartic acid
phosphoaspartic acid
DPO
beta-aspartyl phosphate
[D:po]
(S)-2-aminobutanedioic 4-phosphoric anhydride
Residue modification.nOBSOLETE remap to MOD:00042.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0033
http://purl.org/obo/owl/RESID#RESID_AA0033
s-phospho-cysteine
PSI-MI
S3-phosphocysteine
CPO
cysteine phosphate thioester
(R)-2-amino-3-(phosphonosulfanyl)propanoic acid
[C:po]
Residue modification.nOBSOLETE remap to MOD:00043.
RESID:AA0034
http://purl.org/obo/owl/RESID#RESID_AA0034
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
S-phosphonocysteine
phosphocysteine
S-phospho-L-cysteine
1'-phospho-histidine
PSI-MI
histidine-N(epsilon)-phosphate
[H:po_e]
histidine-3-phosphate [misnomer]
Residue modification.nOBSOLETE remap to MOD:00044.
RESID:AA0035
http://purl.org/obo/owl/RESID#RESID_AA0035
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
HPE
histidine-N1'-phosphate
tele-phosphohistidine
tau-phosphohistidine
1-phosphohistidine
1'-phospho-L-histidine
(S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
3'-phospho-histidine
PSI-MI
[H:po_d]
(S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
3-phosphohistidine
pi-phosphohistidine
pros-phosphohistidine
histidine-1-phosphate [misnomer]
histidine-N(delta)-phosphate
histidine-N3'-phosphate
HPD
Residue modification.nOBSOLETE remap to MOD:00045.
RESID:AA0036
http://purl.org/obo/owl/RESID#RESID_AA0036
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
o-phospho-serine
PSI-MI
O-phosphonoserine
O3-phosphoserine
phosphoserine
serine phosphate ester
2-amino-3-hydroxypropanoic acid 3-phosphate
2-amino-3-hydroxypropanoic acid 3-phosphate;O-phosphonoserine;O3-phosphoserine
[S:po]
O-phospho-L-serine
Residue modification.nOBSOLETE remap to MOD:00046.
RESID:AA0037
http://purl.org/obo/owl/RESID#RESID_AA0037
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(S)-2-amino-3-(phosphonooxy)propanoic acid
SPO
o-phospho-threonine
PSI-MI
threonine phosphate ester
TPO
(2S,3R)-2-amino-3-phosphonooxybutanoic acid
2-amino-3-hydroxybutanoic acid 3-phosphate
[T:po]
O-phospho-L-threonine
Residue modification.nOBSOLETE remap to MOD:00047.
RESID:AA0038
http://purl.org/obo/owl/RESID#RESID_AA0038
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
O3-phosphothreonine
phosphothreonine
o4'-phospho-tyrosine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00048.
RESID:AA0039
http://purl.org/obo/owl/RESID#RESID_AA0039
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
YPO
O4'-phospho-L-tyrosine
O4-phosphotyrosine
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate
[Y:po]
(S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid
tyrosine phosphate
phosphotyrosine
other modification
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00032.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
selenocysteine
PSI-MI
CSE
[C:sel]
L-selenocysteine
selenium cysteine
Residue modification.nOBSOLETE remap to MOD:00031.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0022
http://purl.org/obo/owl/RESID#RESID_AA0022
3-selenylalanine
selenomethionine
PSI-MI
MSE
L-selenomethionine
[M:sel]
Residue modification.nOBSOLETE remap to MOD:00530.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
3-oxoalanine
PSI-MI
L-amino-malonic acid semialdehyde
L-alpha-formylglycine
L-serinesemialdehyde [misnomer]
L-aminomalonaldehydic acid
2-amino-3-oxopropionic acid
Residue modification.nOBSOLETE remap to MOD:01169.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0185
http://purl.org/obo/owl/RESID#RESID_AA0185
L-3-oxoalanine
[S:oxal]
SOX
(S)-2-amino-3-oxopropanoic acid
oxoalanine
2-pyrrolidone-5-carboxylic acid
PSI-MI
pyroglutamic acid
pyroglutamic acid
Residue modification.nOBSOLETE remap to MOD:00040.
RESID:AA0031
http://purl.org/obo/owl/RESID#RESID_AA0031
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
(S)-5-oxo-2-pyrrolidinecarboxylic acid
5-oxoproline
2-oxopyrrolidine-5-carboxylic acid
[E:pyro]
5-oxopyrrolidine-2-carboxylic acid
glutamyl 5-glycerylphosphorylethanolamine
PSI-MI
L-glutamyl 5-glycerophosphorylethanolamine
L-glutamyl 5-glycerylphosphorylethanolamine
[E:gpe]
EGE
glycerylpo4etohamine
L-glutamyl 5-glycerophosphoethanolamine
(S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid
Residue modification.nOBSOLETE remap to MOD:00179.
RESID:AA0170
http://purl.org/obo/owl/RESID#RESID_AA0170
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
2'-[3-carboxamido-3-(trimethylammonio)propyl]-histidine
PSI-MI
diphthamide
[H:diph]
alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium
2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide
2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid
2-[3-carboxamido-3-(trimethylammonio)propyl]histidine
2-[(Xi)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole
HDP
2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine
diphthamide
Residue modification.nOBSOLETE remap to MOD:00049.
RESID:AA0040
http://purl.org/obo/owl/RESID#RESID_AA0040
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
n6-biotinyl-lysine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00126.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0117
http://purl.org/obo/owl/RESID#RESID_AA0117
biotinyllysine
[K:biotin]
biocytin
epsilon-N-biotinyllysine
KBT
N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine
N6-biotinyl-L-lysine
N6-biotinyllysine
(3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine
(S)-2-amino-6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]aminohexanoic acid
n6-(4-amino-2-hydroxybutyl)-lysine
PSI-MI
(S,R)-2-amino-6-(4-amino-2-hydroxybutylamino)hexanoic acid
[K:hypu]
Residue modification.nOBSOLETE remap to MOD:00125.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0116
http://purl.org/obo/owl/RESID#RESID_AA0116
hypusine
hypusine
KHY
N6-(4-amino-2-hydroxybutyl)-L-lysine
n6-retinal-lysine
PSI-MI
(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
[K:retin]
KRT
Residue modification.nOBSOLETE remap to MOD:00129.
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
RESID:AA0120
http://purl.org/obo/owl/RESID#RESID_AA0120
N6-retinylidene-L-lysine
retinallysine
N6-retinal-L-lysine
N6-retinyl-lysine
ubiquitinated lysine
PSI-MI
Residue modification due to a cross-link between a lysine and a glycine from the ubiquitine protein.nOBSOLETE remap to MOD:00134.
RESID:AA0125
http://purl.org/obo/owl/RESID#RESID_AA0125
PMID:11125103
http://purl.org/obo/owl/PMID#PMID_11125103
N6-glycyllysine
N6-glycyl-L-lysine
KUB
[K:ub]
interaction type
PSI-MI
Connection between molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
aggregation
PSI-MI
Physical association among molecules.nOBSOLETE since too non-specific. Consider using physical interaction (MI:0218) instead.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
acetylation reaction
PSI-MI
acetylation
Reaction, that can affect K,C,A,D,E,Q,G,I,K,M,P,S,T,Y,V residues.
RESID:AA0042
http://purl.org/obo/owl/RESID#RESID_AA0042
RESID:AA0053
http://purl.org/obo/owl/RESID#RESID_AA0053
RESID:AA0052
http://purl.org/obo/owl/RESID#RESID_AA0052
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0041
http://purl.org/obo/owl/RESID#RESID_AA0041
RESID:AA0051
http://purl.org/obo/owl/RESID#RESID_AA0051
RESID:AA0049
http://purl.org/obo/owl/RESID#RESID_AA0049
RESID:AA0054
http://purl.org/obo/owl/RESID#RESID_AA0054
RESID:AA0050
http://purl.org/obo/owl/RESID#RESID_AA0050
RESID:AA0055
http://purl.org/obo/owl/RESID#RESID_AA0055
RESID:AA0047
http://purl.org/obo/owl/RESID#RESID_AA0047
RESID:AA0056
http://purl.org/obo/owl/RESID#RESID_AA0056
GO:0006473
http://purl.org/obo/owl/GO#GO_0006473
RESID:AA0048
http://purl.org/obo/owl/RESID#RESID_AA0048
RESID:AA0045
http://purl.org/obo/owl/RESID#RESID_AA0045
RESID:AA0046
http://purl.org/obo/owl/RESID#RESID_AA0046
RESID:AA0043
http://purl.org/obo/owl/RESID#RESID_AA0043
RESID:AA0044
http://purl.org/obo/owl/RESID#RESID_AA0044
amidation reaction
PSI-MI
Irreversible reaction that can affect A,R,N,D,C,Q,E,G,H,I,L,K,M,F,P,S,T,W,Y or V residues.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0081
http://purl.org/obo/owl/RESID#RESID_AA0081
GO:0001519
http://purl.org/obo/owl/GO#GO_0001519
RESID:AA0084
http://purl.org/obo/owl/RESID#RESID_AA0084
RESID:AA0083
http://purl.org/obo/owl/RESID#RESID_AA0083
RESID:AA0100
http://purl.org/obo/owl/RESID#RESID_AA0100
RESID:AA0086
http://purl.org/obo/owl/RESID#RESID_AA0086
RESID:AA0099
http://purl.org/obo/owl/RESID#RESID_AA0099
RESID:AA0085
http://purl.org/obo/owl/RESID#RESID_AA0085
RESID:AA0098
http://purl.org/obo/owl/RESID#RESID_AA0098
RESID:AA0082
http://purl.org/obo/owl/RESID#RESID_AA0082
RESID:AA0092
http://purl.org/obo/owl/RESID#RESID_AA0092
RESID:AA0093
http://purl.org/obo/owl/RESID#RESID_AA0093
RESID:AA0094
http://purl.org/obo/owl/RESID#RESID_AA0094
RESID:AA0095
http://purl.org/obo/owl/RESID#RESID_AA0095
RESID:AA0096
http://purl.org/obo/owl/RESID#RESID_AA0096
RESID:AA0097
http://purl.org/obo/owl/RESID#RESID_AA0097
RESID:AA0088
http://purl.org/obo/owl/RESID#RESID_AA0088
RESID:AA0087
http://purl.org/obo/owl/RESID#RESID_AA0087
RESID:AA0090
http://purl.org/obo/owl/RESID#RESID_AA0090
RESID:AA0089
http://purl.org/obo/owl/RESID#RESID_AA0089
RESID:AA0091
http://purl.org/obo/owl/RESID#RESID_AA0091
amidation
cleavage reaction
PSI-MI
cleavage
Covalent bond breakage in a molecule leading to the formation of smaller molecules.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
covalent binding
PSI-MI
Interaction leading to the formation of covalent bond within an autocatalytic molecule or between partners.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
covalent interaction
PSI-MI
Physical interaction mediated by covalent bond rearrangement.nOBSOLETE use covalent binding (MI:0195) instead.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
deacetylation reaction
PSI-MI
deacetylation
N6-acetyl-L-lysine or S-acetyl-L-cysteine are cleaved and return K or C residues.
GO:0006476
http://purl.org/obo/owl/GO#GO_0006476
RESID:AA0055
http://purl.org/obo/owl/RESID#RESID_AA0055
RESID:AA0056
http://purl.org/obo/owl/RESID#RESID_AA0056
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
defarnesylation reaction
PSI-MI
defarnesylation
S-farnesyl-L-cysteined is cleaved and returns a C residue.
RESID:AA0102
http://purl.org/obo/owl/RESID#RESID_AA0102
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
deformylation reaction
PSI-MI
deformylation
N6-formyl-L-lysine is cleaved and returns a K residue.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0211
http://purl.org/obo/owl/RESID#RESID_AA0211
degeranylation reaction
PSI-MI
degeranylation
S-geranylgeranyl-L-cysteine is cleaved and returns a C residue.
RESID:AA0104
http://purl.org/obo/owl/RESID#RESID_AA0104
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
demyristoylation reaction
PSI-MI
N6-myristoyl-L-lysine is cleaved and returns a K residue.
RESID:AA0078
http://purl.org/obo/owl/RESID#RESID_AA0078
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
demyristoylation
depalmitoylation reaction
PSI-MI
S-palmitoyl-L-cysteine, N6-palmitoyl-L-lysine, O-palmitoyl-L-threonine or O-palmitoyl-L-serine are cleaved and return C,K,T or S residues.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0060
http://purl.org/obo/owl/RESID#RESID_AA0060
RESID:AA0077
http://purl.org/obo/owl/RESID#RESID_AA0077
RESID:AA0106
http://purl.org/obo/owl/RESID#RESID_AA0106
depalmitoylation
dephosphorylation reaction
PSI-MI
Phosphoresidues are cleaved and return D,C,H,S,T,Y or R residues.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0033
http://purl.org/obo/owl/RESID#RESID_AA0033
GO:0016311
http://purl.org/obo/owl/GO#GO_0016311
RESID:AA0036
http://purl.org/obo/owl/RESID#RESID_AA0036
RESID:AA0035
http://purl.org/obo/owl/RESID#RESID_AA0035
RESID:AA0034
http://purl.org/obo/owl/RESID#RESID_AA0034
RESID:AA0222
http://purl.org/obo/owl/RESID#RESID_AA0222
RESID:AA0039
http://purl.org/obo/owl/RESID#RESID_AA0039
RESID:AA0038
http://purl.org/obo/owl/RESID#RESID_AA0038
RESID:AA0037
http://purl.org/obo/owl/RESID#RESID_AA0037
dephosphorylation
deubiquitination reaction
PSI-MI
deubiquitination
Cleavage of the G-K bond and release of ubiquitin or ubiquitin like proteins.
GO:0016579
http://purl.org/obo/owl/GO#GO_0016579
PMID:11583613
http://purl.org/obo/owl/PMID#PMID_11583613
RESID:AA0125
http://purl.org/obo/owl/RESID#RESID_AA0125
disaggregation
PSI-MI
Dissociation of partners interacting via non-covalent bond.nOBSOLETE because considered misleading.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
farnesylation reaction
PSI-MI
Reversible reaction that can affect C residue.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0102
http://purl.org/obo/owl/RESID#RESID_AA0102
GO:0018347
http://purl.org/obo/owl/GO#GO_0018347
farnesylation
formylation reaction
PSI-MI
Reaction that can affect K or G residues. Reside is functionalised with a formyl group.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0018256
http://purl.org/obo/owl/GO#GO_0018256
RESID:AA0211
http://purl.org/obo/owl/RESID#RESID_AA0211
RESID:AA0057
http://purl.org/obo/owl/RESID#RESID_AA0057
formylation
genetic interaction
PSI-MI
Two genes A and B "genetically interact" when the phenotype generated as the result of mutations in both genes (double mutant ab) is unexpectedly not just a combination of the phenotypes of the two single mutants a and b.
PMID:16527956
http://purl.org/obo/owl/PMID#PMID_16527956
geranylgeranylation reaction
PSI-MI
Attachment of one or two 20-carbon lipophilic geranylgeranyl isoprene units from geranylgeranyl diphosphate to one or more cysteine residue(s).Reversible reaction that can affect C residue.
RESID:AA0104
http://purl.org/obo/owl/RESID#RESID_AA0104
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0018348
http://purl.org/obo/owl/GO#GO_0018348
geranylgeranylation
hydroxylation reaction
PSI-MI
Irreversible introduction of a hydroxyl group that can affect K,P,Y or R residues. Hydroxylation is the first step in the oxidative degeneration of organic compounds.
RESID:AA0215
http://purl.org/obo/owl/RESID#RESID_AA0215
RESID:AA0146
http://purl.org/obo/owl/RESID#RESID_AA0146
RESID:AA0030
http://purl.org/obo/owl/RESID#RESID_AA0030
RESID:AA0029
http://purl.org/obo/owl/RESID#RESID_AA0029
RESID:AA0028
http://purl.org/obo/owl/RESID#RESID_AA0028
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0018126
http://purl.org/obo/owl/GO#GO_0018126
hydroxylation
lipid addition
PSI-MI
Covalent or non covalent binding of lipid group on a protein residue.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0006497
http://purl.org/obo/owl/GO#GO_0006497
lipid cleavage reaction
PSI-MI
lipid cleavage
Cleavage of a lipid group covalently bound to a protein residue.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methylation reaction
PSI-MI
The covalent attachment of a methyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological polymer. Irreversible reaction that can affect A,G,M,F,P,C,R,N,Q,E,H,or K residues.
RESID:AA0076
http://purl.org/obo/owl/RESID#RESID_AA0076
RESID:AA0067
http://purl.org/obo/owl/RESID#RESID_AA0067
RESID:AA0068
http://purl.org/obo/owl/RESID#RESID_AA0068
RESID:AA0234
http://purl.org/obo/owl/RESID#RESID_AA0234
RESID:AA0065
http://purl.org/obo/owl/RESID#RESID_AA0065
RESID:AA0272
http://purl.org/obo/owl/RESID#RESID_AA0272
RESID:AA0066
http://purl.org/obo/owl/RESID#RESID_AA0066
RESID:AA0069
http://purl.org/obo/owl/RESID#RESID_AA0069
RESID:AA0070
http://purl.org/obo/owl/RESID#RESID_AA0070
RESID:AA0071
http://purl.org/obo/owl/RESID#RESID_AA0071
RESID:AA0072
http://purl.org/obo/owl/RESID#RESID_AA0072
RESID:AA0063
http://purl.org/obo/owl/RESID#RESID_AA0063
RESID:AA0073
http://purl.org/obo/owl/RESID#RESID_AA0073
RESID:AA0064
http://purl.org/obo/owl/RESID#RESID_AA0064
RESID:AA0074
http://purl.org/obo/owl/RESID#RESID_AA0074
RESID:AA0061
http://purl.org/obo/owl/RESID#RESID_AA0061
RESID:AA0075
http://purl.org/obo/owl/RESID#RESID_AA0075
RESID:AA0062
http://purl.org/obo/owl/RESID#RESID_AA0062
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0043414
http://purl.org/obo/owl/GO#GO_0043414
methylation
myristoylation reaction
PSI-MI
Irreversible covalent addition of a myristoyl group via an amide bond to the alpha-amino group of an amino acid. Reaction that can affect K or G residues.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0018319
http://purl.org/obo/owl/GO#GO_0018319
RESID:AA0078
http://purl.org/obo/owl/RESID#RESID_AA0078
RESID:AA0059
http://purl.org/obo/owl/RESID#RESID_AA0059
myristoylation
non covalent interaction
PSI-MI
non covalent inter
Interaction mediated by non-covalent, weak forces rearrangement.nOBSOLETE use physical interaction (MI:0218) instead.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
palmitoylation reaction
PSI-MI
Covalent attachment of palmitic acid to the cysteine residues of membrane proteins. Reversible reaction that can affect C,K,T or S residues.
RESID:AA0106
http://purl.org/obo/owl/RESID#RESID_AA0106
RESID:AA0079
http://purl.org/obo/owl/RESID#RESID_AA0079
RESID:AA0080
http://purl.org/obo/owl/RESID#RESID_AA0080
RESID:AA0060
http://purl.org/obo/owl/RESID#RESID_AA0060
RESID:AA0077
http://purl.org/obo/owl/RESID#RESID_AA0077
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0018318
http://purl.org/obo/owl/GO#GO_0018318
palmitoylation
phosphorylation reaction
PSI-MI
Reversible reaction that can affect D,C,H,S,T,Y,R residues.
RESID:AA0034
http://purl.org/obo/owl/RESID#RESID_AA0034
RESID:AA0033
http://purl.org/obo/owl/RESID#RESID_AA0033
RESID:AA0036
http://purl.org/obo/owl/RESID#RESID_AA0036
RESID:AA0035
http://purl.org/obo/owl/RESID#RESID_AA0035
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0016310
http://purl.org/obo/owl/GO#GO_0016310
RESID:AA0037
http://purl.org/obo/owl/RESID#RESID_AA0037
RESID:AA0038
http://purl.org/obo/owl/RESID#RESID_AA0038
RESID:AA0039
http://purl.org/obo/owl/RESID#RESID_AA0039
RESID:AA0222
http://purl.org/obo/owl/RESID#RESID_AA0222
phosphorylation
physical interaction
PSI-MI
Interaction among molecules that can be direct or indirect.nOBSOLETE: splitted to 'association' MI:0914 and 'physical association' MI:0915. For remapping consider the experimental setting of an interaction. For bulk remapping a possible criteria is to whatever physical interaction that has among its participant a bait should become 'association' MI:0914 the others can become 'physical association' MI:0915. Two hybrid interactions are an expection and can be 'physical association' MI:0915.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
synthetic lethal
PSI-MI
Death phenotype observed on cells carrying combination of two independently silent mutations.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description (lethal FBcv:0000351)
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
ubiquitination reaction
PSI-MI
Reversible reaction that create a covalent bond between a C-terminus G of ubiquitin and a K residue of the target.
GO:0016567
http://purl.org/obo/owl/GO#GO_0016567
RESID:AA0125
http://purl.org/obo/owl/RESID#RESID_AA0125
PMID:11583613
http://purl.org/obo/owl/PMID#PMID_11583613
ubiquitination
expression level
PSI-MI
Synthesis rate of a molecule under investigation described in comparison with its naturally occurring expression level in a cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
physiological level
PSI-MI
A molecule whose synthesis is under control of its natural gene promoter or estimated to be expressed at a similar rate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
endogenous
endogenous level
under expressed level
PSI-MI
A molecule is estimated to be expressed at lower levels than in physiological condition.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
under-expressed
chromatin immunoprecipitation array
PSI-MI
The method combines a modified chromatin immunoprecipitation (ChIP) procedure, with DNA microarray analysis. Cells are fixed with formaldehyde, harvested, and disrupted by sonication. The DNA fragments cross-linked to a protein of interest are enriched by immunoprecipitation with a specific antibody. After reversal of the cross-links, the enriched DNA is amplified and labeled with a fluorescent dye (Cy5) by using a ligation-mediatedpolymerase chain reaction (LM-PCR). In parallel a sample of DNA that is not enriched by immunoprecipitation is subjected to LM-PCR in the presence of a different fluorophore (Cy3), and both immunoprecipitation (IP)-enriched and unenriched pools of labeled DNA were hybridized to a single DNA microarray containing a set of intergenic sequences. The ratio of the Cy5 to Cy3 fluorescence intensities measured at each DNA element in the microarray provided a measure of the extent of binding of the transcription factor to the corresponding genomic locus.
PMID:11125145
http://purl.org/obo/owl/PMID#PMID_11125145
PMID:11206552
http://purl.org/obo/owl/PMID#PMID_11206552
chip-chip
ion exchange chromatography
PSI-MI
Stable complexes and their component proteins can be separated on the basis of their net charge by ion-exchange chromatography. If a protein has a net positive charge at pH 7, it will usually bind to a column of beads containing carboxylate groups, and can then be eluted by increasing the concentration of sodium chloride or another salt in the eluting buffer by competition of sodium ions with positively charged groups on the protein for binding to the column. Protein that have a low density of net positive charge will tend to emerge first, followed by those having a higher charge density. Positively charged complexes or proteins (cationic proteins) can be separated on negatively charged carboxymethyl-cellulose (CM-cellulose) columns. Conversely, negatively charged complexes or proteins (anionic proteins) can be separated by chromatography on positively charged diethylaminoethyl-cellulose (DEAE-cellulose) columns.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
IEC
ion exchange chrom
reverse phase chromatography
PSI-MI
Reverse phase chromatography operates on the basis of hydrophilicity and lipophilicity. The stationary phase consists of silica based packings with n-alkyl chains covalently bound. For example, C-8 signifies an octyl chain and C-18 an octadecyl ligand in the matrix. The more hydrophobic the matrix on each ligand, the greater is the tendency of the column to retain hydrophobic moieties. Thus hydrophilic compounds elute more quickly than do hydrophobic compounds.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
reverse phase chrom
cytoplasmic complementation assay
PSI-MI
cytoplasmic compl
Protein complementation assay performed by dissecting a cytoplasmic protein activity and restoring it through the two hybrid proteins interaction. OBSOLETE remap to MI:0090 protein complementation assay
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
membrane bound complementation assay
PSI-MI
OBSOLETE remap to MI:0090 protein complementation assay.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
membrane compl
mammalian protein protein interaction trap
PSI-MI
The MAPPIT(mammalian protein-protein interaction Trap) is a screening method for protein-protein interaction in mammalian cells, based on the reconstitution of a membrane STAT (signal transducers and activators of transcription) receptor. The bait protein is fused to a STAT recruitment-deficient receptor and the prey protein to a functional STAT recruitment sites. In such a configuration, a given baitprey interaction restores a STAT-dependent responses leading to the expression of a reporter gene. This system, enable to demonstrate not only protein interaction but also modification-independent and tyrosine phosphorylation- dependent interactions.
PMID:12853652
http://purl.org/obo/owl/PMID#PMID_12853652
mappit
transcriptional complementation assay
PSI-MI
Protein complementation assay performed by dissecting a transcription factor activity (DNA binding domain and transcription activation domain) its restoration through the two hybrid proteins interaction that lead to a reporter gene expression.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
transcription compl
protein dna complex
PSI-MI
A stable set of interacting protein and DNA that can be copurified and operate as a functional unit.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
131i radiolabel
PSI-MI
131I
I131
Molecule labelled with 131 radio isotope of iodine atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
14c radiolabel
PSI-MI
Molecule labelled with the radio isotope 14 of carbon atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
C14
14C
32p radiolabel
PSI-MI
P32
32P
Molecule labelled with the radio isotope 32 of phosphorus atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
33p radiolabel
PSI-MI
Molecule labelled with the radio isotope 33 of phosphorus atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
P33
33P
3h radiolabel
PSI-MI
H3
3H
tritium
Molecules labelled with isotope 3 of hydrogen atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biotin tag
PSI-MI
Biotin, a 244 Dalton vitamin found in tissue and blood, binds with high affinity to avidin and streptavidin protein. Since biotin is a relatively small molecule, it can be conjugated to many proteins or nucleic acids without significantly altering their biological activity. Biotinylation reagents are available for targeting a variety of specific functional groups, including primary amines, sulfhydryls, carboxyls and carbohydrates that lead to nucleotides or amino acid biotinilation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fusion protein
PSI-MI
The protein under study is expressed as a fusion with a labelling protein, having either fluorescence properties or an enzymatic activity that facilitates its purification, identification, localisation or quantification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
horseradish peroxidase tag
PSI-MI
hrp tag
Protein is fused to horseradish peroxidase, and the measure of this enzyme activity can be taken as indicative of presence of protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene ontology definition reference
PSI-MI
go-definition-ref
This qualifier is used when the crossreference is imported from the Gene Ontology tag definition_reference.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
isoform parent sequence reference
PSI-MI
isoform-parent
Reference to the master sequence from which this isoform has been derived.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
reactome complex
PSI-MI
id-validation-regexp:"REACT_[0-9]{1,5}.[0-9]{1,3}|[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"REACT_[0-9]{1,5}.[0-9]{1,3}|[0-9]+"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
Collection of functional complexes within Reactome - a knowledgebase of biological processes.nhttp://www.reactome.org/
PMID:21067998
http://purl.org/obo/owl/PMID#PMID_21067998
reactome protein
PSI-MI
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
Collection of protein within the Reactome database - a knowledgebase of biological processes.nhttp://www.reactome.org/
PMID:21067998
http://purl.org/obo/owl/PMID#PMID_21067998
id-validation-regexp:"REACT_[0-9]{1,4}.[0-9]{1,3}|[OPQ][0-9][A-Z0-9]{3}[0-9]|[OPQ][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z]{3}[0-9]{5}|[OPQ][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"REACT_[0-9]{1,4}.[0-9]{1,3}|[OPQ][0-9][A-Z0-9]{3}[0-9]|[OPQ][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z]{3}[0-9]{5}|[OPQ][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
cabri
PSI-MI
id-validation-regexp:"[0-9]+|ACCs[A-Z0-9]+|ECACCs[A-Z0-9]+|LMBPs[A-Z0-9]+|ICLCs[A-Z0-9]+|CIP-[0-9]+|DSMZ_MUTZ:ACCs[0-9]+_"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+|ACCs[A-Z0-9]+|ECACCs[A-Z0-9]+|LMBPs[A-Z0-9]+|ICLCs[A-Z0-9]+|CIP-[0-9]+|DSMZ_MUTZ:ACCs[0-9]+_"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
CABRI cell lines catalogue available at.nhttp://www.cabri.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
newt
PSI-MI
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
New EBI Web Taxonomy.nhttp://www.ebi.ac.uk/newt OBSOLETE: Consider remapping to uniprot taxonomy MI:0942
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
resid
PSI-MI
The RESID Database of Protein Modifications is a comprehensive collection of annotations and structures for protein modifications including amino-terminal, carboxyl-terminal and peptide chain cross-link post-translational modifications.nhttp://www.ebi.ac.uk/RESID/index.html
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"AA[0-9]{4}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"AA[0-9]{4}"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
huge
PSI-MI
A Database of Human Unidentified Gene-Encoded Large Proteins Analyzed by Kazusa Human cDNA Project.nhttp://www.kazusa.or.jp/huge/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"KIAA[0-9]{4}[A-Z]{0,1}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"KIAA[0-9]{4}[A-Z]{0,1}"
gene
PSI-MI
interactor for genetic interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
SO:0000704
http://purl.org/obo/owl/SO#SO_0000704
gene product
PSI-MI
Reference of a protein object pointing to its genomic or nucleic acid sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biological feature
PSI-MI
Property of a subsequence that may be involved with or interfere with the binding of a molecule and are supported by experimental evidences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
isotope label
PSI-MI
One of several nuclides having the same number of protons in their nuclei and hence having the same atomic number, but differing in the number of neutrons and therefore, in the mass number.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genetic interference
PSI-MI
This term refers to methods that aim at interfering with the activity of a specific gene by altering the gene regulatory or coding sequences. This goal can be achieved either by a classical genetic approach (random mutagenesis followed by phenotype characterization and genetic mapping) or by a reverse genetics approach where a gene of interest is modified by directed mutagenesis.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
post transcriptional interference
PSI-MI
This term refers to methods designed to interfere with gene expression at post-transcriptional level rather than with the gene itself.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
expression interfer
rna interference
PSI-MI
RNA interference (RNAi) is a post-transcriptional gene silencing method reproducing a naturally occurring phenomena. RNAi is the process whereby double-stranded RNA (dsRNA) induces the sequence-specific degradation of homologous mRNA. RNAi or dsRNA-induced silencing phenomena are present in evolutionarily diverse organisms, e.g., nematodes, plants, fungi, and trypanosomes. The mechanisms by which RNAi works is initiated by a progressive cleavage of dsRNA into 21 to 23 nucleotide (nt) short interfering RNAs (siRNAs). These native siRNA duplexes are then incorporated into a protein complex called RNA-induced silencing complex (RISC). ATP-dependent unwinding of the siRNA duplex generates an active RISC complex. Guided by the antisense strand of siRNA, the active RISC complex recognizes and cleaves the corresponding mRNA.
PMID:12110901
http://purl.org/obo/owl/PMID#PMID_12110901
PMID:12408823
http://purl.org/obo/owl/PMID#PMID_12408823
rnai
antisense rna
PSI-MI
This approach is based on the observation that expression of RNA that is complementary to a specific mRNA can decrease the synthesis of its gene product either by increasing the degradation of the targeted mRNA or by interfering with its translation.
PMID:1340158
http://purl.org/obo/owl/PMID#PMID_1340158
inhibitor antibodies
PSI-MI
Intracellular or extracellular expression of antibodies is used to target specific gene products in order to inactivate them. Most of the times the antibody scaffold need s to reengineered for efficient expression and solubility in the cytoplasm.nOBSOLETE as such method can be described using the biological role inhibitor (MI:0586).
PMID:10189716
http://purl.org/obo/owl/PMID#PMID_10189716
perturbagens peptides
PSI-MI
This approach is based on the expression of peptides that bind to specific target proteins thereby interfering with their activity. In a standard approach the interfering peptide is expressed by genetic fusion to a stable protein scaffold. Interfering peptides can also be introduced into cells by fusing them to proteins or peptides (homeodomains, Tat protein.) having the property of penetrating the cell membrane. The peptide-carrier fusion protein is either synthesized chemically or produced in vivo, normally in bacteria. When the purified fusion protein is added to a cell culture, it penetrates the cell membrane thereby permitting the fused peptide to interfere with its target protein.nOBSOLETE as such method can be described using the biological role inhibitor (MI:0586).
PMID:8606778
http://purl.org/obo/owl/PMID#PMID_8606778
PMID:11731788
http://purl.org/obo/owl/PMID#PMID_11731788
perturbagens pep
inhibitor small molecules
PSI-MI
Protein activity is inhibited by small inorganic molecules (drugs) that specifically bind to their targets. Recently this classical pharmacological approach is sometime referred to as 'chemical genetics'.nOBSOLETE as such method can be described using the biological role inhibitor (MI:0586).
PMID:10780927
http://purl.org/obo/owl/PMID#PMID_10780927
PMID:10542155
http://purl.org/obo/owl/PMID#PMID_10542155
inhibitor small mol
suppression
PSI-MI
A supressed gene mutation cause of an altered phenotype that is reverted to wild type phenotype when cell also carry a suppressor gene with a specific mutation or altered expression level.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppression mutation
PSI-MI
A given (suppressed) mutation phenotype is reverted by a supressor gene mutation.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'mutated gene' MI:0804.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppression knockout
PSI-MI
Knocked out gene is the suppressor of a phenotype.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'knock out' MI:0788.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppress knockout
suppression partial alteration
PSI-MI
A mutation is the partial suppressor of a mutant phenotype.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'knock down' MI:0789.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppression partial
suppression expression alteration
PSI-MI
An altered expression is the suppressor of a phenotype.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'expression level alteration' MI:0803.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppress expression
suppression overexpression
PSI-MI
suppress overexpress
Overexpression is the suppressor of a phenotype.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'over expressed' MI:0506.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppression scalable
PSI-MI
Level of over/underexpression scales the 'extend' of a phenotype.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'expression level alteration' MI:0803.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppression underexpression
PSI-MI
Underexpression is the suppressor of a phenotype.nOBSOLETE: remap to CV intraction type 'suppressive interaction' MI:0793 and genetic experimental form 'under expressed' MI:0223.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
suppress underexpres
synthetic phenotype
PSI-MI
Two silent mutations show an altered phenotype when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
conditional synthetic lethal
PSI-MI
cond syntetic lethal
Two silent mutations show a conditional synthetic lethal phenotype when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description (lethal FBcv:0000351)
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
conditional synthetic lethal temperature-sensitivity
PSI-MI
Two silent mutations show a temperature sensitive lethal phenotype when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description (FBcv:0000310 'temperature conditional')
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
temprtr synt lethal
synthetic growth effect
PSI-MI
Two silent mutations show altered growth effect when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description ( FBcv:0000427 'cell growth defective')
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
synt growth effect
synthetic growth defect
PSI-MI
Two silent mutations show growth defect when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description ( FBcv:0000427 'cell growth defective')
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
synt growth defect
synthetic growth increase
PSI-MI
synt growth increase
Two silent mutations show growth increase when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description ( FBcv:0000427 'cell growth defective')
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
blue native page
PSI-MI
bn-page
Blue native PAGE (BN-PAGE) permits a high-resolution separation of multi-protein complexes under native conditions. Blue native (BN)-PAGE is a charge shift method, in which the electrophoretic mobility of a complex is determined by the negative charge of the bound Coomassie dye and the size and shape of the complex. Coomassie does not act as a detergent and preserves the structure of complexes. Importantly, the resolution of BN-PAGE is much higher than that of other methods such as gel filtration or sucrose-gradient ultracentrifugation. Combined with other pre-purifications or dialysis steps this method permits the analysis of multi-protein complexes of whole cellular lysates by BN-PAGE.
PMID:14665681
http://purl.org/obo/owl/PMID#PMID_14665681
alias type
PSI-MI
CvAliasType
Descriptor of type of nomenclature used to describe interactor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene name
PSI-MI
Gene name.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene
gene name synonym
PSI-MI
Gene name synonym.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene ontology synonym
PSI-MI
go synonym
Synonym as used in Gene Ontology.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
isoform synonym
PSI-MI
Isoform synonym.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ordered locus name
For instance HI0934, Rv3245c, At5g34500, YER456W.
PSI-MI
Ordered locus name
ORF number
systematic gene number
locus name
ONL
CDS number
A name used to represent an ORF in a completely sequenced genome or chromosome. It is generally based on a prefix representing the organism and a number which usually represents the sequential ordering of genes on the chromosome. Depending on the genome sequencing center, numbers are attributed only to protein-coding genes, or also to pseudogenes, or also to tRNAs and other features.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
open reading frame name
For instance MtCY277-28c, SYGP-ORF50, SpBC2F12-04, C06E1, CG10954. Also called Sequencing names or Contig names or Temporary ORFNames.
PSI-MI
orf name
A name temporarily attributed by a sequencing project to an open reading frame. This name is generally based on a cosmid numbering system.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
delivery method
PSI-MI
Method by which molecule is delivered or engineered into a cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
electroporation
PSI-MI
Method for temporarily permeabilising cell membranes so as to facilitate the entry of large or hydrophilic molecules (as in transfection). A brief (ca 1 msec) electric pulse is given with potential gradients of about 700V/cm.
PMID:6329708
http://purl.org/obo/owl/PMID#PMID_6329708
genomic tagging
PSI-MI
A cassette coding for a protein tag is inserted by homologous recombination onto the genomic copy of an open reading frame. The advantage of this delivery method is that the resulting engineered protein is expressed under its natural promoter control.nOBSOLETE redundant term. Map to feature type : tag (MI:0507).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genetic tag insertion
infection
PSI-MI
Molecule introduced into a cell via an external organism, usually a virus or bacteria.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
microinjection
PSI-MI
The insertion of a substance into a cell through a microneedle. To extrude the substances through the very fine needle tip, either hydrostatic pressure (pressure injection) or electric currents (ionophoresis) is employed.
PMID:3016916
http://purl.org/obo/owl/PMID#PMID_3016916
micro-injection
nucleic acid transfection
PSI-MI
nucl transfection
Introducing DNA into eukaryotic cells, such as animal cells, is called transfection. Transfection typically involves opening transient "holes" or gates in cells to allow the entry of extracellular molecules, typically supercoiled plasmid DNA, but also siRNA, among others. Transfection differs from transformation since the DNA is not generally incorporated into the cell's genome, it is only transiently expressed.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interactor type
PSI-MI
Molecular species involved in the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
participant type
complex
PSI-MI
Set of interacting molecules that can be copurified. This term and its children should be use only at PARTICIPANT level.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein complex
PSI-MI
A stable set of interacting proteins that can be copurified and operate as a functional unit.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ribonucleoprotein complex
PSI-MI
ribonucleoprot compl
A macromolecular complex containing both protein and RNA molecules.
GO:0030529
http://purl.org/obo/owl/GO#GO_0030529
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein rna complex
interaction
PSI-MI
Previously described interaction now being used as an interactor to describe hierarchical build-up of complexes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid
PSI-MI
Linear polymers of nucleotides, linked by 3',5' phosphodiester linkages.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
SO:0000348
http://purl.org/obo/owl/SO#SO_0000348
deoxyribonucleic acid
PSI-MI
dna
DNA
deoxyribonucleic acid
Polymer formed by the deoxyribose sugar group, and the nucleotides bases adenine, guanine, thymine and cytosine.
SO:0000352
http://purl.org/obo/owl/SO#SO_0000352
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ribonucleic acid
PSI-MI
RNA
rna
Polymer formed by ribose sugar group, and the bases of the nucleotides adenine, guanine, uracil and cytosine.
SO:0000356
http://purl.org/obo/owl/SO#SO_0000356
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
catalytic rna
PSI-MI
catalytic ribonucleic acid
catalytic RNA
crna
Species of RNA that catalyses cleavage or trans-esterification of the phosphodiester link.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
guide rna
PSI-MI
Small RNA molecules that hybridize to specific mRNAs and direct their RNA editing.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
grna
guide RNA
heterogeneous nuclear rna
PSI-MI
heterogeneous nuclear RNA
hnrna
A heterogeneous mixture of RNA molecules with a rapid turnover rate that occurs in cell nuclei during protein synthesis; it is the form of RNA synthesized in eukaryotes by RNA polymerase II, which is translated into protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
heterogeneous nuclear ribonucleic acid
messenger rna
PSI-MI
mrna
Single-stranded RNA molecule that specifies the amino acid sequence of one or more polypeptide chains.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mRNA
transfer rna
PSI-MI
The low molecular weight RNAs that specifically bind amino acids by aminoacetylation to form aminoacyl tRNA and which possess a special nucleotide triplet, the anticodon.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
transfer ribonucleic acid
tRNA
transfer RNA
trna
protein
PSI-MI
A linear polymer of amino acids joined by peptide bonds in a specific sequence.
SO:0000358
http://purl.org/obo/owl/SO#SO_0000358
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
peptide
PSI-MI
oligopeptide
polypeptide
Chains of amino acids joined by peptide bonds. Distinction between peptides, oligopeptides and polypeptides is arbitrarily by length; a polypeptide is perhaps more than 15 residues.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
small molecule
PSI-MI
Molecule not part of or directly encoded by the genome, encompasses any constitutionally or isotopically distinct atom, molecule, ion, ion pair, radical, radical ion, complex, conformer, etc., identifiable as a separately distinguishable entity.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
unknown participant
PSI-MI
Any type of molecule, including complexes, that may be observed but not identified. This term should be use only at PARTICIPANT level.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molecular source
PSI-MI
Defines whether molecule is endogenously expressed or has in any way been altered, in sequence or expression level, from its native state. For a complete description of the experimental molecule form use the orthogonal CVs expression level, delivery method, and sample process.
PMID:14755272
http://purl.org/obo/owl/PMID#PMID_14755272
engineered
PSI-MI
Molecule has been added into system from an external source or altered within the cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
naturally occurring
PSI-MI
Unaltered endogenous molecule in its naturally occurring state.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
endogenous
feature range status
PSI-MI
startStatus
endStatus
CvFuzzyType
Describes sequence positions resolution of a given participant feature. In PSI schema this CV is associated with the start and end position of a feature range.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
c-terminal position
Displayed as 'c'.
PSI-MI
carboxy-terminus
c-terminus
Term describing the last amino acid of a peptide chain.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
c-term
c-terminal
certain sequence position
PSI-MI
certain
Position within the sequence clearly defined.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
greater-than
Displayed as '>'.
PSI-MI
Partially determined sequence position known to be in a location higher than a given position.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
less-than
Displayed as '<'.
PSI-MI
Partially determined sequence position known to be in a position lower than a given position.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
range
For instance when an amino acid modification is known to be in the region from 5 to 7. Displayed as '..'.
PSI-MI
Describes a sequence position known to be in a certain range, where the exact position is unclear.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
undetermined sequence position
Displayed as '?'.
PSI-MI
Term describing a completely unknown or unspecified sequence position.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
undetermined
n-terminal position
Displayed as 'n'.
PSI-MI
n-term
Term describing the first amino acid of a peptide chain.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
amino-terminus
n-terminal
n-terminus
ragged n-terminus
PSI-MI
Mixture of protein forms where N-terminus has been progressively truncated.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
sample process
PSI-MI
Indicates the sample context in which each interacting molecule is presented to its partner.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cdna library
PSI-MI
Mixed population of cDNAs (complementaryDNA) made from mRNA from a defined source, usually a specific cell type. This term should be associated only to nucleic acid interactors not to their proteins product. For instance in 2h screening use living cells (MI:0349) as sample process.
PMID:6110205
http://purl.org/obo/owl/PMID#PMID_6110205
cell lysate
PSI-MI
Cell has been physically or chemically broken open and molecule present in resulting mixture of cellular components.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
author assigned name
PSI-MI
Name assigned to a molecule by the authors within a paper that may differ from the reference database.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental preparation
PSI-MI
experimental prep
Set of terms to describe the participant experimental treatment and status. This term groups a number of orthologous short controlled vocabularies delivery method, expression level, molecular source, and sample process. Each participant can then be annotated with a maximum of 4 terms selected from each short list.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fixed cell
PSI-MI
Cells has been fixed by treatment with organic solvent, staining and inclusion in a resin for microscopic analysis.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
living cell
PSI-MI
Molecule is observed within in a living cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
purified
PSI-MI
Molecule has undergone one or more purification steps to isolate it from the cellular environment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
homogeneous
PSI-MI
pure
The author states a molecule is completely pure, i.e. no other molecular species are present.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
partially purified
PSI-MI
The author states a molecule is only partially purified, i.e. other molecular species also known to be present.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cross-reference type
PSI-MI
xref type
refType
CvXrefQualifier
Qualifier to describe the type of information a cross-reference is pointing to.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene ontology term for cellular component
PSI-MI
go component term
Cross reference pointing to a Gene Ontology -'cellular component' term.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
component
gene ontology term for cellular function
PSI-MI
function
Cross reference pointing to a Gene Ontology -'cellular function' term.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
go function term
identical object
For instance this qualifier, in an interaction entry, can be associated to a cross reference to the same interaction in an other database.
PSI-MI
identity
Reference to the corresponding object in another database. Correspondence may be complete or partial.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
method reference
PSI-MI
Reference to a related paper which more fully describes either the experimental method or one or more of the interactors used within the experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
primary-reference
PSI-MI
Used to indicate the PMID from which the experimental data is extracted.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene ontology term for cellular process
PSI-MI
process
Cross reference pointing to a Gene Ontology -'cellular process' term.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
go process term
secondary accession number
PSI-MI
secondary-ac
Reference to the corresponding object in another database (like identity xref qualifier) but the identifier used in the external database is a secondary identifier or former accession number.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
see-also
PSI-MI
Related object within the same database or pointing to an external database.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
inference
PSI-MI
modeled
Evidence based on human assumption, either when the complete experimental support is not available or when the results are extended by homology to closely related orthologues sequences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
modelled
inferred by author
PSI-MI
modeled by author
Evidence based on the author of a paper assumption, either when the complete experimental support is not available or when the results are extended by homology to closely related orthologues sequences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
modelled by author
inferred by curator
PSI-MI
modelled by curator
modeled by curator
Evidence based on a curator assumption, either when the complete experimental support is not available or when the results are extended by homology to closely related orthologues sequences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
enzyme tag
PSI-MI
Molecule under study is fused to an enzyme, for example alkaline phosphatase, and measure of enzyme activity can be taken as indicative of presence of protein.
PMID:10935637
http://purl.org/obo/owl/PMID#PMID_10935637
alkaline phosphatase tag
PSI-MI
alk phosphatase tag
Protein is fused to alkaline phosphatase, and the measure of this enzyme activity can be taken as indicative of presence of protein.
PMID:10935637
http://purl.org/obo/owl/PMID#PMID_10935637
green fluorescent protein tag
PSI-MI
GFP
gfp tag
green fluorescent protein
The green fluorescent protein of organisms such as the bioluminescent jellyfish Aequorea victoria can be fused to individual proteins which then acquire fluorescence excitation and emission spectra virtually identical to those of the native.
PMID:7491768
http://purl.org/obo/owl/PMID#PMID_7491768
yellow fluorescent protein tag
PSI-MI
Yellow fluorescent protein from species such as Vibrio fischeri can be fused to individual proteins which then acquire fluorescence excitation and emission spectra virtually identical to those of the native.
PMID:10929120
http://purl.org/obo/owl/PMID#PMID_10929120
yellow fluorescent protein
YFP
yfp tag
lex-a dimerization assay
PSI-MI
gallex
The method is based on the repression of a reporter gene activity by two LexA DNA binding domains with different binding specificities. LexA is a transcription factor with an N-terminal DNA binding/activation domain (DBAct) and a C-terminal dimerization domain. LexA dimerization is required to repress transcription efficiently. The discovery of LexA DNA binding domains that bind to different DNA sequence enabled the development of this system.
PMID:12446730
http://purl.org/obo/owl/PMID#PMID_12446730
gallex
tox-r dimerization assay
PSI-MI
toxcat
toxcat
This assay allow identification of interactions in the inner membrane of E. coli. by using a chimeric construct ToxR-TM-MBP composed of the N-terminal DNA binding/transcriptional activation domain of ToxR (a dimerization dependant transcription factor) fused to a transmembrane domain of interest (TM) and a monomeric periplasmic anchor (the maltose binding protein). Association of the two TM results in the ToxR-mediated activation of a reporter gene such as CAT (chloroamphenicol acetyltransferase activity). The level of CAT expression indicates the strength of TM association. CAT expression can then be tested and quantify by measuring CAM resistance with disk diffusion assay or CAT activity assays on cell-free extracts.
PMID:9927659
http://purl.org/obo/owl/PMID#PMID_9927659
35s radiolabel
PSI-MI
Molecule labelled with 35 radio isotope of sulfur. Proteins are often metabolically labelled, usually be growth in 35S labelled culture medium.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
S35
s35 radiolabelled
35S
subcellular preparation
PSI-MI
Cell lysates are partially fractionated to isolate a specific subcellular fraction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
subcellular prep
dye label
PSI-MI
Dye coupled to a molecule allowing its identification isolation and monitoring.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
dye labelled
cyanine label
PSI-MI
The organic cyanine dyes emit in the red range (>550 nm), offer a number of advantages. Their emission range is such that background fluorescence is often reduced. In addition these molecules can be linked directly to specific locations in synthetically produced nucleic acids.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
cy3 label
PSI-MI
The organic cyanine Cy3 emits maximally at 570 nm.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
cy5 label
PSI-MI
The organic cyanine Cy5 emits maximally at 670 nm.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
fluorescein isothiocyanate label
PSI-MI
Fluorescein isothiocyanate is a yellow-green coloured low molecular weight dye which couples to proteins via reaction with primary amine groups at high pH. FITC is excitable at 488nm, close to its absorption maximum at 494nm, and produces maximum fluorescence emission around 520nm.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
FITC labelled
fitc labelled
fluorescein isothiocyanate labbeled
rare isotope label
PSI-MI
Molecule can be labelled including rare isotopes among its constituent atoms that can be used to identify, localize or quantify the full molecule.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
rare isotope label
13c label
PSI-MI
Molecules labelled with isotope 13 of carbon atoms.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
13C
C13
15n label
PSI-MI
Molecules labelled with isotope 15 of nytrogen atoms.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
15N
N15
2h label
PSI-MI
deuterium
D2
2H2
Molecules labelled with isotope 2 of hydrogen atoms.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
mutation increasing interaction
PSI-MI
Region of a molecule whose mutation or deletion increases significantly interaction strength or rate (in the case of interactions inferred from enzymatic reaction).
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
mutation increasing
biopolymer
PSI-MI
Molecule consisting of a specific sequence of amino acidic or nucleotidic monomers strung together through chemical bonds.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
alexa label
PSI-MI
All Alexa dyes are fluorescent iodoacetamide dyes that can be conjugated with the primary amines of biomolecules. All Alexa dyes and their conjugates are more fluorescent and more photostable than the commonly used dyes. The numbers in the Alexa names indicate the approximate excitation wavelength maximum in nm).
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 350 label
PSI-MI
Alexa fluorescent dye analogue to AMCA (7-amino-4-methylcoumarin-3-acetic acid) with an approximate excitation wavelength maximum of 350 nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 430 label
PSI-MI
Alexa fluorescent dye analogue to Lucifer Yellow with an approximate excitation wavelength maximum of 430 nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 488 label
PSI-MI
Alexa fluorescent dye analogue to Oregon Green 488 with an approximate excitation wavelength maximum of 488 nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 532 label
PSI-MI
Alexa fluorescent dye analogue to Rhodamine 6G with an approximate excitation wavelength maximum of 532nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 546 label
PSI-MI
Alexa fluorescent dye analogue to Cy3 with an approximate excitation wavelength maximum of 546nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 568 label
PSI-MI
Alexa fluorescent dye analogue to Rhodamine Red-X with an approximate excitation wavelength maximum of 568nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
alexa 594 label
PSI-MI
Alexa fluorescent dye analogue to Texas Red-X with an approximate excitation wavelength maximum of 594nm.
PMID:10449539
http://purl.org/obo/owl/PMID#PMID_10449539
predetermined participant
PSI-MI
Molecule whose sequence identity is not checked and has been assumed from external or previous experimental evidence(s).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
predetermined
two hybrid array
PSI-MI
Two-hybrid screening can be done in a colony array format, in which each colony expresses a defined pair of proteins. Because the particular protein pair expressed in each colony is defined by its position in the array, positive signals identify interacting proteins without further characterization, thus obviating the need for DNA purification and sequencing. The interrogation of a two-hybrid colony array usually involves a mating strategy in which every DNA binding domain hybrid (the bait) is tested against all activation domain hybrids (the preys) in a grid pattern. Arrays usually use full-length open reading frames.
PMID_for_application_instance:10688190
http://purl.org/obo/owl/PMID_for_application_instance#PMID_for_application_instance_10688190
PMID:11827624
http://purl.org/obo/owl/PMID#PMID_11827624
two hybrid pooling approach
PSI-MI
In the pooling strategy sets of either both bait and prey hybrid vectors are mated or, more commonly, individual baits are mated against pools of preys. This approach required cloning baits and preys into both two-hybrid vectors, followed by pooling sets of transformants. The positive double hybrid clones are the interacting partners. The pooling of both baits and prey molecules is now a rarely used technique as the pooling of baits often leads to misleading results.
PMID:11283351
http://purl.org/obo/owl/PMID#PMID_11283351
PMID:20946815
http://purl.org/obo/owl/PMID#PMID_20946815
two hybrid pooling
two hybrid fragment pooling approach
PSI-MI
2h fragment pooling
Individual baits are mated against pools of random fragmented preys. The usage of degenerated fragment allows identification of the minimal protein region required for the interaction. Since multiple clones that encode overlapping regions of protein are often identified, the minimal domain for interaction may be readily apparent from the initial screen.
PMID:12634794
http://purl.org/obo/owl/PMID#PMID_12634794
affinity technology
PSI-MI
affinity techniques
Techniques which depend upon the strength of the interaction between two entities.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biochemical
PSI-MI
The application of chemical principles and methods to biological experiments to demonstrate an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chromatin immunoprecipitation assay
PSI-MI
ch-ip
Chromatin immunoprecipitation (ChIP) is a powerful approach that allows one to define the interaction of factors with specific chromosomal sites in living cells. An antibody against a protein suspected of binding a given cis-element is used to immunoprecipitate fragmented chromatin fragments. Cells or tissue may first be briefly treated with an agent such formaldehyde to crosslink proteins to DNA. Nucleic acids are then identified by sequencing, for example polymerase chain reaction analysis of the immunoprecipitate with primers flanking the cis-element or next-generation sequencing techniques
PMID:12054902
http://purl.org/obo/owl/PMID#PMID_12054902
colocalization
PSI-MI
Coincident occurrence of molecules in a given subcellular fraction observed with a low resolution methodology from which a physical interaction among those molecules cannot be inferred.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
comigration in non denaturing gel electrophoresis
PSI-MI
comig non denat gel
comigration by non denaturing gel electrophoresis.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
competition binding
PSI-MI
Competitive binding experiments measure equilibrium binding of a single concentration of ligand at various concentrations of an unlabeled competitor. Analysis of these data gives the affinity of the receptor for the competitor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
deacetylase assay
PSI-MI
Measures the catalysis of the hydrolysis of an acetyl group or groups from a substrate molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
direct interaction
PSI-MI
Interaction that is proven to involve only its interactors.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
disulfide bond
PSI-MI
Covalent bond mediated by 2 sulfur atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dna footprinting
PSI-MI
Experimental method used to identify the region of a nucleic acid involved in an interaction with a protein. One sample of a radiolabeled nucleic acid of known sequence is submitted to partial digestion. A second sample is incubated with its interacting partner and then is submitted to the same partial digestion. The two samples are then analyzed in parallel by electrophoresis on a denaturing acrylamide gel. After autoradiography the identification of the bands that correspond to fragments missing from the lane loaded with the second sample reveals the region of the nucleic acid that is protected from nuclease digestion upon binding.nOBSOLETE because redundant with MI:0417 'footprinting' combined with interactor type MI:0319 'DNA' nreplace by:MI:0417
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
electron tomography
PSI-MI
electron tomog
Electron tomography is a general method for three-dimensional (3D) reconstruction of single, transparent objects from a series of projection images (i.e. from a tilt series) recorded with a transmission electron microscope. It offers the opportunity to obtain 3D information on structural cellular arrangements with a high resolution.
PMID:12160704
http://purl.org/obo/owl/PMID#PMID_12160704
enzyme linked immunosorbent assay
PSI-MI
Following non-covalent binding of a purified primary ligand to a solid phase, a blocking reagent is added to prevent any non-specific binding. A specific antigen is then allowed to bind to the primary ligand. Unbound antigen is removed by washing and a secondary antibody conjugated to an enzyme (e.g. horseradish peroxidase) is added. Following a washing step to remove unbound secondary ligand, the extent to which a chromogenic substrate (e.g. 3,3', 5,5' tetramethyl benzidine chromogen [TMB]) is converted to a soluble coloured product by the conjugated enzyme in a given time is determined by spectrophotometry using a standard microplate absorbance reader. A similar type of approach can be utilized to detect enzymatic activities. The substrate, attached to a solid phase is incubated in the presence of the enzyme and the enzymatic modification is monitored by an antibody that is specific for the modified substrate (for instance a phosphorylated protein).
PMID:11906746
http://purl.org/obo/owl/PMID#PMID_11906746
ELISA
elisa
electrophoretic mobility supershift assay
PSI-MI
emsa supershift
The EMSA supershift is a EMSA experiment carried out using a third lane loaded with the radiolabeled nucleic acid, a protein mixture and an antibody for a specific protein. If an extra retardation is observed, this is due to the formation of a larger complex including the antibody. By this approach, at least one protein of the complex is directly identified.
PMID:12169687
http://purl.org/obo/owl/PMID#PMID_12169687
electrophoretic mobility shift assay
PSI-MI
emsa
Gel retardation assay
band shift
This method proves the interaction between a nucleic acid and a protein partner. On the same electrophoresis gel 1 lane is loaded with a radiolabeled nucleic acid of known sequence, a second lane is loaded with the same nucleic acid together with a purified protein (or a protein mixture). After the electrophoresis run and autoradiography by comparing the nucleic acid migration in the two lanes the retardation of the nucleic acid due to its interaction with a protein can be easily observed.
PMID:12169687
http://purl.org/obo/owl/PMID#PMID_12169687
enzymatic reaction
PSI-MI
Biochemical reaction
terms aiming to represent biochemical reactions referring to their resulting product modifications.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
enzymatic study
PSI-MI
Participants are enzyme or substrate in a biochemical reaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence microscopy
PSI-MI
Fluorescent microscopy uses a high intensity light to illuminate the sample. This light excites fluorescence species in the sample, which then emit light of a longer wavelength. A fluorescent microscope also produces a magnified image of the sample, but the image is based on the second light source -- the light emanating from the fluorescent species -- rather than from the light originally used to illuminate, and excite, the sample.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence imaging
footprinting
PSI-MI
footprinting analysis is used to identify regions of molecules directly involved in binding other macromolecules and therefore protected from the effects of degradative enzymes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genetic
PSI-MI
methods supporting genetic interactions.nOBSOLETE as too unspecific use Genetic interference instead MI:0254.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gtpase assay
PSI-MI
Measures the catalysis of the reaction: GTP + H2O = GDP + phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GTPase
gtp hydrolisis
kinase homogeneous time resolved fluorescence
PSI-MI
Measures quenching of the nonradiative energy transfer between fluorescent long-lifetime lanthanide chelates and different acceptors. Relies on a fluorescence energy donor and acceptor being added from close proximity on the phosphorylated substrate due to the action of the kinase.
PMID:14987100
http://purl.org/obo/owl/PMID#PMID_14987100
homogeneous time-resolved fluorescence
kinase HTRF
kinase htrf
identification by antibody
PSI-MI
Antibody mediated participant identification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
antibody detection
immunostaining
PSI-MI
Method using an antibody coupled with some colouring agent to detect a specific protein within a cell or tissue sample. In some cases the primary antibody is directly linked to a colouring agent, more often the primary antibody is targeted by a secondary antibody, targeting the primary antibody.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
in-gel kinase assay
PSI-MI
in gel kinase assay
Substrate protein radio-labelled by kinase transferring an isotope of phosphate from the nucleotide. Substrate isolated by gel electrophoresis and radio-labelling confirmed by autoradiography.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein kinase assay
PSI-MI
Catalysis of the transfer of a phosphate group, usually from ATP, to a protein substrate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
kinase scintillation proximity assay
PSI-MI
Relies on the radiolabelling of a peptide substrate immobilized on a scintillant coated SPA-bead. The kinase transfers a phosphate isotope from the nucleotide to the substrate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
kinase spa
light microscopy
PSI-MI
Light visible microscopy uses environmental light to illuminate the sample and produce a magnified image of the sample.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Identification by mass spectrometry
PSI-MI
ms participant
identification by mass spectrometry.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
imaging technique
PSI-MI
microscopy
Methods that provide images of molecules at various resolution depending on the technology used.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
necessary binding region
PSI-MI
A sequence range within a molecule identified as being absolutely required for an interaction. The sequence may or may not be in direct physical contact with the interaction partner.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
required to bind
necessary binding site
deletion disrupting interaction
nucleic acid uv cross-linking assay
PSI-MI
Radiolabelled nucleic acids with a known sequence are incubated with purified proteins or reproducible protein mixture (HPLC eluate fractions) and then irradiated with UV. The complex are treated with an enzyme to remove the unbound nucleic acid (Rnase A or Dnase I for example), washed and then analyzed by electrophoresis. The eventual complexes are identified by autoradiography. The proteins involved in the complex can be recognized by specific antibodies or by retrieving the original protein mixture and carrying further analysis on it. The affinity of the binding can be estimated by adding a non-labelled nucleic acid as competitor before the UV irradiation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucl ac uv crosslink
obsolete
PSI-MI
Deprecated terms.nOBSOLETE term replaced by the default OBO class 'Obsolete'.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
one hybrid
PSI-MI
yeast one hybrid
one-hybrid
1 hybrid
Protein-DNA complementation assay where a single promoter act as bait and is screened against a library of prey transcription factors.
PMID:10589421
http://purl.org/obo/owl/PMID#PMID_10589421
yeast one-hybrid
partial identification of protein sequence
PSI-MI
partial id prot seq
partial protein sequence identification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphatase assay
PSI-MI
Measures the catalysis of the reaction: a phosphosubstrate + H2O = a substrate + phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protease assay
PSI-MI
Measures the enzymatic hydrolysis of a peptide bond within a peptide or protein substrate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein footprinting
PSI-MI
Protein footprinting is a technique for identifying structural changes modulated by protein-ligand binding, and mapping protein-ligand interfaces This technique involves attaching cutting reagents randomly to amino acid residue (e.g. lysine or cysteine) on the proteins surface and then using this lysine-labelled protein to cleave polypeptide backbone of the other protein at exposed residues adjacent to its binding site.
PMID:14987073
http://purl.org/obo/owl/PMID#PMID_14987073
PMID:14967031
http://purl.org/obo/owl/PMID#PMID_14967031
PMID:14600024
http://purl.org/obo/owl/PMID#PMID_14600024
protein three hybrid
PSI-MI
bridge assay
Two hybrid assay performed with a third protein component co-transfected into a recombinant yeast strain together with a bait and a prey construct. Negative control shows that the interaction between the bait and the prey do not occur when the third protein is not co-transfected.
PMID:12052864
http://purl.org/obo/owl/PMID#PMID_12052864
PMID:12935900
http://purl.org/obo/owl/PMID#PMID_12935900
PMID:12761205
http://purl.org/obo/owl/PMID#PMID_12761205
trihybrid
protein 3-hybrid
protein tri hybrid
rna three hybrid
PSI-MI
In vivo reconstruction of specific RNA-proteins interactions. The DNA binding and transcription activator domains of GAL4 are brought together via the interaction of recombinant RNA. The first hybrid protein contains the DNA binding domain of GAL4 fused to RevM10 (a mutated RNA binding protein of HIV-1 that binds specifically to the Rev responsive element RRE of the env gene). A recombinant RNA contains the RRE sequence and a target RNA sequence X. The second hybrid protein contains the activation domain of GAL4 fused to protein Y tested for its ability to bind the target RNA X. If this interaction occurs the three hybrid reconstructs GAL4 and the transcription of a reporter gene is activated.
PMID:8972875
http://purl.org/obo/owl/PMID#PMID_8972875
PMID:12162957
http://purl.org/obo/owl/PMID#PMID_12162957
rna tri hybrid
rna 3-hybrid
Three hybrid system
rna-three hybrid
random spore analysis
PSI-MI
RSA
spore germination
rsa
A technique used to detect genetic interactions between 2 (or more) genes in a sporulating organism by scoring a large population of haploid spores for a phenotype and correlating the phenotype with the presence of single vs double (multiple) mutations. A diploid heterozygous organism harbouring mutations in two (or more) genes is induced to sporulate. Resulting spores are meiotic segregants that are haploid and are either wild type or mutant at each locus. Spores are scored for a phenotype, such as loss of viability.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
random-spore analysis
saturation binding
PSI-MI
Saturation binding experiments measure specific ligand binding at equilibrium at various concentrations of the ligand. Analysis of these data can determine receptor number and affinity.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
synthetic genetic analysis
PSI-MI
sga
Identification of genetic interactions by generation of an organism harbouring mutations in 2 or more genes and scoring for a phenotype, such as loss of viability, that is not observed for any of the mutations in isolation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
SGA
sufficient binding region
PSI-MI
sufficient to bind
sufficient binding site
Binding will occur when this sequence range is present within a molecule or part of a molecule. This region will contain the direct binding region but may be longer.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ubiquitin binding
PSI-MI
Interaction concerning ubiquitin that is covalently attached to any Lys residue of its interaction partner.nOBSOLETE remap to ubiquitination reaction (MI:0220) or describe ubiquitine as a participant on the interaction using physical interaction (MI:0218) or covalent binding (MI:0195) as interaction type.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
database citation
PSI-MI
Database citation list names of databases commonly used to cross reference interaction data.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
literature database
PSI-MI
experiment xref
Databases acting as a source of literature information.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pubmed
PSI-MI
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
PubMed is designed to provide access to citations from biomedical literature.nhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
feature database
PSI-MI
feature xref
A database describing a feature on a molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene ontology
PSI-MI
id-validation-regexp:"GO:[0-9]{7}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"GO:[0-9]{7}"
go
The objective of Gene Ontology (GO) is to provide controlled vocabularies for the description of the molecular function, biological process and cellular component of gene products.nhttp://www.ebi.ac.uk/GO
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interpro
PSI-MI
InterPro
InterPro combines a number of databases (referred to as member databases) that use different methodologies and a varying degree of biological information on well-characterised proteins to derive protein signatures that predict family membership and domain composition of naive protein sequences.nhttp://www.ebi.ac.uk/interpro/
PMID:1252001
http://purl.org/obo/owl/PMID#PMID_1252001
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"IPR[0-9]{6}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"IPR[0-9]{6}"
cdd
PSI-MI
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
CDD
The Conserved Domain Database may be used to identify the conserved domains present in a protein sequence.nhttp://www.ncbi.nlm.nih.gov/Structure/cdd/cdd.shtml
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pfam
PSI-MI
Pfam
id-validation-regexp:"PF[0-9]{5}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"PF[0-9]{5}"
Pfam is a large collection of multiple sequence alignments and hidden Markov models covering many common protein domains.nhttp://www.sanger.ac.uk/Software/Pfam
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pirsf
PSI-MI
PIRSF is a classification system based on evolutionary relationship of whole proteins.nhttp://pir.georgetown.edu/pirwww/dbinfo/pirsf.shtml
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"PIRSF[0-9]{5}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"PIRSF[0-9]{5}"
PIRSF
prints
PSI-MI
PRINTS
id-validation-regexp:"PR[0-9]{6}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"PR[0-9]{6}"
PRINTS is a compendium of protein fingerprints. A fingerprint is a group of conserved motifs used to characterise a protein family.nhttp://umber.sbs.man.ac.uk/dbbrowser/PRINTS/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
prodom
PSI-MI
id-validation-regexp:"PD[0-9]{6}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"PD[0-9]{6}"
The ProDom protein domain database consists of an automatic compilation of homologous domains.nhttp://protein.toulouse.inra.fr/prodom.html
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ProDom
prosite
PSI-MI
PROSITE is a database of protein families and domains. It consists of biologically significant sites, patterns and profiles.nhttp://us.expasy.org/prosite/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"PS[0-9]{5}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"PS[0-9]{5}"
Prosite
scop superfamily
PSI-MI
SUPERFAMILY is a library of profile hidden Markov models that represent all proteins of known structure. The library is based on the SCOP classification of proteins: each model corresponds to a SCOP domain.nhttp://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
SCOP superfamily
smart
PSI-MI
SMART
SMART (a Simple Modular Architecture Research Tool) allows the identification and annotation of genetically mobile domains and the analysis of domain architectures.nhttp://smart.embl-heidelberg.de/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"SM[0-9]{5}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"SM[0-9]{5}"
tigrfams
PSI-MI
TIGRFAMs
id-validation-regexp:"TIGR[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"TIGR[0-9]+"
TIGRFAMs is a collection of protein families, featuring curated multiple sequence alignments, Hidden Markov Models (HMMs) and annotation.nhttp://www.tigr.org/TIGRFAMs
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mmdb
PSI-MI
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
MMDB (Molecular Modeling DataBase), is a subset of three-dimensional structures obtained from the Protein Data Bank.nhttp://www.ncbi.nlm.nih.gov/Structure
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
MMDB
rcsb pdb
PSI-MI
id-validation-regexp:"[0-9][a-zA-Z0-9]{3}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9][a-zA-Z0-9]{3}"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
PDB
The RCSB PDB provides a variety of tools and resources for studying the structures of biological macromolecules and their relationships to sequence, function, and disease. nhttp://www.pdb.org/
PMID:14634627
http://purl.org/obo/owl/PMID#PMID_14634627
interaction database
PSI-MI
Databases that contain experimental or predictive molecular interaction data.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interaction xref
bind
PSI-MI
BIND
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
The Biomolecular Interaction Network Database (BIND) is a collection of records documenting molecular interactions.nhttp://www.blueprint.org/bind
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biogrid
PSI-MI
BioGRID
The General Repository for Interaction Datasets (BioGRID) is a database of genetic and physical interactions.nhttp://thebiogrid.org
PMID:21071413
http://purl.org/obo/owl/PMID#PMID_21071413
cygd
PSI-MI
CYGD
MPact
CYGD (MIPS)
MIPS
The MIPS Comprehensive Yeast Genome Database (CYGD) aims to present information on the molecular structure and functional network of the entirely sequenced, well-studied model eukaryote, the budding yeast Saccharomyces cerevisiae. In addition the data of various projects on related yeasts are used for comparative analysis.nhttp://mips.gsf.de/proj/yeast/CYGD.nhttp://mips.gsf.de/genre/proj/mpact
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"[0-9]+|[A-Z]{3}[0-9]{3}[A-Za-z](-[A-Za-z])?|[A-Z0-9]+.[0-9]+|YM[A-Z][0-9]{3}[a-z][0-9]"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+|[A-Z]{3}[0-9]{3}[A-Za-z](-[A-Za-z])?|[A-Z0-9]+.[0-9]+|YM[A-Z][0-9]{3}[a-z][0-9]"
dip
PSI-MI
id-validation-regexp:"DIP[0-9]+[NE]"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"DIP[0-9]+[NE]"
DIP
The database of interacting protein (DIP) database stores experimentally determined interactions between proteins. It combines information from a variety of sources to create a single, consistent set of protein-protein interactions.nhttp://dip.doe-mbi.ucla.edu/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ecocyc
PSI-MI
EcoCyc
EcoCyc is a bioinformatics database that describes the genome and the biochemical machinery of E. coli K12 MG1655.nhttp://ecocyc.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
reactome
PSI-MI
The Reactome project is a collaboration among Cold Spring Harbor Laboratory, The European Bioinformatics Institute, and The Gene Ontology Consortium to develop a curated resource of core pathways and reactions in human biology.nhttp://www.reactome.org/
PMID:21067998
http://purl.org/obo/owl/PMID#PMID_21067998
GKB
Reactome
Genome Knowledge Base
hprd
PSI-MI
HPRD
The Human Protein Reference Database represents a centralized platform to visually depict and integrate information pertaining to domain architecture, post-translational modifications, interaction networks and disease association for each protein in the human proteome.nhttp://www.hprd.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
intact
PSI-MI
id-validation-regexp:"EBI-[0-9]+|IA:[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"EBI-[0-9]+|IA:[0-9]+"
INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of protein interactions.nhttp://www.ebi.ac.uk/intact
PMID:22121220
http://purl.org/obo/owl/PMID#PMID_22121220
PMID:19850723
http://purl.org/obo/owl/PMID#PMID_19850723
PMID:14681455
http://purl.org/obo/owl/PMID#PMID_14681455
IntAct
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
kegg
PSI-MI
KEGG (Kyoto Encyclopedia of Genes and Genomes) is a knowledge base for systematic analysis of gene functions, linking genomic information with higher order functional information and also supplies information about chemical compounds, enzyme molecules and enzymatic reactions.nhttp://www.genome.ad.jp/kegg/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"[a-zA-Z]+:[a-zA-Z]+[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[a-zA-Z]+:[a-zA-Z]+[0-9]+"
KEGG
mint
PSI-MI
id-validation-regexp:"MINT_[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"MINT_[0-9]+"
The Moleculer INTeraction database (MINT) is a relational database designed to store interactions between biological molecules.nhttp://mint.bio.uniroma2.it/mint/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
MINT
pdbe
PSI-MI
e-MSD
The Protein Data Bank in Europe - the European project for the collection, management and distribution of data about macromolecular structures, derived in part from the Protein Data Bank (PDB).nhttp://www.ebi.ac.uk/pdbe/
PMID:16381867
http://purl.org/obo/owl/PMID#PMID_16381867
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[0-9][a-zA-Z0-9]{3}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9][a-zA-Z0-9]{3}"
MSD
PQS
<new synonym>
participant database
PSI-MI
participant xref
Database of molecules participating in molecular interactions.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chebi
PSI-MI
A definitive, freely available database of Chemical compounds of Biological Interest (ChEBI).nhttp://www.ebi.ac.uk/chebi/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"CHEBI:[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"CHEBI:[0-9]+"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
ChEBI
ddbj/embl/genbank
PSI-MI
DDBJ EMBL GenBank Nucleotide Sequence Database Collaboration exchange new and updated data on a daily basis to achieve optimal synchronisation.nhttp://www.ebi.ac.uk/embl/Contact/collaboration
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
DDBJ
DDBJ/EMBL/GenBank
EMBL
GenBank
id-validation-regexp:"[A-Z][0-9]{5}|[A-Z][0-9]{5}.[0-9]+|[A-Z]{2}[0-9]{6}|[A-Z]{2}[0-9]{6}.[0-9]+|[A-Z]{4}[0-9]{8}|[A-Z]{4}[0-9]{8}.[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[A-Z][0-9]{5}|[A-Z][0-9]{5}.[0-9]+|[A-Z]{2}[0-9]{6}|[A-Z]{2}[0-9]{6}.[0-9]+|[A-Z]{4}[0-9]{8}|[A-Z]{4}[0-9]{8}.[0-9]+"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
ensembl
PSI-MI
Ensembl is a joint project between the EMBL-EBI and the Wellcome Trust Sanger Institute that aims at developing a system that maintains automatic annotation of large eukaryotic genomes.nhttp://www.ensembl.org
PMID:15078858
http://purl.org/obo/owl/PMID#PMID_15078858
Ensembl
id-validation-regexp:"ENS[A-Z]+[0-9]{11}|[A-Z]{3}[0-9]{3}[A-Za-z](-[A-Za-z])?|CG[0-9]+|[A-Z0-9]+.[0-9]+|YM[A-Z][0-9]{3}[a-z][0-9]"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"ENS[A-Z]+[0-9]{11}|[A-Z]{3}[0-9]{3}[A-Za-z](-[A-Za-z])?|CG[0-9]+|[A-Z0-9]+.[0-9]+|YM[A-Z][0-9]{3}[a-z][0-9]"
entrez gene/locuslink
PSI-MI
Entrez gene/locuslink
id-validation-regexp:"[0-9]+|[A-Z]{1,2}_[0-9]+|[A-Z]{1,2}_[A-Z]{1,4}[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+|[A-Z]{1,2}_[0-9]+|[A-Z]{1,2}_[A-Z]{1,4}[0-9]+"
LocusLink provides a single query interface to curated sequence and descriptive information about genetic loci.nhttp://www.ncbi.nlm.nih.gov/LocusLink/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
entrezgene/locuslink
flybase
PSI-MI
FlyBase
FlyBase is a comprehensive database for information on the genetics and molecular biology of Drosophila.nhttp://fbserver.gen.cam.ac.uk:7081/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"FBgn[0-9]{7}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"FBgn[0-9]{7}"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
mgd/mgi
PSI-MI
id-validation-regexp:"MGI:[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"MGI:[0-9]+"
Mouse Genome Informatics (MGI) provides integrated access to data on the genetics, genomics, and biology of the laboratory mouse.nhttp://www.informatics.jax.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
MGD/MGI
omim
PSI-MI
Online Mendelian Inheritance in Man (OMIM) is a catalogue of human genes and genetic disorders, with links to literature references, sequence records, maps, and related databases.nhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=OMIM
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
OMIM
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
refseq
PSI-MI
id-validation-regexp:"[XNZ][A-Z]_[0-9]+|[0-9]+|[XNZ][A-Z]_[0-9]+.[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[XNZ][A-Z]_[0-9]+|[0-9]+|[XNZ][A-Z]_[0-9]+.[0-9]+"
Refseq
The Reference Sequence (RefSeq) collection aims to provide a comprehensive, integrated, non-redundant set of sequences, including genomic DNA, transcript (RNA), and protein products, for a number of organisms.nhttp://www.ncbi.nlm.nih.gov/RefSeq/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rfam
PSI-MI
id-validation-regexp:"RF[0-9]{5}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"RF[0-9]{5}"
Rfam is a large collection of multiple sequence alignments and covariance models covering many common non-coding RNA families.nhttp://www.sanger.ac.uk/Software/Rfam/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rfam
rgd
PSI-MI
RGD
The Rat Genome Database (RGD) curates and integrates rat genetic and genomic data.nhttp://rgd.mcw.edu/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
sgd
PSI-MI
SGD is a scientific database of the molecular biology and genetics of the yeast Saccharomyces cerevisiae.nhttp://www.yeastgenome.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
SGD
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"S[0-9]{9}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"S[0-9]{9}"
uniparc
PSI-MI
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"UPI[A-F0-9]{10}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"UPI[A-F0-9]{10}"
UniProt Archive (UniParc) is part of UniProt project. It is a non-redundant archive of protein sequences derived from many sources.nhttp://www.ebi.ac.uk/uniparc/
PMID:14681372
http://purl.org/obo/owl/PMID#PMID_14681372
UniParc
uniprot knowledge base
PSI-MI
UniProtKB
UniProt (Universal Protein Resource) is the world's most comprehensive catalogue of information on proteins. It is a central repository of protein sequence and function created by joining the information contained in Swiss-Prot, TrEMBL, and PIR.nhttp://www.uniprot.org
PMID:14681372
http://purl.org/obo/owl/PMID#PMID_14681372
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[A-Z][0-9][A-Z0-9]{3}[0-9]|[A-Z][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[A-Z][0-9][A-Z0-9]{3}[0-9]|[A-Z][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
uniprotkb
wormbase
PSI-MI
WormBase is the central worm database that houses the gene reports, locus reports, translation reports, expression pattern data and genome browser.nhttp://www.wormbase.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
WormBase
id-validation-regexp:"WBGene[0-9]{8}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"WBGene[0-9]{8}"
psi-mi
PSI-MI
PSI-MI.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"MI:[0-9]{4}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"MI:[0-9]{4}"
PSI-MI
source database
PSI-MI
Database that originally provided the interaction record for exchange purposes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experiment condition
PSI-MI
Describes the location of the experiment.nOBSOLETE as a full host organisms description is recommended using tax id == -1 as convention to refer to 'in vitro' interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
in silico
PSI-MI
Results generated by predictive bioinformatics approaches rather than experimental data.nOBSOLETE as a full host organisms description is recommended using tax id == -1 as convention to refer to 'in vitro' interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Predictive
in vitro
PSI-MI
Experiments performed with participants removed from the cellular environment e.g. cell extracts, isolated proteins.nOBSOLETE as a full host organisms description is recommended using tax id == -1 as convention to refer to 'in vitro' interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
in vivo
PSI-MI
Experiment undertaken within a cellular environment, although this may not be the natural host of the proteins in the study.nOBSOLETE as a full host organisms description is recommended using tax id == -1 as convention to refer to 'in vitro' interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
in situ
PSI-MI
Literally, in place i.e. the protein is in its natural environment during the experiment.nOBSOLETE as a full host organisms is recommended using tax id == -1 as convention to refer to 'in vitro' interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental role
PSI-MI
Role played by the participant within the experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bait
PSI-MI
Molecule experimentally treated to capture its interacting partners.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
neutral component
PSI-MI
Molecule role in an experimental setting that does not have an embedded asymmetry.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
prey
PSI-MI
Molecule experimentally identified as being captured by a given bait.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
unspecified role
PSI-MI
Role not specified or not applicable to the data.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biological role
PSI-MI
Physiological role of an interactor in a cell or in vivo environment, which is reproduced in the current experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
enzyme
PSI-MI
Molecule catalyzing a modification on its interacting partner.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
enzyme target
PSI-MI
substrate
Molecule that is the target of its binding partner catalytic activity.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
self
PSI-MI
Molecule that makes intramolecular interactions.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental feature
PSI-MI
The form of a molecule that was actually used to experimentally demonstrate the interaction, that may differ from the sequence described by the identifying accession number.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
over expressed level
PSI-MI
A molecule is estimated to be expressed at higher levels than in physiological condition.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
over-expressed
tag
PSI-MI
Small molecules, peptides or full proteins that can be used as label as they confer some property that facilitates identification purification and monitoring to the labelled molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
deacetylase radiometric assay
PSI-MI
Measures the release of radiolabelled acetic acid from a pre-labeled molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
radiolabeled acetate
phosphatase homogeneous time resolved fluorescence
PSI-MI
homogeneous time-resolved fluorescence
Measures quenching of the nonradiative energy transfer between fluorescent long-lifetime lanthanide chelates and different acceptors. Relies on a fluorescence energy donor and acceptor being removed from close proximity on the phosphorylated substrate due to the action of the phosphatase.
PMID:14987100
http://purl.org/obo/owl/PMID#PMID_14987100
phosphatase HTRF
phosphatase htrf
homogeneous time resolved fluorescence
PSI-MI
homogeneous time-resolved fluorescence
Methods based on the exceptionally long fluorescence lifetime characteristics of certain fluorophores, which allows the elimination of the effects of background fluorescence. Uses nonradiative energy transfer or quenching between fluorescent lanthanide chelates and different acceptors to measure reaction rates.
PMID:14987100
http://purl.org/obo/owl/PMID#PMID_14987100
htrf
protease homogeneous time resolved fluorescence
PSI-MI
Measures quenching of the nonradiative energy transfer between fluorescent long-lifetime lanthanide chelates and different acceptors. Fluorescence donor and acceptor are on the same peptide molecule and separated by the action of the protease.
PMID:14987100
http://purl.org/obo/owl/PMID#PMID_14987100
Protease HTRF
protease htrf
zymography
PSI-MI
Samples run on a gelatine containing gels under non-reducing condition, gels then incubated under conditions in which the enzyme is active. Gels are stained with coomasie and gelatine-free regions of the gel taken as a measure of enzyme activity.
PMID:2071592
http://purl.org/obo/owl/PMID#PMID_2071592
collagen film assay
PSI-MI
Measures the amount of radiolabel released into the medium when enzyme is added onto a film of isotope-labelled collagen.
PMID:6247938
http://purl.org/obo/owl/PMID#PMID_6247938
in gel phosphatase assay
PSI-MI
in gel phosphatase
Substrate pre-radiolabelled either synthetically or through the action of a kinase transferring an isotope of phosphate from a nucleotide. Substrate then exposed to phosphate under assay conditions. Substrate isolated by gel electrophoresis and loss of radiolabelling confirmed by autoradiography.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methyltransferase assay
PSI-MI
Measures the catalysis of the transfer of a methyl group to an acceptor molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methyltransferase as
methyltransferase radiometric assay
PSI-MI
radiolabeled methyl
Measures the transfer of a radiolabelled methyl group of a donor, for example S-adenosyl-L-methionine (SAM) to a carboxyl group of an acceptor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
radiolabel
PSI-MI
A radiolabelled molecule has radio isotopes among its constituent atoms that can be used to identify, localize or quantify the full molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
radiolabeled
radiolabelled
flag tag
PSI-MI
DYKDDDDKV epitope tag
FLAG
FLAG-tagged
The protein of interest is expressed as a fusion to the peptide DYKDDDDKV for which antibodies are commercially available. Sometimes multiple copies of the peptide are fused in tandem.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
glutathione s tranferase tag
PSI-MI
glutathione S-tranferase tag
gst tag
The protein is expressed and purified as a fusion to the glutathione S-tranferase protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ha tag
PSI-MI
YPYDVPDYA epitope tag
The protein of interest is expressed as a fusion to the peptide YPYDVPDYA (a fragment of the influenza hemagglutinin protein) for which antibodies are commercially available.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
his tag
PSI-MI
The protein of interest is expressed as a fusion to a poly-His tail. This permits purification by chromatography over a metal column or by binding to commercially available anti poly-His antibodies.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Histidine-tag
Hexa-His-tag
6-His-tag
myc tag
PSI-MI
The protein of interest is expressed as a fusion to the peptide EUKLISEED (a fragment of the Myc oncogene protein) for which antibodies are commercially available. Sometimes multiple copies of the peptide are fused in tandem.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
EUKLISEED epitope tag
t7 tag
PSI-MI
MASMTGGQQMG epitope tag
The protein of interest is expressed as a fusion to the peptide MASMTGGQQMG for which antibodies are commercially available.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
calmodulin binding peptide plus protein a tag
PSI-MI
Tag encoding a calmodulin binding peptide, a TEV cleavage site, and the Staphylococcus aureus Protein A fused to a target protein and the introduction of the construct into the host cell or organism, maintaining the expression of the fusion protein at, or close to, its natural level. The fusion protein and associated components are recovered from cell extracts by affinity selection on an IgG matrix. After washing, the TEV protease is added to release the bound material. The eluate is incubated with calmodulin-coated beads in the presence of calcium. This second affinity step is required to remove the TEV protease as well as traces of contaminants remaining after the first affinity selection. After washing, the bound material is released with EGTA. This tag allows two steps purification steps ensuring a highly selective purification of the tapped protein (first round of selection on the protein A, a high affinity tag) under mild condition (non denaturant pH or conditions required to remove the tag).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tap tagged
CBP-ProtA tagged
v5 tag
PSI-MI
The protein of interest is expressed as a fusion to the peptide GKPIPNPLLGLDST for which antibodies are commercially available.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GKPIPNPLLGLDST epitope tag
n-acetyl-lysine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00723.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0055
http://purl.org/obo/owl/RESID#RESID_AA0055
RESID:AA0048
http://purl.org/obo/owl/RESID#RESID_AA0048
acetyllysine
adp ribosylated residue
PSI-MI
adp-ribosylated
Residue modification.nOBSOLETE remap to MOD:00752.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
omega-n-(adp-ribosyl)-arginine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00177.
RESID:AA0168
http://purl.org/obo/owl/RESID#RESID_AA0168
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
(S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid
omega-N-(ADP-ribosyl)-L-arginine
N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine
N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
adp-ribosylarginine
s-(adp-ribosyl)-cysteine
PSI-MI
(R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid
S-(ADP-ribosyl)-L-cysteine
adp-ribosylcysteine
S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
Residue modification.nOBSOLETE remap to MOD:00178.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0169
http://purl.org/obo/owl/RESID#RESID_AA0169
glutamyl-5-poly(adp-ribose)
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00300.
RESID:AA0295
http://purl.org/obo/owl/RESID#RESID_AA0295
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
(S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid
adp-ribosylglutamate
L-glutamyl-5-poly(ADP-ribose)
L-isoglutamyl-poly(ADP-ribose)
o-(adp-ribosyl)-serine
PSI-MI
O-(ADP-ribosyl)-L-serine
adp-ribosylserine
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid Formula
O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine
O3-(ADP-ribosyl)-L-serine
Residue modification.nOBSOLETE remap to MOD:00242.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0237
http://purl.org/obo/owl/RESID#RESID_AA0237
n4-(adp-ribosyl)-asparagine
PSI-MI
adpribosylasparagine
N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine
N4-(ADP-ribosyl)-L-asparagine
Residue modification.nOBSOLETE remap to MOD:00236.
RESID:AA0231
http://purl.org/obo/owl/RESID#RESID_AA0231
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid
glycosylated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00693.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
glycosyl-cysteine
PSI-MI
S-glycosyl-L-cysteine
Residue modification.nOBSOLETE remap to MOD:00131.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0122
http://purl.org/obo/owl/RESID#RESID_AA0122
glycosyl-serine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00163.
RESID:AA0154
http://purl.org/obo/owl/RESID#RESID_AA0154
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
O-glycosyl-L-serine
O3-glycosyl-L-serine
glycosyl-threonine
PSI-MI
O-glycosyl-L-threonine
O3-glycosyl-L-threonine
Residue modification.nOBSOLETE remap to MOD:00164.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0155
http://purl.org/obo/owl/RESID#RESID_AA0155
omega-n-glycosyl-arginine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00332.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0327
http://purl.org/obo/owl/RESID#RESID_AA0327
glycosylarginine
omega-N-glycosyl-L-arginine
n4-glycosyl-asparagine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00160.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0151
http://purl.org/obo/owl/RESID#RESID_AA0151
glycosylasparagine
N4-glycosyl-L-asparagine
gpi anchor residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00818.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gpi-anchor amidated alanine
PSI-MI
N-alanyl-glycosylphosphatidylinositolethanolamine
gpi-alanine
Residue modification.nOBSOLETE remap to MOD:00172.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0163
http://purl.org/obo/owl/RESID#RESID_AA0163
gpi-anchor amidated asparagine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00167.
RESID:AA0158
http://purl.org/obo/owl/RESID#RESID_AA0158
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gpi-asparagine
N-asparaginyl-glycosylphosphatidylinositolethanolamine
gpi-anchor amidated aspartate
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00168.
RESID:AA0159
http://purl.org/obo/owl/RESID#RESID_AA0159
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gpi-aspartate
N-aspartyl-glycosylphosphatidylinositolethanolamine
gpi-anchor amidated cysteine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00169.
RESID:AA0160
http://purl.org/obo/owl/RESID#RESID_AA0160
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
N-cysteinyl-glycosylphosphatidylinositolethanolamine
gpi-cysteine
gpi-anchor amidated glycine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00170.
RESID:AA0161
http://purl.org/obo/owl/RESID#RESID_AA0161
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gpi-glycine
N-glycyl-glycosylphosphatidylinositolethanolamine
gpi-anchor amidated serine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00171.
RESID:AA0162
http://purl.org/obo/owl/RESID#RESID_AA0162
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gpi-serine
N-seryl-glycosylphosphatidylinositolethanolamine
gpi-anchor amidated threonine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00173.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0164
http://purl.org/obo/owl/RESID#RESID_AA0164
N-threonyl-glycosylphosphatidylinositolethanolamine
gpi-threonine
s-prenyl-cysteine
PSI-MI
prenylcysteine
Residue modification.nOBSOLETE remap to MOD:01110.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methylated-lysine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00663.
RESID:AA0076
http://purl.org/obo/owl/RESID#RESID_AA0076
RESID:AA0074
http://purl.org/obo/owl/RESID#RESID_AA0074
RESID:AA0075
http://purl.org/obo/owl/RESID#RESID_AA0075
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methylatedlysine
alkylated cysteine
PSI-MI
Artificial residue modification enabling studies of cysteine binding status.nOBSOLETE remap to MOD:00660.
PMID:15325307
http://purl.org/obo/owl/PMID#PMID_15325307
gamma-carboxyglutamic acid
PSI-MI
1-carboxyglutamic acid [misnomer]
4-carboxyglutamic acid
(S)-3-amino-1,1,3-propanetricarboxylic acid
L-gamma-carboxyglutamic acid
carboxyglutamic acid
Residue modification.nOBSOLETE remap to MOD:00041.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0032
http://purl.org/obo/owl/RESID#RESID_AA0032
nitro-tyrosine
PSI-MI
nitrated tyrosine
Residue modification.nOBSOLETE remap to MOD:00461.
PMID:9636206
http://purl.org/obo/owl/PMID#PMID_9636206
PMID:15657065
http://purl.org/obo/owl/PMID#PMID_15657065
s-nitrosyl-cysteine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00235.
RESID:AA0230
http://purl.org/obo/owl/RESID#RESID_AA0230
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
S-nitrosyl-L-cysteine
L-cysteine nitrite ester
(R)-2-amino-3-nitrososulfanyl-propanoic acid
S-nitrosocysteine
nitrosylcysteine
o4'-sulfo-tyrosine
PSI-MI
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate
Residue modification.nOBSOLETE remap to MOD:00181.
RESID:AA0172
http://purl.org/obo/owl/RESID#RESID_AA0172
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
(S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid
O4-sulfotyrosine
O4'-sulfo-L-tyrosine
tyrosine sulfate
sulfotyrosine
sumoylated lysine
PSI-MI
(S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid
Residue modification due to a cross-link between a lysine and a glycine from the sumo (Small Ubiquitin-related MOdifier) protein.nOBSOLETE remap to MOD:01149.
RESID:AA0125
http://purl.org/obo/owl/RESID#RESID_AA0125
PMID:12612601
http://purl.org/obo/owl/PMID#PMID_12612601
N6-glycyllysine
N6-glycyl-L-lysine
phospho-histidine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00890.
RESID:AA0035
http://purl.org/obo/owl/RESID#RESID_AA0035
RESID:AA0036
http://purl.org/obo/owl/RESID#RESID_AA0036
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphoshistidine
transglutamination reaction
PSI-MI
transglutamination
Gln-Lys cross-link catalyzed by a transglutaminase.
RESID:AA0124
http://purl.org/obo/owl/RESID#RESID_AA0124
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
adp ribosylation reaction
PSI-MI
adp ribosylation
Involves the addition of one or more ADP-ribose moieties to proteins. Reaction that can affect Arg, Cys, Glu, Arg and Asn residues.
RESID:AA0295
http://purl.org/obo/owl/RESID#RESID_AA0295
RESID:AA0237
http://purl.org/obo/owl/RESID#RESID_AA0237
RESID:AA0168
http://purl.org/obo/owl/RESID#RESID_AA0168
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0231
http://purl.org/obo/owl/RESID#RESID_AA0231
RESID:AA0169
http://purl.org/obo/owl/RESID#RESID_AA0169
GO:0006471
http://purl.org/obo/owl/GO#GO_0006471
deglycosylation reaction
PSI-MI
deglycosylation
Reaction catalyzed by PNGase, a deglycosylating enzyme that promotes the hydrolysis of the beta-aspartylglycosylamine bond of aspargine-linked glycopeptides and glycoproteins.
PMID:15670854
http://purl.org/obo/owl/PMID#PMID_15670854
GO:0006517
http://purl.org/obo/owl/GO#GO_0006517
glycosylation reaction
PSI-MI
The covalent attachment of a glycosyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological polymer. Reaction that can affect Ser, Thr, Cys, Arg, and Asn residues. This reaction is known to be reversible in the case of Asn substrate.
RESID:AA0155
http://purl.org/obo/owl/RESID#RESID_AA0155
RESID:AA0154
http://purl.org/obo/owl/RESID#RESID_AA0154
RESID:AA0327
http://purl.org/obo/owl/RESID#RESID_AA0327
GO:0043413
http://purl.org/obo/owl/GO#GO_0043413
RESID:AA0151
http://purl.org/obo/owl/RESID#RESID_AA0151
RESID:AA0122
http://purl.org/obo/owl/RESID#RESID_AA0122
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
glycosylation
myristoylated residue
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00438.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
myristoylated aa
palmitoylated residue
PSI-MI
palmitoylated aa
Residue modification.nOBSOLETE remap to MOD:00440.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methylated alanine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00665.
RESID:AA0061
http://purl.org/obo/owl/RESID#RESID_AA0061
RESID:AA0062
http://purl.org/obo/owl/RESID#RESID_AA0062
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methylated arginine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00658.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
RESID:AA0068
http://purl.org/obo/owl/RESID#RESID_AA0068
RESID:AA0069
http://purl.org/obo/owl/RESID#RESID_AA0069
omega-n-methyl-arginine
PSI-MI
Residue modification.nOBSOLETE remap to MOD:00078.
RESID:AA0069
http://purl.org/obo/owl/RESID#RESID_AA0069
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
methylarginine
NG-methylarginine;
omega-N-methyl-L-arginine
(S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid
neddylated lysine
PSI-MI
Residue modification due to a cross-link between a lysine and a glycine from the Nedd8 protein family.nOBSOLETE remap to MOD:01150.
PMID:111
http://purl.org/obo/owl/PMID#PMID_111
sumoylation reaction
PSI-MI
sumoylation
Reversible reaction that create a covalent bond between a C-terminus G of an ubiquitine like sumo protein and a K residue of the target.
GO:0016925
http://purl.org/obo/owl/GO#GO_0016925
PMID:15985640
http://purl.org/obo/owl/PMID#PMID_15985640
neddylation reaction
PSI-MI
neddylation
Reversible reaction that create a covalent bond between a Glycine residue of an ubiquitine like NEDD8 protein and a lysine residue of the target.
GO:0045116
http://purl.org/obo/owl/GO#GO_0045116
PMID:16127432
http://purl.org/obo/owl/PMID#PMID_16127432
desumoylation reaction
PSI-MI
Cleavage of the G-K bond and release of the SUMO ubiquitin like proteins.
GO:0016926
http://purl.org/obo/owl/GO#GO_0016926
PMID:15985640
http://purl.org/obo/owl/PMID#PMID_15985640
desumoylation
deneddylation reaction
PSI-MI
Cleavage of the G-K bond and release of the NEDD8 ubiquitin like proteins. Deneddylation, which removes the NEDD8 moiety, requires the isopeptidase activity of the COP9 signalosome.
GO:0000338
http://purl.org/obo/owl/GO#GO_0000338
PMID:16127432
http://purl.org/obo/owl/PMID#PMID_16127432
deneddylation
protein cleavage
PSI-MI
Covalent modification of a polypeptide occuring during its maturation or its proteolytic degradation.
PMID:14744292
http://purl.org/obo/owl/PMID#PMID_14744292
mrna cleavage
PSI-MI
Any process by which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
GO:0006379
http://purl.org/obo/owl/GO#GO_0006379
dna cleavage
PSI-MI
Covalent bond breakage of a DNA molecule leading to the formation of smaller fragments.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation disrupting interaction
PSI-MI
mutation disrupting
Region of a molecule whose mutation or deletion totally disrupts an interaction strength or rate (in the case of interactions inferred from enzymatic reaction)..
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
digital object identifier
PSI-MI
id-validation-regexp:"d+.d+/[a-zA-Z0-9.:]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"d+.d+/[a-zA-Z0-9.:]+"
Identifier of a publication prior to pubmed indexing.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
doi
alliance for cellular signaling
PSI-MI
AfCS
afcs
Alliance for Cellular Signaling (AfCS -Nature) store yeast 2-hybrid Interaction data and expression data. Information and data are freely available to all.nhttp://www.signaling-gateway.org
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
structural proximity
PSI-MI
Method to identify domain-domain interactions within the same resolved structure. Domains are first projected onto a pdb structure and then the distance between all pairs of residues in different domains are calculated. When the distance between 2 residues is below the non covalent bond threshold, the corresponding pair of domains is predicted to interact.
PMID:15353450
http://purl.org/obo/owl/PMID#PMID_15353450
feature prediction from structure
PSI-MI
Group of method taking advantage of 3D structure to calculate and infer the feature of interacting molecules.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
feature struct pred
maltose binding protein tag
PSI-MI
maltose binding protein tag
mbp tag
The protein is expressed and purified as a fusion to the glutathione maltose-binding protein (MBP). The MBP-fusion protein can be purified by affinity chromatography using an amylose resin.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
electron donor
PSI-MI
Any molecule that is able to transfer an electron to another chemical species.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
electron acceptor
PSI-MI
Molecule to which an electron may be transferred from an electron donor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
suppressor gene
PSI-MI
Gene whose mutation suppress the phenotype associated to a suppressed mutation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
suppressed gene
PSI-MI
Gene whose mutation phenotype is suppressed by a given suppressor mutation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence donor
PSI-MI
Fluorophore which emits electromagnetic radiation of given wavelength.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence acceptor
PSI-MI
Fluorophore able to absorb the electromagnetic radiation at given wavelength from a specific donor fluorophore, the re-emission of its own characteristic fluorescence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence accept
intenz
PSI-MI
IntEnz is the name for the Integrated relational Enzyme database and is the official version of the Enzyme Nomenclature. The Enzyme Nomenclature comprises recommendations of the Nomenclature Committee of the International Union of Bio chemistry and Molecular Biology (NC-IUBMB) on the nomenclature and classification of enzyme-catalysed reactions. IntEnz is supported by NC-IUBMB and contains enzyme data curated and approved by this committee. The database IntEnz is available at.nhttp://www.ebi.ac.uk/intenz
PMID:14681451
http://purl.org/obo/owl/PMID#PMID_14681451
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[0-6]{1}.(d+|-).(d+|-).(d+|-)"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-6]{1}.(d+|-).(d+|-).(d+|-)"
inhibitor
PSI-MI
Molecule inhibiting an interaction by interacting with one or more of its participants.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
inhibited
PSI-MI
Molecule being identified as target of an inhibitor.nOBSOLETE as term is deprecated to describe the target of an inhibitor that can have any other biological role.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
three hybrid
PSI-MI
Group of methods based on complementation assay where a third participant is shown to be necessary for the binding of a given bait prey pair. The molecule fused to the DNA binding domain is the bait, that fused to the transcriptional activator is the prey.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
3 hybrid
tri hybrid
3-hybrid
tri-hybrid assay
in vitro translated protein
PSI-MI
Protein sample collected by in vitro translation of its mRNA taking advantage of purified translation machinery.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
in vitro translated
attribute name
PSI-MI
Collection of topics describing the free text stored as an attribute value.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
CvTopic
experiment description
PSI-MI
The experimental condition text description, should contain information about the organisms hosting the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experiment descripti
ipfam
PSI-MI
Web resource that allows the investigation of protein interactions in the Protein Data Bank structures at the level of Pfam domains and amino acid residues. iPfam is available on the Web for browsing at.nhttp://www.sanger.ac.uk/Software/Pfam/iPfam/
PMID:15353450
http://purl.org/obo/owl/PMID#PMID_15353450
translocation
PSI-MI
Xref pointing to a GO process term describing the start and end location of a migrating molecule, for instance see GO:0006611, 'protein-nucleus export'.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
translocation start
PSI-MI
Xref pointing to a GO compartment term describing the start location of a migrating molecule.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
translocation end
PSI-MI
Xref pointing to a GO compartment term describing the end location of a migrating molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental form description
PSI-MI
experimental form de
Free text description of all the tags and artificial process undergone by a molecule during an experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
feature description
PSI-MI
The feature text description may include information about the feature detection method.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
feature constraint
PSI-MI
The feature constraint free text will specificity whether a biological feature is shown to be possible (just observed) or required (experimentally demonstrated to be necessary for an interaction).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
figure legend
PSI-MI
Text pointing to a specific paper figure legend where the experimental evidences for an interaction are to be found.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
conditional synthetic lethal nutrition-sensitivity
PSI-MI
nutrition synt letal
Two silent mutations show a nutrition sensitive lethal phenotype when they co-occur on the same cell.nOBSOLETE: remap to CV intraction type 'synthetic interaction' MI:0794 and external CV for phenotype description.
PMID:15608217
http://purl.org/obo/owl/PMID#PMID_15608217
sequence ontology
PSI-MI
id-validation-regexp:"SO:[0-9]{7}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"SO:[0-9]{7}"
so
The Sequence Ontology (SO) is a structured controlled vocabulary for the parts of a genomic annotation. SO provides a common set of terms and definitions that will facilitate the exchange, analysis and management of genomic data.
PMID:15892872
http://purl.org/obo/owl/PMID#PMID_15892872
chemical footprinting
PSI-MI
Binding sites are identified by altered reactivity of a complex to a chemical treatment compared to the unbound molecules. Residues in close contact with the binding partner are protected from cleavage by the enzyme. When these chemicals are administrated to intact cells, the pattern of protection from the probes identifies the location of DNA-protein or protein-protein interactions in vivo.
PMID:8238889
http://purl.org/obo/owl/PMID#PMID_8238889
chemical footprint
dimethylsulphate footprinting
PSI-MI
Dimethylsulphate (DMS) is the most commonly used chemical to study DNA-protein interactions. DMS induces methylation of guanine residues so DNA interaction with protein binding to AT rich sequences or to the phosphate backbone may be not detected by DMS footprinting. However as DMS diffuses across membrane it can also be used for in vivo footprinting. The experiment involves the treatment with DMS of two DNA samples with identical sequence, one protein bound and the other naked. The two samples are treated with piperidine to induce chemical cleavage of the DMS modified guanine residues followed by digestion with restriction enzymes. Once labelled the samples are run in parallel on a gel to visualize the pattern of nested fragments sharing a common end generated by restriction enzyme(or PCR primer extension) and a variable end guanine dependent. The missing bands of the protein bound sample correspond to the guanine residues protected from modification by an interaction.
PMID:8238889
http://purl.org/obo/owl/PMID#PMID_8238889
dms footprinting
potassium permanganate footprinting
PSI-MI
k-mn-04 footprinting
Potassium permanganate bind to single-stranded pyrimidine residues, it is commonly used to detect promoters opening regions in vivo. KMnO4 treatment of cells, followed by treatment with piperidine, followed by either PCR and/or acrylamide gel electrophoresis allows detection of interaction between transcription factor and the DNA sequence under their control.
PMID:8238889
http://purl.org/obo/owl/PMID#PMID_8238889
enzymatic footprinting
PSI-MI
Binding sites are identified by altered reactivity of a complex to an enzymatic probe compared to the unbound molecules. Residues in close contact with the binding partner are protected from cleavage by the enzyme. When these enzymes are administrated to intact cells, the pattern of protection from the probes identifies the location of DNA-protein or protein-protein interactions in vivo.
PMID:8238889
http://purl.org/obo/owl/PMID#PMID_8238889
enzymatic footprint
DNase I footprinting
PSI-MI
dnase 1 footprinting
DNase I protection
Deoxyribonuclease I (DNase I) does not have high specificity for given sequences or residues, thus footprinting with DNase I permits the exact delineation of the protein-DNA binding site. Moreover DNase I, can be used for in vivo footprinting by treating intact cells with permeabilising drugs. In this latter case DNase I in vivo footprinting allow studies of the chromatin structure in genomic DNA.
PMID:8238889
http://purl.org/obo/owl/PMID#PMID_8238889
small nuclear rna
PSI-MI
snrna
snRNA
These RNA molecules are relatively short (less than 200 nucleotides each), and there are five of them (U1, U2, U4, U5, and U6) involved in the major form of pre-mRNA splicing. Known as snRNAs (small nuclear RNAs), each is complexed with at least seven protein subunits to form a snRNP (small nuclear ribonucleoprotein). These snRNPs form the core of the spliceosome.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ribosomal rna
PSI-MI
RNA that is transcribed from the DNA of the nucleolus and is found, together with characteristic proteins, in the ribosomes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rrna
rRNA
small nucleolar rna
PSI-MI
The small nucleolar RNAs, are stable RNA contained in the nucleoli and these RNAs exist as snoRNA: protein complexes called snoRNPs (also called 'snorps'). The snoRNPs function is in the maturation of ribosomal RNA and other RNAs, by: creating two types of modified nucleotides, (2'-O-methylated nucleotides and pseudouridine), and mediating endonucleolytic cleavages of pre-rRNA.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
snorna
snoRNA
small interfering rna
PSI-MI
dicer RNA
sirna
micro RNA
siRNA
Ribonucleic acid used in RNAi study. These RNA have the reverse complementary sequence of a target gene's mRNA transcript and inhibit its expression.
PMID:10542148
http://purl.org/obo/owl/PMID#PMID_10542148
signal recognition particle rna
PSI-MI
Small (300 nucleotides) stable RNAs transcribed by RNA pol III that are part of the signal-recognition particle (SRP). This particle comprises one RNA and six proteins bound to the RNA. SRP function is to assist secretory proteins sorting in the endoplasmic reticulum (ER). SRP is a cytosolic particle that transiently binds to the ER signal sequence of a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
srprna
srpRNA
comment
PSI-MI
Comment for public view. This attribute can be associated to interaction, experiment, CV term, an organism and any participant.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
function
PSI-MI
Biological function of a participant or of an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
url
PSI-MI
URL/Web address describing an experiment, an interaction, a Cv term or an organism.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
search-url
PSI-MI
Search engine URL associated to Cv Database terms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
example
PSI-MI
Example generally associated to Cv terms. Test.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
disease
PSI-MI
The interaction has a known or demonstrated disease association.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
caution
PSI-MI
Warning about errors or grounds for confusion. Can be associated to an interaction, experiment, CV term or any participant.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pathway
PSI-MI
Refers to the metabolic or signalling pathway involving an interaction or a complex.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
search-url-ascii
PSI-MI
Search URL to retrieve an external entry in ASCII format. Generally associated to Cv Database terms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
author-confidence
PSI-MI
Confidence classification assigned by the author of the publication to a specific interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
confidence-mapping
PSI-MI
Description of confidence assessment method generally associated to the experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
inhibition
PSI-MI
The interaction between the proteins or the formation of a complex is disrupted by a biological molecule or by a modification of the interactors.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
stimulant
PSI-MI
Reaction occurs at a faster rate in the presence of this compound or molecule i.e. the molecule directly physically co-operates with the interaction. Reaction may not occur at all in the absence of this molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
agonist
PSI-MI
Any chemical applied externally to cells or any type of environmental condition, such as hypoxia, that stimulates an interaction, potentially by causing modification of one or more of the interactors.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
antagonist
PSI-MI
Any chemical applied externally to cells or any type of environmental condition, such as hypoxia, that inhibits an interaction, potentially by alteration of amount or binding affinity of one or more of the interactors.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experiment modification
PSI-MI
Modifications of the standard experimental method described in the CV.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
exp-modification
validation regular expression
PSI-MI
id-validation-regexp
Regular Expression used to check the validity of cross references' identifier. Attribute generally associated to terms in Cv Database.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
complex-properties
PSI-MI
Information on the complex being annotated. Attribute generally associated to an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
3d-structure
PSI-MI
Comments on the 3D structure. This attribute is generally associated to an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
3d-r-factors
PSI-MI
Free R-Factor and working R-Factor for the quality of the crystallographic model. This attribute is generally associated to an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
3d-resolution
PSI-MI
Resolution of the 3D structure. This attribute is generally associated to an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
data-processing
PSI-MI
Information about how the data was processed. This attribute is used mainly for large scale experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
contact-email
PSI-MI
E-mail address to contact the author or organisation which has produced the data. This attribute is generally associated to an experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
contact-comment
PSI-MI
Free text notes on how to contact the author or organisation which has produced the data This attribute is generally associated to an experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
author-list
PSI-MI
List of authors associated to a publication. This attribute is generally associated to an experiment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
isoform-comment
PSI-MI
Participant isoform's comment. This attribute can be attached to interactions or participants.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
prerequisite-ptm
PSI-MI
Post translational modification required for an interaction to occur.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
resulting-ptm
PSI-MI
Post translational modification occurs subsequently to an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
parameter type
PSI-MI
Parameter for enzymatic or binding kinetic studies.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ic50
PSI-MI
IC50
Molar concentration of an antagonist which produces 50% of the maximum possible inhibitory response for that antagonist. Note this measure depends on the specific antagonist used and upon experimental conditions, notably temperature, pH and solution composition (e.g., salts, chelating agents and others). Thus the ic50 is a relative measure and its values can be compared only when sharing the same experimental setting. Unit Molar.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ec50
PSI-MI
Molar concentration of an agonist which produces 50% of the maximum possible response for that agonist. Note this measure depends on the specific agonist used and upon experimental conditions, notably temperature, pH and solution composition (e.g., salts, chelating agents and others). Thus the ec50 is a relative measure and its values can be compared only when sharing the same experimental setting. Unit Molar.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
EC50
ki
PSI-MI
Ki
Equilibrium constant for dissociation of an inhibitor. Unit Molar.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
km
PSI-MI
Michaelis-Menten constant: concentration of substrate at which the reaction rate is equal to half the maximal rate (i.e. Km={s} when Vo=1/2Vmax). Unit Molar.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Km
kcat
PSI-MI
The number of substrate molecules converted to product in a given unit of time, on a single enzyme molecule when the enzyme is saturated with substrate. Unit per second, or s-1.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
turnover number
Kd
PSI-MI
The equilibrium dissociation constant of a receptor/ligand or proteinA/proteinB complex. Unit Molar (generally M-1).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Kd
parameter unit
PSI-MI
Controlled vocabulary for kinetic constant units.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molar
PSI-MI
Molarity is the number of moles of solute dissolved in one liter of solution. The units, therefore are moles per liter, specifically it's moles of solute per liter of solution. These units are abbreviated as M and it means moles per liter (not just moles).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
M
second
PSI-MI
The second is the duration of 9 192 631 770 periods of the radiation corresponding to the transition between the two hyperfine levels of the ground state of the cesium-133 atom. The second was originally defined as 1/86 400 mean solar day until astronomers discovered that the mean solar day is actually not constant.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
s
sec
millimolar
PSI-MI
mM
10E-3 moles per liter of solution.nOBSOLETE: term redundant with the schema exponent attribute of the parameter.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
micromolar
PSI-MI
10E-6 moles per liter of solution.nOBSOLETE: term redundant with the schema exponent attribute of the parameter.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
uM
nanomolar
PSI-MI
10E-9 moles per liter of solution.nOBSOLETE: term redundant with the schema exponent attribute of the parameter.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nM
picomolar
PSI-MI
10E-12 moles per liter of solution.nOBSOLETE: term redundant with the schema exponent attribute of the parameter.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pM
fentomolar
PSI-MI
fM
10E-15 moles per liter of solution.nOBSOLETE: term redundant with the schema exponent attribute of the parameter.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
lambda repressor two hybrid
PSI-MI
BacterioMatch
lambda two hybrid
A protein of interest (the bait) is fused to the full-length bacteriophage lambda repressor protein (lambdacI, 237 amino acids), containing the amino terminal DNA-binding domain and the carboxylterminal dimerization domain. The corresponding target (prey) protein is fused to the N-terminal domain of the alfa-subunit of RNA polymerase (248 amino acids). The bait is tethered to the lambda operator sequence upstream of the reporter promoter through the DNA-binding domain of lambdacI. When the bait and prey interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription of the HIS3 reporter gene. Due to the tendency of both the lambda repressor protein and the N-terminal domain of the alfa-subunit of RNA polymerase to dimerize, this system might not be optimal for the analysis of proteins that self-associate unless their interaction with other protein partners depends on the oligomerization.
PMID:15792953
http://purl.org/obo/owl/PMID#PMID_15792953
identified peptide
PSI-MI
Peptide whose sequence is experimentally identified and can lead to a full protein identification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
systematic evolution of ligands by exponential enrichment
PSI-MI
in vitro evolution of nucleic acids
selex
RNA and cDNA constructs with variable central sequences and a constant flanking region are collected in a complex library. The library is then screened to select either specific binding partners of a bait molecule (generally a protein) or particular enzymatic activities of the nucleic acid molecules themselves. The selected nucleic acids are amplified using the constant flanking regions to increase their abundance. Cycles of selection-amplification can be repeated to increase the specificity of the targets that, at the end, are individually identified by sequencing.
PMID:11539574
http://purl.org/obo/owl/PMID#PMID_11539574
multidimensional protein identification technology
PSI-MI
MudPIT is a method for rapid and large-scale protein identification by multidimensional liquid chromatography associated with tandem mass spectrometry. The chromatography step consists of strong cation exchange material back-to-back with reversed phase material inside fused silica capillaries. The peptides bound to the cation-exchange resin are freed by the gradually increasing salt concentration of the buffer and are subsequently retained by the reversed phase resin. Increasing buffers hydrophobicity progressively elute peptides from the reversed phase packing directly into the mass spectrometer. Typically this mass spectrometer will be a tandem electrospray, so peptides undergo ionization in the liquid phase, are separated in a primary mass spectrometer, analysed in the second mass spectrometer and identified.
PMID:11231557
http://purl.org/obo/owl/PMID#PMID_11231557
mudpit
experimental feature detection
PSI-MI
exp feature detect
Experimental method by which a feature is detected or identified.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
feature prediction
PSI-MI
Feature detection based on computational analysis.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental participant identification
PSI-MI
experimental participant identification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental particp
imex-primary
PSI-MI
IMEx primary identifier that is assigned to an experiment record by the database that created the record in the context of IMEx consortium. The identifiers are unique across all member database as they are all generated by a centralized key-assigner.nhttp://imex.sourceforge.net/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
confocal microscopy
PSI-MI
A confocal is a standard epifluorescence microscope with improvement essentially coming from the rejection of out-of-focus light interference. Confocal imaging system achieves this by two strategies: a) by illuminating a single point of the specimen at any one time with a focused beam, so that illumination intensity drops off rapidly and b) by the use of blocking a pinhole aperture in a conjugate focal plane to the specimen so that light emitted away from the point in the specimen being illuminated is blocked from reaching the detector. Only the light from the single point illuminated of the specimen passing through the image pinhole is detected by a photodetector. Usually a computer is used to control the sequential scanning of the sample and to assemble the image for display onto a video screen.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interaction attribute name
PSI-MI
Attribute name of annotation associated to an interaction element.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interaction att name
experiment attibute name
PSI-MI
Attribute name of annotation associated to an experiment element.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experiment att name
participant attribute name
PSI-MI
participant att name
Attribute name of annotation associated to a participant element.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
controlled vocabulary attribute name
PSI-MI
Attribute name of annotation associated to a CV term.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cv att name
feature attribute name
PSI-MI
feature att name
Attribute name of annotation associated to a feature element.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
organism attribute name
PSI-MI
organism att name
Attribute name of annotation associated to an organism element.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
imex
PSI-MI
IMEx
International Molecular Interaction Exchange.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
antibodies
PSI-MI
This annotation topic should contain information about antibodies when specific antibodies (monoclonal or polyclonal raised against specific regions of the proteins or purified in a specific manner) have been used.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
library-used
PSI-MI
This annotation topic will be used to store information about the cDNA library. If a name is available this should be reported along with a short description of the library.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
complex-synonym
PSI-MI
Alternative names to describe a complex.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
peptide parent sequence reference
PSI-MI
Describe a cross reference pointing to a peptide parent sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
peptide-parent
international protein index
PSI-MI
IPI provides a top level guide to the main databases that describe the proteomes of higher eukaryotic organisms. IPI effectively maintains a database of cross references between the primary data sources, provides minimally redundant yet maximally complete sets of proteins for featured species (one sequence per transcript) and maintains stable identifiers (with incremental versioning) to allow the tracking of sequences in IPI between IPI releases. IPI is updated monthly in accordance with the latest data released by the primary data sources.
PMID:15221759
http://purl.org/obo/owl/PMID#PMID_15221759
id-validation-regexp:"IPI[0-9]+.[0-9]+|IPI[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"IPI[0-9]+.[0-9]+|IPI[0-9]+"
ipi
tandem affinity purification
PSI-MI
TAP
tap
Tandem affinity purification allows rapid purification under native conditions of complexes, even when expressed at their natural level. Prior knowledge of complex composition or function is not required. The TAP method requires fusion of the a multiple tag, either N- or C-terminally, to the target (or bait) protein of interest. The multiple tag allows two steps purification steps ensuring a highly selective complex purification.
PMID:11403571
http://purl.org/obo/owl/PMID#PMID_11403571
tandem tag
PSI-MI
A tandem tag consists of the concatenation of simple distinct tags that is engineered to be cloned as a unique element onto a sequence of interest. Note that when a protein is fused to many simple tags that are inserted individually and possibly in different sequence positions these should be reported as independent features.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
antibody array
PSI-MI
A microarray consisting of antibodies spotted on a solid support in appropriate orientation is incubated with a biological sample (or antigen). Some proteins are captured by the antibodies in the array. Protein of forming complexes on the array are identified according to their prior labelling (tag, ELISA, biotin and others).
PMID:12454649
http://purl.org/obo/owl/PMID#PMID_12454649
sandwich immunoassay
antigen capture assay
poly adenine
PSI-MI
poly a
poly A
A sequence of adenine nucleotides that is added to the 3' end of some primary transcript messenger RNA molecules in eukaryotes during post-transcriptional processing. The added tail is believed to confer stability to the molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
single stranded deoxyribonucleic acid
PSI-MI
ss dna
ss DNA
DNA that consists of only one chain of nucleotides rather than the two base pairing strands found in DNA in the double helix form.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
double stranded deoxyribonucleic acid
PSI-MI
ds dna
DNA that consists of two base pairing strands. The 2 nucleotide chains are held together by hydrogen bonds between base pairs of nucleotides.n
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ds DNA
cofactor
PSI-MI
coenzyme
A cofactor is a small molecule required for the catalysis of an enzyme.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
sequence database
PSI-MI
Database collecting nucleic or amino acid sequences mainly derived from genomic or mRNA sequencing.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ancillary
PSI-MI
Molecule required for an observed binary interaction to occur. This molecule may act as stabilizer of any of the interaction partners or may act as a bridge molecule between them but the method does not provide resolution or evidence to demonstrate its actual molecular function (i.e.Mudpit, tri hybrid etc).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
source reference
PSI-MI
Publication or document describing the originating resource where an interaction, or other curated information, was first described.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
unspecified method
PSI-MI
Yet to be identified interaction detection method associated with interaction data imported from a third party database. This database may have potentially different standards of curation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescent protein tag
PSI-MI
Protein having well characterized fluorescence excitation and emission spectra used as fusion with a protein under study to facilitate its localisation or identification.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescent prot tag
dna binding domain tag
PSI-MI
Part of a transcription factor responsible for the binding of gene regulatory region prior to their transcription. Such tags are generally used in two hybrid experiments where they are fused to a bait polypeptide tested for its ability to interact with a prey fused to an activation domain tag.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dna binding domain
activation domain tag
PSI-MI
Part of a transcription factor responsible for the activation of DNA transcription. Such tags are generally used in two hybrid experiments where they are fused to a prey polypeptide tested for its ability to interact with a bait fused to a DNA binding domain tag.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
activation domain
gal4 activation domain
PSI-MI
Part of the yeast transcription factor GAL4 (amino acids 766-881) specifically responsible for DNA transcription activation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gal4 ad
vp16 activation domain
PSI-MI
Full viral protein vp16 exclusively responsible for preferential transcriptional activation of viral genes. Activation requires the formation of a complex with the host cell transcription factor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
vp16 ad
b42 activation domain
PSI-MI
b42 ad
B42 is an acidic sequence of 89 residues derived from Escherichia coli acting as weak transcription activation domain. When use in two hybrid experiments, the weakness of B42 as activator increases the sensitivity of the interaction detection.
PMID:14613974
http://purl.org/obo/owl/PMID#PMID_14613974
gal4 dna binding domain
PSI-MI
Part of the yeast transcription factor GAL4 (amino acids 11-38) specifically responsible for DNA binding of a 17 base-pair long sequence in the upstream activating sequence of galactose-induced genes.n
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gal4 dna bd
lexa dna binding domain
PSI-MI
Amino terminal (1-220) part of the Escherichia coli lexA repressor, binding to 16 base pair palindromic DNA sequences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
lexa dna bd
sandwich immunoassay
PSI-MI
Antibody array where proteins retained by the arrayed antibodies are identified using a detector antibody. The detector antibody is either modified with a directly detectable label (enzyme, fluorescent molecule, isotope, etc.), or it is biotinylated for detection after subsequent probing with labeled streptavidin.
PMID:12454649
http://purl.org/obo/owl/PMID#PMID_12454649
polymerase assay
PSI-MI
nucleotidyltransferase assay
Measures the catalysis of the transfer of a free nucleotidyl group to a nucleic acid chain.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dna directed dna polymerase assay
PSI-MI
dna dna pol assay
Measures the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template or primer.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dna directed rna polymerase assay
PSI-MI
dna rna pol assay
Measures the catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Utilizes a DNA template, i.e. the catalysis of DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. Can initiate a chain 'de novo'.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rna directed dna polymerase assay
PSI-MI
Measures the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Catalyzes RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rna dna pol assay
rna directed rna polymerase assay
PSI-MI
rna rna pol assay
Measures the catalysis of the reaction: nucleoside triphosphate + RNA (n) = diphosphate + RNA (n+1); uses an RNA template.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dna strand elongation
PSI-MI
The process by which a DNA strand is synthesized from template DNA by the action of polymerases, which add nucleotides to the 3' end of the nascent DNA strand.
GO:0006271
http://purl.org/obo/owl/GO#GO_0006271
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dna elongation
DNA replication elongation
panther
PSI-MI
PANTHER
The PANTHER (Protein ANalysis THrough Evolutionary Relationships) Classification System is a unique resource that classifies genes by their functions using published scientific experimental evidence and evolutionary relationships to predict function even in the absence of direct experimental evidence.nwww.pantherdb.org/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene3d
PSI-MI
The Gene3D database provides a combined structural, functional and evolutionary view of the protein world. It is focused on providing structural annotation for protein sequences without structural representatives--including the complete proteome sets of over 240 different species.nhttp://cathwww.biochem.ucl.ac.uk:8080/Gene3D/
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
Gene3D
nucleic acid delivery
PSI-MI
Method by which nucleic acids are delivered or engineered into a cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucl delivery
anti tag western blot
PSI-MI
Western blot assay performed when specific antibodies for the protein of interest are not available. Therefore the protein is expressed as a hybrid protein fused to a tag for which efficient antibodies are available. The antibody may be either monoclonal or polyclonal.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
anti tag western
nucleic acid transformation
PSI-MI
Transformation is the genetic alteration of a cell resulting from the introduction, uptake and expression of foreign genetic material incorporated into the cell's genome (DNA or RNA).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucl transformation
anti tag immunostaining
PSI-MI
Immunostaining assay performed when specific antibodies for the protein of interest are not available. Therefore the protein is expressed as a hybrid protein fused to a tag peptide/protein for which efficient antibodies are available. The anti tag antibody may be either monoclonal or polyclonal.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
anti tag immunost
monoclonal antibody immunostaining
PSI-MI
A monospecific antibody for the protein of interest is available, this is used to detect a specific protein within a cell or tissue sample.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
monoclonal immunost
polyclonal antibody immunostaining
PSI-MI
polyclonal immunost
Immunostaining assay carried out using a mixture of different antibodies that represent the immune response, normally in an experimental animal, to the protein of interest. These antibodies are used to detect the protein within a cell or tissue sample.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid transformation by treatment with divalent cation
PSI-MI
Stable introduction and expression of nucleic acid carried out by treatment with divalent cation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
n transformat cation
nucleic acid electroporation
PSI-MI
nucl electroporation
Electroporation, or electropermeabilization, is a significant increase in the electrical conductivity and permeability of the cell plasma membrane caused by externally applied electrical field. It is usually used in molecular biology as a way of introducing some substance inside the cell, such as loading it with a molecular probe, a drug that can change cell's function, or a piece of coding DNA.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid microinjection
PSI-MI
nucl microinjection
Microinjection refers to the process of using a micro needle to insert substances at a microscopic level into a single living cell. It is a simple mechanical process in which an extremely fine micro needle penetrates the cell membrane and sometimes the nuclear envelope and releases nucleic acids.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid passive uptake
PSI-MI
nucl passive uptake
Nucleic acid entrance into cells that does not involved specific treatments but rely on natural cellular processes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid transduction
PSI-MI
nucl transduction
Transduction is the process by which bacterial DNA is moved from one bacterium to another by a virus.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid conjugation
PSI-MI
nucl conjugation
Bacterial conjugation is the transfer of genetic material between bacteria through cell-to-cell contact. Bacterial conjugation is often incorrectly regarded as the bacterial equivalent of sexual reproduction or mating. It is not actually sexual, as it does not involve the fusing of gametes and the creation of a zygote. It is merely the transfer of a conjugative plasmid from a donor cell to a recipient
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
passive uptake
PSI-MI
Entrance of molecules into cells that does not involved specific treatments but relies on natural cellular processes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid transfection with liposome
PSI-MI
nucl lipotransfect
Lipofection (or liposome transfection) is a technique used to inject genetic material into a cell by means of liposomes which are vesicles that can easily merge with the cell membrane since they are both made of a phospholipid bilayer.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid transfection by treatment
PSI-MI
Transient introduction and expression of nucleic acid carried out by treatment with chemicals.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
n transfection treat
calcium phosphate nucleic acid transfection
PSI-MI
ca po nuc transfect
Transient introduction and expression of nucleic acid carried out by treatment with calcium phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid delivery by infection
PSI-MI
Nucleic acid introduced into a cell via an external organism, usually a virus or bacteria..
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucl infection
protein delivery
PSI-MI
Method by which proteins are delivered into a cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein electroporation
PSI-MI
prot electroporation
Method for temporarily permeabilising cell membranes in order to facilitate the entry of a protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein microinjection
PSI-MI
Microinjection refers to the process of using a micro needle to insert substances at a microscopic level into a single living cell. It is a simple mechanical process in which an extremely fine micro needle penetrates the cell membrane and sometimes the nuclear envelope and releases proteins.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
prot microinjection
protein delivery by cationic lipid treatment
PSI-MI
Proteins are delivered into cells by treatment with cationic lipids.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
prot cationic lipid
protein delivery by infection
PSI-MI
prot infection
Protein introduced into a cell via an external organism, usually a virus or bacteria.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
reverse two hybrid
PSI-MI
Yeast strains are generated in which expression of DB-X/AD-Y or DBPX hybrid proteins is toxic under particular conditions (negative selection). Under these conditions, dissociation of an interaction should provide a selective advantage thereby facilitating detection: a few growing yeast colonies in which DB-X/AD-Y (or DBPX/binding site) fail to interact should be identified among many nongrowing colonies containing interacting DB-X/AD-Y or DBPX/binding site.
PMID:8816797
http://purl.org/obo/owl/PMID#PMID_8816797
lexa b52 complementation
PSI-MI
Yeast two-hybrid system using Escherichia coli LexA amino acids 1-202 as the DNA-binding domain (BD), E. coli B42 acidic sequence as the activation domain (AD), and two reporters, lacZ and LEU2, each containing upstream LexA binding elements.
PMID:14613974
http://purl.org/obo/owl/PMID#PMID_14613974
lexa b52 complement
LexA B52 transcription complementation
gal4 vp16 complementation
PSI-MI
mammalian two hybrid
KISS
karyoplasmic interaction ion strategy
gal4 vp16 complement
A chimeric protein consisting of the GAL4 DNA-binding domain (aa 1-147 of GAL4) and a transcriptional activation domain from the herpes simplex virus protein VP16 (either aa 411-490 or aa 411-455) can specifically activate transcription of a reporter gene located downstream ofGAL4 DNA binding sites and the E1B minimal promoter. Similarly, two chimeric proteins, one encoding a chimeric GAL4 protein and the other encoding a chimeric VP16 protein, can activate the reporter gene, if the domains fused to the GAL4 and VP16 sequences can complex with appropriate conformation. However, if the domains fused to the GAL4 and VP16 sequences do not interact specifically to form a + complex that reconstitutes GAL4 function, the reporter gene cannot be activated.
PMID:1387709
http://purl.org/obo/owl/PMID#PMID_1387709
luminescence based mammalian interactome mapping
PSI-MI
This strategy uses Renilla luciferase enzyme (RL) fused to proteins of interest, which are then coexpressed with individual Flag-tagged partners in mammalian cells. Their interactions are determined by performing an RL enzymatic assay on anti-Flag immunoprecipitates.
PMID:15761153
http://purl.org/obo/owl/PMID#PMID_15761153
lumier
pubchem
PSI-MI
PubChem provides information on the biological activities of small molecules.nhttp://pubchem.ncbi.nlm.nih.gov/
PMID:16381840
http://purl.org/obo/owl/PMID#PMID_16381840
PubChem
3d repertoire
PSI-MI
The aim of 3D Repertoire is to determine the structures of all amenable complexes in a cell at medium or high resolution, which will later serve to integrate in toponomic and dynamic analyses of protein complexes in a cell. Complex models, EM pictures, expression and purification protocols obtained in the project will be collected in a database connected to the PDB repository.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
3D Repertoire
red fluorescent protein tag
PSI-MI
The red fluorescent protein derived from marine anemone Discosoma striata and reef corals belonging to the class Anthozoacan be fused to individual proteins which then acquire fluorescence excitation and emission spectra virtually identical to those of the native.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rfp tag
RFP
red fluorescent protein
cyan fluorescent protein tag
PSI-MI
cfp tag
CFP
The cyan fluorescent protein derived from Anthozoa reef coral can be fused to individual proteins which then acquire fluorescence excitation and emission spectra virtually identical to those of the native.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cyan fluorescent protein
enhanced green fluorescent protein tag
PSI-MI
EGFP
Variation of the green fluorescent protein derived from the bioluminescent jellyfish Aequorea victoria, can be fused to individual proteins which then acquire fluorescence excitation and emission spectra virtually identical to those of the native.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
egfp tag
enhanced green fluorescent protein
transactivating tag
PSI-MI
Tat tag
tat tag
Tag derived from the transactivating (Tat) protein of human immunodeficiency virus 1 (HIV-1) that can enter cells efficiently when added exogenously in tissue culture. The Tat tag can carry other molecules into cells, by fusion of Tat peptides (residues 1-72 or 37-72,) to any molecule under study. Tat-mediated uptake may allow the delivery of macromolecules previously thought to be impermeable to living cells.
PMID:8290579
http://purl.org/obo/owl/PMID#PMID_8290579
protein passive uptake
PSI-MI
Proteins entrance into cells that does not involved specific treatments but rely on natural cellular processes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
prot passive uptake
peptide sequence database
PSI-MI
pep seq db
database storing sequences detected by peptide identification methods.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pride
PSI-MI
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
PRIDE is a public repository of protein and peptide identifications for the proteomics community.nhttp://www.ebi.ac.uk/pride/
PMID:16381953
http://purl.org/obo/owl/PMID#PMID_16381953
penetrating tag
PSI-MI
Membrane shuttling peptide derived from the Drosophila homeobox protein Antennapedia: RQIKIWFQNRRMKWKK
PMID:16574060
http://purl.org/obo/owl/PMID#PMID_16574060
cell penetrating peptide tag
PSI-MI
The peptides named CPPs vary greatly in size, amino acid sequence, and charge, but share the common feature that they have the ability to rapidly translocate the plasma membrane and enable delivery to the cytoplasm or nucleus.
PMID:16574060
http://purl.org/obo/owl/PMID#PMID_16574060
Trojan peptides
PTDs
cell penetrating pep
CPPs
cell-penetrating peptides
MTS
protein transduction domains
membrane translocating sequences
peptide atlas
PSI-MI
PeptideAtlas addresses these needs by identifying peptides by tandem mass spectrometry (MS/MS), statistically validating those identifications and then mapping identified sequences to the genomes of eukaryotic organisms.nhttp://www.peptideatlas.org/
PMID:15642101
http://purl.org/obo/owl/PMID#PMID_15642101
PMID:16381952
http://purl.org/obo/owl/PMID#PMID_16381952
PeptideAtlas
gpm
PSI-MI
Global Proteome Machine aim to improve the quality of analysis, make the results portable and to provide a common platform for testing and validating proteomics results.nhttp://www.thegpm.org
PMID:15595733
http://purl.org/obo/owl/PMID#PMID_15595733
Global Proteome Machine
genetic experimental form
PSI-MI
Descriptor of an experimental form involved in a genetic interaction
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genetic exp form
knock out
PSI-MI
The gene has been completely removed e.g. by genetic engineering
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
knock-out
knock down
PSI-MI
The gene expression has been significantly reduced compared to wild-type by introduction of an external substance, e.g. by RNA interference.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
knock-down
hypermorph
PSI-MI
The gene function has been partially improved compared to wild-type by altering its sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
hypomorph
PSI-MI
The gene function has been partially reduced compared to wild-type by altering its sequence e.g. a temperature sensitive mutant.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
antimorph
PSI-MI
The gene function has been antagonized by a mutation in another copy of the gene.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
amorph
PSI-MI
The gene function has been abolished by mutation, though the type of mutation is not known.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
synthetic genetic interaction defined by inequality
PSI-MI
synthetic
synthetic genetic interaction (sensu inequality)
The phenotype resulting from genetic perturbation a and the phenotype resulting from genetic perturbation b have no effect on the WT background, but the combined genetic perturbation of A and B has a phenotypic effect. E. g., WT = a = b > ab.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
asynthetic genetic interaction defined by inequality
PSI-MI
asynthetic
asynthetic genetic interaction (sensu inequality)
The phenotype resulting from genetic perturbation of A alone, B alone and AB combined have the same effect on the WT background. E. g., WT > a = b = ab.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
suppressive genetic interaction defined by inequality
PSI-MI
suppression
The phenotype resulting from genetic perturbation of A has an effect on WT, but that effect is abolished by adding the suppressor b, which itself shows no single-mutant effect. E. g., WT = b = ab > a.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
suppressive genetic interaction (sensu inequality)
epistatic genetic interaction defined by inequality
PSI-MI
epistatic genetic interaction (sensu inequality)
epistatic
The phenotype resulting from genetic perturbation of A and B have different effects (in terms of direction or magnitude) on the wild-type background and the double mutant has the same phenotype as either A or B (for example, A < WT < B = AB).
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
conditional genetic interaction defined by inequality
PSI-MI
conditional
conditional genetic interaction (sensu inequality)
The phenotype resulting from genetic perturbation of A has an effect only in the b background, or the b mutant has an effect only in the a background. a has an effect only in the b background, or the b mutant has an effect only in the a background. E. g., WT = a > ab > b or WT > a > b > ab.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
additive genetic interaction defined by inequality
PSI-MI
additive
additive genetic interaction (sensu inequality)
Single-mutant phenotype effects combine to give a double-mutant effect different from the wild type and different from single mutant effect. For instance, WT < a = b < ab, b < WT = ab < a, WT < a < b < ab, b < WT < ab < a, and all additional inequalities obtained by interchanging a and b, or reversing the effect of both a and b.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
single nonmonotonic genetic interaction defined by inequality
PSI-MI
single nonmonotonic genetic interaction (sensu inequality)
single nonmonotonic
The phenotype resulting from genetic perturbation of B shows opposing effects in the WT and a backgrounds (for example, b > WT and ab < a); or, a shows opposing effects in the WT and b backgrounds, but not both. E.g., WT > a > ab > b.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
double nonmonotonic genetic interaction defined by inequality
PSI-MI
double nonmonotonic genetic interaction (sensu inequality)
The phenotype resulting from genetic perturbation of both A and B show opposing effects in the WT background and the background with the other mutant gene. E.g., WT >= ab > a >= b
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
double nonmonotonic
enhancement interaction
PSI-MI
enhancement
The A genetic perturbation enhances the phenotype of the B perturbation, or vice versa (e.g. WT = A < B < AB or WT = B < A < AB). This could be conditional or additive by the above scheme.nOBSOLETE: remap to MI:0933 'negative genetic interaction'
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
expression level alteration
PSI-MI
Synthesis rate of a molecule under investigation differs from its naturally occurring expression level in a cell.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
expression modif
mutated gene
PSI-MI
The gene is mutated in some unknown manner
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
wwpdb
PSI-MI
wwPDB
The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. The founding members are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan). The BMRB (USA) group joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single Protein Data Bank Archive of macromolecular structural data that is freely and publicly available to the global community.nhttp://www.wwpdb.org/
PMID:14634627
http://purl.org/obo/owl/PMID#PMID_14634627
id-validation-regexp:"[0-9][a-zA-Z0-9]{3}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9][a-zA-Z0-9]{3}"
pdbj
PSI-MI
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
PDBj(Protein Data Bank Japan) maintains the database for the protein structures with financial assistance from the Institute for Bioinformatics Research and Development of Japan Science and Technology Corporation(BIRD-JST), collaborating with the Research Collaboration for Structural Bioinformatics(RCSB) and the MSD in the European Bioinformatics Institute(MSD-EBI) in EU. All three organizations serve as deposition, data processing and distribution sites.nhttp://www.pdbj.org/
PMID:12099029
http://purl.org/obo/owl/PMID#PMID_12099029
id-validation-regexp:"[0-9][a-zA-Z0-9]{3}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9][a-zA-Z0-9]{3}"
PDBj
comigration in gel electrophoresis
PSI-MI
The interaction of two molecules is determine by their very close proximity or the overlap of their relative bands in a gel.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
comigration in gel
comigration in sds page
PSI-MI
comigration in sds
Method allowing the detection of strong interactions between two molecules by their very close proximity or the overlap of their relative bands in a denaturing SDS gel.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
PMID:16732283
http://purl.org/obo/owl/PMID#PMID_16732283
bimolecular fluorescence complementation
MI:0229
PSI-MI
bifc
gfp complementation
green fluorescence protein complementation assay
The bimolecular fluorescence complementation (BiFC) is an assay for determination of protein interactions and/or their location in living cells. This approach is based on complementation between two non- fluorescent fragments of a protein fluorophore such as green fluorescent protein (GFP) or its derivatives. Interactions between proteins fused to each fragment bring the fragments together resulting in the reconstitution of a fully functional flourophore that can be identified through fluorescence spectroscopy or microscopy.
PMID:11983170
http://purl.org/obo/owl/PMID#PMID_11983170
substitution analysis
PSI-MI
substitut analysis
In this approach, once a molecule is demonstrated to participate in an interaction, several substitution mutants are produced and tested in the binding assay to identify the residues which identity is crucial for the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
insertion analysis
PSI-MI
In this approach, once a molecule is demonstrated to participate in an interaction, several insertion derivatives are produced and tested in the binding assay to detect the regions that are important for the interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
calmodulin binding protein tag
PSI-MI
The protein is expressed and purified as a fusion to the calmoduling-binding protein. The fusion protein can be purified by affinity chromatography using a calmodulin resin.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cam tag
proximity enzyme linked immunosorbent assay
PSI-MI
pLISA
proximity ligation
Method allowing efficient and precise interaction detection, along with extensive repertoires of specific binding reagents. It is based on proximity a ligation mechanism that enables sensitive high-capacity protein measurements by converting the detection of specific proteins to the analysis of DNA sequences. Proximity probes containing oligonucleotide extensions are designed to bind pairwise to target proteins and to form amplifiable tag sequences by ligation when brought in proximity.
PMID::17072308
http://purl.org/obo/owl/PMID#PMID_:17072308
PMID:15155907
http://purl.org/obo/owl/PMID#PMID_15155907
pELISA
p elisa
protease accessibility laddering
PSI-MI
In protease accessibility laddering (PAL) tagged proteins are purified on magnetic beads in their natively folded state. While attached to the beads, proteins are probed with proteases. Proteolytic fragments are eluted and detected by immunoblotting with antibodies against the tag (e.g., Protein A, GFP, and 6xHis).
PMID:16615907
http://purl.org/obo/owl/PMID#PMID_16615907
pal
protease access
confirmation by molecular weight
PSI-MI
weight identificat
Molecule whose sequence identity is derived from their molecular weight
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molecular weight estimation by staining
PSI-MI
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
weight by staining
molecular weight estimation by silver staining
PSI-MI
weight silver stain
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker and staining of the molecules with silver.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molecular weight estimation by coomasie staining
PSI-MI
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker and staining of the molecules with comassie dye.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
weight by comassie
molecular weight estimation by bromide staining
PSI-MI
weight by bromide
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker and staining of the molecules with bromide dyes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molecular weight estimation by sybr staining
PSI-MI
safe DNA gel stain
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker and staining of the molecules with sybr dyes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
weight by sybr
molecular weight estimation by autoradiography
PSI-MI
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker and staining by autoradiography.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
weight autoradiogra
molecular weight estimation by hoechst staining
PSI-MI
Molecule whose sequence identity is derived from their molecular weight after a comigration in a gel with molecular weight marker and staining of the molecules with Hoechst dyes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
weight by hoechst
predetermined feature
PSI-MI
predetermined featur
Feature detection not verified in the context of an experiment but assumed from external or previous experimental evidence(s).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
x-ray powder diffraction
PSI-MI
Analysis of a diffraction pattern generated by an isotropic sample composed of many randomly oriented crystals.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
X-ray
x-ray powder diffrac
x-ray fiber diffraction
PSI-MI
x-ray fiber diffrac
X-ray
Analysis of the diffraction pattern of a partially ordered sample composed of fibers oriented parallel to each other using X-ray.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
x ray scattering
PSI-MI
saxs
Method where the internal structure of a sample is derived from the intensity distribution of the scattered monochromatic X-ray beam at very low scattering angles.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
x-ray tomography
PSI-MI
X-ray Tomography is a branch of X-ray microscopy. A series of projection images are used to calculate a three dimensional reconstruction of an object. The technique has found many applications in materials science and later in biology and biomedical research. In terms of the latter, the National Center for X-ray Tomography (NCXT) is one of the principle developers of this technology, in particular for imaging whole, hydrated cells.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
polyprotein fragment
PSI-MI
Subpart of a polyprotein that is naturally cleaved in vivo.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
chain
polyprotein frag
multiple parent reference
PSI-MI
multiple parent
This qualifier is used for hybrid or composite molecules with more than one cross-reference to parent molecules.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tissue list
PSI-MI
List of tissue used as topic in UniProt RC line.nhttp://www.expasy.org/cgi-bin/lists?tisslist.txt
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cell ontology
PSI-MI
Ontology of cell types.nhttp://obo.sourceforge.net/cgi-bin/detail.cgi?cell
PMID:16381901
http://purl.org/obo/owl/PMID#PMID_16381901
half cystine
PSI-MI
A protein modification that is effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed
RESID:AA0025
http://purl.org/obo/owl/RESID#RESID_AA0025
MOD:00798
http://purl.org/obo/owl/MOD#MOD_00798
Half of a disulfide bridge
autoradiography
PSI-MI
Experimental method by which radiolabel is detected by exposure to a photographic emulsion forming a pattern on the film.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ka
PSI-MI
Association rate constant or rate of complex formation. Unit MOLE per SECOND (M-1 s-1)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
kon
koff
PSI-MI
Dissociation rate constant measuring the stability of a complex. Unit SECOND (s-1)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
koff
Kd
temperature of interaction
PSI-MI
temp interaction
Tint
Temperature at which interaction was determined. Unit KELVIN (K)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
T interaction
pH of interaction
PSI-MI
pHint
pH at which interaction was determined.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
kelvin
PSI-MI
A scale that measures an object's temperature over absolute zero, the theoretical coolest temperature where all molecular and atomic motion ceases. On the Kelvin scale, the freezing point of water is 273 (273 K = 0 o C = 32 o F).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
K
mole per second
PSI-MI
M-1s-1
Per mole per second, unit for association rate constant
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
stimulator
PSI-MI
Molecule stimulating an interaction by interacting with one or more of the participants.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphotransferase assay
PSI-MI
Measures the rate of a phosphate transfer between two molecules.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphotransfer assay
phosphotransferase
phosphate donor
PSI-MI
Any molecule that is able to transfer an phosphate to another chemical species.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphate acceptor
PSI-MI
Molecule to which a phosphate may be transferred from a phosphate donor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phosphotransfer reaction
PSI-MI
phosphotransfer
Reaction where a phosphate is transferred between two proteins of a phosphorelay system.
PMID:16712436
http://purl.org/obo/owl/PMID#PMID_16712436
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
spin label
PSI-MI
Paramagnetic fragment, most often a cyclic nitroxide derivative, covalently attached to a molecule of interest.
PMID:10966640
http://purl.org/obo/owl/PMID#PMID_10966640
r1 spin label
PSI-MI
Paramagnetic molecule (1-oxyl-2,2,5,5-tetramethylpyrroline-n3-methyl)-methanethiosulfonate. that can be covalently attached to any cysteine aminoacid producing a nitroxidenside chain designated R1.
PMID:10966640
http://purl.org/obo/owl/PMID#PMID_10966640
dansyl tag
PSI-MI
dansyl label
5-dimethylaminonaphthalene-1-sulfonyl tag
Dansyl is fluorescent tag. Dansyl is the acronyme of 5-dimethylaminonaphthalene-1-sulfonyl radical group reacting with any NH2 groups.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
125i radiolabel
PSI-MI
I125
Molecule labelled with 125 radio isotope of iodine atoms.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
125I
ncbi taxonomy
PSI-MI
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
The NCBI taxonomy database indexes over 55 000 organisms that are represented in the sequence databases with at least one nucleotide or protein sequence. The Taxonomy Browser can be used to view the taxonomic position or retrieve sequence and structural data for a particular organism or group of organisms. Searches of the NCBI taxonomy may be made on the basis of whole or partial organism names, and direct links to organisms commonly used in biological research are also provided. The Taxonomy Browser can also be used to display the number of nucleic acid sequences, protein sequences, and protein structures available for organisms included in the branch. From the data display for a particular organism, one can retrieve and download the sequence data for that organism, or protein 3D structure data if available.nhttp://www.ncbi.nlm.nih.gov/Taxonomy/
PMID:10592169
http://purl.org/obo/owl/PMID#PMID_10592169
encode
PSI-MI
ENCODE (the Encyclopedia Of DNA Elements) seeks to identify all protein-coding genes. The current ENCODE data set is derived from 1% of the human genome and has been selected for analysis in the pilot phase of the project.nhttp://www.genome.gov/10005107
PMID:17372197
http://purl.org/obo/owl/PMID#PMID_17372197
Encyclopedia Of DNA Elements
ENCODE
protein genbank identifier
PSI-MI
GenBank Protein GI
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
genpept id
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
GenBank Identifier or GI numbers for proteins.
PMID:17170002
http://purl.org/obo/owl/PMID#PMID_17170002
genbank protein gi
genbank_protein_gi
nucleotide genbank identifier
PSI-MI
GenBank Identifier or GI numbers for nucleotide.
PMID:17170002
http://purl.org/obo/owl/PMID#PMID_17170002
genbank_nucl_gi
GenBank Nucleotide
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
genbank nucleotide
dna overhang
PSI-MI
An overhang is a stretch of unpaired nucleotides in the end of a DNA molecule. These unpaired nucleotides can be in either strand, creating either 3' or 5' overhangs. Longer overhangs are called cohessive ends or sticky ends. They are most often created by restriction endonucleases when they cut DNA. Very often they cut the two DNA strands four base pairs from each other, creating a four-base 3' overhang in the other molecule and a complementary 5' overhang in the other. These ends are called cohessive since they are easily joined back together by a ligase
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
sticky ends
cohessive ends
3 prime overhang
PSI-MI
An overhang is a stretch of unpaired nucleotides in the end of a 3' strand of a DNA molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
3 prime sticky end
5 prime overhang
PSI-MI
An overhang is a stretch of unpaired nucleotides in the end of a 5' strand of a DNA molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
5 prime sticky end
fluorophore
PSI-MI
A fluorophore is a component of a molecule which causes a molecule to be fluorescent. It is a functional group in a molecule which will absorb energy of a specific wavelength and re-emit energy at a different (but equally specific) wavelength. The amount and wavelength of the emitted energy depend on both the fluorophore and the chemical environment of the fluorophore.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescent dye label
PSI-MI
fluorescent dye
Dye label containing a fluorophore which absorb energy of a specific wavelength and re-emit energy at a different (but equally specific) wavelength.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
immunodepleted coimmunoprecipitation
PSI-MI
immunodepleted coip
Method involving consecutive coimmunoimmunoprecipitations on the same sample, a control where an interaction is detected, and other CoIPs where the sample is previously treated with a specific antibody that precipitates a candidate interactor and leads to the suppression of an interaction or a change in composition of a complex.
PMID:17081976
http://purl.org/obo/owl/PMID#PMID_17081976
immunodepletion
intermolecular force
PSI-MI
surface adhesion force measurement
single molecule force measurement
optical tweezer
force measurement
An optical tweezer is a scientific instrument that uses a focused laser beam to provide an attractive or repulsive force, depending on the index mismatch (typically on the order of piconewtons) to physically hold and move microscopic dielectric objects (i.e.highly resistants to the flow of an electric current). This instrument allow to measure the forces generated between interacting molecules - either at the level of just single interacting pair of molecules or at the level of larger molecular assemblies.
PMID:17023539
http://purl.org/obo/owl/PMID#PMID_17023539
PMID:17081984
http://purl.org/obo/owl/PMID#PMID_17081984
molecular force measurement
genbank indentifier
PSI-MI
id-validation-regexp:"ENS[A-Z]+[0-9]{11}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"ENS[A-Z]+[0-9]{11}"
edit
PMID:15078858
http://purl.org/obo/owl/PMID#PMID_15078858
protein a tag
PSI-MI
The protein A is a bacterial cell wall isolated from Staphylococcus aureus that binds to mammalian IgGs mainly through Fc regions. The protein A can be use to retaint antibodies or as fusion tag of a protein under analysis.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein A
zz tag
PSI-MI
ZZ tag
The ZZ tag is a tag made out of two tandem repeats of the Protein A IgG binding domain.
PMID:11694505
http://purl.org/obo/owl/PMID#PMID_11694505
thiol reactive lanthanide label
PSI-MI
Thiol-reactive lanthanide complexes have been synthesized that are luminescent when bound to terbium and/or europium. The Tb3+-DTPA-cs124-EMCH complexes consist of a diethylenetriaminepentaacetate (DTPA) chelate covalently joined through one amide bond to a chromophore, carbostyril 124, and via a second amide bond to a maleimide, bromoacetamide, or pyridyldithio moiety. This label can be Site-specific attachted to both proteins and DNA.
PMID:10077482
http://purl.org/obo/owl/PMID#PMID_10077482
thiol lanthanide
Tb3+-DTPA-cs124-EMCH
brenda
PSI-MI
A structured controlled vocabulary for the source of an enzyme. It comprises terms for tissues, cell lines, cell types and cell cultures from uni- and multicellular organisms.nhttp://www.brenda-enzymes.info
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescence acceptor donor pair
PSI-MI
fret pair
Pair of fluorophores attached to the same molecule used in a fret experiment to observe the details of conformational changes .
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tag visualisation
PSI-MI
Molecule whose sequence identity is not checked after the interaction but its presence is detected through its tag
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tag visualisation by fluorescence
PSI-MI
The protein is either expressed as a hybrid protein fused to a tag containing a fluorophore, such as green fluorescent protein, or a fluorophore has been chemically attached to the protein. Subsequence observation or measurement of fluorescence is used to identify the presence of the molecule in an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tag fluorescence
author identifier
PSI-MI
Author published identifier.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
originally assigned identifier
PSI-MI
original identifier
Identifier assigned when the record was created by a source database.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
demethylase assay
PSI-MI
Measures the catalysis of the hydrolysis of an methyl group from a substrate molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
demethylation reaction
PSI-MI
demethylation
The cleavage of a methyl group from a polypeptide. Methylation is generally an irreversible reaction except in mamalian.
PMID:17277772
http://purl.org/obo/owl/PMID#PMID_17277772
GO:0006482
http://purl.org/obo/owl/GO#GO_0006482
atomic force microscopy
PSI-MI
The atomic force microscope (AFM) is a very high-resolution type of scanning probe microscope, with demonstrated resolution of fractions of a nanometer, more than 1000 times better than the optical diffraction limit. The AFM was invented by Binnig, Quate and Gerber in 1986, and is one of the foremost tools for imaging, measuring and manipulating matter at the nanoscale.The term 'microscope' in the name is actually a misnomer because it implies looking, while in fact the information is gathered by feeling out the surface with a mechanical feeler.nhttp://en.wikipedia.org/wiki/Atomic_force_microscope
PMID:17502105
http://purl.org/obo/owl/PMID#PMID_17502105
atomic force microsc
AFM
curation request
PSI-MI
Annotation of a published paper which has been externally requested.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
dataset
PSI-MI
Targeted curation dataset grouping experiments by topic or dataset origin.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
author submitted
PSI-MI
Data directly submitted by the authors to a database prior to publication.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleoside triphosphatase assay
PSI-MI
Measures the catalysis of the hydrolysis of a nucleoside triphosphate into a nucleoside diphosphate plus phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
triphosphatase ass
atpase assay
PSI-MI
Measures the catalysis of the hydrolysis of ATP+ H2O = ADP + phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleoside triphosphatase reaction
PSI-MI
Catalysis of the hydrolysis of a nucleoside triphosphate into a nucleoside diphosphate plus phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0017111
http://purl.org/obo/owl/GO#GO_0017111
triphosphatase react
atpase reaction
PSI-MI
Catalysis of the hydrolisis of ATP+ H2O = ADP + phosphate.
GO:0016887
http://purl.org/obo/owl/GO#GO_0016887
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gtpase reaction
PSI-MI
Catalysis of the hydrolisis of GTP+ H2O = GDP + phosphate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:0003924
http://purl.org/obo/owl/GO#GO_0003924
vsv tag
PSI-MI
vesicular stomatitis virus tag
Epitope tag derived from vesicular stomatitis virus (VSV) glycoprotein. The tag sequence is YTDIEMNRLGK and many antibodies against it are commercially available.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
journal
PSI-MI
Name and details of a journal from which paper has been taken.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
publication year
PSI-MI
Year of publication of a paper.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
histone acetylase assay
PSI-MI
In histone acetylation the histones are acetylated on lysine residues in the N-terminal tail as part of gene regulation. Typically, these reactions are catalyzed by enzymes with "histone acetyltransferase" (HAt)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
histone acetylation
hat
HAt
small angle neutron scattering
PSI-MI
During a SANS experiment a beam of neutrons is directed at a sample. The neutrons are elastically scattered by a sample and the resulting scattering pattern is analyzed to provide information about the size, shape and orientation of some component of the sample.
PMID:11578931
http://purl.org/obo/owl/PMID#PMID_11578931
sans
SANS
acetylase assay
PSI-MI
acetylation
Measures the catalysis of the addition of an acetyl group to a target molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
qdot
PSI-MI
Qdot are nanocrystals fluorophores . Nanocrystals a are extremely efficient materials for generating and they have a highly customizable surface for directing their bioactivity, producing a fluorescent probe that outperforms traditional dyes in many fluorescence applications.
PMID:17569782
http://purl.org/obo/owl/PMID#PMID_17569782
neutron fiber diffraction
PSI-MI
Analysis of diffraction pattern of a partially ordered sample composed of fibers oriented parallel to each other using neutron beam.
PMID:16707576
http://purl.org/obo/owl/PMID#PMID_16707576
PMID:15914673
http://purl.org/obo/owl/PMID#PMID_15914673
PMID:16041074
http://purl.org/obo/owl/PMID#PMID_16041074
PMID:15272083
http://purl.org/obo/owl/PMID#PMID_15272083
PMID:15546977
http://purl.org/obo/owl/PMID#PMID_15546977
PMID:10771422
http://purl.org/obo/owl/PMID#PMID_10771422
neutron fiber diff
solid phase assay
PSI-MI
Assay where at least one molecule under analysis is bound to a solid surface, such as a microplate wall or the sides of a tube, the other reactants being free in solution.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
neutron diffraction
PSI-MI
Analysis of diffraction pattern using neutron beam
PMID:15272083
http://purl.org/obo/owl/PMID#PMID_15272083
PMID:15546977
http://purl.org/obo/owl/PMID#PMID_15546977
PMID:10771422
http://purl.org/obo/owl/PMID#PMID_10771422
PMID:15914673
http://purl.org/obo/owl/PMID#PMID_15914673
PMID:16041074
http://purl.org/obo/owl/PMID#PMID_16041074
PMID:16707576
http://purl.org/obo/owl/PMID#PMID_16707576
electron diffraction
PSI-MI
Analysis of diffraction pattern using electron beam.
PMID:16325200
http://purl.org/obo/owl/PMID#PMID_16325200
PMID:15141214
http://purl.org/obo/owl/PMID#PMID_15141214
PMID:11700061
http://purl.org/obo/owl/PMID#PMID_11700061
PMID:11532455
http://purl.org/obo/owl/PMID#PMID_11532455
PMID:11171962
http://purl.org/obo/owl/PMID#PMID_11171962
PMID:11034202
http://purl.org/obo/owl/PMID#PMID_11034202
PMID:10949309
http://purl.org/obo/owl/PMID#PMID_10949309
protein kinase A complementation
PSI-MI
This method uses Renilla luciferase (Rluc)-based protein fragment complementation assay (PCA) that is designed specifically to investigate dynamic protein complexes (association and dissociation). It is chose to generate a PCA based on the Rluc, which is, because of its simplicity and sensitivity, a widely used bioluminescence reporter. The general scheme for construction and detection of the Rluc-PCA PKA sensor consists of fusing complementary fragments of Rluc to the regulatory (Reg) and catalytic (Cat) PKA subunits of PKA.
PMID:17942691
http://purl.org/obo/owl/PMID#PMID_17942691
pka complementation
renilla luciferase protein tag
PSI-MI
Renilla luciferase, is an enzyme of the sea pansy catalyzing the oxidation of the coelenterazine pigment) that produces light.. Renilla luciferase produces a blue light of 480nm.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
renilla lucirefase
protein modification ontology
PSI-MI
Catalogue of covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
id-validation-regexp:"MOD:[0-9]{5}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"MOD:[0-9]{5}"
psi-mod
putative self
PSI-MI
Molecule that is reported to self-interact but the experimental condition does not allow to resolve whether the interaction is intramolecular (true self interaction) or intermolecular (homodimer).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
p3 filamentous phage display
PSI-MI
pIII is one of the minor coat proteins that decorates in five copies the emerging tip of filamentous phage. Similarly to pVIII pIII also tolerates peptide insertions at the amino-terminus. The sequences to be displayed can either be encoded in the phage copy of the coat gene or in an extra pIII gene copy carried on a phagemid. In the first case 5 copies o the hybrid proteins are displayed while in the latter only a few capsid display one copy and the majority display none. Because of the low copy number pIII display is often referred to as low valency display.
PMID:1696028
http://purl.org/obo/owl/PMID#PMID_1696028
p3 filamentous phage
low valency display
p8 filamentous phage display
PSI-MI
pVIII is the major coat protein of filamentous phage. Its amino-terminus is exposed to solvent and tolerates the insertion of relatively large peptide fragments. By inserting the peptide coding sequence into the phage copy of the pVIII gene up to 3000 copies of the hybrid proteins can be displayed along the phage capsid. Alternatively the hybrid protein can be encoded on a phagemid that is incorporated in a virus like particle by infection with a helper phage. In this latter case one obtains a chimeric capsid where hybrid proteins are interspersed at different density in an otherwise wild type coat. Because of the high copy number pVIII display is also referred to as high valency display.
PMID:1720463
http://purl.org/obo/owl/PMID#PMID_1720463
high valency display
p8 filamentous phage
isotope label footprinting
PSI-MI
isotope footprinting
Exposed amino acid residues undergo a rapid exchange of a specific radio-isotope e.g. hydrogen/deuterium. Residues involved in a molecular interaction are protected from this exchange and exhibit a much slower rate of exchange. This method of binding range identification must be coupled to NMR or mass spectrometry technologies in order to detect the radio-isotope exchange.
PMID:18184591
http://purl.org/obo/owl/PMID#PMID_18184591
rna cleavage
PSI-MI
Any process by which an RNA molecule is cleaved at specific sites or in a regulated manner.
PMID:14681407
http://purl.org/obo/owl/PMID#PMID_14681407
GO:0006396
http://purl.org/obo/owl/GO#GO_0006396
mpidb
PSI-MI
MPDIB
The microbial protein-protein interactions database (MPDIB) aims to collect and provide all known physical prokaryotic interactions.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
polysaccharide
PSI-MI
A polysaccharide is a complex polymer of carbohydrate monormers. They are polymers made up of many monosaccharides joined together by glycosidic bonds. They are therefore very large, often branched, macromolecules.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
amplified luminescent proximity homogeneous assay
PSI-MI
alfa-screen
AlphaScreen
AlphaScreen relies on the use of Donor and Acceptor beads that are coated with a layer of hydrogel providing functional groups for bioconjugation. When a biological interaction between molecules brings the beads into proximity, a cascade of chemical reactions is initiated to produce a greatly amplified signal. Upon laser excitation, a photosensitizer in the Donor bead converts ambient oxygen to a more excited singlet state. The singlet state oxygen molecules diffuse across to react with a chemiluminescer in the Acceptor bead that further activates fluorophores contained within the same bead. The fluorophores subsequently emit light at 520-620 nm. In the absence of a specific biological interaction, the singlet state oxygen molecules produced by the Donor bead go undetected without the close proximity of the Acceptor bead. AlphaScreen has successfully been developed for enzyme assays (kinase, helicase, protease, ...), interaction assays (ligand/receptor, protein/protein, protein/DNA), immunoassays, and GPCR functional assays (cAMP, IP3).
PMID:17092917
http://purl.org/obo/owl/PMID#PMID_17092917
au1 tag
PSI-MI
DTYRYI epitope tag
The protein of interest is expressed as a fusion to the peptide DTYRYI for which antibodies are commercially available.
PMID:18216269
http://purl.org/obo/owl/PMID#PMID_18216269
conformational status
PSI-MI
conformation
Statement about the native/denatured conformation of the protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
denatured
PSI-MI
Altered conformation state of the protein as a result of heat or chemical modification resulting in a changed structure of the protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
native
PSI-MI
State of the protein without interference i.e. the natural form.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleic acid cleavage
PSI-MI
Covalent bond breakage of a nucleic acid molecule leading to the formation of smaller fragments.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ncl acid cleavage
cross linker
PSI-MI
A variety of crosslinkers are used to analyze subunit structure of proteins, protein interactions and various parameters of protein function. Subunit structure is deduced since crosslinkers only bind surface amino residues in relatively close proximity in the native state. Protein interactions are often too weak or transient to be easily detected, but by crosslinking, the interactions can be captured and analyzed.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
crosslinker
spdp cross linker
PSI-MI
N -Succinimidyl 3-(2-pyridyldithio)-propionate, is heterobifunctional, thiol-cleavable nand membrane permeable crosslinkers. It contains an amine-reactive N-hydroxysuccinimide (NHS) ester nthat will react with lysine residues to form a stable amide bond. The other end of the spacer arm is terminated in the pyridyl disulfide group that will react with sulfhydryls to form a reversible disulfide bond.
PMID:17360572
http://purl.org/obo/owl/PMID#PMID_17360572
N -Succinimidyl 3-(2-pyridyldithio)-propionate
lc-spdp cross linker
PSI-MI
Succinimidyl 6-(3-[2-pyridyldithio]-propionamido)hexanoate, is an heterobifunctional, thiol-cleavable nand membrane permeable crosslinkers. It contains an amine-reactive N-hydroxysuccinimide (NHS) ester nthat will react with lysine residues to form a stable amide bond. The other end of the spacer arm is terminated in the pyridyl disulfide group that will react with sulfhydryls to form a reversible disulfide bond. LC-SPDP is a derivative of the classical SPDP with a longer spacer arm.
PMID:17360572
http://purl.org/obo/owl/PMID#PMID_17360572
Succinimidyl 6-(3-[2-pyridyldithio]-propionamido)hexanoate
association
PSI-MI
Molecules that are experimentally shown to be associated potentially by sharing just one interactor. Often associated molecules are co-purified by a pull-down or coimmunoprecipitation and share the same bait molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
physical association
PSI-MI
Molecules that are experimentally shown to belong to the same functional or structural complex.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
lexa vp16 complementation
PSI-MI
lexa vp16 complement
LexA VP16 transcription complementation
Yeast two-hybrid system using Escherichia coli LexA amino acids 1-202 as the DNA-binding domain (BD), and a transcriptional activation domain from the herpes simplex virus protein VP16 (either aa 411-490 or aa 411-455) that can specifically activate transcription of a reporter gene located downstream.
PMID:9371806
http://purl.org/obo/owl/PMID#PMID_9371806
matrixdb
PSI-MI
Knowledgebase of the extracellular matrix storing experimentally determined interactions involving extracellular biomolecules. It includes protein-protein, protein-polysaccharide, and protein-lipid interactions.
PMID:19147664
http://purl.org/obo/owl/PMID#PMID_19147664
donor
PSI-MI
Molecule which emits electrons or ions that are transfered to an acceptor molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
acceptor
PSI-MI
Molecule able to receive electrons or ions from a donor molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ribonuclease assay
PSI-MI
Measures the catalysis of the hydrolysis of phosphodiester bonds in chains of RNA.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
surface plasmon resonance array
PSI-MI
Biacore Flexchip(r)
SPRi-Plex
spr array
This array technology allows the screening of binding abilities of hundreds or thousands of biomolecules (small molecule, peptide, protein, sugar, lipid, nucleic acid, and their fragments) printed onto the gold-coated chip by using an instrument (micro-arrayer) that is capable of spotting liquid samples in a reproducible manner onto a planar support. The ordered protein array can then be probed with a non-labelled sample (small molecule, peptide, protein, sugar, lipid, nucleic acid, and their fragments) to identify the baits that can bind to it. This is done in real time, allowing direct measurement of both the on-rate and the off-rate and of the affinity constant of complex formation on each spot.
PMID:16837183
http://purl.org/obo/owl/PMID#PMID_16837183
PMID:17889820
http://purl.org/obo/owl/PMID#PMID_17889820
PMID:16510109
http://purl.org/obo/owl/PMID#PMID_16510109
SPRImager
imex evidence
PSI-MI
Experimental evidence supporting an interaction curated and released under the IMEx agreement.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
irefindex
PSI-MI
iRefIndex
iRefIndex provides an index of protein interactions available in a number of primary interaction databases including BIND, BioGRID, DIP, HPRD, IntAct, MINT, MPact, MPPI and OPHID. This index allows the user to search for a protein and retrieve a non-redundant list of interactors for that protein. iRefIndex uses the Sequence Global Unique Identifier (SEGUID) to group proteins and interactions into redundant groups. This method allows users to integrate their own data with the iRefIndex in a way that ensures proteins with the exact same sequence will be represented only once.nhttp://irefindex.uio.no/
PMID:18823568
http://purl.org/obo/owl/PMID#PMID_18823568
camjedb
PSI-MI
Camjedb is a comprehensive database for information on the genome of Campylobacter jejuni.nhttp://www.sanger.ac.uk/Projects/C_jejuni/
PMID:106882042
http://purl.org/obo/owl/PMID#PMID_106882042
observed ptm
PSI-MI
Post translational modification observed on a protein in the context of an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fiash label
PSI-MI
4',5'-bis(1,3,2-dithioarsolan-2-yl)fluorescein
FIAsH label
This fluorescent label is a small ligand membrane-permeant and nonfluorescent until it binds with high affinity and specificity to the tetracysteine domain. Such in situ labeling adds much less mass than does green fluorescent protein and offers greater versatility in attachment sites as well as potential spectroscopic and chemical properties.
PMID:9657724
http://purl.org/obo/owl/PMID#PMID_9657724
iaedans label
PSI-MI
IAEDANS is fluorescent tag that bind to cysteines. IAEDANS is the acronyme of (5((((2-iodoacetyl)amino)ethyl)amino)-naphthalene-1-sulfonic acid) with free SH groups.
PMID:11052891
http://purl.org/obo/owl/PMID#PMID_11052891
IAEDANS
1,5-IAEDANS
(5((((2-iodoacetyl)amino)ethyl)amino)-naphthalene-1-sulfonic acid)
filter trap assay
PSI-MI
Biomolecules are mixed in a buffer and the resulting mixture isnpassed through a filter. Largenaggregates are retained on the filter and the pariticipants may then be identified.
PMID:10859365
http://purl.org/obo/owl/PMID#PMID_10859365
membrane filtration
Filter retention assay
filter binding
filter retardation assay
<new synonym>
northern blot
PSI-MI
northen
A standard procedure to identify RNA fragments containing specificnsequences. In this procedure RNA fragments are separated bynelectrophoresis, the fragments are transferred to a membrane and thenmembrane is incubated with a radio labelled probe that hybridises anyncomplementary subsequence.
PMID:414220
http://purl.org/obo/owl/PMID#PMID_414220
epistatic genetic interaction
PSI-MI
The genetic interaction between a group of genes, in which the effects of an allele of one member gene of the group hide the effects of alleles of other genes in the group.
PMID:11988766
http://purl.org/obo/owl/PMID#PMID_11988766
epistatis
genetic interaction defined by inequality
PSI-MI
Two genes A and B present an genetic interaction defined by inequality if the phenotypes of the two single mutants a and b, the double mutant ab and the wild-type WT can be measured quantitatively and described relative to each other by an inequality relationship.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genetic inequality
noninteractive genetic interaction defined by inequality
PSI-MI
noninteractive genetic interaction (sensu inequality)
noninteractive
Mutation that has no effect in the WT and b backgrounds, or b has no effect in the a and WT backgrounds, or both hold true. E. g., WT = a > b = ab.
PMID:15833125
http://purl.org/obo/owl/PMID#PMID_15833125
negative genetic interaction
PSI-MI
The phenotype of the double mutant ab is stronger than expected from the combination of the individual effects of a and b.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
negative gen int
neutral genetic interaction
PSI-MI
The phenotype of the double mutant ab is equal to the phenotype expected from the combination of the individual effects of a and b.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
neutral gent int
positive genetic interaction
PSI-MI
The phenotype of the double mutant ab is weaker than expected from the combination of the individual effects of a and b.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
positive gent int
emdb
PSI-MI
Electron Microscopy Data Bank
The Electron Microscopy Data Bank (EMDB) contains experimentally determined three-dimensional maps and associated experimental data and files.
PMID:14643225
http://purl.org/obo/owl/PMID#PMID_14643225
eMDB
glu tag
PSI-MI
glu tag
This peptide is a 314 to 319 amino acids fragment of the middle T antigen of mouse polymavirus. Glu-Glu epitope peptide.
PMID:8077219
http://purl.org/obo/owl/PMID#PMID_8077219
rheology measurement
PSI-MI
Characterization of viscoelastic properties of biomolecule solution is used to infer interactions between molecules.
PMID:18445655
http://purl.org/obo/owl/PMID#PMID_18445655
rheology
fluorescein label
PSI-MI
Fluorescence label used to monitor the presence of a protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fluorescein
fluorescein-5-maleimide label
PSI-MI
fluor-5-maleimide
Fluorescein-5-maleimide is one of the most popular fluorescent dyes for thiol modifications of proteins at cysteine residues that either are intrinsically present or result from reduction of cystines. Unlike iodoacetamides, maleimides do not react with histidines and methionines under physiological conditions.
PMID:18066077
http://purl.org/obo/owl/PMID#PMID_18066077
competitor
PSI-MI
Binds to the bait molecule in competition with other prey molecules, for example at a shared binding site.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
competitor
uniprot taxonomy
PSI-MI
Based on NCBO Taxonomy but adapted for UniProtnhttp://www.uniprot.org/taxonomy/
PMID:18836194
http://purl.org/obo/owl/PMID#PMID_18836194
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
uniprot taxon
detection by mass spectrometry
PSI-MI
ms interact detect
'Study of interactions by an analytical technique based on measurements of mass-to-charge ratio of charged particles in a mass spectrometer.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mass spectrometry study of hydrogen/deuterium exchange
PSI-MI
h1-h2 ms
Mass spectroscopy based measurement of the rate and/or extent of the hydrogen/deuterium exchange.
PMID:18948593
http://purl.org/obo/owl/PMID#PMID_18948593
oxidoreductase activity electron transfer reaction
PSI-MI
redox reaction
An oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
GO:GO:0016491
http://purl.org/obo/owl/GO#GO_GO:0016491
ping
PSI-MI
Combines on-chip in-vitro protein synthesis with an in situ microfluidic affinity assay.
PMID:19098921
http://purl.org/obo/owl/PMID#PMID_19098921
bead aggregation assay
PSI-MI
Binding of proteins bound to beads leads to a measurable aggregation of the beads.
PMID:19114658
http://purl.org/obo/owl/PMID#PMID_19114658
bead aggregation
kinetic conditions
PSI-MI
A brief description (such as temp, pH) of the conditions under which a kinetic measurment has been performed.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
kinetic_conditions
gdp/gtp exchange assay
PSI-MI
Experiments monitoringninteractions of GTP-GDP exchange factors with their cognate GTPases.
PMID:17925023
http://purl.org/obo/owl/PMID#PMID_17925023
guanine nucleotide exchange assay
gtp/gdp exchange
gdp_gtp exchange
trapping mutant
PSI-MI
trap-mutant
Permits the identification of substrates of enzymes by mutating residues, usually in the active site such that the enzyme will bind but not act on its substrate.
PMID:9050838
http://purl.org/obo/owl/PMID#PMID_9050838
chain parent sequence reference
PSI-MI
chain-parent
Reference to the master sequence from which this chain has been derived.
PMID:17925023
http://purl.org/obo/owl/PMID#PMID_17925023
imex secondary
PSI-MI
Deprecated IMEx identifiers should be exchanged in IMEx records and stored as cross reference with this qualifier.
PMID:17925023
http://purl.org/obo/owl/PMID#PMID_17925023
polymerization
PSI-MI
polymerization
Interaction inferred by monitoring polymerization/depolymerization of an interactor
PMID:19081060
http://purl.org/obo/owl/PMID#PMID_19081060
curation quality
PSI-MI
An assessment of the depth and extent to which a paper has been curated
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
curation depth
PSI-MI
Assessment of the depth to which a paper has been curated
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
curation coverage
PSI-MI
Assessment to the extent of interactions captured in this paper
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
full coverage
PSI-MI
All interactions which can be ascribed to an unambiguous identified in this paper have been captured.
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
partial coverage
PSI-MI
Not all interactions which can be ascribed to an unambiguous identified in this paper have been captured.
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
imex curation
PSI-MI
Paper has been curated to full IMEx specifications
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
mimix curation
PSI-MI
Paper has been curated to meet MIMIx specifications
PMID:17687370
http://purl.org/obo/owl/PMID#PMID_17687370
rapid curation
PSI-MI
Minimal interaction data has been extracted from the paper
PMID:17687370
http://purl.org/obo/owl/PMID#PMID_17687370
strep ii tag
PSI-MI
Strep II
The protein of interest is expressed with a StrepII fusion peptide Ser-Ala-Trp-Ser-His-Pro-Gln-Phe-Glu-Lys (SAWSHPQFEK).
PMID:17571060
http://purl.org/obo/owl/PMID#PMID_17571060
Strep (II)
interactome parallel affinity capture
PSI-MI
ipac
A specific pull down method where the protein of interest (bait) is endogenously expressed with at least two affinity tags (GFP, FLAG or others). The bait is purified in parallel using different purification protocols in contrast to tandem affinity purification (TAP) (publication currently in press).
PMID:14681455
http://purl.org/obo/owl/PMID#PMID_14681455
infrared spectroscopy
PSI-MI
ir spectrometry
Subset of spectroscopy that deals with the infrared region of the electromagnetic spectrum.
PMID:15212548
http://purl.org/obo/owl/PMID#PMID_15212548
2d-infrared spectrometry
PSI-MI
2d-ir
Two-dimensional infrared correlation spectroscopy analysis is the application of 2D correlation analysis on infrared spectra. 2D IR spectroscopy probes molecular structures by means of vibrational frequencies, couplings, and transition dipole angles.
PMID:17502604
http://purl.org/obo/owl/PMID#PMID_17502604
ultraviolet-visible spectroscopy
PSI-MI
ultraviolet-visible spectrophotometry
uv-vis
UV/Vis
Ultraviolet-visible spectroscopy or ultraviolet-visible spectrophotometry (UV-Vis or UV/Vis) involves the spectroscopy of photons in the UV-visible region. This means it uses light in the visible and adjacent (near ultraviolet (UV) and near infrared (NIR)) ranges.
PMID:18799738
http://purl.org/obo/owl/PMID#PMID_18799738
chembl
PSI-MI
ChEMBL focuses on mapping the interactions of small molecules binding to their macromolecular targets.
PMID:19194660
http://purl.org/obo/owl/PMID#PMID_19194660
id-validation-regexp:"[0-9]+"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[0-9]+"
search-url:http://www.ebi.ac.uk/chembldb/index.php/compound/inspect/$(ac)
http://purl.org/obo/owl/search-url#search-url_http://www.ebi.ac.uk/chembldb/index.php/compound/inspect/$(ac)
biosensor
PSI-MI
A biosensor is a device for the detection of an analyte that combines a biological component with a physicochemical detector component
PMID:10872504
http://purl.org/obo/owl/PMID#PMID_10872504
bio-layer interferometry
PSI-MI
BLI is an optical analytical technique that analyzes the interference pattern of white light reflected from two surfaces: a layer of immobilized protein on the biosensor tip, and an internal reference layer
PMID:19561609
http://purl.org/obo/owl/PMID#PMID_19561609
bli
inchi key
PSI-MI
inchi key
InChIKeys consist of 14 characters resulting from a hash of the connectivity information of the InChI, followed by a hyphen, followed by 9 characters resulting from a hash of the remaining layers of the InChI, followed by a single character indication the version of InChI used, another hyphen, followed by single checksum character
PMID:15889163
http://purl.org/obo/owl/PMID#PMID_15889163
phosphopantetheinylation
PSI-MI
The posttranslational phosphopantetheinylation of peptidyl-serine to form peptidyl-O-phosphopantetheine-L-serine.
PMID:19679086
http://purl.org/obo/owl/PMID#PMID_19679086
p_patetheinylation
phosphopantetheinylase assay
PSI-MI
Assay of the posttranslational phosphopantetheinylation of peptidyl-serine to form peptidyl-O-phosphopantetheine-L-serine.
PMID:19346479
http://purl.org/obo/owl/PMID#PMID_19346479
p_pantethinyl assay
phosphopantetheinylation
imex source
PSI-MI
Databases that contain curated experimental interaction data and exchanging it with other IMEx databases.
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
innatedb
PSI-MI
Human and mouse experimentally verified interactions and pathways involved in innate immunity.
PMID:18766178
http://purl.org/obo/owl/PMID#PMID_18766178
fc-igg tag
PSI-MI
A fusion protein tag consisting of a portion of the constant region of human IgG1.
PMID:11757069
http://purl.org/obo/owl/PMID#PMID_11757069
total internal reflection fluorescence spectroscopy
PSI-MI
tirfs
Used to study surface-associated interactions at the molecular level. In this method, the evanescent field from an internally reflected excitation source selectively excites fluorescent molecules on or near a surface.
PMID:9013655
http://purl.org/obo/owl/PMID#PMID_9013655
no-imex-export
PSI-MI
Prevents export of experiment and associated interactions to IMEx
PMID:17893861
http://purl.org/obo/owl/PMID#PMID_17893861
author-name
PSI-MI
Author given name for a participant, not commonly found in source databases.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
oxidoreductase assay
PSI-MI
Catalysis of oxido-reductions. The substrate oxidized is regarded as the hydrogen or electron donor. The classification is based on 'donor:acceptor oxidoreductase'. The common name is 'dehydrogenase', wherever this is possible; as an alternative, 'acceptor reductase' can be used. 'Oxidase' is used only where O2 is an acceptor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
oxidoreduct assay
tag visualisation by enzyme assay
PSI-MI
The protein is expressed as a hybrid protein fused to a tag containing an enzyme activity e.g. peroxidase. Subsequence observation or measurement of enzyme activity is used to identify the presence of the molecule in an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tag enzyme assay
XX:<new_dbxref>
http://purl.org/obo/owl/XX#XX_<new_dbxref>
tag visualisation by peroxidase activity
PSI-MI
tag perox activity
The protein is expressed as a hybrid protein fused to a tag containing a peroxidase activity. Subsequence observation or measurement of peroxidase activity is used to identify the presence of the molecule in an interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
electrophoretic mobility-based method
PSI-MI
electrophoresis
Any method which relies on the motion of particles relative to a matrix under the influence of an electrical field.
PMID:19517512
http://purl.org/obo/owl/PMID#PMID_19517512
gemma
PSI-MI
GEMMA is a method to study protein complexes in solution: a diluted protein sample is transmittedninto the gas phase by a charged reduced electrospray process. The generated particles, eachncontaining one protein molecule with a +1 charge, are separated according to size in a differentialnmobility analyzer and subsequently quantified by a particle counter. In contrast to mass spectrometry,nthis method is run at atmospheric pressure and measures the diameter of the particle rather than the mass.
PMID:16861739
http://purl.org/obo/owl/PMID#PMID_16861739
deaminase assay
PSI-MI
deamination
The measurement of the removal of an amine group from a molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
deamination reaction
PSI-MI
deamination
The removal of an amine group from a molecule.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
nucleic acid strand elongation reaction
PSI-MI
strand elongation
The lengthening of a strand of a nucleic acid by the systematic addition of bases by a polymerase.
PMID:159156
http://purl.org/obo/owl/PMID#PMID_159156
rna strand elongation
PSI-MI
rna elongation
The process by which an RNA strand is synthesized from template DNA by the action of polymerases, which add nucleotides to the 3' end of the nascent RNA strand.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
strep tag
PSI-MI
Synthetic peptide consisting of 8 amino acids Trp-Ser-His-Pro-Gln-Phe-Glu-Lys (WSHPQFEK).
PMID:17571060
http://purl.org/obo/owl/PMID#PMID_17571060
amidase assay
PSI-MI
The measurement of the addition of an amine group to a molecule.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
amidation
cleavage assay
PSI-MI
cleavage
The cleavage of a biomolecule either into its component parts or sub-parts.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
lipid cleavage assay
PSI-MI
The cleavage of a lipid molecule from a larger biomolecule.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
defarnesylase assay
PSI-MI
Measures the removal of S-farnesyl-L-cysteined, which is cleaved and returns a C residue.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
defarnesylation assay
degeranylase assay
PSI-MI
degeranylation assay
Measures the removal of S-geranylgeranyl-L-cysteine, which is cleaved and returns a C residue.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
demyristoylase assay
PSI-MI
measures the removal of N6-myristoyl-L-lysine, which is cleaved and returns a K residue.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
demyristoylation assay
depalmitoylase assay
PSI-MI
depalmitoylation assay
Measures the removal of S-palmitoyl-L-cysteine, N6-palmitoyl-L-lysine, O-palmitoyl-L-threonine or O-palmitoyl-L-serine, which are cleaved and return C,K,T or S residues.
PMID:<new_dbxref>14760721
http://purl.org/obo/owl/PMID#PMID_<new_dbxref>14760721
deformylase assay
PSI-MI
deformylation
deformylase reaction
Measures the removal of N6-formyl-L-lysine, which is cleaved and returns a K residue.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
ubiquitinase assay
PSI-MI
ubiquitinase assay
ubiquitination
Measures the reversible reaction that creates a covalent bond between a C-terminus G of ubiquitin and a K residue of the target.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
deubiquitinase assay
PSI-MI
deubiquinase assay
deubiquitination
deubiquitinase assay
Measures the cleavage of the G-K bond and release of ubiquitin or ubiquitin like proteins.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
formylase assay
PSI-MI
Measurement of the reaction that can affect K or G residues. Reside is functionalised with a formyl group.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
hydroxylase assay
PSI-MI
Measurement of the irreversible introduction of a hydroxyl group that can affect K,P,Y or R residues.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
lipidase assay
PSI-MI
lipidation
The covalent binding of a lipid group to a peptide chain.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
myristoylase assay
PSI-MI
myristoylation
Measurement of the irreversible covalent addition of a myristoyl group via an amide bond to the alpha-amino group of an amino acid.
PMID:14707621
http://purl.org/obo/owl/PMID#PMID_14707621
geranylgeranylase assay
PSI-MI
Measurement of the attachment of one or two 20-carbon lipophilic geranylgeranyl isoprene units from geranylgeranyl diphosphate to one or more cysteine residue(s).
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
geranylgeranylation
geranylgeranylase
palmitoylase assay
PSI-MI
Measurement of the covalent attachment of palmitic acid to a protein.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
myristoylation
palmitoylase assay
adp ribosylase assay
PSI-MI
Measurement of the addition of one or more ADP-ribose moieties to molecules.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
adp ribosylation
adp ribosylase
deglycosylase assay
PSI-MI
Measurement of the removal of a glycosyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological polymer.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
glycosylase assay
PSI-MI
glycosylation
Measurement of the covalent attachment of a glycosyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological polymer.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
sumoylase assay
PSI-MI
sumoylation
Measurement of the reversible reaction that creates a covalent bond between a C-terminus G of an ubiquitine like sumo protein and a K residue of the target.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
desumoylase assay
PSI-MI
desumylation
Measurement of the reaction that breaks a covalent bond between a C-terminus G of an ubiquitine like sumo protein and a K residue of the target.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
neddylase assay
PSI-MI
neddylation
Measurement of a reversible reaction that create a covalent bond between a Glycine residue of an ubiquitine like NEDD8 protein and a lysine residue of the target.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
deneddylase assay
PSI-MI
deneddylation
Measurement of the reaction that breaks a covalent bond between a Glycine residue of an ubiquitine like NEDD8 protein and a lysine residue of the target.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
sbp
PSI-MI
38 amino acid (MDEKTTGWRGGHWEGLAGELEQLRARLEHHPQGQREP) Streptavidin binding peptide.
PMID:117222181
http://purl.org/obo/owl/PMID#PMID_117222181
steptavidin binding peptide
ensemblgenomes
PSI-MI
Genome browser complementary to Ensembl which extends the search space across a broader taxonomic range.nhttp://www.ensemblgenomes.org
PMID:19884133
http://purl.org/obo/owl/PMID#PMID_19884133
string
PSI-MI
STRING is a database and web resource dedicated to protein interactions, including both physical and functional interactions. It weights and integrates information from numerous sources, including experimental repositories, computational prediction methods and public text collections, thus acting as a meta-database that maps all interaction evidence onto a common set of genomes and proteins.
PMID:18940858
http://purl.org/obo/owl/PMID#PMID_18940858
dictybase
PSI-MI
dictyBase (http://dictybase.org) is the model organism database for Dictyostelium discoideum. It houses the complete genome sequence, ESTs and the entire body of literature relevant to Dictyostelium. This information is curated to provide accurate gene models and functional annotations, with the goal of fully annotating the genome.
id-validation-regexp:"DDB_G(0-9){7}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"DDB_G(0-9){7}"
fluorescence recovery after photobleaching
PSI-MI
Slow rate of FRAP recovery when molecule is bound to another compared to inert, non-binding molecule taken as a measure of an interaction.
PMID:17711354
http://purl.org/obo/owl/PMID#PMID_17711354
PMID:15695095
http://purl.org/obo/owl/PMID#PMID_15695095
frap
<new synonym>
rna immunoprecipitation
PSI-MI
Proteins are crosslinked to nucleic acids, for example by the addition of formaldehyde. RNA sequences that cross-link with a given protein are isolated by immunoprecipitation of the protein, and reversal of the cross-linking permits recovery and quantitative analysis of the immunoprecipitated RNA by reverse transcription PCR.
PMID:18265380
http://purl.org/obo/owl/PMID#PMID_18265380
rna-ip
rip
deltamass
PSI-MI
A database of protein post translational modifications. www.abrf.org/index.cfm/dm.home
PMID:8322616
http://purl.org/obo/owl/PMID#PMID_8322616
protein phosphatase assay
PSI-MI
Measures the catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate.
hilyte fluor 488
PSI-MI
hilyte 488
A carbonyl-reactive fluorescent labelling dye.
PMID:19795889
http://purl.org/obo/owl/PMID#PMID_19795889
qx 520
PSI-MI
Nonfluorescent dye, act as a quencher in FRET assays.
field flow fractionation
PSI-MI
A separation technique where a field is applied to a mixture perpendicular to the mixtures flow. The filed can be graviational, centrifugal, magnetic or a cross flow of fluids.
PMID:959835
http://purl.org/obo/owl/PMID#PMID_959835
luminogreen
PSI-MI
A nonfluorescent, biarsenical derivative of fluorescein. LumioGreen is supplied pre-complexed to EDT, is membrane-permeable, and readily enters the cell.
PMID:19935683
http://purl.org/obo/owl/PMID#PMID_19935683
scanning electron microscopy
PSI-MI
A type of electron microscope that images the sample surface by scanning it with a high-energy beam of electrons in a raster scan pattern. The electrons interact with the atoms that make up the sample producing signals that contain information about the sample's surface topography, composition and other properties such as electrical conductivity.
PMID:20463740
http://purl.org/obo/owl/PMID#PMID_20463740
sem
unimod
PSI-MI
A database of protein modifications for mass spectrometry. www.unimod.org
PMID:15174123
http://purl.org/obo/owl/PMID#PMID_15174123
diphtamidase assay
PSI-MI
Measurement of a modification that converts an L-histidine residue to diphthamide.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
diphtamidase
diphtamidation reaction
PSI-MI
diphthamidation
A modification that converts an L-histidine residue to diphthamide.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
modified chromatin immunoprecipitation
PSI-MI
mch-ip
Chromatin-bound protein networks isolated using magnetic beads coated with antibodies.
PMID:19106085
http://purl.org/obo/owl/PMID#PMID_19106085
proteomics of isolated chromatin segments
PSI-MI
pich
Specific nucleic acid probes are fixed to solid supports (e.g. beads) and act as affinity probes. The molecules associated with the nucleic acid probes can then be isolated and identified.
PMID:19135898
http://purl.org/obo/owl/PMID#PMID_19135898
excimer fluorescence
PSI-MI
Excimer (excited-dimer) fluorescence is produced by complexes formed by two molecules, at least one of which is in an excited state. It is characterized by a lower energy (i.e. red shift) than fluorescence of a single, non-interacting molecule.
PMID:18480256
http://purl.org/obo/owl/PMID#PMID_18480256
excimer fluoresc
protein folding/unfolding
PSI-MI
A change in the rate of protein folding/unfolding is taken as a measure of chaperone protein binding.
PMID:19940245
http://purl.org/obo/owl/PMID#PMID_19940245
protein folding
atto 488
PSI-MI
atto488
Fluorescent tag - maleimide couples to thiols.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
atto 488 maleimide
atto 550
PSI-MI
Fluorescent tag - maleimide couples to thiols.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
atto550
nuclease assay
PSI-MI
Measures the cleavage of phosphodiesterase bonds between the nucleotide subunits of nucleic acids.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
deoxyribonuclease assay
PSI-MI
Measures the catalysis of the hydrolysis of phosphodiester bonds in chains of DNA.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
deoxyribonuclease
nucleotide exchange assay
PSI-MI
Experiments monitoringninteractions of nucleotide exchange factors with their cognate nucleotidases.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
nucleotide exchange
Split renilla luciferase complementation
PSI-MI
renilla luciferase
The N-terminal portion of synthetic renilla luciferase (hrluc) is attached to one protein through the linker peptide (GGGS)2 and C-terminal portion of synthetic renilla luciferase is connected to the second protein through the linker (GGGGS)2. Interaction of the 2 proteins recovers hrluc activity and produces light.
PMID:22070901
http://purl.org/obo/owl/PMID#PMID_22070901
PMID:12705589
http://purl.org/obo/owl/PMID#PMID_12705589
silicon nanowire field-effect transistor
PSI-MI
nanowire transistor
Measures selective electrical response to molecules binding to the immobilised bait.
PMID:20080536
http://purl.org/obo/owl/PMID#PMID_20080536
c-terminal range
PSI-MI
The C-terminal region of a sequence, exact coordinates not available.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
<new synonym>
c-term range
n-terminal range
PSI-MI
n-term range
The N-terminal region of a sequence, exact coordinates not available.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
synonym
PSI-MI
Alternative name or descriptor for an entity.
PMID:14681455
http://purl.org/obo/owl/PMID#PMID_14681455
pubmed central
PSI-MI
PubMed Central is the US National Institute of Health free digital archive of biomedical and life science journals.
PMID:12519941
http://purl.org/obo/owl/PMID#PMID_12519941
<pmc
flannotator
PSI-MI
id-validation-regexp:"CPTO-[0-9]{6}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"CPTO-[0-9]{6}"
A repository for collecting, storing and and searching the annotation of gene or protein expression patterns in Drosophila melongaster. CPTI (Cambridge Protein Trap Identifier)
PMID:19126575
http://purl.org/obo/owl/PMID#PMID_19126575
rice genome annotation project
PSI-MI
RGAP
NSF funded annotation project.
PMID:17145706
http://purl.org/obo/owl/PMID#PMID_17145706
curation content
PSI-MI
Indicates source, depth and standards by which an entry has been added to a database.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interacting molecules
PSI-MI
Defines an interaction by the type of binary molecule pairs it can generates.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein-protein
PSI-MI
Interaction between a protein or peptide and a corresponding protein or peptide.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
smallmolecule-protein
PSI-MI
Interaction between a small molecule and a corresponding protein or peptide.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nucleicacid-protein
PSI-MI
Interaction between a nucleic acid and a corresponding protein or peptide.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
interaction representation
PSI-MI
Provides an indication of the level of post-processing of experimental data relating to specific binary pairs
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
evidence
PSI-MI
Binary pair is defined by a single piece of experimental evidence.
PMID:<new_dbxref>14755292
http://purl.org/obo/owl/PMID#PMID_<new_dbxref>14755292
clustered
PSI-MI
Binary pair is defined by multiple pieces of experimental evidence which have been clustered together.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
data source
PSI-MI
The source of the data entered into the database.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimentally-observed
PSI-MI
Data has been directly curated into the database from the paper describing the experimental evidence or by direct submission by the experimenter.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
internally-curated
PSI-MI
Data has been directly curated into this database from the paper describing the experimental evidence
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
text-mining
PSI-MI
The data has been entered into the database following extraction from the literature by a computational process.
PMID:<new_dbxref>14755292
http://purl.org/obo/owl/PMID#PMID_<new_dbxref>14755292
predicted
PSI-MI
The interaction has been predicted using a specific algorithm.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
imported
PSI-MI
The data has been imported into the database form an external resource.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
complex expansion
PSI-MI
The method by which complex n-ary data is expanded into binary data. This may be performed manually on data input, or computationally on data export.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
spoke expansion
PSI-MI
Complex n-ary data has been expanded to binary using the spoke model. This assumes that all molecules in the complex interact with a single designated molecule, usually the bait.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
matrix expansion
PSI-MI
Complex n-ary data has been expanded to binary using the spoke model. This assumes that all molecules in the complex interact with each other.
PMID:<new_dbxref>14755292
http://purl.org/obo/owl/PMID#PMID_<new_dbxref>14755292
bipartite expansion
PSI-MI
Complex n-ary data has been expanded to binary using the bipartite model. This assumes that all molecules in the complex interact with a single externally designated entity.
PMID:<new_dbxref>14755292
http://purl.org/obo/owl/PMID#PMID_<new_dbxref>14755292
consensuspathdb
PSI-MI
ConsensusPathDB-human integrates functional interaction networks including complex protein-protein, metabolic, signaling and gene regulatory interaction networks in Homo sapiens. Data originate from currently 20 public resources for functional interactions (listed below), as well as interactions that we have curated from literature. Data are integrated in a complementary manner and redundancies are avoided.
PMID:21071422
http://purl.org/obo/owl/PMID#PMID_21071422
interaction confidence
PSI-MI
confidence
A method used to derive a numerical or empirical measure of confidence in a particular interaction, or in the identification of the participants in an interaction.
PMID:19420069
http://purl.org/obo/owl/PMID#PMID_19420069
scoring system
replication-based confidence
PSI-MI
replication-based scoring system
replication score
Methods based on counting the number of replicates in which an interaction has been observed.
PMID:19420069
http://purl.org/obo/owl/PMID#PMID_19420069
structure-based confidence
PSI-MI
structure score
structure-based scoring system
Confidence score based on similarity to interacting molecules of known structure, presence of known interacting domains etc.
PMID:15044803
http://purl.org/obo/owl/PMID#PMID_15044803
function-based confidence
PSI-MI
function score
function-based scoring system
Confidence in an interaction is based on shared functionality of interacting molecules e.g. co-occurrence of GO function terms.
PMID:21443973
http://purl.org/obo/owl/PMID#PMID_21443973
location-based confidence
PSI-MI
Confidence in an interaction is based on shared functionality of interacting molecules e.g. co-occurrence of GO component terms or co-occurrence in the same tissues.
PMID:18624398
http://purl.org/obo/owl/PMID#PMID_18624398
location-based scoring system
colocation score
network-based confidence
PSI-MI
Network-based confidence scoring systems assign confidence based on multiple parameters, potentially shared by interacting proteins e.g. interaction partners, topological parameters, comparisonnwith genetic interactions.
PMID:19010802
http://purl.org/obo/owl/PMID#PMID_19010802
network score
network-based scoring system
standard-based confidence
PSI-MI
Confidence scoring system based on comparison to a 'gold standard' set of known interacting molecules.
PMID:16554755
http://purl.org/obo/owl/PMID#PMID_16554755
standard score
standard-based scoring system
gold standard
literature-based confidence
PSI-MI
Confidence in an interaction is based on co-occurrence of an interacting pair or molecules in the same article, or sentence within an article, usually identified by text-mining.
PMID:18005433
http://purl.org/obo/owl/PMID#PMID_18005433
literature-based scoring system
literature score
method-based confidence
PSI-MI
The confidence of an interaction is assessed on the number of different methods by which it is observed.
PMID:19420069
http://purl.org/obo/owl/PMID#PMID_19420069
method-based scoring system
method score
statistical-based confidence
PSI-MI
Confidence in an interaction is based on a measure of the probability of these molecules interacting.
PMID:19420069
http://purl.org/obo/owl/PMID#PMID_19420069
statistical-based scoring system
statistical score
rgs-his tag
PSI-MI
rgs-his
The protein of interest is expressed as a fusion to a RGS(His)n tag.
PMID:19223579
http://purl.org/obo/owl/PMID#PMID_19223579
beilstein
PSI-MI
The Beilstein database is in the field of organic chemistry, in which compounds are uniquely identified by their Beilstein Registry Number.
PMID:ID:11604014
http://purl.org/obo/owl/PMID#PMID_ID:11604014
beilstein
einecs
PSI-MI
einecs
European Inventory of Existing Commercial Chemical Substances
The EINECS database provides general information such as CAS number, EINECS number, Substance Name and Chemical Formula for 100,204 chemical substances. Where available each compound entry is linked to risk and safety phrases and IUCLID and OECD chemical data sheets.
PMID:17125194
http://purl.org/obo/owl/PMID#PMID_17125194
merck index
PSI-MI
Comprehensive information on chemicals, drugs, and biologicals.
PMID:17832605
http://purl.org/obo/owl/PMID#PMID_17832605
merck index
plantgdb
PSI-MI
PlantGDB develops plant species-specific EST and GSS databases, to provide web-accessible tools and inter-species query capabilities, and to provide genome browsing and annotation capabilities.
PMID:18063570
http://purl.org/obo/owl/PMID#PMID_18063570
plantgdb
ratmap
PSI-MI
The rat genome database RatMap (http://ratmap.org or http://ratmap.gen.gu.se) has been one of the main resources for rat genome information since 1994. The database is maintained by CMB Genetics at Gothenburg University in Sweden and provides information on rat genes, polymorphic rat DNA-markers and rat quantitative trait loci (QTLs), all curated at RatMap.
PMID:15608244
http://purl.org/obo/owl/PMID#PMID_15608244
ratmap
tair
PSI-MI
The Arabidopsis Information Resource (TAIR) maintains a database of genetic and molecular biology data for the model higher plant Arabidopsis thaliana . Data available from TAIR includes the complete genome sequence along with gene structure, gene product information, metabolism, gene expression, DNA and seed stocks, genome maps, genetic and physical markers, publications, and information about the Arabidopsis research community.
PMID:20521243
http://purl.org/obo/owl/PMID#PMID_20521243
tair
The Arabidopsis Information Resource
tigr/jcvi
PSI-MI
The J. Craig Venter Institute was formed in October 2006 through the merger of several affiliated and legacy organizations including The Institute for Genomic Research (TIGR).
PMID:18287690
http://purl.org/obo/owl/PMID#PMID_18287690
J. Craig Venter Institute
The Institute for Genomic Research
tigr/jcvi
zfin
PSI-MI
Extensive information on Danio rerio, including genomics databases, developmental stages, publications and molecular tools.
PMID:21036866
http://purl.org/obo/owl/PMID#PMID_21036866
The Zebrafish Model Organism Database
zfin
cog
PSI-MI
Clusters of Orthologous Groups
cogg
Clusters of Orthologous Groups of proteins (COGs) were delineated by comparing protein sequences encoded in complete genomes, representing major phylogenetic lineages. Each COG consists of individual proteins or groups of paralogs from at least 3 lineages and thus corresponds to an ancient conserved domain.
PMID:11125040
http://purl.org/obo/owl/PMID#PMID_11125040
photon donor
PSI-MI
Any molecule that is able to transfer a photon to another chemical species.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
photon donor
photon acceptor
PSI-MI
Molecule to which a photon may be transferred from an photon donor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
photon acceptor
equilibrium dialysis
PSI-MI
equilib. dialysis
Two chambers are separated by a dialysis membrane. The molecular weight cut offn(MWCO) of this membrane isnchosen such that it will retain thenreceptor component of the samplen(the element which will bindnthe ligand).nA known concentration and volumenof ligand is placed into one ofnthe chambers. The ligand is smallnenough to pass freely through thenmembrane.nA known concentration of receptornis then placed in the remainingnchamber in an equivalent volumento that placed in the first chamber.nAs the ligand diffuses across thenmembrane some of it will bind tonthe receptor and some will remainnfree in solution. The higher thenaffinity of the interaction, the highernthe concentration of ligand thatnwill be bound at any time.
PMID:21609686
http://purl.org/obo/owl/PMID#PMID_21609686
monoclonal antibody blockade
PSI-MI
Method to block a binding site on a molecule, such as a protein, using a monoclonal antibody to test that the binding site is involved in an interaction with another molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mab blockade
phenotype-based detection assay
PSI-MI
phenotype-based
Assays that are used to determine interactions by monitoring, for example activation of a certain pathway when screening for inhibitors of a given receptor.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nuclear translocation assay
PSI-MI
Method to detect interaction by inducing nuclear localization of one participant, which would then pull an interacting participant along with it into the nucleus. As both participants are labeled, the difference in nuclear localization between the induced and non-induced states provides an indication of the interaction between the two molecules.
PMID:21684252
http://purl.org/obo/owl/PMID#PMID_21684252
nuclear translocation
bimane label
PSI-MI
bimane
Bromobimanes are low molecular weight non-fluorescent alkyl halides which react with thiol groups to produce highly fluorescent derivatives. The bimane labels, monobromobimane, dibromobimane, and monobromotrimethylammoniobimane, are derivatives of syn-9,10-dioxabimane:1,5-diazabicyclo[3.3.0]octa-3,6-diene-2,8-dione.
PMID:7378449
http://purl.org/obo/owl/PMID#PMID_7378449
publication title
PSI-MI
title
Title of the publication.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
atto label
PSI-MI
atto label
Fluorescent dyes - spectral range 500 to 700 nm.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bibliographic attribute name
PSI-MI
publication attribute
bib attribute
Attributes specific to the publication.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genome databases
PSI-MI
genome databases
Databases which are the responsible for the maintenance and subsequent annotation of one or more genomic sequences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
hgnc
PSI-MI
HGNC is the nomenclature committee responsible for the naming of human genes.
PMID:20929869
http://purl.org/obo/owl/PMID#PMID_20929869
hgnc
Human Genome Nomenclature Committee
protein sequence databases
PSI-MI
Databases dedicated to the collection and annotation of protein sequences.
PMID:21447597
http://purl.org/obo/owl/PMID#PMID_21447597
protein seq db
uniprot
PSI-MI
UniProt is a centralized repository of protein sequences with comprehensive coverage and a systematic approach to protein annotation, incorporating, interpreting, integrating and standardizing data from numerous sources and is the most comprehensive catalog of protein sequences and functional annotation.
PMID:21051339
http://purl.org/obo/owl/PMID#PMID_21051339
uniprot
uniprot/swiss-prot
PSI-MI
id-validation-regexp:"[A-Z][0-9][A-Z0-9]{3}[0-9]|[A-Z][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[A-Z][0-9][A-Z0-9]{3}[0-9]|[A-Z][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
UniProt (Universal Protein Resource) is the world's most comprehensive catalogue of information on proteins. It is a central repository of protein sequence and function created by joining the information contained in Swiss-Prot, TrEMBL, and PIR.nhttp://www.uniprot.org. UniProtKB/Swiss-Prot is manually curated which means that the information in each entry is annotated and reviewed by a curator
PMID:14681372
http://purl.org/obo/owl/PMID#PMID_14681372
PMID:21447597
http://purl.org/obo/owl/PMID#PMID_21447597
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
swiss-prot
UniProt
uniprot/trembl
PSI-MI
trembl
UniProt (Universal Protein Resource) is the world's most comprehensive catalogue of information on proteins. It is a central repository of protein sequence and function created by joining the information contained in Swiss-Prot, TrEMBL, and PIR.nhttp://www.uniprot.org. The records in UniProtKB/TrEMBL are automatically generated and are enriched with automatic annotation and classification.
PMID:14681372
http://purl.org/obo/owl/PMID#PMID_14681372
PMID:21447597
http://purl.org/obo/owl/PMID#PMID_21447597
search-url:NULL
http://purl.org/obo/owl/search-url#search-url_NULL
id-validation-regexp:"[A-Z][0-9][A-Z0-9]{3}[0-9]|[A-Z][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
http://purl.org/obo/owl/id-validation-regexp#id-validation-regexp_"[A-Z][0-9][A-Z0-9]{3}[0-9]|[A-Z][0-9][A-Z0-9]{3}[0-9]-[0-9]+|[A-Z][0-9][A-Z0-9]{3}[0-9]-PRO_[0-9]{10}"
UniProt
bioactive entity
PSI-MI
bioactive entity
Molecules showing activity in a living system but not encoded by a genomic sequence.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
standard inchi key
PSI-MI
The Standard InChIKey has five distinct components, a 14-character hash of the basic (Mobile-H) InChI layer, an 8-character hash of the remaining layers (except for the /p segment, which accounts for added or removed protons: it is not hashed at all; the number of protons is encoded at the end of the standard InChIKey.) , a 1 flag character, a 1 version character and the last character is a [de]protonation indicator. The overall length of InChIKey is fixed at 27 characters, including separators (dashes)
PMC:2867152
http://purl.org/obo/owl/PMC#PMC_2867152
standard inchikey
standard inchi key
mapped-identity
PSI-MI
Sequence has been computationally remapped following removal or update of the original sequence in the underlying sequence database.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
mapped-identity
solution state nmr
PSI-MI
NMR solution state analysis provides useful data regarding the type, quantity and arrangement of different atoms in chemical systems, liquids and solids. Samples are dissolved in deuterated solvents and spectra consist of a series of very sharpntransitions, due to averaging of anisotropic NMR interactionsnby rapid random tumbling. Solution-state NMR only requires that the molecule be soluble at sufficient concentration for data collection, but becomes increasingly difficult for biomolecules over 30 kDa so that a practical size limitation is placed on full structure determinations.
PMID:20951674
http://purl.org/obo/owl/PMID#PMID_20951674
soultion nmr
solution state nmr
solid state nmr
PSI-MI
Solid-state NMR (ssNMR) does not require that the sample be soluble or form a crystal, and the approach can be used to study molecules larger than 100 kD. Solid-state NMR spectra are very broad, as the fullneffects of anisotropic or orientation-dependent interactions are observed in the spectrum.
PMID:20951674
http://purl.org/obo/owl/PMID#PMID_20951674
solid state nmr
ssnmr
biocyc
PSI-MI
biocyc
BioCyc is a collection of Pathway/Genome Databases. Each database in the BioCyc collection describes the genome and metabolic pathways of a single organism. (http://biocyc.org/).
PMID:19850718
http://purl.org/obo/owl/PMID#PMID_19850718
pathways database
PSI-MI
pathways db
Databases which primarily exist to display biomolecular information in structured pathways. Interactions data can be inferred from the published pathways.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pid
PSI-MI
pathways interaction database
pid
Curated collection of information about known biomolecular interactions and key cellular processes assembled into signaling pathways. It is a collaborative project between the US National Cancer Institute (NCI) and Nature Publishing Group (NPG), and is an open access online resource (http://pid.nci.nih.gov/).
PMID:18832364
http://purl.org/obo/owl/PMID#PMID_18832364
biocarta
PSI-MI
biocarta
BioCarta, whose core business is in assays and reagents, has also developed a collection of diagrams representing molecular and cellular signal transduction pathways.
PMID:14760721
http://purl.org/obo/owl/PMID#PMID_14760721
gene database
PSI-MI
Primarily nomenclature/cross-reference databases, used by curators to establish a link between a gene and protein ID. In some cases, database records do not contain actual sequence but point to loci on specific reference genomes.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
gene dbs
predicted interaction
PSI-MI
Interaction has been predicted by either interologue mapping, by an algorithm or by a computational method.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
predicted
two hybrid bait or prey pooling approach
PSI-MI
Individual baits are mated against pools of preys, or pools of baits are mated against individual preys. This approach required cloning baits and preys into both two-hybrid vectors, followed by pooling sets of transformants. The positive double hybrid clones are the interacting partners.
PMID:20946815
http://purl.org/obo/owl/PMID#PMID_20946815
PMID:11283351
http://purl.org/obo/owl/PMID#PMID_11283351
two hybrid prey pooling approach
PSI-MI
Individual baits are mated against pools of preys. This approach required cloning baits and preys into both two-hybrid vectors, followed by pooling sets of transformants. The positive double hybrid clones are the interacting partners.
PMID:20946815
http://purl.org/obo/owl/PMID#PMID_20946815
two hybrid bait and prey pooling approach
PSI-MI
def
PMID:10655498
http://purl.org/obo/owl/PMID#PMID_10655498
virhostnet
PSI-MI
A database of viral-host interactions.
PMID:18984613
http://purl.org/obo/owl/PMID#PMID_18984613
spike
PSI-MI
Signalling Pathways Integrated Knowledge Engine
SPIKE
PMID:21097778
http://purl.org/obo/owl/PMID#PMID_21097778
genemania
PSI-MI
GeneMANIA predicts interactions based on multiple evidences including physical and genetic interactions, pathways, co-localisation, co-expression and protein domain similarity.
PMID:20576703
http://purl.org/obo/owl/PMID#PMID_20576703
topfind
PSI-MI
TopFIND provides information on protein N- and C-termini. Information of proteases and their substrates is provided.
PMID:21822272
http://purl.org/obo/owl/PMID#PMID_21822272
Termini-oriented protein function inferred database
enhanced yellow fluorescent protein tag
PSI-MI
eyfp
A variation of yellow fluorescent protein derived from eGFP.
PMID:10929120
http://purl.org/obo/owl/PMID#PMID_10929120
nYFP
PSI-MI
n-terminal fragment of yellow fluorescent protein used as a tag in bimolecular fluorescence complementation (BiFC).
PMID:11983170
http://purl.org/obo/owl/PMID#PMID_11983170
N-terminal part of YFP
cYFP
PSI-MI
c-terminal fragment of yellow fluorescent protein used as a tag in bimolecular fluorescence complementation (BiFC).
PMID:11983170
http://purl.org/obo/owl/PMID#PMID_11983170
C-terminal part of YFP
ceYFP
PSI-MI
c-terminal fragment of enhanced yellow fluorescent protein used as a tag in bimolecular fluorescence complementation (BiFC).
PMID:11983170
http://purl.org/obo/owl/PMID#PMID_11983170
C-terminal part of EYFP
neYFP
PSI-MI
N-terminal part of EYFP
n-terminal fragment of enhanced yellow fluorescent protein used as a tag in bimolecular fluorescence complementation (BiFC).
PMID:11983170
http://purl.org/obo/owl/PMID#PMID_11983170
bindingdb
PSI-MI
BindingDB is a web-accessible public database of experimentally determined protein-ligand binding affinities for drug discovery. http://BindingDB.org
PMID:17145705
http://purl.org/obo/owl/PMID#PMID_17145705
PMID:11836221
http://purl.org/obo/owl/PMID#PMID_11836221
PMID:11987162
http://purl.org/obo/owl/PMID#PMID_11987162
PMID:11812264
http://purl.org/obo/owl/PMID#PMID_11812264
pathwaycommons
PSI-MI
Allows the user to browse and search pathways across multiple public pathway databases.nhttp://www.pathwaycommons.org
PMID:21071392
http://purl.org/obo/owl/PMID#PMID_21071392
Pathway Commons
direct binding region
Should normally be used with X-ray crystallography or NMR data.
PSI-MI
direct binding
The defined region of protein which makes physical contact with the interacting partner.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
self interaction
The corresponding experimental role will be self/putative self. Not to be used for autocatalysis, when the additional biological role self/putative self will supply this information.
PSI-MI
A region of a molecule which is involved in an inter-molecular interaction.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
putative self interaction
The corresponding experimental role should be self/putative self. Not to be used for autocatalysis, when the additional biological role self/putative self will supply this information.
PSI-MI
A region of a molecule which is putatively involved in an inter-molecular interaction.
PMID:<new_dbxref>14755292
http://purl.org/obo/owl/PMID#PMID_<new_dbxref>14755292
mutation disrupting interaction strength
PSI-MI
Region of a molecule whose mutation or deletion totally disrupts an interaction strength.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation disrupting strength
mutation disrupting interaction rate
PSI-MI
mutation disrupting rate
Region of a molecule whose mutation or deletion totally disrupts an interaction rate (in the case of interactions inferred from enzymatic reaction)..
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation decreasing interaction rate
PSI-MI
Region of a molecule whose mutation or deletion decreases significantly interaction rate (in the case of interactions inferred from enzymatic reaction).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation decreasing rate
mutation increasing interaction rate
PSI-MI
Region of a molecule whose mutation or deletion increases significantly interaction rate (in the case of interactions inferred from enzymatic reaction).
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
mutation increasing rate
mutation increasing interaction strength
PSI-MI
Region of a molecule whose mutation or deletion increases significantly interaction strength.
PMID:14577292
http://purl.org/obo/owl/PMID#PMID_14577292
mutation increasing strength
mutation decreasing interaction strength
PSI-MI
Region of a molecule whose mutation or deletion decreases significantly interaction strength.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutation decreasing strength
mcherry fluorescent protein tag
PSI-MI
mcherry
mCherry is a red monomer which matures extremely rapidly, making it possible to see results very soon after activating transcription. It is highly photostable and resistant to photobleaching. Excitation maximum: 587 nm. Emission maximum: 610 nm.
venus fluorescent protein tag
PSI-MI
Introduction of a point mutation into Aequorea-derived YFP, the substitution of leucine for phenylalanine at position 46 (F46L), produced Venus. This mutation dramatically accelerates oxidation of the chromophore, the rate-limiting step in fluorescent protein maturation. Additional mutations were also introduced in order to increase the tolerance of Venus to acidic environments and to reduce the sensitivity to chloride. The absorption and emission spectral peaks are 515 and 528 nanometers, respectively.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
venus
kusabira-green protein tag
PSI-MI
kusabira-green
Monomeric coral fluorescent reporter protein.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
carboxylation assay
PSI-MI
carboxylation assay
The measurement of a the introduction of a carboxylic acid group into a substrate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
decarboxylation assay
PSI-MI
decarboxxylation assay
The measurement of a the introduction of a carboxylic acid group into a substrate.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
carboxylation reaction
PSI-MI
Carboxylation is a posttranslational modification of glutamate residues, to gamma-carboxyglutamate, in proteins.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
carboxylation
decarboxylation reaction
PSI-MI
Decarboxylation is a chemical reaction that releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain. Enzymes that catalyze decarboxylations are called decarboxylases or, the more formal term, carboxy-lyases (EC number 4.1.1).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
decarboxylation
s tag
PSI-MI
S-tag is the name of an oligopeptide derived from pancreatic ribonuclease A (RNase A). The amino acid sequence of the S-tag is: Lys-Glu-Thr-Ala-Ala-Ala-Lys-Phe-Glu-Arg-Gln-His-Met-Asp-Ser.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
aminoacylation assay
PSI-MI
aminoacylation
The measurement of the addition of an aminoacyl group to a compound.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
aminoacylation reaction
PSI-MI
Aminoacylation is the process of adding an aminoacyl group to a compound.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
aminoacylation
protein a tag visualisation
PSI-MI
Protein A tag is visualized by interacting with IgG antibodies (or their derivatives) that are specifically recognized by protein A.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein a visualisation
phospholipase assay
PSI-MI
A phospholipase is an enzyme that hydrolyzes phospholipids into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C and D, distinguished by the type of reaction which they catalyze.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phospholipase reaction
PSI-MI
Measurement of the hydrolysis of phospholipids into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C and D, distinguished by the type of reaction which they catalyze.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ampylation assay
PSI-MI
ampylation assay
Measurement of AMPylation, the formation of a phosphodiester or phosphoramide ester of AMP on Tyr (RESID:AA0203), Lys (RESID:AA0227), Thr (RESID:AA0267), His (RESID:AA0371) and other aminonacids.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ampylation reaction
PSI-MI
AMPylation, previously known as adenylylation, is formation of anphosphodiester or phosphoramide ester of AMP on Tyr (RESID:AA0203), Lysn(RESID:AA0227), Thr (RESID:AA0267), His (RESID:AA0371) and other aminonacids.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ampylation
cooperative interaction
PSI-MI
A set of molecular binding events that influence each other either positively or negatively through allostery or pre-assembly. In this context, covalent post-translational modifications are considered as binding events. CV terms that are part of this term allow the description of cooperative interactions using the current PSI-MI schema.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
cooperativity
affected interaction
PSI-MI
For an interaction that has a cooperative effect on a subsequent interaction, this term indicates which subsequent interaction is affected. The affected interaction is identified by referring to its interaction id.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
participant-ref
PSI-MI
Referring to a previously described interaction as a participant allows the description of ordered assembly of molecular complexes in PSI-MI2.5. When one of the components of the preformed complex has a feature, the participant-ref term indicates on which component this feature is located. The component is identified by referring to its participant id in the previous interaction.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
cooperative effect value
PSI-MI
cooperative coupling
This value quantifies the cooperative effect of an interaction on a subsequent interaction. It is the fold change of the affinity or a catalytic parameter of a molecule for one ligand in the absence, versus presence, of a second ligand or a post-translational modification.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
cooperative effect outcome
PSI-MI
For an interaction that has a cooperative effect on a subsequent interaction, this term indicates whether this effect is positive or negative, i.e. whether the subsequent interaction is augmented or diminished.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
positive cooperative effect
PSI-MI
This term specifies that an interaction augments a subsequent interaction.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
negative cooperative effect
PSI-MI
This term specifies that an interaction diminishes a subsequent interaction.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
cooperative mechanism
PSI-MI
For an interaction that has a cooperative effect on a subsequent interaction, this term indicates the process that mediates this effect.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
allostery
PSI-MI
Reciprocal energetic coupling between two binding events at distinct sites on the same molecule. The first binding event alters the binding or catalytic properties of the molecule for the second binding event.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allosteric regulation
pre-assembly
PSI-MI
A non-allosteric mechanism where the strength of an interaction depends on whether or not a particular molecular complex already exists.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
allosteric molecule
PSI-MI
A molecule whose binding or catalytic properties at one site are altered by allosteric post-translational modification or binding of an allosteric effector at a distinct site. An allosteric molecule is identified by referring to its participant id.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allosteric effector
PSI-MI
A ligand that elicits an allosteric response upon binding to a target molecule.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allosteric response
PSI-MI
This term describes the effect of an allosteric binding event. It specifies which properties of the allosteric molecule are altered, i.e. whether the interaction alters either (a) binding or (b) catalytic properties of the allosteric molecule at a site distinct from the allosteric site.
allosteric k-type response
PSI-MI
An allosteric response in which the affinity of a molecule is altered.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allosteric v-type response
PSI-MI
An allosteric response in which catalysis (kcat or Vmax) of an enzyme is altered.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allosteric mechanism
PSI-MI
The process that mediates the allosteric response of a molecule upon allosteric post-translational modification or binding of an allosteric effector.
allosteric change in structure
PSI-MI
The allosteric mechanism where changes in the local structure of an allosteric molecule result in altered binding or catalytic properties.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allosteric change in dynamics
PSI-MI
The allosteric mechanism where changes in the local dynamics of an allosteric molecule result in altered binding or catalytic properties.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
allostery type
PSI-MI
This term indicates the chemical relationship between the two ligands whose binding is allosterically coupled.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
heterotropic allostery
PSI-MI
The type of allostery that occurs when the two ligands whose binding is allosterically coupled are not chemically identical.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
homotropic allostery
PSI-MI
The type of allostery that occurs when the two ligands whose binding is allosterically coupled are chemically identical.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
pre-assembly response
PSI-MI
This term describes the way in which preformation of a molecular complex has a non-allosteric cooperative effect on subsequent interactions of its components.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
composite binding site formation
PSI-MI
The preformation of a complex results in the generation of a continuous binding site that spans more than one component of this complex. The functional binding site does not exist outside the context of the preformed complex.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
altered physicochemical compatibility
PSI-MI
The addition of a PTM to an interaction interface affects the physicochemical compatibility of the binding site with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction. Multisite modification can mediate rheostatic regulation of the interaction.
PMID:22480932
http://purl.org/obo/owl/PMID#PMID_22480932
XX:<new_dbxref>
http://purl.org/obo/owl/XX#XX_<new_dbxref>
binding site hiding
PSI-MI
The occurrence of overlapping or adjacent, mutually exclusive binding sites promotes competitive binding. When there is a large difference in affinity of the different sites or in local abundance of competitors, binding at one site results in hiding of the second site, thereby precluding it from interacting when the hiding molecule is present.
PMID:22480932
http://purl.org/obo/owl/PMID#PMID_22480932
configurational pre-organization
PSI-MI
Multivalent ligands form multiple discrete interactions with one or more binding partners. In some cases, An initial binding event can pre-organize other sites for binding. This reduces the degrees of freedom of these sites, thus reducing the entropic costs of their interactions. In addition, the combined strength of multiple interactions increases the enthalpic stability of each interaction (avidity effect). As a result of such effects, interactions of this kind can have a cooperative effect on subsequent interactions.
PMID:18641616
http://purl.org/obo/owl/PMID#PMID_18641616
allosteric post-translational modification
PSI-MI
allosteric ptm
A post-translational modification that elicits an allosteric response upon addition to a target molecule. An allosteric post-translational modification is identified by referring to its feature id.
PMID:18706817
http://purl.org/obo/owl/PMID#PMID_18706817
sequence based prediction of gene regulatory region binding sites
PSI-MI
sequence based prediction of TG regulatory region binding sites for TF
gene regulatory region prediction
Sequence analysis of the regulatory region of a gene used to predict specific elements, transcription factor binding sites (TFBS), where binding of specific transcription factors can occur.
PMID:15131651
http://purl.org/obo/owl/PMID#PMID_15131651
phylogenetic profiling of predicted gene regulatory region binding sites
PSI-MI
phylogenetic footprinting
Sequence analysis based on multiple homologous alignments of the regulatory region of a gene used to predict specific elements, transcription factor binding sites (TFBS), where binding of specific transcription factors can occur. These methods often also use transcription factor binding motif models.
PMID:12671656
http://purl.org/obo/owl/PMID#PMID_12671656
gene regulatory region phylogeny
sequence based prediction of binding of transcription factor to transcribed gene regulatory elements
PSI-MI
Computational methods based on evolutionary hypothesis, used as criteria to browse sequences and predict a transcription factor using structural and sequence features of the protein, e.g., by evaluating if the potential transcription factor protein contains a DNA-binding domain that is known to bind to some regulatory elements, or prediction of transcription factor functional domains (DNA binding, transcription factor dimerization, etc.), all based on sequence or structural features of the transcription factor.
PMID:16381970
http://purl.org/obo/owl/PMID#PMID_16381970
transcription factor prediction
sequence based prediction of binding of TF to TG promoter
partial nucleotide sequence identification
PSI-MI
partial nucleotide sequence
Identification of a part of a nucleotide sequence, usually then related to the full length sequence by alignment. Depending on the experimental design, nucleotide sequence can be determined before the interaction detection while building a collection of clones or after the selection of randomly generated clone.s
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
partial DNA sequence identification
PSI-MI
partial dna sequence
Identification of a part of a DNA sequence, usually then related to the full length sequence by alignment. Depending on the experimental design, nucleotide sequence can be determined before the interaction detection while building a collection of clones or after the selection of randomly generated clone.s
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
paired end tags sequence identification
PSI-MI
Paired-end tags (PET) are the short sequences at the 5 prime and 3 prime ends of the DNA fragment of interest, which can be a piece of genomic DNA or cDNA.
PMID:19339662
http://purl.org/obo/owl/PMID#PMID_19339662
paired end tags
full identification by RNA sequencing
PSI-MI
Sequencing occurs during the course of the experiment. To sequence RNA, the usual method is first to reverse transcribe the sample to generate cDNA fragments.
nuclease footprinting
PSI-MI
Binding of a molecule to a strand of nucleic acid protects that region of nucleic acid from the action of a nuclease. The protected region can subsequently be sequenced and the binding site identified.
PMID:7685766
http://purl.org/obo/owl/PMID#PMID_7685766
nuclease protection
<new synonym>
dna adenine methyltransferase identification
PSI-MI
DNA adenine methyltransferase identification is used to map the binding sites of DNA- and chromatin-binding proteins in eukaryotes. DamID identifies binding sites by expressing the proposed DNA-binding protein as a fusion protein with DNA methyltransferase. Binding of the protein of interest to DNA localizes the methyltransferase in the region of the binding site. Adenosine methylation does not occur naturally in eukaryotes and therefore adenine methylation in any region can be concluded to have been caused by the fusion protein, implying the region is located near a binding site.
PMID:10748524
http://purl.org/obo/owl/PMID#PMID_10748524
DamID
tag visualisation by dna adenine methyltransferase
PSI-MI
Proteins of interest are tagged with Escherichia coli DNA adenine methyltransferase (dam). Expression of this fusion protein in vivo leads to preferential methylation of adenines in DNA surrounding the native binding sites of the dam fusion partner. Because adenine methylation does not occur endogenously in most eukaryotes, it provides a unique tag to mark protein interaction sites. The adenine-methylated DNA fragments are isolated by selective polymerase chain reaction amplification and can be identified by microarray hybridization.
PMID:10748524
http://purl.org/obo/owl/PMID#PMID_10748524
tag DNA methyltransferase
dna methyltransferase tag
PSI-MI
The protein of interest is fused to Escherichia coli DNA adenine methyltransferase (dam). Expression of this fusion protein in vivo leads to preferential methylation of adenines in DNA surrounding the native binding sites of the dam fusion partner. Because adenine methylation does not occur endogenously in most eukaryotes, it provides a unique tag to mark protein interaction sites.
PMID:10748524
http://purl.org/obo/owl/PMID#PMID_10748524
damip
PSI-MI
A mutant form of DNA adenine methyltransferase (DamK9A) from E. coli is fused to the protein of interest and expressed. The fusion protein will bind to target binding sites and introduce N-6-adenine methylation in nearby sites in the genomic DNA. Methylated DNA fragments are enriched with an antibody against N-6-methyladenine and used for further analysis.
PMID:21472695
http://purl.org/obo/owl/PMID#PMID_21472695
tag visualisation by mutated dna adenine methyltransferase
PSI-MI
A mutant form of DNA adenine methyltransferase (DamK9A) from E. coli is fused to the protein of interest and expressed. The fusion protein will bind to target binding sites and introduce N-6-adenine methylation in nearby sites in the genomic DNA.
methylation interference assay
PSI-MI
contact point analysis
methylation interference
methylation protection assay
In interference assays, the DNA will be methylated before the binding assay. Protein binding to DNA protects DNA from methylation by dimethylsulphate. If the contact points are methylated, the protein binding is prevented. After isolating the protein-DNA complex, the methylation sites are cleaved by chemical method. As a result, only those regions out of the binding sites will be cleaved. The protein binding region is not methylated; hence, this region is not cleaved. Although the pattern looks like a footprint, the blank region means "contact points".
PMID:21720958
http://purl.org/obo/owl/PMID#PMID_21720958
hydroxy radical footprinting
PSI-MI
Hydroxyl radicals are created from the Fenton reaction, which involves reducing Fe2+ with H2O2 to form free hydroxyl molecules. These hydroxyl molecules react with the DNA backbone, resulting in a break. Protein bound regions of the DNA are protected.
PMID:3090544
http://purl.org/obo/owl/PMID#PMID_3090544
ultraviolet (uv) footprinting
PSI-MI
Ultraviolet irradiation excites nucleic acids and creates photoreactions, which results in damaged bases in the DNA strand. Protein bound regions of the DNA are protected. UV footprinting technique can detect sequence-specific protein-DNA interactions in vivo. Protein contacts can inhibit of enhance UV photoproduct formation by affecting the ability of DNA to adopt a geometry necessary for the formation of a UV photoproduct. Thus, differences in the strand-breakage patterns of protein-free and protein-bound DNA can be used to detect protein-DNA contacts.
PMID:2842760
http://purl.org/obo/owl/PMID#PMID_2842760
PMID:6728031
http://purl.org/obo/owl/PMID#PMID_6728031
antisense oligonucleotides
PSI-MI
This approach is based on the observation that a synthesized nucleic acid that is complementary to a specific mRNA can decrease the synthesis of its gene product either by increasing the degradation of the targeted mRNA or by interfering with its translation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
partial RNA sequence identification
PSI-MI
Identification of a part of a RNA sequence, usually then related to the full length sequence by alignment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
partial rna sequence
reverse transcription pcr
PSI-MI
Reverse Transcription PCR (RT-PCR) is used for amplifying DNA from RNA. Reverse transcriptase reverse transcribes RNA into cDNA, which is then amplified by PCR.
PMID:12958470
http://purl.org/obo/owl/PMID#PMID_12958470
RPCR
RT-PCR
reverse PCR
quantitative pcr
PSI-MI
q-pcr
QRT-PCR
RQ-PCR
RTQ-PCR
Quantitative PCR (Q-PCR) is used to measure the quantity of a PCR product (commonly in real-time). It quantitatively measures starting amounts of DNA, cDNA, or RNA.
PMID:12958470
http://purl.org/obo/owl/PMID#PMID_12958470
quantitative reverse transcription pcr
PSI-MI
QRT-PCR
RTQ-PCR
Technique used to measure the quantity of DNA amplified from RNA.
PMID:12958470
http://purl.org/obo/owl/PMID#PMID_12958470
radioimmunoassay
PSI-MI
To perform a radioimmunoassay, a known quantity of an antigen is made radioactive, frequently by labeling it with gamma-radioactive isotopes of iodine attached to tyrosine. This radiolabeled antigen is then mixed with a known amount of antibody for that antigen, and as a result, the two chemically bind to one another. Then, a sample containing an unknown quantity of that same antigen is added. This causes the unlabeled (or "cold") antigen from the serum to compete with the radiolabeled antigen ("hot") for antibody binding sites. As the concentration of "cold" antigen is increased, more of it binds to the antibody, displacing the radiolabeled variant, and reducing the ratio of antibody-bound radiolabeled antigen to free radiolabeled antigen. The bound antigens are then separated from the unbound ones, and the radioactivity of the free antigen remaining in the supernatant is measured.
PMID:13846364.
http://purl.org/obo/owl/PMID#PMID_13846364.
RIA
immunohistochemistry
PSI-MI
Method using an antibody coupled with some colouring agent to detect a specific protein within a tissue sample. In some cases the primary antibody is directly linked to a colouring agent, more often the primary antibody is targeted by a secondary antibody, targeting the primary antibody.
PMID:16006601
http://purl.org/obo/owl/PMID#PMID_16006601
anti-tag immunohistochemistry
PSI-MI
Method using an antibody coupled with some colouring agent to detect a tag fused to a specific protein within a tissue sample. In some cases the primary antibody is directly linked to a colouring agent, more often the primary antibody is targeted by a secondary antibody, targeting the primary antibody.
PMID:16006601
http://purl.org/obo/owl/PMID#PMID_16006601
immunocytochemistry
PSI-MI
Method using an antibody coupled with some colouring agent to detect a specific protein within a cell. In some cases the primary antibody is directly linked to a colouring agent, more often the primary antibody is targeted by a secondary antibody, targeting the primary antibody.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
anti-tag immunocytochemistry
PSI-MI
Method using an antibody coupled with some colouring agent to detect a specific tag fused to a protein within a cell. In some cases the primary antibody is directly linked to a colouring agent, more often the primary antibody is targeted by a secondary antibody, targeting the primary antibody.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
one-strep-tag
PSI-MI
Synthetic peptide tag (SAWSHPQFEK-(GGGS)2-SAWSHPQFEK)
PMID:19688738
http://purl.org/obo/owl/PMID#PMID_19688738
split luciferase complementation
PSI-MI
Two proteins of interest, a bait and prey, which are genetically fused to amino- and carboxy-terminal fragments of luciferase, are transiently expressed. Physical interactions of these bait and prey proteins reconstitute some of the luciferase activity and result in light emission in the presence of the luciferase substrate.
PMID:20734273
http://purl.org/obo/owl/PMID#PMID_20734273
split firefly luciferase complementation
PSI-MI
Two proteins of interest, a bait and prey, which are genetically fused to amino- and carboxy-terminal fragments of firefly (Photinus pyralis) luciferase, are transiently expressed. Physical interactions of these bait and prey proteins reconstitute some of the luciferase activity and result in light emission in the presence of the luciferase substrate.
PMID:20734273
http://purl.org/obo/owl/PMID#PMID_20734273
PMID:22070901
http://purl.org/obo/owl/PMID#PMID_22070901
luciferase tag
PSI-MI
Luciferase is a generic term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which requires the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm.
renilla-n
PSI-MI
The n-terminus of the renilla luciferase protein, fused to a protein of interest for use in the split renilla complementation assay.
PMID:12705589
http://purl.org/obo/owl/PMID#PMID_12705589
N-terminal fragment of renilla luciferase
renilla-c
PSI-MI
C-terminal fragment of renilla luciferase
The c-terminus of the renilla luciferase protein, fused to a protein of interest for use in the split renilla complementation assay.
PMID:12705589
http://purl.org/obo/owl/PMID#PMID_12705589
firefly luciferase protein tag
PSI-MI
Firefly luciferase, is an enzyme from beetles (Photinus pyralis) catalyzing the oxidation of the lucifering pigment (reaction with ATP or oxygen) that produces light. Firefly luciferase produces a greenish yellow light in the 550-570nm range.
PMID:22070901
http://purl.org/obo/owl/PMID#PMID_22070901
firefly-c
PSI-MI
The c-terminus of the firefly luciferase protein, fused to a protein of interest for use in the split renilla complementation assay.
PMID:22070901
http://purl.org/obo/owl/PMID#PMID_22070901
C-terminal fragment of firefly luciferase
firefly-n
PSI-MI
N-terminal fragment of firefly luciferase
The n-terminus of the firefly luciferase protein, fused to a protein of interest for use in the split renilla complementation assay.
PMID:22070901
http://purl.org/obo/owl/PMID#PMID_22070901
liposome binding assay
PSI-MI
liposome centrifugation assay
Lipid binding proteins incubated with liposomes of known lipid content. Mixture is then centrifuged and proteins bound to liposomes separated out.
PMID:14734570
http://purl.org/obo/owl/PMID#PMID_14734570
checksum
PSI-MI
A fixed-size datum calculated (by using a hash function) for a molecular sequence or structure, typically for purposes of error detection or indexing.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
hashsum
n-venus
PSI-MI
N-terminal region of the Venus fusion protein, created by the introduction of a point mutation into Aequorea-derived YFP, the substitution of leucine for phenylalanine at position 46 (F46L). This tag is used for split flurescence complementation assays.
PMID:22229727
http://purl.org/obo/owl/PMID#PMID_22229727
c-venus
PSI-MI
C-terminal region of the Venus fusion protein, created by the introduction of a point mutation into Aequorea-derived YFP, the substitution of leucine for phenylalanine at position 46 (F46L). This tag is used for split flurescence complementation assays.
PMID:22229727
http://purl.org/obo/owl/PMID#PMID_22229727
bifc tag
PSI-MI
Fusion protein which consists of either the N- or C-terminal sequence of a fluorescent or luciferase protein. Binding of the proteins of interest enable the reassembly of the molecule, indicating that an interaction has occured.
PMID:17406412
http://purl.org/obo/owl/PMID#PMID_17406412
cGFP
PSI-MI
c-terminal fragment of green fluorescent protein used as a tag in bimolecular fluorescence complementation (BiFC).
PMID:17406412
http://purl.org/obo/owl/PMID#PMID_17406412
nGFP
PSI-MI
n-terminal fragment of green fluorescent protein used as a tag in bimolecular fluorescence complementation (BiFC).
PMID:17406412
http://purl.org/obo/owl/PMID#PMID_17406412
chromosome conformation capture assay
PSI-MI
Chromosome conformation capture,[1] or 3C, is a high-throughput molecular biology technique used to analyze the organization of chromosomes in a cell's natural state. The basic 3C technique consists of cross-linking by addition of formaldehyde followed by addition of a restriction enzyme in excess to the cross-linked DNA, separating the non-cross-linked DNA from the cross-linked chromatin. A intramolecular ligation step using very low concentrations of DNA favors the ligation of relevant DNA fragments with the corresponding junctions instead of the ligation of random fragments. There are two major types of ligation junctions that are over-represented. One is the junction that forms between neighboring DNA fragments due to incomplete digestion, which represents about 20-30% of all junctions. This number is decreased by reducing the cross-linking stringency in the first step. The other type of junctions over-represented in this technique is the junction that forms when one end of the fragment ligates with the other end of the same fragment, and contributes up to 30% of all junctions formed. High temperature then results in the reversal of the previously formed cross-links. The resulting linear DNA fragment has specific restriction ends as well as a central restriction site corresponding to the site of ligation. The pool of these fragments is collectively referred to as the 3C library.
PMID:11847345
http://purl.org/obo/owl/PMID#PMID_11847345
chip-3c
enzyme-mediated activation of radical sources
PSI-MI
Enzyme-mediated activation of radical sources is used to identify partners of a given molecule on the cell surface in living cells Activation of the cross-linking reagent arylazide-biotin tag is accomplished by an enzyme, horseradish peroxidase is featured by radical formation of the labelling reagent by horseradish peroxidase (HRP).
PMID:21214558
http://purl.org/obo/owl/PMID#PMID_21214558
emars
tag visualisation by luciferase assay
PSI-MI
The protein is expressed as a hybrid protein fused to a tag containing a luciferase activity. Subsequence observation or measurement of luciferase activity is used to identify the presence of the molecule in an interaction.
PMID:20609414
http://purl.org/obo/owl/PMID#PMID_20609414
tag luciferase
author-based confidence
PSI-MI
A score generated by an author, usually only relevant for that particular dataset.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
author score
mbinfo
PSI-MI
MBInfo is a wiki based, multimedia, educational resource providing up to date reviews on topics relating to mechanobiology (http://www.mechanobio.info/).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ptm decreasing an interaction
PSI-MI
Post translational modification on a protein observed to decrease the strength or rate of an interaction.
PMID:14744292
http://purl.org/obo/owl/PMID#PMID_14744292
decreasing-ptm
ptm increasing an interaction
PSI-MI
Post translational modification on a protein observed to increase the strength or rate of an interaction.
PMID:14744292
http://purl.org/obo/owl/PMID#PMID_14744292
increasing-ptm
ptm disrupting an interaction
PSI-MI
Post translational modification on a protein observed to disrupt the strength or rate of an interaction.
PMID:14744292
http://purl.org/obo/owl/PMID#PMID_14744292
disrupting-ptm
ampylation assay
PSI-MI
ampylation
Formation of phosphodiester or phosphoramide ester of AMP on Tyr (RESID:AA0203), Lys (RESID:AA0227), Thr (RESID:AA0267), His (RESID:AA0371) and other amino acids
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
lap tag
PSI-MI
Tag encoding green fluorescent protein (GFP) , a TEV cleavage site, and a second purification tag such as S peptide or 6xHis. The tag can therefore be used for both localisation and affinity purification.
PMID:15644491
http://purl.org/obo/owl/PMID#PMID_15644491
location and purification tag
lap tag
drugbank
PSI-MI
DrugBank Accession number consisting of the 4 letter prefix and a 5 number suffix. Each Accession number is unique to the drug's generic name. The 4 letter suffix (APRD, EXPT, BIOD, NUTR) indicates the type of drug (APRD=approved small molecule drug, EXPT=experimental drug, BIOD=biotech drug, NUTR=nutraceutical or natural product). Biotech drugs consist of FDA approved peptide, protein or nucleic acid drugs, approved small molecule drugs are FDA approved non-biotech drugs, nutraceuticals are natural products (amino acids, vitamins, other metabolites) and experimental drugs include drugs under trial, pre-clinical drugs, unapproved drugs, well known inhibitors and possible toxins.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
commercial name
PSI-MI
Standard name of drug or any reagent as provided by its manufacturer.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
generic name
drug brand name
PSI-MI
Alternate names of the drug, brand names from different manufacturers.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
drug mixture brand name
PSI-MI
mix brand name
Brand names and composition of mixtures that include the drug described in this DrugCard file.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biotech product preparation
PSI-MI
biotech prep
Description of the drug (for biotech drugs) describing its composition and/or preparation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
iupac name
PSI-MI
IUPAC or standard chemical name for a drug, or a chemical.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chemical formula
PSI-MI
Chemical formula describing atomic or elemental composition
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chemical structure
PSI-MI
Image of the drug structure (if small molecule) or its sequence (if biotech drug)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
standard inchi
PSI-MI
IUPAC International Chemical Identifier (InChI) - a machine-readable character string describing a chemical structure, developed by IUPAC and the InChI Trust as a standard to allow interoperability and linking between chemical resources. The standard InChI differs from the non-standard InChI in that it is generated with a fixed set of parameters, ensuring consistency between different resources. The current version of the standard InChI software is 1.03.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
standard inchi
inchi id
cas registry number
PSI-MI
Chemical Abstract Service identification number
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
kegg compound
PSI-MI
KEGG Compound ID
Kyoto Encyclopedia of Genes and Genomes compound identification number (if molecule is in KEGG)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pubchem
PSI-MI
NCBI's PubChem database identification number (if molecule is in PubChem).nOBSOLETE as redudant with MI:0730
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
PubChem ID
pharmgkb
PSI-MI
Pharmacogenomics Knowledge Base identification number (if molecule is in PharmGKB)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bind smid
May not be publicly available any more since now owned by Thompson Scientific.
PSI-MI
BIND database Small Molecule Identification number (if molecule is in BIND)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
heterogen
PSI-MI
het
The HET records are used to describe non-standard residues, such as prosthetic groups, inhibitors, solvent molecules, and ions fornwhich coordinates are supplied. Groups are considered HET if they are: n- not one of the standard amino acids, and n- not one of the nucleic acids (C, G, A, T, U, and I), and n- not one of the modified versions of nucleic acids (+C, +G, +A,n+T, +U, and +I), and n- not an unknown amino acid or nucleic acid where UNK is used tonindicate the unknown residue name. nHet records also describe heterogens for which the chemical identity is unknown, in which case the group is assigned the hetID UNK.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
canadian drug identification number
PSI-MI
din
Drug Identification Number (Canadian Drug ID system)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
rxlist link
PSI-MI
Hyperlink to RxList entry for the given drug (if it exists)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
material safety data sheet
PSI-MI
msds
MSDS Material Safety Sheet
Material Safety Data Sheet (if it exists). A Material Safety Data Sheet (MSDS) is designed to provide both workers and emergency personnel with the proper procedures for handling or working with a particular substance. MSDS's include information such as physical data (melting point, boiling point, flash point etc.), toxicity, health effects, first aid, reactivity, storage, disposal, protective equipment, andspill/leak procedures. These are of particular use if a spill or other accident occurs.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
patent number
PSI-MI
number of the patent describing a drug's synthesis or use.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
molecular weight
PSI-MI
Molecular weight in g/mol, determined from molecular formula or sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
melting point
PSI-MI
The melting point of a solid is the temperature range at which it changes state from solid to liquid.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
water solubility
PSI-MI
logSw
Water solubility in mg/mL or g/L
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
logp
PSI-MI
Water/octanol partition coefficient of a small molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
isoelectric point
PSI-MI
The isoelectric point (pI) is the pH at which a particular molecule or surface carries no net electrical charge. For an amino acid with only one amine and one carboxyl group, the pI can be calculated from the pKas of this molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
hydrophobicity
PSI-MI
Physical property of a molecule (known as a hydrophobe) that is repelled from a mass of water. Gravy score.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
boiling point
PSI-MI
The boiling point of a liquid is the temperature at which the vapor pressure of the liquid equals the environmental pressure surrounding the liquid. A liquid in a vacuum environment has a lower boiling point than when the liquid is at atmospheric pressure. A liquid in a high pressure environment has a higher boiling point than when the liquid is at atmospheric pressure. In other words, the boiling point of liquids varies with and depends upon the surrounding environmental pressure.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
smiles string
PSI-MI
SMILES string corresponding to drug structure
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
drug type
PSI-MI
Type of drug (approved, experimental, biotech, nutraceutical)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
drug category
PSI-MI
Therapeutic category or general category of drug (anti-convulsant, antibacterial, etc.).
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
disease indication
Source of further terms could be MeSH term or SNOWMAN.
PSI-MI
Description or common names of diseases that the drug is used to treat.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pharmacology
PSI-MI
Text description of how the drug works at a clinical or physiological level.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mechanism of action
PSI-MI
Description of how the drug works or what it binds to at a molecular level.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
drug absorption
PSI-MI
Determination of how quickly and how much of a drug reaches its intended target (site) of action.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
lethal dose 50
PSI-MI
The LD50 is the dose that kills half (50%) of the animals tested
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ld50
lethal dose 50 %
percentage of plasma protein binding
PSI-MI
Percentage of the drug that is bound in plasma proteins
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
plasma prot binding
protein binding %
drug biotransformation
PSI-MI
The chemical conversion of drugs to other compounds in the body, excluding degradation due to any inherent chemical instability of drugs in biological media.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
drug metabolism
elimination half life
PSI-MI
Rate The time it takes for the body to eliminate or breakdown half of a dose of a pharmacologic agent, in practice the time taken for plasma concentration to reduce by 50%.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
elimin half life
distribution halflife
t1/2
dosage form
PSI-MI
How the drug is dispensed (tablets, capsules, solutions), packing material.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
patient information
PSI-MI
Information on the disease indications and treatment regime for the drug. May also include contra-indications.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
contraindications
PSI-MI
Cautions or conditions indicating why or when the drug should not be taken or prescribed.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bioactive entity reference
PSI-MI
bioactive entity ref
General on-line reference to other details about a drug or other bioactive entity.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chemical stability
PSI-MI
thermodynamic stability
chemical stability occurs when a substance is in a (dynamic) chemical equilibrium with its environment. In this well-defined state, the substance is expected to persist indefinitely (assuming that the environment does not change). A substance which is not chemically stable (yet exists) is metastable or kinetically persistent.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
solubility
PSI-MI
dt theoretical pi
Potential ability of a substance to dissolve in a liquid.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
organisms affected
PSI-MI
Names of organisms which are affected, positively or negatively, by the drug.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
physicochemical attribute name
PSI-MI
Chemical and physical properties of a molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
physicochemical att
bioactive entity attribute name
PSI-MI
Properties of a chemical tested or used as a drug, herbicide, insecticide etc.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bioactive entity att
structure representation attribute name
PSI-MI
struc representation
Human artefact to describe and report the structure of a molecule.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
anti-convulsant
PSI-MI
Therapeutic category or general category of drug -anti-convulsant
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
anti-bacterial
PSI-MI
Therapeutic category or general category of drug -anti-bacterial
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
fda approved drug
PSI-MI
A drug licensed for sale in the USA by the FDA.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental drug
PSI-MI
A drug which has yet to be formally approved for the indication which it is currently being used to treat.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
biotech drug
PSI-MI
A natural product, such as a protein or peptide, which is produced used biotechnology as a drug.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
nutraceutical drug
PSI-MI
A drug which may also be regarded as a foodstuff.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pka
Quantitative prediction of this parameter is possible.
PSI-MI
Negative decimal logarithm of Ka, acid dissociation equilibrium constant for the dissociation of a weak acid.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
degree of ionisation ph 7.4
Quantitative prediction of this parameter is possible.
PSI-MI
ionisation ph 7.4
The degree of ionization refers to the proportion of neutral particles such as those in a gas or aqueous solution, that are ionized into charged particles. A low degree of ionization is sometimes called partially ionized, and a very high degree of ionization as fully ionized. This measurment is performed at pH 7.4
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
logd
Quantitative prediction of this parameter is possible.
PSI-MI
The LogD is the ratio of the equilibrium concentrations of all species (unionized and ionized) of a molecule in octanol to same species in the water phase at a given temperature, normally 25 C. It differs from LogP in that ionized species are considered as well as the neutral form of the molecule.pH 7.4
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
solubility ph 7.4
Quantitative prediction of this parameter is possible.
PSI-MI
Solubility pH 7.4
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
solubility in dmso
PSI-MI
Solubility in DMSO
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
diffusion coefficient
Quantitative prediction of this parameter is possible.
PSI-MI
diffusion coeff
Diffusion coefficient D is proportional to the velocity of the diffusing particles, which depends on the temperature, viscosity of the fluid and the size of the particles according to the Stokes-Einstein relation. In dilute aqueous solutions the diffusion coefficients of most ions are similar and have values that at room temperature are in the range of 0.6x10-9 to 2x10-9 m2/s. For biological molecules the diffusion coefficients normally range from 10-11 to 10-10 m2/s.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chemical stability at pH 2
Qualitative prediction of this parameter is possible.
PSI-MI
Chemical stability at pH 2
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chem stab ph 2
dissolution profile
The prediction of the value for this paramter is currently not possible.
PSI-MI
The rate of dissolution is a key target for controlling the duration of a drug's effect, and as such, several dosage forms that contain the same active ingredient may be available, differing only in the rate of dissolution. If a drug is supplied in a form that is not readily dissolved, the drug may be released more gradually over time with a longer duration of action. Having a longer duration of action may improve compliance since the medication will not have to be taken as often. Additionally, slow-release dosage forms may maintain concentrations within an acceptable therapeutic range over a long period of time, as opposed to quick-release dosage forms which may result in sharper peaks and troughs in serum concentrations.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pharmacokinetics attribute name
PSI-MI
Determination of the fate of substances administered externally to a living organism i.e. the study of what the body does to a drug.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cell permeability
Quantitative prediction of this parameter is possible.
PSI-MI
The permitting or activating of the passage of substances into, out of, or through cells.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
volume of distribution
Quantitative prediction of this parameter is possible.
PSI-MI
The Volume of Distribution is the amount of drug in the body divided by the concentration in the blood. Drugs that are highly lipid soluble have a very high volume of distribution (500 litres). Drugs which are lipid insoluble remain in the blood, and have a low Vd.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
distribution volume
vol of distribution
vd
tissue distribution
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
transporter binding
The prediction of the value for this parameter is currently not possible.
PSI-MI
Substrate of a carrier system allowing the intake of an agent into an organ or part of body.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
clearance
PSI-MI
The ratio of excretion is or measure of the speed at which a constituent is lost from the body.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
renal clearance
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
The renal clearance ratio or fractional excretion is a measure of the speed at which a constituent of urine passes through the kidneys, in this context the rate at which a pharmacological agent is lost from the body via urine.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
total clearance
The prediction of the value for this paramter is currently not possible.
PSI-MI
The clearance of a drug is the volume of plasma from which the drug is completely removed per unit time. The amount eliminated is proportional to the concentration of the drug in the blood.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cl
clearance
maximum absorbable dose
Quantitative prediction of this parameter is possible.
PSI-MI
mad
The Maximum Absorbable Dose (MAD) represents the amount of drug that can permeate across a barrier.
PMID:8987073
http://purl.org/obo/owl/PMID#PMID_8987073
paracellular absorption
Quantitative prediction of this parameter is possible.
PSI-MI
paracellular absorp
Water soluble compounds are absorbed in the small intestine mainly via two pathways, the transcellular and the paracellular pathways. The paracellular absorption involves movement of solutes through a restrictive aqueous channel in the tight junctions of adjoining cells by diffusion.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
tmax/cmax
The prediction of the value for this paramter is currently not possible.
PSI-MI
Ratio between the time value at Cmax (maximum concentration) in a dose response curve, and the Cmax value itself.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
ABCB1 transporter substrate
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Substrate for the representitive member of the ABC transprorter family ABCB1 (MDR1, pgy1, P08183). ABC transporters preventing uptake or facilitating clearance of toxic substances, playing an important role in drug excretion through the bile.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
abcb1 substrate
pgp(mdr1) substrate
bile transporter substrate
The prediction of the value for this paramater is currently not possible.
PSI-MI
Substrate of the bile acid carrier system in both the intestinal tract and the liver. System catalyses of the transfer of bile acid from one side of the membrane to the other. Bile acids are any of a group of steroid carboxylic acids occurring in bile, where they are present as the sodium salts of their amides with glycine or taurine.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
bile trans substrate
cyp-450 inhibition
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Cytochrome P450 inhibition
cyp-450 inhibition
Inhibitor of one or more of the family of cytochrome p450 enzymes, probably the most important elements of oxidative metabolism of exogenous compounds.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
metabolite identification
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Identification of the breakdown products of a substance, either through chemical instability or the actions of enzymes within the body
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
metabolite identific
gsh adducts
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Derivative molecule which has formed from a reaction with glutathione.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
neutralization by glucuronidation or sulfatation
Quantitative prediction of this parameter is possible.
PSI-MI
Neutralization of a compound occuring via its glucuronidation or sulfatation.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
neutraliz gluc/sulf
toxicity attribute name
PSI-MI
The mechanism by which a substance can harm humans or animals.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
herg binding
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Binds to the hERG (human Ether-a-go-go Related Gene) (Q12809) which encodes the Kv11.1 potassium ion channel responsible for the repolarizing IKr current in the cardiac action potential.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
genotoxicity
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Tendency of a bioactive entity to induce damage at the level of the gene.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
mutagenicity
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Tendency of a bioactive entity to induce genetic mutations at the nucleotide level e.g. substitution of nucleotide base-pairs and insertions and deletions of one or more nucleotides in DNA sequences.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
carcinogenicity
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Tendency of a bioactive entity to induce a cancer.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
cancerogenicity
chromosome damage
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Tendency of a bioactive entity to induce damage at the level of the chromosome e.g. induce a change in chromosome structure and number.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
hepatotoxicity
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Tendency of a bioactive entity to affect liver function.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
phospholipidosis
Algorithms have been published to predict the value of this parameter but the quality of the prediction is unknown.
PSI-MI
Causes excess phospholipids to accumulate within cells.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
solubility ph 6.5
Quantitative prediction of this parameter is possible.
PSI-MI
Solubility pH 6.5.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
solubility ph 2.0
Quantitative prediction of this parameter is possible.
PSI-MI
solubility ph2.0
Solubility pH 2.0
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chemical stability at pH 7.4
Qualitative prediction of this parameter is possible.
PSI-MI
Chemical stabilityat at pH 7.4
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
chem stab ph 7.4
investigational drug
Intact.
PSI-MI
A drug currently under clinical development.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
withdrawn drug
Intact.
PSI-MI
A drug for which the licencing for prescriptive use has been withdrawn.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
illicit drug
PSI-MI
A drug which has not been approved for sale, a drug taken for recreational purposes or a licensed drug sold without a prescription.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
other drug interaction
PSI-MI
drug interaction
Effect of additional drug treatments on a given drug action.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
food interaction
IntAct MeSH term or SNOWMAN.
PSI-MI
Effect of food ingestion on a given drug treatment.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
pdr health
PSI-MI
PDRhealth
Hyperlink to PDRhealth entry for the given drug (if it exists)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
wikipedia
PSI-MI
Hyperlink to wikipedia entry for the given drug (if it exists)
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
average molecular weight
PSI-MI
avrg mol weight
Molecular weight in g/mol, determined from molecular formula or sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
monoisotopic molecular weight
PSI-MI
monoisotopic mol wgt
Molecular weight in g/mol, determined from molecular formula or sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental water solubility
PSI-MI
Water solubility in mg/mL or g/L.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
exp h2o solubilty
experimental h2o solubility
predicted water solubility
PSI-MI
Water solubility in mg/mL or g/L
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
predicted h2o solub
predicted h2o solubility
logs
PSI-MI
logS
Solubility of a molecule in a given solvant.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental logs
Quantitative prediction of this parameter is possible.
PSI-MI
Experimental derived value for the solubility of a molecule in a given solvant.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
experimental logS
experimental CaCO2 permeability
Quantitative prediction of this parameter is possible.
PSI-MI
Experimentally derived value for ability of a compound to cross epithelial and endothelial cell barriers Using the CaCo2 cell line derived from a human colorectal adenocarcinoma. Used as an in vitro permeability models to predict human intestinal absorption
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
caco2 permeability
by homology
PSI-MI
Reference assigned to a molecule by sequence homology with another similar sequence.
PMID:14755292
http://purl.org/obo/owl/PMID#PMID_14755292
protein modification
PSI-MOD
ModRes
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
alkylated residue
PSI-MOD
A protein modification that effectively replaces a hydrogen atom with an alkyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
AlkylRes
O-glycosyl-L-serine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-serine residue to O3-glycosylserine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
OGlycoSer
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-glycosyl-L-threonine
PSI-MOD
OGlycoThr
A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-glycosylated residue
PSI-MOD
NGlycoRes
A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
natural residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Res
A protein modification that inserts or replaces a residue with a natural, standard or nonstandard, encoded residue.
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-alanine residue
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts a source amino acid residue to an L-alanine.
RESID:AA0001
http://purl.org/obo/owl/RESID#RESID_AA0001
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:29948
http://purl.org/obo/owl/ChEBI#ChEBI_29948
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
alpha-aminopropionic acid
(S)-2-aminopropanoic acid
2-aminopropionic acid
Ala
alpha-alanine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-arginine residue
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-amino-5-guanidinovaleric acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-amino-5-guanidinopentanoic acid
Arg
alpha-amino-delta-guanidinovaleric acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-amino-5-[(aminoiminomethyl)amino]pentanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-5-(carbamimidamido)pentanoic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts a source amino acid residue to an L-arginine.
ChEBI:29952
http://purl.org/obo/owl/ChEBI#ChEBI_29952
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:518876
http://purl.org/obo/owl/PubMed#PubMed_518876
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0002
http://purl.org/obo/owl/RESID#RESID_AA0002
L-asparagine residue
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
alpha-amino-beta-carbamylpropionic acid
alpha-aminosuccinamic acid
2-amino-3-carbamoylpropanoic acid
2-aminosuccinamic acid
(S)-2-amino-4-butanediamic acid
2,4-diamino-4-oxobutanoic acid
A protein modification that effectively converts a source amino acid residue to an L-asparagine.
PubMed:5681232
http://purl.org/obo/owl/PubMed#PubMed_5681232
PubMed:15736973
http://purl.org/obo/owl/PubMed#PubMed_15736973
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:29956
http://purl.org/obo/owl/ChEBI#ChEBI_29956
PubMed:9789001
http://purl.org/obo/owl/PubMed#PubMed_9789001
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0003
http://purl.org/obo/owl/RESID#RESID_AA0003
aspartic acid beta-amide
Asn
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-aspartic acid residue
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts a source amino acid residue to an L-aspartic acid.
PubMed:9521123
http://purl.org/obo/owl/PubMed#PubMed_9521123
ChEBI:29958
http://purl.org/obo/owl/ChEBI#ChEBI_29958
PubMed:9582379
http://purl.org/obo/owl/PubMed#PubMed_9582379
RESID:AA0004
http://purl.org/obo/owl/RESID#RESID_AA0004
PubMed:8089117
http://purl.org/obo/owl/PubMed#PubMed_8089117
PubMed:5764436
http://purl.org/obo/owl/PubMed#PubMed_5764436
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:339692
http://purl.org/obo/owl/PubMed#PubMed_339692
PubMed:4399050
http://purl.org/obo/owl/PubMed#PubMed_4399050
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:1097438
http://purl.org/obo/owl/PubMed#PubMed_1097438
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
aminosuccinic acid
Asp
(S)-2-aminobutanedioic acid
L-cysteine residue
From DeltaMass: Average Mass: 121.
PSI-MOD
3-mercapto-L-alanine
2-amino-3-mercaptopropionic acid
alpha-amino-beta-mercaptopropanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(R)-2-amino-3-sulfanylpropanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(R)-cysteine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
2-amino-3-mercaptopropanoic acid
A protein modification that effectively converts a source amino acid residue to an L-cysteine.
PubMed:15790858
http://purl.org/obo/owl/PubMed#PubMed_15790858
PubMed:1310545
http://purl.org/obo/owl/PubMed#PubMed_1310545
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:29950
http://purl.org/obo/owl/ChEBI#ChEBI_29950
PubMed:3447159
http://purl.org/obo/owl/PubMed#PubMed_3447159
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:7338899
http://purl.org/obo/owl/PubMed#PubMed_7338899
RESID:AA0005
http://purl.org/obo/owl/RESID#RESID_AA0005
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
beta-mercaptoalanine
Cys
alpha-amino-beta-mercaptopropionic acid
alpha-amino-beta-thiolpropionic acid
L-(+)-cysteine
thioserine
Cysteine (C, Cys)
half-cystine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-glutamic acid residue
PSI-MOD
glutaminic acid
Glu
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a source amino acid residue to an L-glutamic acid.
RESID:AA0006
http://purl.org/obo/owl/RESID#RESID_AA0006
PubMed:4922541
http://purl.org/obo/owl/PubMed#PubMed_4922541
ChEBI:29972
http://purl.org/obo/owl/ChEBI#ChEBI_29972
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:9326660
http://purl.org/obo/owl/PubMed#PubMed_9326660
PubMed:957425
http://purl.org/obo/owl/PubMed#PubMed_957425
PubMed:1881881
http://purl.org/obo/owl/PubMed#PubMed_1881881
PubMed:4565668
http://purl.org/obo/owl/PubMed#PubMed_4565668
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(S)-2-aminopentanedioic acid
alpha-aminoglutaric acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
1-aminopropane-1,3-dicarboxylic acid
L-glutamine residue
PSI-MOD
Gln
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
alpha-amino-gamma-carbamylbutyric acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-aminoglutaramic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-amino-4-carbamoylbutanoic acid
glutamide
glutamic acid gamma-amide
glutamic acid 5-amide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts a source amino acid residue to an L-glutamine.
RESID:AA0007
http://purl.org/obo/owl/RESID#RESID_AA0007
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:9342308
http://purl.org/obo/owl/PubMed#PubMed_9342308
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:3340166
http://purl.org/obo/owl/PubMed#PubMed_3340166
ChEBI:30011
http://purl.org/obo/owl/ChEBI#ChEBI_30011
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-5-pentanediamic acid
2,5-diamino-5-oxopentanoic acid
glycine residue
PSI-MOD
glycocoll
Gly
aminoethanoic acid
aminoacetic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a source amino acid residue to a glycine.
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0008
http://purl.org/obo/owl/RESID#RESID_AA0008
ChEBI:29947
http://purl.org/obo/owl/ChEBI#ChEBI_29947
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:1310545
http://purl.org/obo/owl/PubMed#PubMed_1310545
L-histidine residue
PSI-MOD
A protein modification that effectively converts a source amino acid residue to an L-histidine.
PubMed:6129252
http://purl.org/obo/owl/PubMed#PubMed_6129252
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:6876174
http://purl.org/obo/owl/PubMed#PubMed_6876174
RESID:AA0009
http://purl.org/obo/owl/RESID#RESID_AA0009
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:14342316
http://purl.org/obo/owl/PubMed#PubMed_14342316
ChEBI:29979
http://purl.org/obo/owl/ChEBI#ChEBI_29979
PubMed:2722967
http://purl.org/obo/owl/PubMed#PubMed_2722967
PubMed:5460889
http://purl.org/obo/owl/PubMed#PubMed_5460889
PubMed:512
http://purl.org/obo/owl/PubMed#PubMed_512
alpha-amino-beta-(4-imidazole)propionic acid
His
(S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid
4-(2-amino-2-carboxyethyl)imidazole
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-isoleucine residue
PSI-MOD
A protein modification that effectively converts a source amino acid residue to an L-isoleucine.
RESID:AA0010
http://purl.org/obo/owl/RESID#RESID_AA0010
ChEBI:30009
http://purl.org/obo/owl/ChEBI#ChEBI_30009
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-threo-isoleucine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
alpha-amino-beta-methylvaleric acid
(2S,3S)-2-amino-3-methylpentanoic acid
Isoleucyl
Ile
L-leucine residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts a source amino acid residue to an L-leucine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:30006
http://purl.org/obo/owl/ChEBI#ChEBI_30006
PubMed:11478885
http://purl.org/obo/owl/PubMed#PubMed_11478885
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0011
http://purl.org/obo/owl/RESID#RESID_AA0011
Leu
alpha-aminoisocaproic acid
alpha-amino-gamma-methylvaleric acid
(S)-2-amino-4-methylpentanoic acid
L-lysine residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2,6-diaminohexanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
alpha,epsilon-diaminocaproic acid
Lys
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts a source amino acid residue to L-lysine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:29967
http://purl.org/obo/owl/ChEBI#ChEBI_29967
RESID:AA0012
http://purl.org/obo/owl/RESID#RESID_AA0012
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:6120171
http://purl.org/obo/owl/PubMed#PubMed_6120171
PubMed:3106962
http://purl.org/obo/owl/PubMed#PubMed_3106962
L-methionine residue
From DeltaMass: Average Mass: 149
PSI-MOD
gamma-methylthio-alpha-aminobutyric acid
alpha-amino-gamma-methylthiobutyric acid
Met
L-(-)-methionine
2-amino-4-(methylthio)butanoic acid
(S)-2-amino-4-(methylsulfanyl)butanoic acid
alpha-amino-gamma-methylmercaptobutyric acid
2-amino-4-(methylthio)butyric acid
A protein modification that effectively converts a source amino acid residue to L-methionine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:6411710
http://purl.org/obo/owl/PubMed#PubMed_6411710
ChEBI:29983
http://purl.org/obo/owl/ChEBI#ChEBI_29983
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0013
http://purl.org/obo/owl/RESID#RESID_AA0013
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-methyl-L-homocysteine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-phenylalanine residue
PSI-MOD
alpha-amino-beta-phenylpropionic acid
(S)-2-amino-3-phenylpropanoic acid
A protein modification that effectively converts a source amino acid residue to L-phenylalanine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0014
http://purl.org/obo/owl/RESID#RESID_AA0014
ChEBI:29997
http://purl.org/obo/owl/ChEBI#ChEBI_29997
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Phe
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
L-proline residue
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a source amino acid residue to L-proline.
ChEBI:30017
http://purl.org/obo/owl/ChEBI#ChEBI_30017
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0015
http://purl.org/obo/owl/RESID#RESID_AA0015
PubMed:8547259
http://purl.org/obo/owl/PubMed#PubMed_8547259
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
pyrrolidine-2-carboxylic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Pro
(S)-2-pyrrolidinecarboxylic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
L-serine residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-3-hydroxypropanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
beta-hydroxyalanine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Ser
3-hydroxy-L-alanine
alpha-amino-beta-hydroxypropionic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts a source amino acid residue to L-serine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:4399050
http://purl.org/obo/owl/PubMed#PubMed_4399050
ChEBI:29999
http://purl.org/obo/owl/ChEBI#ChEBI_29999
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0016
http://purl.org/obo/owl/RESID#RESID_AA0016
L-threonine residue
PSI-MOD
Thr
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
beta-methylserine
L-threo-threonine
(2S,3R)-2-amino-3-hydroxybutanoic acid
alpha-amino-beta-hydroxybutyric acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts a source amino acid residue to L-threonine.
ChEBI:30013
http://purl.org/obo/owl/ChEBI#ChEBI_30013
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2989287
http://purl.org/obo/owl/PubMed#PubMed_2989287
RESID:AA0017
http://purl.org/obo/owl/RESID#RESID_AA0017
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
L-tryptophan residue
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts a source amino acid residue to L-tryptophan.
ChEBI:29954
http://purl.org/obo/owl/ChEBI#ChEBI_29954
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2059637
http://purl.org/obo/owl/PubMed#PubMed_2059637
PubMed:9324768
http://purl.org/obo/owl/PubMed#PubMed_9324768
RESID:AA0018
http://purl.org/obo/owl/RESID#RESID_AA0018
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S)-2-amino-3-(1H-indol-3-yl)propanoic acid
alpha-amino-beta-(3-indolyl)propionoic acid
beta-3-indolylalanine
Trp
L-tyrosine residue
PSI-MOD
p-tyrosine
para-hydroxyphenylalanine
(S)-2-amino-3-(4-hydoxyphenyl)propanoic acid
Tyr
alpha-amino-beta-(para-hydroxyphenyl)propionic acid
A protein modification that effectively converts a source amino acid residue to L-tyrosine.
PubMed:2542938
http://purl.org/obo/owl/PubMed#PubMed_2542938
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2190093
http://purl.org/obo/owl/PubMed#PubMed_2190093
ChEBI:29975
http://purl.org/obo/owl/ChEBI#ChEBI_29975
PubMed:6120171
http://purl.org/obo/owl/PubMed#PubMed_6120171
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0019
http://purl.org/obo/owl/RESID#RESID_AA0019
PubMed:5550972
http://purl.org/obo/owl/PubMed#PubMed_5550972
PubMed:6061414
http://purl.org/obo/owl/PubMed#PubMed_6061414
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-valine residue
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts a source amino acid residue to an L-valine.
ChEBI:30015
http://purl.org/obo/owl/ChEBI#ChEBI_30015
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0020
http://purl.org/obo/owl/RESID#RESID_AA0020
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-2-amino-3-methylbutanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
alpha-amino-beta-methylbutyric acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
alpha-aminoisovaleric acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Val
N-formyl-L-methionine
PSI-MOD
N-formylmethionine
N-formylated L-methionine
FormylMet
fMet
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Addition of N-formyl met
2-formamido-4-(methylsulfanyl)butanoic acid
2-formylamino-4-(methylthio)butanoic acid
(S)-2-formylamino-4-(methylsulfanyl)butanoic acid
A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.
PubMed:2165784
http://purl.org/obo/owl/PubMed#PubMed_2165784
PubMed:11152118
http://purl.org/obo/owl/PubMed#PubMed_11152118
PubMed:8758896
http://purl.org/obo/owl/PubMed#PubMed_8758896
PubMed:3042771
http://purl.org/obo/owl/PubMed#PubMed_3042771
UniMod:107
http://purl.org/obo/owl/UniMod#UniMod_107
RESID:AA0021
http://purl.org/obo/owl/RESID#RESID_AA0021
PubMed:10825024
http://purl.org/obo/owl/PubMed#PubMed_10825024
ChEBI:33718
http://purl.org/obo/owl/ChEBI#ChEBI_33718
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-selenocysteine residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(R)-2-amino-3-selanylpropanoic acid
A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification.
PubMed:2037562
http://purl.org/obo/owl/PubMed#PubMed_2037562
PubMed:2963330
http://purl.org/obo/owl/PubMed#PubMed_2963330
PubMed:4734725
http://purl.org/obo/owl/PubMed#PubMed_4734725
PubMed:6217842
http://purl.org/obo/owl/PubMed#PubMed_6217842
PubMed:6076213
http://purl.org/obo/owl/PubMed#PubMed_6076213
RESID:AA0022
http://purl.org/obo/owl/RESID#RESID_AA0022
PubMed:6714945
http://purl.org/obo/owl/PubMed#PubMed_6714945
PubMed:10523135
http://purl.org/obo/owl/PubMed#PubMed_10523135
PubMed:1066676
http://purl.org/obo/owl/PubMed#PubMed_1066676
ChEBI:30000
http://purl.org/obo/owl/ChEBI#ChEBI_30000
SeCys
selenium cysteine
3-selenylalanine
Sec
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
crosslinked residues
The covalent bond is formed directly between sidechain atoms. If non-aminoacid atoms are involved in connecting two or more peptide chain residues peptide chain, the connection is classified as a multivalent binding site.
PSI-MOD
A protein modification that crosslinks two or more amino acid residues with covalent bonds.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
L-cystine (cross-link)
Cross-link 2; for formation of a disulfide bond between a peptide cysteine and a free cysteine, see MOD:00765.
PSI-MOD
dicysteine
Cystine ((Cys)2)
Cysteine (covalent)
Cys2
bis(beta-amino-beta-carboxyethyl)disulfide
3,3'-dithiodialanine
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
3,3'-dithiobisalanine
3,3'-dithiobis(2-aminopropanoic acid)
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid [misnomer]
(R,R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
A protein modification that effectively cross-links two L-cysteine residues to form L-cystine.
PubMed:1988019
http://purl.org/obo/owl/PubMed#PubMed_1988019
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:16283
http://purl.org/obo/owl/ChEBI#ChEBI_16283
PubMed:366603
http://purl.org/obo/owl/PubMed#PubMed_366603
PubMed:3083866
http://purl.org/obo/owl/PubMed#PubMed_3083866
PubMed:2076469
http://purl.org/obo/owl/PubMed#PubMed_2076469
PubMed:2001356
http://purl.org/obo/owl/PubMed#PubMed_2001356
PubMed:8344916
http://purl.org/obo/owl/PubMed#PubMed_8344916
PubMed:7918467
http://purl.org/obo/owl/PubMed#PubMed_7918467
RESID:AA0025
http://purl.org/obo/owl/RESID#RESID_AA0025
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(2S,3R)-3-hydroxyasparagine
PSI-MOD
(3R)3HyAsn
L-erythro-beta-hydroxyasparagine
erythro-beta-hydroxylated L-asparagine
A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine.
PubMed:11823643
http://purl.org/obo/owl/PubMed#PubMed_11823643
RESID:AA0026
http://purl.org/obo/owl/RESID#RESID_AA0026
PubMed:2820791
http://purl.org/obo/owl/PubMed#PubMed_2820791
(3R)-3-hydroxyasparagine
(2S,3R)-2-amino-3-hydroxy-4-butanediamic acid
(2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(2S,3R)-3-hydroxyaspartic acid
PSI-MOD
2-amino-3-hydroxysuccinic acid
(2S,3R)-2-amino-3-hydroxybutanedioic acid
(3R)3HyAsp
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
3-hydroxyaspartic acid
3-hydroxyaspartate
A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid.
RESID:AA0027
http://purl.org/obo/owl/RESID#RESID_AA0027
PubMed:6871167
http://purl.org/obo/owl/PubMed#PubMed_6871167
PubMed:8355279
http://purl.org/obo/owl/PubMed#PubMed_8355279
PubMed:6572939
http://purl.org/obo/owl/PubMed#PubMed_6572939
L-erythro-beta-hydroxyaspartic acid
erythro-beta-hydroxylated L-aspartic acid
5-hydroxy-L-lysine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
5-hydroxylysine
5HyLys
2,6-diamino-2,3,4,6-tetradeoxyhexonic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
5-hydroxylated L-lysine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
alpha,epsilon-diamino-delta-hydroxycaproic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-erythro-delta-hydroxylysine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-lysine residue to 5-hydroxy-L-lysine.
PubMed:2857489
http://purl.org/obo/owl/PubMed#PubMed_2857489
PubMed:16101297
http://purl.org/obo/owl/PubMed#PubMed_16101297
RESID:AA0028
http://purl.org/obo/owl/RESID#RESID_AA0028
ChEBI:18040
http://purl.org/obo/owl/ChEBI#ChEBI_18040
PubMed:15504407
http://purl.org/obo/owl/PubMed#PubMed_15504407
PubMed:13375629
http://purl.org/obo/owl/PubMed#PubMed_13375629
3-hydroxy-L-proline
PSI-MOD
beta-hydroxypyrrolidine-alpha-carboxylic acid
3HyPro
L-threo-3-hydroxyproline
3-hydroxylated L-proline
(2S,3R)-3-hydroxy-2-pyrrolidinecarboxylic acid
3-trans-hydroxy-L-proline
3-hydroxyproline
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline.
ChEBI:16889
http://purl.org/obo/owl/ChEBI#ChEBI_16889
PubMed:3734192
http://purl.org/obo/owl/PubMed#PubMed_3734192
PubMed:2400108
http://purl.org/obo/owl/PubMed#PubMed_2400108
PubMed:4343807
http://purl.org/obo/owl/PubMed#PubMed_4343807
RESID:AA0029
http://purl.org/obo/owl/RESID#RESID_AA0029
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
4-hydroxy-L-proline
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
gamma-hydroxypyrrolidine-alpha-carboxylic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-threo-4-hydroxyproline
A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline
ChEBI:18095
http://purl.org/obo/owl/ChEBI#ChEBI_18095
PubMed:2400108
http://purl.org/obo/owl/PubMed#PubMed_2400108
PubMed:3734192
http://purl.org/obo/owl/PubMed#PubMed_3734192
PubMed:11292863
http://purl.org/obo/owl/PubMed#PubMed_11292863
RESID:AA0030
http://purl.org/obo/owl/RESID#RESID_AA0030
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
4HyPro
4-trans-hydroxy-L-proline
4-hydroxyproline
4-hydroxyproline
4-hydroxylated L-proline
(2S,4R)-4-hydroxy-2-pyrrolidinecarboxylic acid
2-pyrrolidone-5-carboxylic acid (Gln)
DeltaMass gives a formula C 5 H 5 N 1 O 2 with mass 111.1
PSI-MOD
Pyroglutamic Acid formed from Gln
pyroglutamic acid
Pyro-glu from Q
PyrGlu(Gln)
N-pyrrolidone carboxyl (N terminus)
A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid.
UniMod:28
http://purl.org/obo/owl/UniMod#UniMod_28
PubMed:3473473
http://purl.org/obo/owl/PubMed#PubMed_3473473
RESID:AA0031
http://purl.org/obo/owl/RESID#RESID_AA0031
PubMed:1836357
http://purl.org/obo/owl/PubMed#PubMed_1836357
PubMed:26343
http://purl.org/obo/owl/PubMed#PubMed_26343
PubMed:10214721
http://purl.org/obo/owl/PubMed#PubMed_10214721
DeltaMass:123
http://purl.org/obo/owl/DeltaMass#DeltaMass_123
ChEBI:30652
http://purl.org/obo/owl/ChEBI#ChEBI_30652
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Pyroglutamyl
Pyrrolidone carboxylic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
2-oxopyrrolidine-5-carboxylic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
5-oxoproline
5-oxopyrrolidine-2-carboxylic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Gln->pyro-Glu
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-5-oxo-2-pyrrolidinecarboxylic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-gamma-carboxyglutamic acid
DeltaMass has an incorrect formula C 6 H 7 N 5 O 1 (N and O reversed) with mass 173.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Carboxy Glutamyl
Carboxy
4CbxGlu
4-carboxyglutamic acid
4-carboxyglutamate
1-carboxyglutamic acid [misnomer]
(S)-3-amino-1,1,3-propanetricarboxylic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid.
RESID:AA0032
http://purl.org/obo/owl/RESID#RESID_AA0032
DeltaMass:217
http://purl.org/obo/owl/DeltaMass#DeltaMass_217
PubMed:9188685
http://purl.org/obo/owl/PubMed#PubMed_9188685
UniMod:299
http://purl.org/obo/owl/UniMod#UniMod_299
PubMed:10517147
http://purl.org/obo/owl/PubMed#PubMed_10517147
PubMed:1807167
http://purl.org/obo/owl/PubMed#PubMed_1807167
PubMed:3263814
http://purl.org/obo/owl/PubMed#PubMed_3263814
PubMed:4528109
http://purl.org/obo/owl/PubMed#PubMed_4528109
PubMed:7457858
http://purl.org/obo/owl/PubMed#PubMed_7457858
PubMed:8135347
http://purl.org/obo/owl/PubMed#PubMed_8135347
PubMed:8868490
http://purl.org/obo/owl/PubMed#PubMed_8868490
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
gamma-carboxylated L-glutamic acid
Carboxylation
L-aspartic 4-phosphoric anhydride
PSI-MOD
2-aminobutanedioic 4-phosphoric anhydride
(2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid
4-aspartylphosphate
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
4-oxo-O-phosphono-L-homoserine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
4-phosphoaspartic acid
Phosphorylation
PhosAsp
Phospho
4-phosphorylated L-aspartatic acid
beta-aspartyl phosphate
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride.
PubMed:4357737
http://purl.org/obo/owl/PubMed#PubMed_4357737
RESID:AA0033
http://purl.org/obo/owl/RESID#RESID_AA0033
ChEBI:15836
http://purl.org/obo/owl/ChEBI#ChEBI_15836
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-phospho-L-cysteine
PSI-MOD
(R)-2-amino-3-(phosphonosulfanyl)propanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
cysteine phosphate thioester
A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine.
RESID:AA0034
http://purl.org/obo/owl/RESID#RESID_AA0034
PubMed:3142516
http://purl.org/obo/owl/PubMed#PubMed_3142516
PubMed:7961745
http://purl.org/obo/owl/PubMed#PubMed_7961745
PubMed:8128219
http://purl.org/obo/owl/PubMed#PubMed_8128219
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Phosphocysteine
Phosphorylation
PhosCys
Phospho
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S3-phosphocysteine
S-phosphorylated L-cysteine
S-phosphonocysteine
1'-phospho-L-histidine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Phosphorylation
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Phospho
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
NtauPhosHis
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Ntau-phosphorylated L-histidine
tele-phosphohistidine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
tau-phosphohistidine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
NE2-phosphonohistidine
(S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
histidine-N(epsilon)-phosphate
A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine).
PubMed:11038361
http://purl.org/obo/owl/PubMed#PubMed_11038361
PubMed:5642389
http://purl.org/obo/owl/PubMed#PubMed_5642389
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
RESID:AA0035
http://purl.org/obo/owl/RESID#RESID_AA0035
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
histidine-3-phosphate [misnomer]
N1-phosphonohistidine
histidine-N1'-phosphate
3'-phospho-L-histidine
PSI-MOD
A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine).
PubMed:7669763
http://purl.org/obo/owl/PubMed#PubMed_7669763
PubMed:1549615
http://purl.org/obo/owl/PubMed#PubMed_1549615
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
RESID:AA0036
http://purl.org/obo/owl/RESID#RESID_AA0036
PubMed:5642389
http://purl.org/obo/owl/PubMed#PubMed_5642389
PubMed:7803390
http://purl.org/obo/owl/PubMed#PubMed_7803390
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
histidine-1-phosphate [misnomer]
histidine-N(delta)-phosphate
histidine-N3'-phosphate
N3-phosphonohistidine
ND1-phosphonohistidine
pi-phosphohistidine
Phosphorylation
pros-phosphohistidine
Pros-phosphohistidine
Npi-phosphorylated L-histidine
Phospho
NpiPhosHis
O-phospho-L-serine
PSI-MOD
(S)-2-amino-3-(phosphonooxy)propanoic acid
2-amino-3-hydroxypropanoic acid 3-phosphate
O-phosphonoserine
O-phosphorylated L-serine
O3-phosphoserine
OPhosSer
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
serine phosphate ester
Phosphoserine
Phosphorylation
Phospho Seryl
Phospho
A protein modification that effectively converts an L-serine residue to O-phospho-L-serine.
PubMed:8061611
http://purl.org/obo/owl/PubMed#PubMed_8061611
RESID:AA0037
http://purl.org/obo/owl/RESID#RESID_AA0037
PubMed:4065410
http://purl.org/obo/owl/PubMed#PubMed_4065410
ChEBI:15811
http://purl.org/obo/owl/ChEBI#ChEBI_15811
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
PubMed:12923550
http://purl.org/obo/owl/PubMed#PubMed_12923550
O-phospho-L-threonine
PSI-MOD
2-amino-3-hydroxybutanoic acid 3-phosphate
(2S,3R)-2-amino-3-phosphonooxybutanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine.
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
ChEBI:21967
http://purl.org/obo/owl/ChEBI#ChEBI_21967
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:12923550
http://purl.org/obo/owl/PubMed#PubMed_12923550
PubMed:7678926
http://purl.org/obo/owl/PubMed#PubMed_7678926
RESID:AA0038
http://purl.org/obo/owl/RESID#RESID_AA0038
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Phospho Threonyl
Phosphorylation
Phosphothreonine
O-phosphorylated L-threonine
O3-phosphothreonine
OPhosThr
Phospho
threonine phosphate ester
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
O4'-phospho-L-tyrosine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
tyrosine phosphate
Phosphorylation
Phosphotyrosine
Phospho
Phospho Tyrosinyl
OPhosTyr
A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine.
RESID:AA0039
http://purl.org/obo/owl/RESID#RESID_AA0039
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
PubMed:10226369
http://purl.org/obo/owl/PubMed#PubMed_10226369
PubMed:1725475
http://purl.org/obo/owl/PubMed#PubMed_1725475
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
O4'-phosphorylated L-tyrosine
O4-phosphotyrosine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate
2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine
PSI-MOD
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide
2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid
Diphth
alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium
Diphthamide
diphthamide (from histidine)
Diphthamide
diphthamide
Diphthamide
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-histidine residue to diphthamide.
DeltaMass:122
http://purl.org/obo/owl/DeltaMass#DeltaMass_122
PubMed:15316019
http://purl.org/obo/owl/PubMed#PubMed_15316019
ChEBI:16692
http://purl.org/obo/owl/ChEBI#ChEBI_16692
PubMed:7430147
http://purl.org/obo/owl/PubMed#PubMed_7430147
UniMod:375
http://purl.org/obo/owl/UniMod#UniMod_375
RESID:AA0040
http://purl.org/obo/owl/RESID#RESID_AA0040
2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole
2-[3-carboxamido-3-(trimethylammonio)propyl]histidine
(2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium
(3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium
N-acetyl-L-alanine
PSI-MOD
A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.
PubMed:4700463
http://purl.org/obo/owl/PubMed#PubMed_4700463
RESID:AA0041
http://purl.org/obo/owl/RESID#RESID_AA0041
PubMed:363452
http://purl.org/obo/owl/PubMed#PubMed_363452
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
AcAla
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
acetylalanine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
2-(acetylamino)propanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S)-2-(acetamido)propanoic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N-acetylated L-alanine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N-acetylalanine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-acetyl-L-aspartic acid
PSI-MOD
N-acetylated L-aspartic acid
N-acetylaspartate
acetylaspartic acid
AcAsp
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(S)-2-(acetamido)butanedioic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid.
ChEBI:21547
http://purl.org/obo/owl/ChEBI#ChEBI_21547
PubMed:2395459
http://purl.org/obo/owl/PubMed#PubMed_2395459
PubMed:1560020
http://purl.org/obo/owl/PubMed#PubMed_1560020
RESID:AA0042
http://purl.org/obo/owl/RESID#RESID_AA0042
2-(acetylamino)butanedioic acid
N-acetyl-L-cysteine
incidental to RESID:AA0223
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-acetylcysteine
NAcCys
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Acetyl
2-acetylamino-3-sulfanylpropanoic acid
N-acetylcysteine
N-acetylated cysteine
2-acetylamino-3-mercaptopropanoic acid
(R)-2-acetamido-3-sulfanylpropanoic acid
A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:1500421
http://purl.org/obo/owl/PubMed#PubMed_1500421
ChEBI:28939
http://purl.org/obo/owl/ChEBI#ChEBI_28939
PubMed:6725286
http://purl.org/obo/owl/PubMed#PubMed_6725286
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
RESID:AA0043
http://purl.org/obo/owl/RESID#RESID_AA0043
N-acetyl-L-glutamic acid
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-acetylglutamate
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.
RESID:AA0044
http://purl.org/obo/owl/RESID#RESID_AA0044
PubMed:6725286
http://purl.org/obo/owl/PubMed#PubMed_6725286
ChEBI:17533
http://purl.org/obo/owl/ChEBI#ChEBI_17533
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N-acetylated L-glutamic acid
acetylglutamic acid
AcGlu
(S)-2-(acetamido)pentanedioic acid
2-(acetylamino)pentanedioic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-acetyl-L-glutamine
PSI-MOD
A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine.
RESID:AA0045
http://purl.org/obo/owl/RESID#RESID_AA0045
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-2-acetamido-5-pentanediamic acid
2-acetylamino-5-pentanediamic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
acetylglutamine
AcGln
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-acetylated L-glutamine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-acetylglycine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N-acetylglycine
A protein modification that effectively converts a glycine residue to N-acetylglycine.
PubMed:272676
http://purl.org/obo/owl/PubMed#PubMed_272676
PubMed:6754709
http://purl.org/obo/owl/PubMed#PubMed_6754709
PubMed:5545094
http://purl.org/obo/owl/PubMed#PubMed_5545094
RESID:AA0046
http://purl.org/obo/owl/RESID#RESID_AA0046
N-acetylated glycine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
aceturic acid
AcGly
2-(acetamido)ethanoic acid
2-(acetylamino)ethanoic acid
N-acetyl-L-isoleucine
This modification has not been observed to occur naturally.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
AcIle
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
acetylisoleucine
2-acetylamino-3-methylpentanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N-acetylated L-isoleucine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N-acetylisoleucine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine.
RESID:AA0047
http://purl.org/obo/owl/RESID#RESID_AA0047
PubMed:8034631
http://purl.org/obo/owl/PubMed#PubMed_8034631
(2S,3S)-2-acetamido-3-methylpentanoic acid
N2-acetyl-L-lysine
This modification has not been observed to occur naturally.
PSI-MOD
A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine.
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
RESID:AA0048
http://purl.org/obo/owl/RESID#RESID_AA0048
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N2-acetylated L-lysine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N2-acetyllysine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N2AcLys
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-2-acetamido-6-aminohexanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-acetylamino-6-aminohexanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Acetyl
N-acetyl-L-methionine
PSI-MOD
N-acetylmethionine
N-acetylated L-methionine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
AcMet
A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.
RESID:AA0049
http://purl.org/obo/owl/RESID#RESID_AA0049
PubMed:7944406
http://purl.org/obo/owl/PubMed#PubMed_7944406
methionamine
2-acetylamino-4-(methylthio)butanoic acid
acetylmethionine
2-acetylamino-4-(methylsulfanyl)butanoic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-acetamido-4-(methylsulfanyl)butanoic acid
N-acetyl-L-proline
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline.
RESID:AA0050
http://purl.org/obo/owl/RESID#RESID_AA0050
PubMed:2928307
http://purl.org/obo/owl/PubMed#PubMed_2928307
(2S)-1-acetyl-2-pyrrolidinecarboxylic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
acetylproline
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
1-acetylproline [misnomer]
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
NAcPro
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-acetylproline
N-acetylproline
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-acetylated L-proline
N-acetyl-L-serine
PSI-MOD
A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.
PubMed:2106685
http://purl.org/obo/owl/PubMed#PubMed_2106685
PubMed:6997045
http://purl.org/obo/owl/PubMed#PubMed_6997045
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
PubMed:1880797
http://purl.org/obo/owl/PubMed#PubMed_1880797
RESID:AA0051
http://purl.org/obo/owl/RESID#RESID_AA0051
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(S)-2-acetamido-3-hydroxypropanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-acetylated L-serine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N-acetylserine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-acetylamino-3-hydroxypropanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Acetyl
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
NAcSer
N-acetylserine
N-acetyl-L-threonine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
RESID:AA0052
http://purl.org/obo/owl/RESID#RESID_AA0052
PubMed:6997045
http://purl.org/obo/owl/PubMed#PubMed_6997045
PubMed:2106685
http://purl.org/obo/owl/PubMed#PubMed_2106685
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(2S,3R)-2-acetamido-3-hydroxybutanoic acid
NAcThr
N-acetylthreonine
N-acetylthreonine
N-acetylated L-threonine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Acetylation
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Acetyl
2-acetylamino-3-hydroxybutanoic acid
N-acetyl-L-tyrosine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.
PubMed:2506074
http://purl.org/obo/owl/PubMed#PubMed_2506074
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
RESID:AA0053
http://purl.org/obo/owl/RESID#RESID_AA0053
PubMed:475783
http://purl.org/obo/owl/PubMed#PubMed_475783
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
(S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid
2-acetylamino-3-(4-hydoxyphenyl)propanoic acid
Acetyl
AcTyr
N-acetylated L-tyrosine
N-acetyltyrosine
N-acetyltyrosine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-acetyl-L-valine
PSI-MOD
N-acetylvaline
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
2-acetylamino-3-methylbutanoic acid
(S)-2-acetamido-3-methylbutanoic acid
N-acetylated L-valine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
AcVal
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N-acetylvaline
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine.
PubMed:1735421
http://purl.org/obo/owl/PubMed#PubMed_1735421
RESID:AA0054
http://purl.org/obo/owl/RESID#RESID_AA0054
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N6-acetyl-L-lysine
PSI-MOD
A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine.
PubMed:670159
http://purl.org/obo/owl/PubMed#PubMed_670159
ChEBI:17752
http://purl.org/obo/owl/ChEBI#ChEBI_17752
RESID:AA0055
http://purl.org/obo/owl/RESID#RESID_AA0055
UniMod:1
http://purl.org/obo/owl/UniMod#UniMod_1
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:1680872
http://purl.org/obo/owl/PubMed#PubMed_1680872
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
PubMed:11369851
http://purl.org/obo/owl/PubMed#PubMed_11369851
DeltaMass:214
http://purl.org/obo/owl/DeltaMass#DeltaMass_214
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
(S)-2-amino-6-acetamidohexanoic acid
2-amino-6-acetylaminohexanoic acid
Acetylation
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Acetyl
N(zeta)-acetyllysine
epsilon-acetyllysine
N6-acetylated L-lysine
N6-acetyllysine
N6AcLys
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S-acetyl-L-cysteine
PSI-MOD
A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine.
UniMod:1
http://purl.org/obo/owl/UniMod#UniMod_1
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
RESID:AA0056
http://purl.org/obo/owl/RESID#RESID_AA0056
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:1310545
http://purl.org/obo/owl/PubMed#PubMed_1310545
S-acetylcysteine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
cysteine acetate thioester
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
SAcCys
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(R)-2-amino-3-(acetylsulfanyl)propanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-amino-3-(acetylthio)propanoic acid
Acetyl
Acetylation
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-formylglycine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
NFoGly
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-formylglycine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N-formylated glycine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a glycine residue to N-formylglycine.
PubMed:5139483
http://purl.org/obo/owl/PubMed#PubMed_5139483
RESID:AA0057
http://purl.org/obo/owl/RESID#RESID_AA0057
N(alpha)-formylglycine
formylaminoethanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-D-glucuronoylglycine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.
RESID:AA0058
http://purl.org/obo/owl/RESID#RESID_AA0058
PubMed:7398618
http://purl.org/obo/owl/PubMed#PubMed_7398618
UniMod:54
http://purl.org/obo/owl/UniMod#UniMod_54
PubMed:10858503
http://purl.org/obo/owl/PubMed#PubMed_10858503
PubMed:6493057
http://purl.org/obo/owl/PubMed#PubMed_6493057
PubMed:12716131
http://purl.org/obo/owl/PubMed#PubMed_12716131
NGlcAGly
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-myristoylglycine
PSI-MOD
(tetradecanoylamino)ethanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a glycine residue to N-myristoylglycine.
PubMed:11955008
http://purl.org/obo/owl/PubMed#PubMed_11955008
PubMed:1326520
http://purl.org/obo/owl/PubMed#PubMed_1326520
PubMed:1386601
http://purl.org/obo/owl/PubMed#PubMed_1386601
PubMed:6436247
http://purl.org/obo/owl/PubMed#PubMed_6436247
PubMed:11955007
http://purl.org/obo/owl/PubMed#PubMed_11955007
PubMed:7543369
http://purl.org/obo/owl/PubMed#PubMed_7543369
RESID:AA0059
http://purl.org/obo/owl/RESID#RESID_AA0059
UniMod:45
http://purl.org/obo/owl/UniMod#UniMod_45
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Myristoyl
N-(1-oxotetradecyl)glycine
Myristoylation
N-myristoylated glycine
N-myristoyl glycine
N-tetradecanoylglycine
N-myristylglycine
NMyrGly
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-palmitoyl-L-cysteine
incidental to RESID:AA0107 incidental to RESID:AA0309
PSI-MOD
(R)-2-hexadecanoylamino-3-sulfanylpropanoic acid
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine.
PubMed:4575979
http://purl.org/obo/owl/PubMed#PubMed_4575979
PubMed:10896212
http://purl.org/obo/owl/PubMed#PubMed_10896212
PubMed:9056182
http://purl.org/obo/owl/PubMed#PubMed_9056182
PubMed:9593755
http://purl.org/obo/owl/PubMed#PubMed_9593755
RESID:AA0060
http://purl.org/obo/owl/RESID#RESID_AA0060
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
NPamCys
N-palmitoylated L-cysteine
N-palmitoyl cysteine
N-(1-oxahexadecyl)-L-cysteine
2-hexadecanoylamino-3-mercaptopropanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Palmitoylation
Palmitoyl
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-methyl-L-alanine
PSI-MOD
N-methylalanine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(S)-2-methylaminopropanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N-methylalanine
A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine.
PubMed:337304
http://purl.org/obo/owl/PubMed#PubMed_337304
PubMed:323502
http://purl.org/obo/owl/PubMed#PubMed_323502
ChEBI:17519
http://purl.org/obo/owl/ChEBI#ChEBI_17519
RESID:AA0061
http://purl.org/obo/owl/RESID#RESID_AA0061
PubMed:7007074
http://purl.org/obo/owl/PubMed#PubMed_7007074
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-methylated L-alanine
NMeAla
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N,N,N-trimethyl-L-alanine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine.
PubMed:12590383
http://purl.org/obo/owl/PubMed#PubMed_12590383
PubMed:332162
http://purl.org/obo/owl/PubMed#PubMed_332162
PubMed:3979397
http://purl.org/obo/owl/PubMed#PubMed_3979397
PubMed:6778808
http://purl.org/obo/owl/PubMed#PubMed_6778808
PubMed:7715456
http://purl.org/obo/owl/PubMed#PubMed_7715456
RESID:AA0062
http://purl.org/obo/owl/RESID#RESID_AA0062
UniMod:37
http://purl.org/obo/owl/UniMod#UniMod_37
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-1-carboxy-N,N,N-trimethylethanaminium
(S)-2-(trimethylammonio)propanoic acid
N,N,N-trimethylalanine
N,N,N-trimethylated L-alanine
tri-Methylation
NMe3Ala
Trimethyl
N-methylglycine
DeltaMass also has an entry for the free amino acid
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a glycine residue to N-methylglycine.
RESID:AA0063
http://purl.org/obo/owl/RESID#RESID_AA0063
ChEBI:15611
http://purl.org/obo/owl/ChEBI#ChEBI_15611
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:1593629
http://purl.org/obo/owl/PubMed#PubMed_1593629
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
methylaminoacetic acid
methylaminoethanoic acid
L-sarcosine
Sarcosyl
Sar
Sarcosine
N-methylated glycine
NMeGly
N-methyl-L-methionine
PSI-MOD
NMeMet
N-methylmethionine
N-methylmethionine
N-methylated L-methionine
Methyl Methionyl
A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine.
DeltaMass:169
http://purl.org/obo/owl/DeltaMass#DeltaMass_169
PubMed:3298225
http://purl.org/obo/owl/PubMed#PubMed_3298225
RESID:AA0064
http://purl.org/obo/owl/RESID#RESID_AA0064
PubMed:323502
http://purl.org/obo/owl/PubMed#PubMed_323502
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(S)-2-methylamino-4-(methylsulfanyl)butanoic acid
2-methylamino-4-(methylthio)butanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N-methyl-L-phenylalanine
PSI-MOD
A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine.
PubMed:2577730
http://purl.org/obo/owl/PubMed#PubMed_2577730
PubMed:413571
http://purl.org/obo/owl/PubMed#PubMed_413571
RESID:AA0065
http://purl.org/obo/owl/RESID#RESID_AA0065
(S)-2-methylamino-3-phenylpropanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-methylated L-phenylalanine
N-methylphenylalanine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-methylphenylalanine
NMePhe
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N,N-dimethyl-L-proline
UniMod terminal specification corrected. [JSG]
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
NMe2Pro
stachydrin
N,N-dimethylated L-proline
N,N-dimethylproline
Dimethylation of proline residue
N,N-dimethyl-L-prolinium
Dimethyl
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
1,1-dimethyl-L-prolinium [misnomer]
Delta:H(5)C(2)
(S)-2-carboxy-1,1-dimethylpyrrolidinium
(S)-2-carboxy-1,1-dimethylpyrrolidinium
A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline.
ChEBI:21451
http://purl.org/obo/owl/ChEBI#ChEBI_21451
PubMed:12964758
http://purl.org/obo/owl/PubMed#PubMed_12964758
PubMed:14570711
http://purl.org/obo/owl/PubMed#PubMed_14570711
PubMed:193025
http://purl.org/obo/owl/PubMed#PubMed_193025
RESID:AA0066
http://purl.org/obo/owl/RESID#RESID_AA0066
UniMod:529
http://purl.org/obo/owl/UniMod#UniMod_529
PubMed:3882426
http://purl.org/obo/owl/PubMed#PubMed_3882426
PubMed:6254758
http://purl.org/obo/owl/PubMed#PubMed_6254758
omega-N,omega-N'-dimethyl-L-arginine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-arginine residue to N(omega),N'(omega)-dimethyl-L-arginine.
PubMed:14570711
http://purl.org/obo/owl/PubMed#PubMed_14570711
PubMed:12964758
http://purl.org/obo/owl/PubMed#PubMed_12964758
PubMed:2426402
http://purl.org/obo/owl/PubMed#PubMed_2426402
PubMed:15835918
http://purl.org/obo/owl/PubMed#PubMed_15835918
RESID:AA0067
http://purl.org/obo/owl/RESID#RESID_AA0067
PubMed:5128665
http://purl.org/obo/owl/PubMed#PubMed_5128665
UniMod:36
http://purl.org/obo/owl/UniMod#UniMod_36
Symmetric dimethylarginine
symmetric dimethylarginine
NG,N'G-dimethylarginine
NoNo'Me2Arg
omega-N,omega-N'-dimethylated L-arginine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N5-[(methylamino)(methylimino)methyl]ornithine
N3,N4-dimethylarginine
Dimethyl
di-Methylation
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid
omega-N,omega-N-dimethyl-L-arginine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-arginine residue to N(omega),N(omega)-dimethyl-L-arginine.
PubMed:15835918
http://purl.org/obo/owl/PubMed#PubMed_15835918
PubMed:14570711
http://purl.org/obo/owl/PubMed#PubMed_14570711
PubMed:3032834
http://purl.org/obo/owl/PubMed#PubMed_3032834
UniMod:36
http://purl.org/obo/owl/UniMod#UniMod_36
RESID:AA0068
http://purl.org/obo/owl/RESID#RESID_AA0068
PubMed:12964758
http://purl.org/obo/owl/PubMed#PubMed_12964758
PubMed:11152131
http://purl.org/obo/owl/PubMed#PubMed_11152131
ChEBI:17929
http://purl.org/obo/owl/ChEBI#ChEBI_17929
NG,NG-dimethylarginine
omega-N,omega-N-dimethlyated L-arginine
N5-[(dimethylamino)(imino)methyl]ornithine
asymmetric dimethylarginine
Asymmetric dimethylarginine
Dimethyl
di-Methylation
(S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
NoNoMe2Arg
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
omega-N-methyl-L-arginine
PSI-MOD
Methyl
A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine.
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0069
http://purl.org/obo/owl/RESID#RESID_AA0069
PubMed:5128665
http://purl.org/obo/owl/PubMed#PubMed_5128665
PubMed:2426402
http://purl.org/obo/owl/PubMed#PubMed_2426402
PubMed:15835918
http://purl.org/obo/owl/PubMed#PubMed_15835918
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
NG-methylarginine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Methylation
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
omega-N-methylated L-arginine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Omega-N-methylarginine
(S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
NoMeArg
N4-methyl-L-asparagine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine.
RESID:AA0070
http://purl.org/obo/owl/RESID#RESID_AA0070
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
PubMed:2356973
http://purl.org/obo/owl/PubMed#PubMed_2356973
PubMed:3782095
http://purl.org/obo/owl/PubMed#PubMed_3782095
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N4MeAsn
N4-methylated L-asparagine
N4-methylasparagine
N-methylasparagine
N(gamma)-methylasparagine
Methylation
beta-methylasparagine [misnomer]
Methyl
(S)-2-amino-N4-methylbutanediamic acid
N5-methyl-L-glutamine
PSI-MOD
Methyl
2-amino-N5-methylpentanediamic acid
gamma-methylglutamine
(2S)-2-amino-5-methylamino-5-oxopentanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine.
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0071
http://purl.org/obo/owl/RESID#RESID_AA0071
PubMed:365579
http://purl.org/obo/owl/PubMed#PubMed_365579
ChEBI:17592
http://purl.org/obo/owl/ChEBI#ChEBI_17592
DeltaMass:166
http://purl.org/obo/owl/DeltaMass#DeltaMass_166
PubMed:11118225
http://purl.org/obo/owl/PubMed#PubMed_11118225
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
N5-methylglutamine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N5MeGln
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Methylation
N(delta)-methylglutamine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N-methylglutamine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N5-methylated L-glutamine
L-glutamic acid 5-methyl ester (Glu)
DeltaMass gives the formula "C 6 H 9 O 1 N 3" with mass 143 [JSG].
PSI-MOD
O5MeGlu
O-methyl Glutamyl
Glutamate methyl ester (Glu)
5-methyl esterified L-glutamic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester.
PubMed:16888
http://purl.org/obo/owl/PubMed#PubMed_16888
PubMed:6300110
http://purl.org/obo/owl/PubMed#PubMed_6300110
RESID:AA0072
http://purl.org/obo/owl/RESID#RESID_AA0072
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
DeltaMass:167
http://purl.org/obo/owl/DeltaMass#DeltaMass_167
3'-methyl-L-histidine
PSI-MOD
N(delta)-methylhistidine
NprosMeHis
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
pi-methylhistidine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine).
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0073
http://purl.org/obo/owl/RESID#RESID_AA0073
PubMed:8645219
http://purl.org/obo/owl/PubMed#PubMed_8645219
PubMed:10660523
http://purl.org/obo/owl/PubMed#PubMed_10660523
PubMed:3467365
http://purl.org/obo/owl/PubMed#PubMed_3467365
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:8076
http://purl.org/obo/owl/PubMed#PubMed_8076
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
1-methylhistidine [misnomer]
(S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid
Methylation
Methyl
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
pros-methylhistidine
Pros-methylhistidine
pros-methylated L-histidine
N6,N6,N6-trimethyl-L-lysine
DeltaMass calculates the mass difference from protonated lysine rather than neutral lysine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine.
PubMed:8453381
http://purl.org/obo/owl/PubMed#PubMed_8453381
RESID:AA0074
http://purl.org/obo/owl/RESID#RESID_AA0074
UniMod:37
http://purl.org/obo/owl/UniMod#UniMod_37
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:12590383
http://purl.org/obo/owl/PubMed#PubMed_12590383
ChEBI:17311
http://purl.org/obo/owl/ChEBI#ChEBI_17311
PubMed:6778808
http://purl.org/obo/owl/PubMed#PubMed_6778808
PubMed:7093227
http://purl.org/obo/owl/PubMed#PubMed_7093227
PubMed:3145979
http://purl.org/obo/owl/PubMed#PubMed_3145979
PubMed:4304194
http://purl.org/obo/owl/PubMed#PubMed_4304194
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Trimethyl
tri-Methylation
(S)-2-amino-6-(trimethylammonio)hexanoic acid
(S)-5-amino-5-carboxy-N,N,N-trimethyl-1-pentanaminium
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-trimethylation (of lysine)
N6,N6,N6-trimethylated L-lysine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
epsilon-trimethyllysine
N(zeta)-trimethyllysine
N6,N6,N6-trimethyllysin-N6-ium
N6Me3Lys
N6,N6,N6-trimethyllysine
N6,N6-dimethyl-L-lysine
PSI-MOD
(S)-2-amino-6-dimethylaminohexanoic acid
di-Methylation
Dimethyl
epsilon-dimethyllysine
lysine derivative Lys(y)
N(zeta)-dimethyllysine
N6,N6-dimethylated L-lysine
A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine.
PubMed:10550045
http://purl.org/obo/owl/PubMed#PubMed_10550045
RESID:AA0075
http://purl.org/obo/owl/RESID#RESID_AA0075
UniMod:36
http://purl.org/obo/owl/UniMod#UniMod_36
PubMed:12964758
http://purl.org/obo/owl/PubMed#PubMed_12964758
PubMed:14570711
http://purl.org/obo/owl/PubMed#PubMed_14570711
PubMed:3100523
http://purl.org/obo/owl/PubMed#PubMed_3100523
PubMed:8453381
http://purl.org/obo/owl/PubMed#PubMed_8453381
N6,N6-dimethyllysine
N6Me2Lys
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N6-methyl-L-lysine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Methylation
Methyl
epsilon-methyllysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N(zeta)-methyllysine
A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
PubMed:3926756
http://purl.org/obo/owl/PubMed#PubMed_3926756
RESID:AA0076
http://purl.org/obo/owl/RESID#RESID_AA0076
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
ChEBI:17604
http://purl.org/obo/owl/ChEBI#ChEBI_17604
DeltaMass:165
http://purl.org/obo/owl/DeltaMass#DeltaMass_165
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
(S)-2-amino-6-methylaminohexanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N-methyl Lysyl
N6-methylated L-lysine
N6-methyllysine
N6MeLys
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N6-palmitoyl-L-lysine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N(zeta)-palmitoyllysine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N6-(1-oxohexadecyl)-L-lysine
N6-palmitoyl lysine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N6-palmitoylated L-lysine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N6PamLys
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Palmitoyl
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Palmitoylation
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine.
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
RESID:AA0077
http://purl.org/obo/owl/RESID#RESID_AA0077
PubMed:2498336
http://purl.org/obo/owl/PubMed#PubMed_2498336
PubMed:7801126
http://purl.org/obo/owl/PubMed#PubMed_7801126
PubMed:7939682
http://purl.org/obo/owl/PubMed#PubMed_7939682
epsilon-palmitoyllysine
(S)-2-amino-6-(hexadecanoylamino)hexanoic acid
N6-myristoyl-L-lysine
PSI-MOD
N6-myristoyl lysine
N6MyrLys
N6-myristoylated L-lysine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine.
RESID:AA0078
http://purl.org/obo/owl/RESID#RESID_AA0078
UniMod:45
http://purl.org/obo/owl/UniMod#UniMod_45
PubMed:8346241
http://purl.org/obo/owl/PubMed#PubMed_8346241
PubMed:1402651
http://purl.org/obo/owl/PubMed#PubMed_1402651
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Myristoylation
Myristoyl
epsilon-myristoyllysine
(S)-2-amino-6-(tetradecanoylamino)hexanoic acid
N6-(1-oxotetradecyl)-L-lysine
N(zeta)-myristoyllysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-palmitoyl-L-threonine
PSI-MOD
O3-palmitoyl-threonine
O-palmitoylated L-threonine
threonine palmitate ester
Palmitoylation
Palmitoyl
OPamThr
(2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid
L-threonine hexadecanoate ester
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine.
PubMed:8413602
http://purl.org/obo/owl/PubMed#PubMed_8413602
RESID:AA0079
http://purl.org/obo/owl/RESID#RESID_AA0079
PubMed:6642431
http://purl.org/obo/owl/PubMed#PubMed_6642431
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
O-palmitoyl threonine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
O-palmitoyl-L-serine
PSI-MOD
A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine.
RESID:AA0080
http://purl.org/obo/owl/RESID#RESID_AA0080
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
PubMed:3467339
http://purl.org/obo/owl/PubMed#PubMed_3467339
(2S,3R)-2-amino-3-(hexadecanoyloxy)propanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-serine hexadecanoate ester
O-palmitoylated L-serine
O-palmitoyl serine
OPamSer
O3-palmitoyl-serine
Palmitoylation
Palmitoyl
serine palmitate ester
L-alanine amide
PSI-MOD
A protein modification that effectively converts an L-alanine residue to L-alanine amide.
RESID:AA0081
http://purl.org/obo/owl/RESID#RESID_AA0081
PubMed:952951
http://purl.org/obo/owl/PubMed#PubMed_952951
PubMed:8472537
http://purl.org/obo/owl/PubMed#PubMed_8472537
PubMed:2069951
http://purl.org/obo/owl/PubMed#PubMed_2069951
PubMed:1377792
http://purl.org/obo/owl/PubMed#PubMed_1377792
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-2-aminopropanamide
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
AlaN
alaninamide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Alanine amide
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
amidated L-alanine
L-arginine amide
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-arginine residue to L-arginine amide.
PubMed:2229025
http://purl.org/obo/owl/PubMed#PubMed_2229025
PubMed:2753890
http://purl.org/obo/owl/PubMed#PubMed_2753890
RESID:AA0082
http://purl.org/obo/owl/RESID#RESID_AA0082
PubMed:743209
http://purl.org/obo/owl/PubMed#PubMed_743209
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Arginine amide
argininamide
ArgN
(S)-2-amino-5-carbamimidamidopentanamide
amidated L-arginine
2-amino-5-guanidinopentanamide
L-asparagine amide
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-2-amino-butanediamide
amidated L-asparagine
AsnN
asparaginamide
Asparagine amide
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-asparagine residue to L-asparagine amide.
PubMed:279902
http://purl.org/obo/owl/PubMed#PubMed_279902
PubMed:2753132
http://purl.org/obo/owl/PubMed#PubMed_2753132
RESID:AA0083
http://purl.org/obo/owl/RESID#RESID_AA0083
PubMed:3415690
http://purl.org/obo/owl/PubMed#PubMed_3415690
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-aspartic acid 1-amide
PSI-MOD
isoasparagine
AspN
(S)-2-amino-1-butanediamic acid
Aspartic acid 1-amide
3,4-diamino-4-oxabutanoic acid
1-amidated L-aspartic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide.
PubMed:2542051
http://purl.org/obo/owl/PubMed#PubMed_2542051
RESID:AA0084
http://purl.org/obo/owl/RESID#RESID_AA0084
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
L-cysteine amide
PSI-MOD
amidated L-cysteine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
CysN
cysteinamide
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Cysteine amide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.
PubMed:7149738
http://purl.org/obo/owl/PubMed#PubMed_7149738
RESID:AA0085
http://purl.org/obo/owl/RESID#RESID_AA0085
PubMed:1892838
http://purl.org/obo/owl/PubMed#PubMed_1892838
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(R)-2-amino-3-sulfanylpropanamide
2-amino-3-mercaptopropanamide
L-glutamine amide
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
GlnN
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-glutamine residue to L-glutamine amide.
PubMed:7673220
http://purl.org/obo/owl/PubMed#PubMed_7673220
RESID:AA0086
http://purl.org/obo/owl/RESID#RESID_AA0086
PubMed:9048550
http://purl.org/obo/owl/PubMed#PubMed_9048550
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
amidated L-glutamine
(S)-2-amino-pentanediamide
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
glutaminamide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Glutamine amide
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-glutamic acid 1-amide
PSI-MOD
(S)-2-amino-1-pentanediamic acid
A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide.
PubMed:1093875
http://purl.org/obo/owl/PubMed#PubMed_1093875
PubMed:14550575
http://purl.org/obo/owl/PubMed#PubMed_14550575
RESID:AA0087
http://purl.org/obo/owl/RESID#RESID_AA0087
4,5-diamino-5-oxapentanoic acid
1-amidated L-glutamic acid
Glutamic acid 1-amide
GluN
isoglutamine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
glycine amide
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Glycine amide
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
amidated glycine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
2-aminoethanamide
2-aminoacetamide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
GlyN
A protein modification that effectively converts a glycine residue to glycine amide.
PubMed:13591312
http://purl.org/obo/owl/PubMed#PubMed_13591312
RESID:AA0088
http://purl.org/obo/owl/RESID#RESID_AA0088
L-histidine amide
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
amidated L-histidine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-amino-3-(1H-imidazol-4-yl)propanamide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-histidine residue to L-histidine amide.
PubMed:2839478
http://purl.org/obo/owl/PubMed#PubMed_2839478
RESID:AA0089
http://purl.org/obo/owl/RESID#RESID_AA0089
PubMed:2307683
http://purl.org/obo/owl/PubMed#PubMed_2307683
PubMed:2153586
http://purl.org/obo/owl/PubMed#PubMed_2153586
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Histidine amide
histidinamide
HisN
L-isoleucine amide
PSI-MOD
IleN
isoleucinamide
Isoleucine amide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide.
RESID:AA0090
http://purl.org/obo/owl/RESID#RESID_AA0090
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
amidated L-isoleucine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(2S,3S)-2-amino-3-methylpentanamide
L-leucine amide
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
amidated L-leucine
(S)-2-amino-4-methylpentanamide
Leucine amide
leucinamide
LeuN
A protein modification that effectively converts an L-leucine residue to L-leucine amide.
RESID:AA0091
http://purl.org/obo/owl/RESID#RESID_AA0091
PubMed:2578459
http://purl.org/obo/owl/PubMed#PubMed_2578459
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-lysine amide
PSI-MOD
Lysine amide
LysN
amidated L-lysine
lysinamide
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-lysine residue to L-lysine amide.
RESID:AA0092
http://purl.org/obo/owl/RESID#RESID_AA0092
PubMed:6579533
http://purl.org/obo/owl/PubMed#PubMed_6579533
(S)-2,6-diaminohexanamide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-methionine amide
PSI-MOD
A protein modification that effectively converts an L-methionine residue to L-methionine amide.
PubMed:4375977
http://purl.org/obo/owl/PubMed#PubMed_4375977
RESID:AA0093
http://purl.org/obo/owl/RESID#RESID_AA0093
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
2-amino-4-(methylthio)butanamide
amidated L-methionine
methioninamide
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Methionine amide
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MetN
(S)-2-amino-4-(methylsulfanyl)butanamide
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
L-phenylalanine amide
PSI-MOD
A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.
PubMed:8868490
http://purl.org/obo/owl/PubMed#PubMed_8868490
RESID:AA0094
http://purl.org/obo/owl/RESID#RESID_AA0094
PubMed:2905621
http://purl.org/obo/owl/PubMed#PubMed_2905621
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
amidated L-phenylalanine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-amino-3-phenylpropanamide
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
PheN
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Phenylalanine amide
phenylalaninamide
L-proline amide
PSI-MOD
Proline amide
amidated L-proline
A protein modification that effectively converts an L-proline residue to L-proline amide.
PubMed:5760861
http://purl.org/obo/owl/PubMed#PubMed_5760861
RESID:AA0095
http://purl.org/obo/owl/RESID#RESID_AA0095
PubMed:4982117
http://purl.org/obo/owl/PubMed#PubMed_4982117
prolinamide
(S)-pyrrolidine-2-carboxamide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
ProN
L-serine amide
PSI-MOD
(S)-2-amino-3-hydroxypropanamide
amidated L-serine
serinamide
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Serine amide
SerN
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-serine residue to L-serine amide.
RESID:AA0096
http://purl.org/obo/owl/RESID#RESID_AA0096
PubMed:743209
http://purl.org/obo/owl/PubMed#PubMed_743209
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
L-threonine amide
PSI-MOD
ThrN
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(2S,3R)-2-amino-3-hydroxybutanamide
amidated L-threonine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
threoninamide
Threonine amide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-threonine residue to L-threonine amide.
RESID:AA0097
http://purl.org/obo/owl/RESID#RESID_AA0097
PubMed:1390774
http://purl.org/obo/owl/PubMed#PubMed_1390774
L-tryptophan amide
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
TrpN
amidated L-tryptophan
(S)-2-amino-3-(1H-indol-3-yl)propanamide
tryptophanamide
Tryptophan amide
A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.
RESID:AA0098
http://purl.org/obo/owl/RESID#RESID_AA0098
PubMed:3947348
http://purl.org/obo/owl/PubMed#PubMed_3947348
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-tyrosine amide
PSI-MOD
Tyrosine amide
amidated L-tyrosine
TyrN
(S)-2-amino-3-(4-hydoxyphenyl)propanamide
tyrosinamide
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.
RESID:AA0099
http://purl.org/obo/owl/RESID#RESID_AA0099
PubMed:3562898
http://purl.org/obo/owl/PubMed#PubMed_3562898
PubMed:6509012
http://purl.org/obo/owl/PubMed#PubMed_6509012
PubMed:1377792
http://purl.org/obo/owl/PubMed#PubMed_1377792
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
L-valine amide
PSI-MOD
(S)-2-amino-3-methylbutanamide
valinamide
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
ValN
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Valine amide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-valine residue to L-valine amide.
PubMed:2578459
http://purl.org/obo/owl/PubMed#PubMed_2578459
PubMed:5465996
http://purl.org/obo/owl/PubMed#PubMed_5465996
RESID:AA0100
http://purl.org/obo/owl/RESID#RESID_AA0100
L-cysteine methyl disulfide
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-amino-3-(methyldithio)propanoic acid
Beta-methylthiolation
(R)-2-amino-3-(methyldisulfanediyl)propanoic acid
Methylthio
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide.
PubMed:2056535
http://purl.org/obo/owl/PubMed#PubMed_2056535
UniMod:39
http://purl.org/obo/owl/UniMod#UniMod_39
RESID:AA0101
http://purl.org/obo/owl/RESID#RESID_AA0101
PubMed:6381494
http://purl.org/obo/owl/PubMed#PubMed_6381494
PubMed:10555576
http://purl.org/obo/owl/PubMed#PubMed_10555576
S-methyl thiocysteine
Cysteine methyl disulfide
L-3-(methyldithio)alanine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-farnesyl-L-cysteine
From DeltaMass: (name misspelled "S-farnesyl cystenyl")
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
S-farnesyl Cystenyl
S-farnesyl cysteine
SFarnCys
2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid
Farnesylation
(R,E,E)-2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylsulfanyl)propanoic acid
Farnesyl
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine.
UniMod:44
http://purl.org/obo/owl/UniMod#UniMod_44
RESID:AA0102
http://purl.org/obo/owl/RESID#RESID_AA0102
PubMed:2684976
http://purl.org/obo/owl/PubMed#PubMed_2684976
PubMed:1872463
http://purl.org/obo/owl/PubMed#PubMed_1872463
PubMed:15609361
http://purl.org/obo/owl/PubMed#PubMed_15609361
PubMed:1409665
http://purl.org/obo/owl/PubMed#PubMed_1409665
DeltaMass:293
http://purl.org/obo/owl/DeltaMass#DeltaMass_293
S-12-hydroxyfarnesyl-L-cysteine
PSI-MOD
Hydroxyfarnesyl
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine.
UniMod:376
http://purl.org/obo/owl/UniMod#UniMod_376
RESID:AA0103
http://purl.org/obo/owl/RESID#RESID_AA0103
PubMed:17790543
http://purl.org/obo/owl/PubMed#PubMed_17790543
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
S12HyFarnCys
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid
(R,E,E,Z)-2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylsulfanyl)propanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S-12-hydroxyfarnesyl cysteine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
hydroxyfarnesyl
S-geranylgeranyl-L-cysteine
DeltaMass calculates the mass with two double bonds rather than four
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-geranylgeranyl cysteine
SGergerCys
S-geranylgeranyl
GeranylGeranyl
Geranyl-geranyl
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:1483450
http://purl.org/obo/owl/PubMed#PubMed_1483450
PubMed:15609361
http://purl.org/obo/owl/PubMed#PubMed_15609361
RESID:AA0104
http://purl.org/obo/owl/RESID#RESID_AA0104
UniMod:48
http://purl.org/obo/owl/UniMod#UniMod_48
(R,E,E,E)-2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylsulfanyl)propanoic acid
2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-cysteine methyl ester
Secondary to RESID:AA0102; secondary to RESID:AA0103; secondary to RESID:AA0104.
PSI-MOD
2-amino-3-mercaptopropanoic methyl ester
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
methyl L-cysteinate
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Methylation
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
methyl (2R)-2-amino-3-sulfanylpropanoate
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
methyl esterified L-cysteine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
OMeCys
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester.
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0105
http://purl.org/obo/owl/RESID#RESID_AA0105
PubMed:1872463
http://purl.org/obo/owl/PubMed#PubMed_1872463
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
mecysteine
Methyl
2-amino-3-sulfanylpropanoic methyl ester
Cysteine methyl ester
S-palmitoyl-L-cysteine
From DeltaMass: (name misspelled "S-palmityl Cystenyl" and formula incorrect, N and O reversed) Formula: C19H35O1N2S1 Monoisotopic Mass Change: 341.239 Average Mass Change: 341.556
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Palmitoyl
A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.
PubMed:3166978
http://purl.org/obo/owl/PubMed#PubMed_3166978
PubMed:8180229
http://purl.org/obo/owl/PubMed#PubMed_8180229
PubMed:8824274
http://purl.org/obo/owl/PubMed#PubMed_8824274
RESID:AA0106
http://purl.org/obo/owl/RESID#RESID_AA0106
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
DeltaMass:303
http://purl.org/obo/owl/DeltaMass#DeltaMass_303
PubMed:1872406
http://purl.org/obo/owl/PubMed#PubMed_1872406
Palmitoylation
S-palmitoyl cysteine
S-palmitoylated L-cysteine
S-palmityl Cystenyl
SPamCys
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid
cysteine hexadecanoate thioester
2-amino-3-(hexadecanoylthio)propanoic acid
cysteine palmitate thioester
S-diacylglycerol-L-cysteine
Incidental to RESID:AA0060.
PSI-MOD
S-diacylglycerol cysteine
S-(2',3'-diacylglycerol)-L-cysteine
S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine
diacylglycerol
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(R)-2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid
Diacylglycerol
2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid
A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine.
PubMed:10896212
http://purl.org/obo/owl/PubMed#PubMed_10896212
PubMed:4575979
http://purl.org/obo/owl/PubMed#PubMed_4575979
PubMed:9056182
http://purl.org/obo/owl/PubMed#PubMed_9056182
RESID:AA0107
http://purl.org/obo/owl/RESID#RESID_AA0107
UniMod:377
http://purl.org/obo/owl/UniMod#UniMod_377
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
S-(L-isoglutamyl)-L-cysteine
Cross-link 2; DeltaMass calculates the mass difference from glutamic acid rather than glutamine.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(S)-2-amino-5-((R)-2-amino-2-carboxyethyl)sulfanyl-5-oxopentanoic acid
(S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid
gamma-(S-cysteinyl)glutamic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond to form S-(L-isoglutamyl)-L-cysteine.
ChEBI:22021
http://purl.org/obo/owl/ChEBI#ChEBI_22021
RESID:AA0108
http://purl.org/obo/owl/RESID#RESID_AA0108
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:6838833
http://purl.org/obo/owl/PubMed#PubMed_6838833
S-gamma-glutamyl (crosslinked to cysteine)
Isoglutamyl cysteine thioester (Cys-Gln)
2'-(S-L-cysteinyl)-L-histidine
Cross-link 2.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(S)-2-amino-3-[2-((R)-2-amino-2-carboxyethyl)sulfanylimidazol-4-yl]propanoic acid
2'-(S-cysteinyl)-histidine (Cys-His)
S-(2'-histidyl)cysteine
A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0109
http://purl.org/obo/owl/RESID#RESID_AA0109
PubMed:6210696
http://purl.org/obo/owl/PubMed#PubMed_6210696
S-(2-histidyl)- (crosslinked to cysteine)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-lanthionine
Cross-link 2.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
ChEBI:21347
http://purl.org/obo/owl/ChEBI#ChEBI_21347
DeltaMass:7
http://purl.org/obo/owl/DeltaMass#DeltaMass_7
RESID:AA0110
http://purl.org/obo/owl/RESID#RESID_AA0110
(R,R)-bis(2-amino-2-carboxyethyl)sulfanediyl
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-2,6-diamino-4-thiaheptanedioic acid
(R)-S-(2-amino-2-carboxyethyl)-L-cysteine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
3,3'-thiobis-L-alanine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
(R,R)-bis(2-amino-2-carboxyethyl)sulfide
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
meso-lanthionine
Cross-link 2. This modification has not been observed to occur naturally.
PSI-MOD
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine.
PubMed:15023056
http://purl.org/obo/owl/PubMed#PubMed_15023056
RESID:AA0111
http://purl.org/obo/owl/RESID#RESID_AA0111
PubMed:3769923
http://purl.org/obo/owl/PubMed#PubMed_3769923
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(R,S)-bis(2-amino-2-carboxyethyl)sulfanediyl
(R,S)-3,3'-thiobis-(2-aminopropanoic acid)
(R,S)-2,6-diamino-4-thiaheptanedioic acid
(R)-S-(2-amino-2-carboxyethyl)-D-cysteine
Lanthionine (Ser-Cys)
cysteine-3-D-alanine thioether
3,3'-thiobis-meso-alanine
(R,S)-bis(2-amino-2-carboxyethyl)sulfide
3-methyl-L-lanthionine
Cross-link 2.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyl-L-lanthionine.
PubMed:3769923
http://purl.org/obo/owl/PubMed#PubMed_3769923
RESID:AA0112
http://purl.org/obo/owl/RESID#RESID_AA0112
(2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)sulfanyl]butanoic acid
(2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
(2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
(2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
Beta-methyllanthionine (Thr-Cys)
cysteine-3-D-butyrine thioether
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
3'-(S-L-cysteinyl)-L-tyrosine
Cross-link 2.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine.
PubMed:15917234
http://purl.org/obo/owl/PubMed#PubMed_15917234
RESID:AA0113
http://purl.org/obo/owl/RESID#RESID_AA0113
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2002850
http://purl.org/obo/owl/PubMed#PubMed_2002850
S-(3-Tyr) (Crosslinked to Cysteine)
S-(3'-tyrosinyl)cysteine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
XLNKSCys3'Tyr
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S,R)-2-amino-3-[3-(2-amino-2-carboxyethylsulfanyl)-4-hydroxyphenyl]propanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
3'-(S-cysteinyl)-tyrosine (Tyr-Cys)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N6-carboxy-L-lysine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N6CbxLys
N6-carboxylysine
N6-carboxylysine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine.
PubMed:11369851
http://purl.org/obo/owl/PubMed#PubMed_11369851
PubMed:4436319
http://purl.org/obo/owl/PubMed#PubMed_4436319
PubMed:637859
http://purl.org/obo/owl/PubMed#PubMed_637859
PubMed:7754395
http://purl.org/obo/owl/PubMed#PubMed_7754395
RESID:AA0114
http://purl.org/obo/owl/RESID#RESID_AA0114
UniMod:299
http://purl.org/obo/owl/UniMod#UniMod_299
2-amino-6-carbamic hexanoic acid
(S)-2-amino-6-(carboxyamino)hexanoic acid
Carboxylation
Carboxy
N6-carbamyllysine [misnomer]
lysine NZ-carboxylic acid
N6-1-carboxyethyl-L-lysine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine.
PubMed:3123486
http://purl.org/obo/owl/PubMed#PubMed_3123486
RESID:AA0115
http://purl.org/obo/owl/RESID#RESID_AA0115
UniMod:378
http://purl.org/obo/owl/UniMod#UniMod_378
PubMed:8253186
http://purl.org/obo/owl/PubMed#PubMed_8253186
PubMed:8421682
http://purl.org/obo/owl/PubMed#PubMed_8421682
Carboxyethyl
(S,S)-2-amino-6-(1-carboxyethyl)aminohexanoic acid
NZ-(1-carboxyethyl)lysine
N6-1-carboxyethyl lysine
N6-(1-carboxyethyl)lysine
carboxyethyl
Hypusine
PSI-MOD
A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine.
UniMod:379
http://purl.org/obo/owl/UniMod#UniMod_379
RESID:AA0116
http://purl.org/obo/owl/RESID#RESID_AA0116
PubMed:8108861
http://purl.org/obo/owl/PubMed#PubMed_8108861
PubMed:6806267
http://purl.org/obo/owl/PubMed#PubMed_6806267
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S,R)-2-amino-6-(4-amino-2-hydroxybutylamino)hexanoic acid
N-(4-NH2-2-OH-butyl)- (of Lysine)
Hypusine
hypusine
Hypusine
hypusine
Hypu
N6-biotinyl-L-lysine
From DeltaMass: Average Mass: 354 Formula:C 16 H 26 O 4 N 3 S 1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:354.172 Average Mass Change:354.471 References:PE Sciex.
PSI-MOD
A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine.
PubMed:7948875
http://purl.org/obo/owl/PubMed#PubMed_7948875
PubMed:16109483
http://purl.org/obo/owl/PubMed#PubMed_16109483
PubMed:3178228
http://purl.org/obo/owl/PubMed#PubMed_3178228
DeltaMass:305
http://purl.org/obo/owl/DeltaMass#DeltaMass_305
UniMod:3
http://purl.org/obo/owl/UniMod#UniMod_3
RESID:AA0117
http://purl.org/obo/owl/RESID#RESID_AA0117
PubMed:8747466
http://purl.org/obo/owl/PubMed#PubMed_8747466
(S)-2-amino-6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]aminohexanoic acid
biocytin
(3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Biotin (covalent)
Biotin
Biotinylation
biotinyl lysyl
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
epsilon-N-biotinyllysine
N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine
N6-biotinyllysine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N6-lipoyl-L-lysine
From DeltaMass: Average Mass: 188.
PSI-MOD
(S)-2-amino-6-[5-((R)-1,2-dithiolan-3-yl)pentanamido]hexanoic acid
2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid
Lipoyl
Lipoyl
Lipoyl (covalent)
N-Lipoyl- (on Lysine)
N6-6,8-dithiooctanoyllysine
N6-lipoyllysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine.
PubMed:3522581
http://purl.org/obo/owl/PubMed#PubMed_3522581
PubMed:3421911
http://purl.org/obo/owl/PubMed#PubMed_3421911
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:42
http://purl.org/obo/owl/UniMod#UniMod_42
RESID:AA0118
http://purl.org/obo/owl/RESID#RESID_AA0118
PubMed:7719855
http://purl.org/obo/owl/PubMed#PubMed_7719855
N6-pyridoxal phosphate-L-lysine
From DeltaMass: Average Mass: 231
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine.
PubMed:1544460
http://purl.org/obo/owl/PubMed#PubMed_1544460
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0119
http://purl.org/obo/owl/RESID#RESID_AA0119
UniMod:46
http://purl.org/obo/owl/UniMod#UniMod_46
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Pyridoxal phosphate (Schiff Base formed to lysine)
PyridoxalPhosphate
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-2-amino-6-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-4-pyridine)methyleneamino]hexanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Pyridoxal phosphate
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Pyridoxal phosphate (covalent)
N6-retinylidene-L-lysine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Retinylidene
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Retinal chromophore (covalent)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
retinal
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N6-retinyl-lysine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N6-retinal-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.
UniMod:380
http://purl.org/obo/owl/UniMod#UniMod_380
RESID:AA0120
http://purl.org/obo/owl/RESID#RESID_AA0120
PubMed:6870827
http://purl.org/obo/owl/PubMed#PubMed_6870827
PubMed:6794028
http://purl.org/obo/owl/PubMed#PubMed_6794028
(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-allysine
From DeltaMass: Average Mass: -1
PSI-MOD
Lys->Allysine
alpha-amino-adipic acid delta-semialdahyde
Oxidation of lysine (to aminoadipic semialdehyde)
Lysine oxidation to aminoadipic semialdehyde
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
5-formyl-norvaline
6-oxonorleucine
Allysine
Allysine (from Lysine)
A protein modification that effectively converts an L-lysine residue to L-allysine.
PubMed:358196
http://purl.org/obo/owl/PubMed#PubMed_358196
ChEBI:17917
http://purl.org/obo/owl/ChEBI#ChEBI_17917
PubMed:11332453
http://purl.org/obo/owl/PubMed#PubMed_11332453
PubMed:5529814
http://purl.org/obo/owl/PubMed#PubMed_5529814
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:11120890
http://purl.org/obo/owl/PubMed#PubMed_11120890
PubMed:5337886
http://purl.org/obo/owl/PubMed#PubMed_5337886
UniMod:352
http://purl.org/obo/owl/UniMod#UniMod_352
RESID:AA0121
http://purl.org/obo/owl/RESID#RESID_AA0121
(S)-2-amino-6-oxohexanoic acid
2-amino-5-formylvaleric acid
2-amino-adipic acid semialdahyde
2-aminoadipate 6-semialdehyde
L-2-aminoadipic acid
From DeltaMass: Average Mass: 15 Monoisotopic Mass Change:14.97 Average Mass Change:15 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. Notes:Expected reaction following oxidation of lysine to aminoadipic semialdehyde. Not proven experimentally but deduced by reference to the similar known reaction of oxidation of Arg to Glu via the semialdehyde.
PSI-MOD
modification from RESID
PubMed:358196
http://purl.org/obo/owl/PubMed#PubMed_358196
PubMed:336041
http://purl.org/obo/owl/PubMed#PubMed_336041
PubMed:7419498
http://purl.org/obo/owl/PubMed#PubMed_7419498
RESID:AA0122
http://purl.org/obo/owl/RESID#RESID_AA0122
DeltaMass:353
http://purl.org/obo/owl/DeltaMass#DeltaMass_353
UniMod:381
http://purl.org/obo/owl/UniMod#UniMod_381
(S)-2-aminohexanedioic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
alpha-amino adipic acid
2-amino-1,4-butanedicarboxylic acid
Lys->AminoadipicAcid
L-alpha-aminoadipic acid
Oxidation of lysine (to aminoadipic acid)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-lysinoalanine
Cross-link 2 From DeltaMass: Average Mass: -34.
PSI-MOD
(2S)-2-amino-6-((2Xi)-2-amino-2-carboxyethylamino)hexanoic acid
(2Xi,9S)-lysinoalanine
Lysinoalanine (from Cysteine)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2544544
http://purl.org/obo/owl/PubMed#PubMed_2544544
RESID:AA0123
http://purl.org/obo/owl/RESID#RESID_AA0123
Lysinoalanine (Ser-Lys)
N6-(L-isoglutamyl)-L-lysine (Gln)
Cross-link 2.
PSI-MOD
A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine.
RESID:AA0124
http://purl.org/obo/owl/RESID#RESID_AA0124
PubMed:5656070
http://purl.org/obo/owl/PubMed#PubMed_5656070
PubMed:8598899
http://purl.org/obo/owl/PubMed#PubMed_8598899
PubMed:5637041
http://purl.org/obo/owl/PubMed#PubMed_5637041
ChEBI:21863
http://purl.org/obo/owl/ChEBI#ChEBI_21863
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2461365
http://purl.org/obo/owl/PubMed#PubMed_2461365
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N(epsilon)-(gamma-glutamyl)lysine
N alpha -(gamma-Glutamyl)-lysine
(S,S)-2-amino-6-[(4-amino-4-carboxybutanoyl)amino]hexanoic acid
Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-...)
gamma-(N6-lysyl)glutamic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N6-glycyl-L-lysine
Cross-link 2; this is the common crosslink structure formed by ubiquitin, SUMO, and similar proteins.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine.
RESID:AA0125
http://purl.org/obo/owl/RESID#RESID_AA0125
ChEBI:21885
http://purl.org/obo/owl/ChEBI#ChEBI_21885
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N6-glycyllysine
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...)
(S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-(L-isoaspartyl)glycine
Cross-link 2.
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
isoaspartyl glycine
2-amino-N4-(carboxymethyl)-butanediamic acid
(S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
N-beta-aspartylglycine
Isoaspartyl glycine isopeptide (Gly-Asn)
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoaspartyl)glycine.
ChEBI:21479
http://purl.org/obo/owl/ChEBI#ChEBI_21479
RESID:AA0126
http://purl.org/obo/owl/RESID#RESID_AA0126
PubMed:1826288
http://purl.org/obo/owl/PubMed#PubMed_1826288
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
pyruvic acid (Cys)
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-cysteine residue to pyruvic acid.
UniMod:382
http://purl.org/obo/owl/UniMod#UniMod_382
RESID:AA0127
http://purl.org/obo/owl/RESID#RESID_AA0127
PubMed:8464063
http://purl.org/obo/owl/PubMed#PubMed_8464063
PubMed:3042771
http://purl.org/obo/owl/PubMed#PubMed_3042771
PubMed:10085076
http://purl.org/obo/owl/PubMed#PubMed_10085076
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Pyruvic acid (Cys)
L-3-phenyllactic acid
This modification is not the result of deamidation, instead the alpha amino group is replaced with an hydroxyl group.
PSI-MOD
3-phenyllactic acid
(S)-2-hydroxy-3-phenylpropanoic acid
A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid.
UniMod:7
http://purl.org/obo/owl/UniMod#UniMod_7
RESID:AA0128
http://purl.org/obo/owl/RESID#RESID_AA0128
PubMed:1973541
http://purl.org/obo/owl/PubMed#PubMed_1973541
Deamidation
Deamidated
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-oxobutanoic acid
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid.
PubMed:15023056
http://purl.org/obo/owl/PubMed#PubMed_15023056
PubMed:2253617
http://purl.org/obo/owl/PubMed#PubMed_2253617
PubMed:1680314
http://purl.org/obo/owl/PubMed#PubMed_1680314
RESID:AA0129
http://purl.org/obo/owl/RESID#RESID_AA0129
PubMed:2764678
http://purl.org/obo/owl/PubMed#PubMed_2764678
UniMod:385
http://purl.org/obo/owl/UniMod#UniMod_385
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Ammonia-loss
Loss of ammonia
2-oxobutanoic acid
2-oxobutanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N2-succinyl-L-tryptophan
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N2-succinyltryptophan
(S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid
A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan.
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:8471040
http://purl.org/obo/owl/PubMed#PubMed_8471040
RESID:AA0130
http://purl.org/obo/owl/RESID#RESID_AA0130
UniMod:64
http://purl.org/obo/owl/UniMod#UniMod_64
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Succinic anhydride labeling reagent light form (N-term & K)
Succinyl
S-phycocyanobilin-L-cysteine
From DeltaMass: Average Mass: 587.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin.
UniMod:387
http://purl.org/obo/owl/UniMod#UniMod_387
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:16644722
http://purl.org/obo/owl/PubMed#PubMed_16644722
ChEBI:15617
http://purl.org/obo/owl/ChEBI#ChEBI_15617
PubMed:7918400
http://purl.org/obo/owl/PubMed#PubMed_7918400
RESID:AA0131
http://purl.org/obo/owl/RESID#RESID_AA0131
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
PubMed:3838747
http://purl.org/obo/owl/PubMed#PubMed_3838747
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione
phycobilin cysteine
phycocyanobilin cysteine adduct
S-Phycocyanobilin (on Cysteine)
Phycocyanobilin
phycocyanobilin
S-phycoerythrobilin-L-cysteine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
phycoerythrobilin cysteine adduct
phycoerythrobilin
Phycoerythrobilin
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
(2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin.
PubMed:3838747
http://purl.org/obo/owl/PubMed#PubMed_3838747
RESID:AA0132
http://purl.org/obo/owl/RESID#RESID_AA0132
PubMed:8876649
http://purl.org/obo/owl/PubMed#PubMed_8876649
UniMod:388
http://purl.org/obo/owl/UniMod#UniMod_388
PubMed:14588022
http://purl.org/obo/owl/PubMed#PubMed_14588022
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
ChEBI:15618
http://purl.org/obo/owl/ChEBI#ChEBI_15618
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S-phytochromobilin-L-cysteine
PSI-MOD
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin.
UniMod:389
http://purl.org/obo/owl/UniMod#UniMod_389
PubMed:1634523
http://purl.org/obo/owl/PubMed#PubMed_1634523
ChEBI:15619
http://purl.org/obo/owl/ChEBI#ChEBI_15619
PubMed:16593380
http://purl.org/obo/owl/PubMed#PubMed_16593380
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
PubMed:7918400
http://purl.org/obo/owl/PubMed#PubMed_7918400
RESID:AA0133
http://purl.org/obo/owl/RESID#RESID_AA0133
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid
phytochrome chromophore
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3-dihydro-(21H,24H)-biline-1,19-dione
phytochromobilin
phytochromobilin cysteine adduct
Phytochromobilin
heme-bis-L-cysteine
Cross-link 2.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
RESID:AA0134
http://purl.org/obo/owl/RESID#RESID_AA0134
ChEBI:17627
http://purl.org/obo/owl/ChEBI#ChEBI_17627
PubMed:5545094
http://purl.org/obo/owl/PubMed#PubMed_5545094
PubMed:8827449
http://purl.org/obo/owl/PubMed#PubMed_8827449
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Heme (covalent)
biscysteinyl heme
[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
heme-L-cysteine
From DeltaMass: Average Mass: 617.
PSI-MOD
S-Heme (on Cysteine)
Heme (covalent; via 1 link)
heme
Heme
A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:170910
http://purl.org/obo/owl/PubMed#PubMed_170910
PubMed:192772
http://purl.org/obo/owl/PubMed#PubMed_192772
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:9535866
http://purl.org/obo/owl/PubMed#PubMed_9535866
PubMed:2536325
http://purl.org/obo/owl/PubMed#PubMed_2536325
UniMod:390
http://purl.org/obo/owl/UniMod#UniMod_390
RESID:AA0135
http://purl.org/obo/owl/RESID#RESID_AA0135
ChEBI:17627
http://purl.org/obo/owl/ChEBI#ChEBI_17627
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
4-[1-(S-cysteinyl)ethyl]protoporphyrin IX
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
cysteinyl heme
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
[12-ethenyl-7-((S)-1-[(R)-2-amino-2-carboxy]ethylsulfanyl)ethyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
tetrakis-L-cysteinyl iron
Cross-link 4.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modification from RESID
PubMed:2244884
http://purl.org/obo/owl/PubMed#PubMed_2244884
RESID:AA0136
http://purl.org/obo/owl/RESID#RESID_AA0136
PubMed:1303768
http://purl.org/obo/owl/PubMed#PubMed_1303768
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-iron
tetrakis-L-cysteinyl diiron disulfide
Cross-link 4.
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
di-mu-sulfidobis[bis(cysteinato)-kappaS,KappaS-iron]
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
tetrakis(cysteinato)-1kappaS,1kappaS,2kappaS,2kappaS-di-mu-sulfidodiiron
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
modification from RESID
PubMed:2123937
http://purl.org/obo/owl/PubMed#PubMed_2123937
PubMed:6801028
http://purl.org/obo/owl/PubMed#PubMed_6801028
PubMed:7763242
http://purl.org/obo/owl/PubMed#PubMed_7763242
PubMed:8688437
http://purl.org/obo/owl/PubMed#PubMed_8688437
RESID:AA0137
http://purl.org/obo/owl/RESID#RESID_AA0137
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
hexakis-L-cysteinyl triiron trisulfide
Cross-link 6.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
tri-mu-sulfidotris(biscysteinato-kappaS-iron)
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from RESID
RESID:AA0138
http://purl.org/obo/owl/RESID#RESID_AA0138
PubMed:3379067
http://purl.org/obo/owl/PubMed#PubMed_3379067
PubMed:7354058
http://purl.org/obo/owl/PubMed#PubMed_7354058
PubMed:3932661
http://purl.org/obo/owl/PubMed#PubMed_3932661
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
tris-L-cysteinyl triiron tetrasulfide
Cross-link 3.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
tris-L-cysteinyl triiron tetrasulfide cuboid cluster
tris-L-cysteinyl triiron tetrasulfide trigonal cluster
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
tris-L-cysteinyl triiron tetrasulfide cubane form
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from RESID
PubMed:7819255
http://purl.org/obo/owl/PubMed#PubMed_7819255
PubMed:9063899
http://purl.org/obo/owl/PubMed#PubMed_9063899
PubMed:3422475
http://purl.org/obo/owl/PubMed#PubMed_3422475
PubMed:6848518
http://purl.org/obo/owl/PubMed#PubMed_6848518
RESID:AA0139
http://purl.org/obo/owl/RESID#RESID_AA0139
PubMed:2056535
http://purl.org/obo/owl/PubMed#PubMed_2056535
PubMed:10555576
http://purl.org/obo/owl/PubMed#PubMed_10555576
tris-L-cysteinyl triiron tetrasulfide C3 cluster
mu3-sulfido-tri-mu-sulfidotris(cysteinato-kappaS-iron)
mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron
tetrakis-L-cysteinyl tetrairon tetrasulfide
Cross-link 4.
PSI-MOD
tetra-mu3-sulfidotetrakis(S-cysteinyliron)
tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetra-mu3-sulfido-tetrahedro-tetrairon
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
modification from RESID
PubMed:7819196
http://purl.org/obo/owl/PubMed#PubMed_7819196
PubMed:7803404
http://purl.org/obo/owl/PubMed#PubMed_7803404
PubMed:3351918
http://purl.org/obo/owl/PubMed#PubMed_3351918
RESID:AA0140
http://purl.org/obo/owl/RESID#RESID_AA0140
PubMed:932007
http://purl.org/obo/owl/PubMed#PubMed_932007
L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide
Cross-link 2; incidental to RESID:AA0300.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from RESID
PubMed:10525412
http://purl.org/obo/owl/PubMed#PubMed_10525412
PubMed:12215645
http://purl.org/obo/owl/PubMed#PubMed_12215645
PubMed:8027059
http://purl.org/obo/owl/PubMed#PubMed_8027059
RESID:AA0141
http://purl.org/obo/owl/RESID#RESID_AA0141
PubMed:12733878
http://purl.org/obo/owl/PubMed#PubMed_12733878
PubMed:1529354
http://purl.org/obo/owl/PubMed#PubMed_1529354
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
nitrogenase iron-molybdenum cofactor
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-cysteinyl molybdopterin
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modification from UniMod and Resid
RESID:AA0142
http://purl.org/obo/owl/RESID#RESID_AA0142
UniMod:391
http://purl.org/obo/owl/UniMod#UniMod_391
PubMed:9428520
http://purl.org/obo/owl/PubMed#PubMed_9428520
PubMed:7878465
http://purl.org/obo/owl/PubMed#PubMed_7878465
PubMed:14527393
http://purl.org/obo/owl/PubMed#PubMed_14527393
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
8-amino-2-(2-amino-2-carboxyethyl)sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
molybdoenzyme molybdenum cofactor
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
cysteinyl Mo-pterin
molybdopterin
Molybdopterin
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
S-(8alpha-FAD)-L-cysteine
PSI-MOD
S8aFADCys
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-8alpha-FAD cysteine
Flavin adenine dinucleotide
FAD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
modification from RESID
UniMod:50
http://purl.org/obo/owl/UniMod#UniMod_50
RESID:AA0143
http://purl.org/obo/owl/RESID#RESID_AA0143
PubMed:10220347
http://purl.org/obo/owl/PubMed#PubMed_10220347
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid
8alpha-(S-cysteinyl)FAD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
3'-(8alpha-FAD)-L-histidine
PSI-MOD
modification from RESID
PubMed:241294
http://purl.org/obo/owl/PubMed#PubMed_241294
UniMod:50
http://purl.org/obo/owl/UniMod#UniMod_50
PubMed:8076
http://purl.org/obo/owl/PubMed#PubMed_8076
RESID:AA0144
http://purl.org/obo/owl/RESID#RESID_AA0144
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
8alpha-(N(delta)-histidyl)FAD
8alpha-(N3'-histidyl)FAD
pi-(8alpha-FAD)-histidine
pros-(8alpha-FAD)-histidine
Pros-8alpha-FAD histidine
8alpha-N1-histidyl FAD [misnomer]
FAD
Flavin adenine dinucleotide
Npros8aFADHis
O4'-(8alpha-FAD)-L-tyrosine
From DeltaMass: Average Mass: 783
PSI-MOD
8alpha-(O4'-tyrosyl)FAD
(S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid
Flavin adenine dinucleotide
FAD
O-8alpha-FAD tyrosine
O-8 alpha-Flavin [FAD])- (of Tyrosine)
modification from RESID
PubMed:7391034
http://purl.org/obo/owl/PubMed#PubMed_7391034
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:50
http://purl.org/obo/owl/UniMod#UniMod_50
RESID:AA0145
http://purl.org/obo/owl/RESID#RESID_AA0145
O8aFADTyr
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
3'-hydroxylation of L-tyrosine to L-3',4'-dihydroxyphenylalanine
incidental to RESID:AA0368 From DeltaMass: Average Mass: 16
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-3'-hydroxytyrosine
A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:3734192
http://purl.org/obo/owl/PubMed#PubMed_3734192
RESID:AA0146
http://purl.org/obo/owl/RESID#RESID_AA0146
PubMed:1610822
http://purl.org/obo/owl/PubMed#PubMed_1610822
PubMed:1903612
http://purl.org/obo/owl/PubMed#PubMed_1903612
levodopa
L-DOPA
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
3HyTyr
(S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid
3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA)
3',4'-dihydroxyphenylalanine
oxidation of tyrosine to L-2',4',5'-topaquinone
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TopaQ
quinone
Quinone
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-2,4,5-TOPAquinone
5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone
2,4,5-trihydroxyphenylalanine quinone
2',4',5'-topaquinone
(S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone.
RESID:AA0147
http://purl.org/obo/owl/RESID#RESID_AA0147
UniMod:392
http://purl.org/obo/owl/UniMod#UniMod_392
PubMed:1569055
http://purl.org/obo/owl/PubMed#PubMed_1569055
PubMed:2111581
http://purl.org/obo/owl/PubMed#PubMed_2111581
PubMed:10387067
http://purl.org/obo/owl/PubMed#PubMed_10387067
PubMed:1457410
http://purl.org/obo/owl/PubMed#PubMed_1457410
ChEBI:21187
http://purl.org/obo/owl/ChEBI#ChEBI_21187
oxidation of tryptophan to L-tryptophyl quinone
incidental to RESID:AA0149; incidental to RESID:AA0313; From DeltaMass: Average Mass: 30.
PSI-MOD
A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone.
RESID:AA0148
http://purl.org/obo/owl/RESID#RESID_AA0148
UniMod:392
http://purl.org/obo/owl/UniMod#UniMod_392
PubMed:2028257
http://purl.org/obo/owl/PubMed#PubMed_2028257
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(S)-3-(2-amino-2-carboxyethyl)-6,7-indolinedione
Quinone
6,7 Dione (from Tryptophan)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
quinone
TQ
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Tryptophylquinone
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
4'-(L-tryptophan)-L-tryptophyl quinone
Cross-link 2; secondary to RESID:AA0148; From DeltaMass: Average Mass: 28.
PSI-MOD
2,4-BisTrp-6,7-dione (from Tryptophan)
(S,S)-3-(2-amino-2-carboxyethyl)-4-[3-(2-amino-2-carboxyethyl)-1H-indol-2-yl]-6,7-indolinedione
4-(2'-tryptophyl)tryptophan-6,7-dione
4'-tryptophan-tryptophylquinone
A protein modification that effectively converts two L-tryptophan residues to 4'-(L-tryptophan)-L-tryptophyl quinone.
PubMed:2028257
http://purl.org/obo/owl/PubMed#PubMed_2028257
RESID:AA0149
http://purl.org/obo/owl/RESID#RESID_AA0149
ChEBI:20251
http://purl.org/obo/owl/ChEBI#ChEBI_20251
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Tryptophan tryptophylquinone (Trp-Trp)
alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
O-phosphopantetheine-L-serine
UniMod has DiffFormula C 11 H 20 N 2 O 6 P 1 S 1 From DeltaMass: Average Mass: 339
PSI-MOD
(2R)-4-((2S)-2-amino-2-carboxyethyl)phosphonato-2-hydroxy-N-[3-(2-sulfanylethyl)amino-3-oxopropyl]-3,3-dimethylbutanamide
Phosphopantetheine (covalent)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Phosphopantetheine
4'-Phosphopantetheine
A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:10320345
http://purl.org/obo/owl/PubMed#PubMed_10320345
RESID:AA0150
http://purl.org/obo/owl/RESID#RESID_AA0150
UniMod:49
http://purl.org/obo/owl/UniMod#UniMod_49
PubMed:12869567
http://purl.org/obo/owl/PubMed#PubMed_12869567
PubMed:4568609
http://purl.org/obo/owl/PubMed#PubMed_4568609
PubMed:10997907
http://purl.org/obo/owl/PubMed#PubMed_10997907
PubMed:12057197
http://purl.org/obo/owl/PubMed#PubMed_12057197
Phosphopantetheine
N4-glycosyl-L-asparagine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-linked (GlcNAc)
N4GlycoAsn
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.
PubMed:111247
http://purl.org/obo/owl/PubMed#PubMed_111247
PubMed:1694179
http://purl.org/obo/owl/PubMed#PubMed_1694179
PubMed:5490222
http://purl.org/obo/owl/PubMed#PubMed_5490222
RESID:AA0151
http://purl.org/obo/owl/RESID#RESID_AA0151
S-glucosyl-L-cysteine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Hexose
Hex
(R)-2-amino-3-(beta-D-glucopyranosylsulfanyl)propanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
SGlcCys
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-linked (Glc)
S-glycosyl-cysteine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-(beta-D-glucopyranosyl)cysteine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.
PubMed:1145128
http://purl.org/obo/owl/PubMed#PubMed_1145128
UniMod:41
http://purl.org/obo/owl/UniMod#UniMod_41
RESID:AA0152
http://purl.org/obo/owl/RESID#RESID_AA0152
PubMed:15279557
http://purl.org/obo/owl/PubMed#PubMed_15279557
PubMed:5286858
http://purl.org/obo/owl/PubMed#PubMed_5286858
O5-glucosylgalactosyl-L-hydroxylysine
secondary to RESID:AA0028
PSI-MOD
5-[(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy]-L-lysine
(2S,5R)-2,6-diamino-5-[4,5-dihydroxy-6-(hydroxymethyl)-3-[3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-oxan-2-yl]oxy-hexanoic acid
glucosylgalactosyl hydroxylysine
Glucosylgalactosyl
OGlcGal5HyLys
O-linked (Gal-Glc)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modification from RESID
PubMed:15149698
http://purl.org/obo/owl/PubMed#PubMed_15149698
UniMod:393
http://purl.org/obo/owl/UniMod#UniMod_393
PubMed:4288358
http://purl.org/obo/owl/PubMed#PubMed_4288358
RESID:AA0153
http://purl.org/obo/owl/RESID#RESID_AA0153
PubMed:4319110
http://purl.org/obo/owl/PubMed#PubMed_4319110
O-(N-acetylaminogalactosyl)-L-serine
PSI-MOD
modification from RESID
PubMed:16005634
http://purl.org/obo/owl/PubMed#PubMed_16005634
PubMed:115869
http://purl.org/obo/owl/PubMed#PubMed_115869
RESID:AA0154
http://purl.org/obo/owl/RESID#RESID_AA0154
PubMed:9092502
http://purl.org/obo/owl/PubMed#PubMed_9092502
PubMed:8948436
http://purl.org/obo/owl/PubMed#PubMed_8948436
PubMed:3086323
http://purl.org/obo/owl/PubMed#PubMed_3086323
UniMod:43
http://purl.org/obo/owl/UniMod#UniMod_43
OGalNAcSer
O3-(N-acetylgalactosaminyl)serine
O-linked (GalNAc)
N-Acetylhexosamine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-(alpha-D-2-acetamido-2-deoxygalactopyranosyloxy)propanoic acid
HexNAc
mucin type O-glycosylserine
O-(N-acetylaminogalactosyl)-L-threonine
PSI-MOD
O-linked (GalNAc)
O3-(N-acetylgalactosaminyl)threonine
modification from RESID
RESID:AA0155
http://purl.org/obo/owl/RESID#RESID_AA0155
UniMod:43
http://purl.org/obo/owl/UniMod#UniMod_43
PubMed:16005634
http://purl.org/obo/owl/PubMed#PubMed_16005634
PubMed:1997327
http://purl.org/obo/owl/PubMed#PubMed_1997327
PubMed:3086323
http://purl.org/obo/owl/PubMed#PubMed_3086323
PubMed:8948436
http://purl.org/obo/owl/PubMed#PubMed_8948436
PubMed:9092502
http://purl.org/obo/owl/PubMed#PubMed_9092502
OGalNAcThr
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxygalactopyranosyloxy)butanoic acid
HexNAc
mucin type O-glycosylthreonine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-Acetylhexosamine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
1'-mannosyl-L-tryptophan
PSI-MOD
N1'ManTrp
N1-mannosyl-tryptophan
N-linked (Man)
N-mannosyl-tryptophan
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan.
PubMed:16150691
http://purl.org/obo/owl/PubMed#PubMed_16150691
PubMed:1482345
http://purl.org/obo/owl/PubMed#PubMed_1482345
RESID:AA0156
http://purl.org/obo/owl/RESID#RESID_AA0156
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid
1'-glycosyl-L-tryptophan
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
O4'-glucosyl-L-tyrosine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.
PubMed:15279557
http://purl.org/obo/owl/PubMed#PubMed_15279557
UniMod:41
http://purl.org/obo/owl/UniMod#UniMod_41
PubMed:3181138
http://purl.org/obo/owl/PubMed#PubMed_3181138
RESID:AA0157
http://purl.org/obo/owl/RESID#RESID_AA0157
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-(4-alpha-glucopyranosyloxy)phenylpropanoic acid
O4GlcTyr
O4'-glycosyl-L-tyrosine
Hexose
Hex
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N-asparaginyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine.
RESID:AA0158
http://purl.org/obo/owl/RESID#RESID_AA0158
PubMed:8276756
http://purl.org/obo/owl/PubMed#PubMed_8276756
PubMed:1824714
http://purl.org/obo/owl/PubMed#PubMed_1824714
GPIAsn
GPI-anchor amidated asparagine
N-aspartyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine.
RESID:AA0159
http://purl.org/obo/owl/RESID#RESID_AA0159
PubMed:7120400
http://purl.org/obo/owl/PubMed#PubMed_7120400
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
GPI-anchor amidated aspartate
GPIAsp
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N-cysteinyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
GPICys
GPI-anchor amidated cysteine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine.
PubMed:2897081
http://purl.org/obo/owl/PubMed#PubMed_2897081
RESID:AA0160
http://purl.org/obo/owl/RESID#RESID_AA0160
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-glycyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine.
PubMed:2341397
http://purl.org/obo/owl/PubMed#PubMed_2341397
RESID:AA0161
http://purl.org/obo/owl/RESID#RESID_AA0161
GPIGly
GPI-anchor amidated glycine
N-seryl-glycosylphosphatidylinositolethanolamine
PSI-MOD
GPI-anchor amidated serine
GPISer
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine.
PubMed:8448158
http://purl.org/obo/owl/PubMed#PubMed_8448158
RESID:AA0162
http://purl.org/obo/owl/RESID#RESID_AA0162
PubMed:2111324
http://purl.org/obo/owl/PubMed#PubMed_2111324
N-alanyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
GPIAla
GPI-anchor amidated alanine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine.
PubMed:7744038
http://purl.org/obo/owl/PubMed#PubMed_7744038
PubMed:7682556
http://purl.org/obo/owl/PubMed#PubMed_7682556
RESID:AA0163
http://purl.org/obo/owl/RESID#RESID_AA0163
N-threonyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
GPI-anchor amidated threonine
GPIThr
A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine.
RESID:AA0164
http://purl.org/obo/owl/RESID#RESID_AA0164
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N-glycyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
GPI-like-anchor amidated glycine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine.
RESID:AA0165
http://purl.org/obo/owl/RESID#RESID_AA0165
PubMed:8404891
http://purl.org/obo/owl/PubMed#PubMed_8404891
PubMed:12626404
http://purl.org/obo/owl/PubMed#PubMed_12626404
GSIGly
N-seryl-glycosylsphingolipidinositolethanolamine
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
GPI-like-anchor amidated serine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
GSISer
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine.
PubMed:8269952
http://purl.org/obo/owl/PubMed#PubMed_8269952
PubMed:2721485
http://purl.org/obo/owl/PubMed#PubMed_2721485
PubMed:12626404
http://purl.org/obo/owl/PubMed#PubMed_12626404
RESID:AA0166
http://purl.org/obo/owl/RESID#RESID_AA0166
O-(phosphoribosyl dephospho-coenzyme A)-L-serine
pRibodePcoA
PSI-MOD
modification from RESID
PubMed:11052675
http://purl.org/obo/owl/PubMed#PubMed_11052675
PubMed:179809
http://purl.org/obo/owl/PubMed#PubMed_179809
PubMed:368065
http://purl.org/obo/owl/PubMed#PubMed_368065
RESID:AA0167
http://purl.org/obo/owl/RESID#RESID_AA0167
UniMod:395
http://purl.org/obo/owl/UniMod#UniMod_395
PubMed:180526
http://purl.org/obo/owl/PubMed#PubMed_180526
PubMed:10924139
http://purl.org/obo/owl/PubMed#PubMed_10924139
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
PhosphoribosyldephosphoCoA
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine
phosphoribosyl dephospho-coenzyme A
Phosphoribosyl dephospho-coenzyme A (covalent)
O3-(phosphoribosyl dephospho-coenzyme A)-L-serine
O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
omega-N-(ADP-ribosyl)-L-arginine
From DeltaMass: Average Mass: 541.
PSI-MOD
A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine.
UniMod:213
http://purl.org/obo/owl/UniMod#UniMod_213
RESID:AA0168
http://purl.org/obo/owl/RESID#RESID_AA0168
PubMed:3090031
http://purl.org/obo/owl/PubMed#PubMed_3090031
PubMed:209022
http://purl.org/obo/owl/PubMed#PubMed_209022
PubMed:6582062
http://purl.org/obo/owl/PubMed#PubMed_6582062
PubMed:3923473
http://purl.org/obo/owl/PubMed#PubMed_3923473
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:15842200
http://purl.org/obo/owl/PubMed#PubMed_15842200
ADP Ribose addition
(S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-(ADP-ribosyl)- (on Arginine)
N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine
ADP-ribosylarginine
ADP-Ribosyl
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-(ADP-ribosyl)-L-cysteine
From DeltaMass: Average Mass: 541.
PSI-MOD
A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine.
RESID:AA0169
http://purl.org/obo/owl/RESID#RESID_AA0169
UniMod:213
http://purl.org/obo/owl/UniMod#UniMod_213
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:15842200
http://purl.org/obo/owl/PubMed#PubMed_15842200
PubMed:3863818
http://purl.org/obo/owl/PubMed#PubMed_3863818
ADP-ribosylcysteine
ADP-Ribosyl
ADP Ribose addition
(R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid
S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
S-(ADP-ribosyl)- (on Cysteine)
S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-glutamyl 5-glycerylphosphorylethanolamine
glycerylPE
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine.
RESID:AA0170
http://purl.org/obo/owl/RESID#RESID_AA0170
UniMod:396
http://purl.org/obo/owl/UniMod#UniMod_396
PubMed:9662537
http://purl.org/obo/owl/PubMed#PubMed_9662537
PubMed:2569467
http://purl.org/obo/owl/PubMed#PubMed_2569467
PubMed:2511205
http://purl.org/obo/owl/PubMed#PubMed_2511205
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
L-glutamyl 5-glycerophosphorylethanolamine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-glutamyl 5-glycerophosphoethanolamine
Glycerylphosphorylethanolamine (covalent)
glycerylphosphorylethanolamine
GlycerylPE
(S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid
S-sulfo-L-cysteine
PSI-MOD
A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine.
PubMed:12876326
http://purl.org/obo/owl/PubMed#PubMed_12876326
UniMod:40
http://purl.org/obo/owl/UniMod#UniMod_40
RESID:AA0171
http://purl.org/obo/owl/RESID#RESID_AA0171
PubMed:643076
http://purl.org/obo/owl/PubMed#PubMed_643076
PubMed:14752058
http://purl.org/obo/owl/PubMed#PubMed_14752058
Sulfo
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(R)-2-amino-3-(sulfosulfanyl)propanoic acid
2-amino-3-(sulfothio)propanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-sulfocysteine
S-sulfocysteine
cysteine sulfate thioester
O-Sulfonation
O4'-sulfo-L-tyrosine
From DeltaMass: Average Mass: 80 Average Mass Change:80 PubMed:9624161.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
tyrosine-O-sulphonic acid
tyrosine-O-sulfonic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
tyrosine sulfate
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Sulphation (of O of Tyrosine)
Sulfotyrosine
Sulfo
O4-sulfotyrosine
O-Sulfonation
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate
(S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid
Tyrosinyl Sulphate [misnomer]
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine.
UniMod:40
http://purl.org/obo/owl/UniMod#UniMod_40
RESID:AA0172
http://purl.org/obo/owl/RESID#RESID_AA0172
PubMed:3801003
http://purl.org/obo/owl/PubMed#PubMed_3801003
PubMed:3778455
http://purl.org/obo/owl/PubMed#PubMed_3778455
PubMed:2303439
http://purl.org/obo/owl/PubMed#PubMed_2303439
PubMed:14752058
http://purl.org/obo/owl/PubMed#PubMed_14752058
PubMed:10226369
http://purl.org/obo/owl/PubMed#PubMed_10226369
DeltaMass:88
http://purl.org/obo/owl/DeltaMass#DeltaMass_88
L-bromohistidine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Bromo
Bromohistidine
A protein modification that effectively converts an L-histidine residue to L-bromohistidine.
PubMed:2076468
http://purl.org/obo/owl/PubMed#PubMed_2076468
UniMod:340
http://purl.org/obo/owl/UniMod#UniMod_340
RESID:AA0173
http://purl.org/obo/owl/RESID#RESID_AA0173
PubMed:9033387
http://purl.org/obo/owl/PubMed#PubMed_9033387
Br1His
bromination
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-2'-bromophenylalanine
From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine.
PubMed:2059627
http://purl.org/obo/owl/PubMed#PubMed_2059627
PubMed:2076468
http://purl.org/obo/owl/PubMed#PubMed_2076468
DeltaMass:83
http://purl.org/obo/owl/DeltaMass#DeltaMass_83
PubMed:9033387
http://purl.org/obo/owl/PubMed#PubMed_9033387
UniMod:340
http://purl.org/obo/owl/UniMod#UniMod_340
RESID:AA0174
http://purl.org/obo/owl/RESID#RESID_AA0174
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(S)-2-amino-3-(2-bromophenyl)propanoic acid
2'-BrPhe
bromination
Bromo
L-o-bromination of Phe with 79Br
o-bromophenylalanine
ortho-bromophenylalanine
L-3'-bromophenylalanine
PSI-MOD
3'-BrPhe
bromination
(S)-2-amino-3-(3-bromophenyl)propanoic acid
meta-bromophenylalanine
Bromo
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
m-bromophenylalanine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine.
PubMed:2076468
http://purl.org/obo/owl/PubMed#PubMed_2076468
PubMed:9033387
http://purl.org/obo/owl/PubMed#PubMed_9033387
RESID:AA0175
http://purl.org/obo/owl/RESID#RESID_AA0175
UniMod:340
http://purl.org/obo/owl/UniMod#UniMod_340
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-4'-bromophenylalanine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
bromination
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Bromo
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S)-2-amino-3-(4-bromophenyl)propanoic acid
4'-BrPhe
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
p-bromophenylalanine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
para-bromophenylalanine
A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine.
PubMed:9033387
http://purl.org/obo/owl/PubMed#PubMed_9033387
PubMed:2076468
http://purl.org/obo/owl/PubMed#PubMed_2076468
UniMod:340
http://purl.org/obo/owl/UniMod#UniMod_340
RESID:AA0176
http://purl.org/obo/owl/RESID#RESID_AA0176
3',3'',5'-triiodo-L-thyronine
From DeltaMass: Average Mass: 470
PSI-MOD
3,3',5-triiodo-L-thyronine
(S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid
liothyronine
4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine
3,5,3'-Triiodothyronine (from Tyrosine)
3,5,3'-triiodo-L-thyronine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Triiodothyronine
O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine
Triiodothyronine
triiodo
A protein modification that effectively substitutes an L-tyrosine residue with 3',3'',5'-triiodo-L-thyronine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0177
http://purl.org/obo/owl/RESID#RESID_AA0177
ChEBI:18258
http://purl.org/obo/owl/ChEBI#ChEBI_18258
UniMod:397
http://purl.org/obo/owl/UniMod#UniMod_397
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-thyroxine
PSI-MOD
(S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid
3',3'',5',5''-tetraiodo-L-thyronine
3,3',5,5'-tetraiodo-L-thyronine
3,5,3',5'-tetraiodo-L-thyronine
4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine
O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine
A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine.
ChEBI:18332
http://purl.org/obo/owl/ChEBI#ChEBI_18332
PubMed:6704086
http://purl.org/obo/owl/PubMed#PubMed_6704086
RESID:AA0178
http://purl.org/obo/owl/RESID#RESID_AA0178
UniMod:398
http://purl.org/obo/owl/UniMod#UniMod_398
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Thyroxine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Thyroxine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
tetraiodo
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-6'-bromotryptophan
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
6'-bromotryptophan
(S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Bromo
bromination
6'-BrTrp
A protein modification that effectively converts an L-tryptophan residue to L-6'-bromotryptophan.
PubMed:9033387
http://purl.org/obo/owl/PubMed#PubMed_9033387
PubMed:9030520
http://purl.org/obo/owl/PubMed#PubMed_9030520
PubMed:12118011
http://purl.org/obo/owl/PubMed#PubMed_12118011
PubMed:9434739
http://purl.org/obo/owl/PubMed#PubMed_9434739
UniMod:340
http://purl.org/obo/owl/UniMod#UniMod_340
RESID:AA0179
http://purl.org/obo/owl/RESID#RESID_AA0179
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
dehydroalanine (Ser)
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-serine residue to dehydroalanine.
PubMed:10220322
http://purl.org/obo/owl/PubMed#PubMed_10220322
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:7947813
http://purl.org/obo/owl/PubMed#PubMed_7947813
PubMed:2914619
http://purl.org/obo/owl/PubMed#PubMed_2914619
RESID:AA0181
http://purl.org/obo/owl/RESID#RESID_AA0181
PubMed:8239649
http://purl.org/obo/owl/PubMed#PubMed_8239649
PubMed:1815586
http://purl.org/obo/owl/PubMed#PubMed_1815586
PubMed:1547888
http://purl.org/obo/owl/PubMed#PubMed_1547888
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
dHAla(Ser)
2,3-didehydroalanine (Ser)
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
dehydrobutyrine
PSI-MOD
2,3-didehydrobutyrine
2,3-didehydrobutyrine
2-amino-butenoic acid
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
Dehydrated
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Dehydroamino butyric acid
Dehydration
methyl-dehydroalanine
dHyThr
A protein modification that effectively converts an L-threonine residue to dehydrobutyrine
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0182
http://purl.org/obo/owl/RESID#RESID_AA0182
PubMed:3769923
http://purl.org/obo/owl/PubMed#PubMed_3769923
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
PubMed:1547888
http://purl.org/obo/owl/PubMed#PubMed_1547888
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(Z)-2,3-didehydrotyrosine
incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Z-dHTyr
red fluorescent protein chromophore
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
para-hydroxybenzylidene-imidazolidinone chromophore
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
green fluorescent protein chromophore
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.
PubMed:9631087
http://purl.org/obo/owl/PubMed#PubMed_9631087
RESID:AA0183
http://purl.org/obo/owl/RESID#RESID_AA0183
UniMod:401
http://purl.org/obo/owl/UniMod#UniMod_401
PubMed:1347277
http://purl.org/obo/owl/PubMed#PubMed_1347277
Didehydro
cis-dehydrotyrosine
amino-(para-hydroxybenzylidenyl)acetic acid
2-amino-3-oxo-butanoic_acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid
(Z)-2,3-didehydrogenated tyrosine
(Z)-2,3-didehydrotyrosine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-serine 5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine.
ChEBI:21393
http://purl.org/obo/owl/ChEBI#ChEBI_21393
PubMed:1347277
http://purl.org/obo/owl/PubMed#PubMed_1347277
PubMed:9631087
http://purl.org/obo/owl/PubMed#PubMed_9631087
RESID:AA0184
http://purl.org/obo/owl/RESID#RESID_AA0184
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
5-imidazolinone (Ser-Gly)
green fluorescent protein chromophore
2-[(R)-1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one
para-hydroxybenzylidene-imidazolidinone chromophore
seryl-5-imidazolinone glycine
L-3-oxoalanine (Cys)
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
3-oxoalanine (Cys)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-cysteine residue to L-oxoalanine.
PubMed:14563551
http://purl.org/obo/owl/PubMed#PubMed_14563551
PubMed:8681943
http://purl.org/obo/owl/PubMed#PubMed_8681943
PubMed:7628016
http://purl.org/obo/owl/PubMed#PubMed_7628016
PubMed:9478923
http://purl.org/obo/owl/PubMed#PubMed_9478923
RESID:AA0185
http://purl.org/obo/owl/RESID#RESID_AA0185
UniMod:402
http://purl.org/obo/owl/UniMod#UniMod_402
DeltaMass:350
http://purl.org/obo/owl/DeltaMass#DeltaMass_350
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
lactic acid
PSI-MOD
2-hydroxypropanoic acid
Ser->LacticAcid
lactic acid from N-term Ser
Lactic acid
alpha-hydroxypropionic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid.
PubMed:7607233
http://purl.org/obo/owl/PubMed#PubMed_7607233
RESID:AA0186
http://purl.org/obo/owl/RESID#RESID_AA0186
UniMod:403
http://purl.org/obo/owl/UniMod#UniMod_403
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-alanine 5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine.
RESID:AA0187
http://purl.org/obo/owl/RESID#RESID_AA0187
PubMed:10220322
http://purl.org/obo/owl/PubMed#PubMed_10220322
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
2-[(S)-1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one
5-imidazolinone (Ala-Gly)
4-methylidene-imidazole-5-one active site
para-hydroxybenzylidene-imidazolidinone chromophore
alanyl-5-imidazolinone glycine
L-cysteine 5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
para-hydroxybenzylidene-imidazolidinone chromophore
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
cysteinyl-5-imidazolinone glycine
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine.
RESID:AA0188
http://purl.org/obo/owl/RESID#RESID_AA0188
PubMed:1537807
http://purl.org/obo/owl/PubMed#PubMed_1537807
5-imidazolinone (Cys-Gly)
2-[(R)-1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-imino-glutamine 5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine.
PubMed:11209050
http://purl.org/obo/owl/PubMed#PubMed_11209050
RESID:AA0189
http://purl.org/obo/owl/RESID#RESID_AA0189
PubMed:11050230
http://purl.org/obo/owl/PubMed#PubMed_11050230
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
2,N-didehydroglutaminyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
fluorescent protein FP583 chromophore
red fluorescent protein chromophore
2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one
[2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
2-iminomethyl-5-imidazolinone (Gln-Gly)
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
D-alanine (Ala)
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
D-alanine (Ala)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
D-Ala(Ala)
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-alanine residue to D-alanine.
RESID:AA0191
http://purl.org/obo/owl/RESID#RESID_AA0191
PubMed:7961627
http://purl.org/obo/owl/PubMed#PubMed_7961627
PubMed:7287302
http://purl.org/obo/owl/PubMed#PubMed_7287302
PubMed:15023056
http://purl.org/obo/owl/PubMed#PubMed_15023056
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
D-allo-isoleucine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
D-allo-isoleucine
D-Ile
(2R,3S)-2-amino-3-methylpentanoic acid
A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine.
RESID:AA0192
http://purl.org/obo/owl/RESID#RESID_AA0192
PubMed:8223491
http://purl.org/obo/owl/PubMed#PubMed_8223491
ChEBI:30007
http://purl.org/obo/owl/ChEBI#ChEBI_30007
D-methionine
PSI-MOD
D-Met
A protein modification that effectively converts an L-methionine residue to D-methionine.
PubMed:2542051
http://purl.org/obo/owl/PubMed#PubMed_2542051
RESID:AA0193
http://purl.org/obo/owl/RESID#RESID_AA0193
PubMed:16033333
http://purl.org/obo/owl/PubMed#PubMed_16033333
ChEBI:29984
http://purl.org/obo/owl/ChEBI#ChEBI_29984
2-amino-4-(methylthio)butanoic acid
(R)-2-amino-4-(methylsulfanyl)butanoic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
D-methionine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
D-phenylalanine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
D-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine.
PubMed:2597281
http://purl.org/obo/owl/PubMed#PubMed_2597281
ChEBI:29996
http://purl.org/obo/owl/ChEBI#ChEBI_29996
PubMed:1644179
http://purl.org/obo/owl/PubMed#PubMed_1644179
RESID:AA0194
http://purl.org/obo/owl/RESID#RESID_AA0194
PubMed:1548227
http://purl.org/obo/owl/PubMed#PubMed_1548227
(R)-2-amino-3-phenylpropanoic acid
D-Phe
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
D-serine (Ser)
PSI-MOD
A protein modification that effectively converts an L-serine residue to D-serine.
PubMed:7973665
http://purl.org/obo/owl/PubMed#PubMed_7973665
RESID:AA0195
http://purl.org/obo/owl/RESID#RESID_AA0195
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
D-serine (Ser)
D-Ser(Ser)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
D-asparagine
PSI-MOD
A protein modification that effectively converts an L-asparagine residue to D-asparagine.
RESID:AA0196
http://purl.org/obo/owl/RESID#RESID_AA0196
ChEBI:29957
http://purl.org/obo/owl/ChEBI#ChEBI_29957
PubMed:1859408
http://purl.org/obo/owl/PubMed#PubMed_1859408
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
D-Asn
D-alpha-aminosuccinamic acid
(R)-2-amino-4-butanediamic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
D-aspartic acid beta-amide
D-asparagine
D-leucine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
D-leucine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-leucine residue to D-leucine.
PubMed:1358533
http://purl.org/obo/owl/PubMed#PubMed_1358533
PubMed:12135762
http://purl.org/obo/owl/PubMed#PubMed_12135762
PubMed:10461743
http://purl.org/obo/owl/PubMed#PubMed_10461743
ChEBI:30005
http://purl.org/obo/owl/ChEBI#ChEBI_30005
PubMed:1548227
http://purl.org/obo/owl/PubMed#PubMed_1548227
RESID:AA0197
http://purl.org/obo/owl/RESID#RESID_AA0197
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(R)-2-amino-4-methylpentanoic acid
D-Leu
alpha-aminoisocaproic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
D-tryptophan
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-tryptophan residue to D-tryptophan.
RESID:AA0198
http://purl.org/obo/owl/RESID#RESID_AA0198
PubMed:8910408
http://purl.org/obo/owl/PubMed#PubMed_8910408
ChEBI:29955
http://purl.org/obo/owl/ChEBI#ChEBI_29955
(R)-2-amino-3-(1H-indol-3-yl)propanoic acid
D-tryptophan
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
D-Trp
alpha-amino-beta-(3-indolyl)propionoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-isoglutamyl-polyglycine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
gamma-glutamylpolyglycine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
modification from RESID
PubMed:7992051
http://purl.org/obo/owl/PubMed#PubMed_7992051
RESID:AA0201
http://purl.org/obo/owl/RESID#RESID_AA0201
PubMed:10074368
http://purl.org/obo/owl/PubMed#PubMed_10074368
PubMed:16368691
http://purl.org/obo/owl/PubMed#PubMed_16368691
ChEBI:21343
http://purl.org/obo/owl/ChEBI#ChEBI_21343
L-isoglutamyl-polyglutamic acid
PSI-MOD
gamma-glutamylpolyglutamic acid
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid.
RESID:AA0202
http://purl.org/obo/owl/RESID#RESID_AA0202
PubMed:1680872
http://purl.org/obo/owl/PubMed#PubMed_1680872
PubMed:10747868
http://purl.org/obo/owl/PubMed#PubMed_10747868
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O4'-(phospho-5'-adenosine)-L-tyrosine
From DeltaMass: Average Mass: 329.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid
A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0203
http://purl.org/obo/owl/RESID#RESID_AA0203
PubMed:5543675
http://purl.org/obo/owl/PubMed#PubMed_5543675
UniMod:405
http://purl.org/obo/owl/UniMod#UniMod_405
5'-adenylic-O-tyrosine
AMP binding site
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
hydrogen 5'-adenylate tyrosine ester
O-AMP-tyrosine
O-5'-Adenosylation ( of Tyrosine)
Phosphoadenosine
O4'-L-tyrosine 5'-adenosine phosphodiester
S-(2-aminovinyl)-D-cysteine
Cross-link 2.
PSI-MOD
S-(2-aminovinyl)-D-cysteine (Ser-Cys)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S,Z)-S-(2-aminovinyl)cysteine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-2-amino-3-[((Z)-2-aminovinyl)sulfanyl]propanoic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
RESID:AA0204
http://purl.org/obo/owl/RESID#RESID_AA0204
PubMed:3769923
http://purl.org/obo/owl/PubMed#PubMed_3769923
PubMed:3181159
http://purl.org/obo/owl/PubMed#PubMed_3181159
oxidation to L-cysteine sulfenic acid
From DeltaMass: Average Mass: 16 Average Mass Change:16 Notes:Green et al. in J. B. C. 270, 18209-18211 (1995) quote Kim and Raines in Eur. J. Biochem. 224, 109-114 (1994). Kim and Raines using ESI-MS and sulfhydryl group titration found that bovine seminal ribonuclease contains a single oxidized sulfhydryl group, which cannot participate in a disulfide bond. This form of cysteine is called sulfenic acid (-SOH).
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-amino-3-sulfenopropanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Cysteine sulfenic acid (-SOH)
S-hydroxycysteine
(R)-2-amino-2-carboxyethanesulfenic acid
A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.
PubMed:2501303
http://purl.org/obo/owl/PubMed#PubMed_2501303
PubMed:8756456
http://purl.org/obo/owl/PubMed#PubMed_8756456
DeltaMass:41
http://purl.org/obo/owl/DeltaMass#DeltaMass_41
PubMed:10964927
http://purl.org/obo/owl/PubMed#PubMed_10964927
PubMed:9587003
http://purl.org/obo/owl/PubMed#PubMed_9587003
RESID:AA0205
http://purl.org/obo/owl/RESID#RESID_AA0205
PubMed:9214307
http://purl.org/obo/owl/PubMed#PubMed_9214307
PubMed:9586994
http://purl.org/obo/owl/PubMed#PubMed_9586994
Sulfenic Acid (from Cysteine)
3-sulfenoalanine
CysOH
S-glycyl-L-cysteine
Cross-link 2.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
glycine cysteine thioester
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(R)-2-amino-3-(aminoacetyl)sulfanylpropanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine.
RESID:AA0206
http://purl.org/obo/owl/RESID#RESID_AA0206
PubMed:3306404
http://purl.org/obo/owl/PubMed#PubMed_3306404
ChEBI:22050
http://purl.org/obo/owl/ChEBI#ChEBI_22050
S-(2-amino-1-oxoethyl)cysteine
S-4-hydroxycinnamyl-L-cysteine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S-para-coumaryl-L-cysteine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Hydroxycinnamyl
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
hydroxycinnamyl
modification from RESID
PubMed:7981196
http://purl.org/obo/owl/PubMed#PubMed_7981196
PubMed:7947803
http://purl.org/obo/owl/PubMed#PubMed_7947803
UniMod:407
http://purl.org/obo/owl/UniMod#UniMod_407
RESID:AA0207
http://purl.org/obo/owl/RESID#RESID_AA0207
4-hydroxycinnamyl (covalent)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
cinnamate cysteine thioester
(S,E)-2-amino-3-[3-(4-hydroxyphenyl)propenoylsulfanyl]propanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from RESID
PubMed:1898736
http://purl.org/obo/owl/PubMed#PubMed_1898736
PubMed:1794445
http://purl.org/obo/owl/PubMed#PubMed_1794445
RESID:AA0208
http://purl.org/obo/owl/RESID#RESID_AA0208
PubMed:3472204
http://purl.org/obo/owl/PubMed#PubMed_3472204
chondroitin 4-sulfate (chondroitin sulfate A)
O-linked (Xyl...) (chondroitin sulfate)
chondroitin 6-sulfate (chondroitin sulfate C)
poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
O-linked (Xyl...) (dermatan sulfate)
chondroitin sulfate B
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
beta-heparin
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
modification from RESID
RESID:AA0209
http://purl.org/obo/owl/RESID#RESID_AA0209
PubMed:2914936
http://purl.org/obo/owl/PubMed#PubMed_2914936
PubMed:3472204
http://purl.org/obo/owl/PubMed#PubMed_3472204
heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
O-linked (Xyl...) (heparan sulfate)
heparitin sulfate
heparin
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
modification from RESID
PubMed:3472204
http://purl.org/obo/owl/PubMed#PubMed_3472204
RESID:AA0210
http://purl.org/obo/owl/RESID#RESID_AA0210
N6-formyl-L-lysine
PSI-MOD
Formylation
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N(zeta)-formyllysine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N6-formylated L-lysine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S)-2-amino-6-(formylamino)hexanoic acid
epsilon-formyllysine
Formyl
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N6FoLys
N6-formyllysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine.
UniMod:122
http://purl.org/obo/owl/UniMod#UniMod_122
RESID:AA0211
http://purl.org/obo/owl/RESID#RESID_AA0211
PubMed:15799070
http://purl.org/obo/owl/PubMed#PubMed_15799070
O4-arabinosyl-L-hydroxyproline
secondary to RESID:AA0030; From DeltaMass: Average Mass: 147.
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
4-Glycosyloxy- (pentosyl,C5) (of Proline)
4-(beta-L-arabinofuranosyloxy)proline
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
glycosyl-L-hydroxyproline
Glycosyl
OAra4HyPro
O4-glycosyl-hydroxyproline
beta-arabinofuranosyl-4-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:666730
http://purl.org/obo/owl/PubMed#PubMed_666730
PubMed:7852316
http://purl.org/obo/owl/PubMed#PubMed_7852316
RESID:AA0212
http://purl.org/obo/owl/RESID#RESID_AA0212
UniMod:408
http://purl.org/obo/owl/UniMod#UniMod_408
O-(phospho-5'-RNA)-L-serine
PSI-MOD
O3-L-serine 5'-RNA phosphodiester
A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine.
PubMed:1705009
http://purl.org/obo/owl/PubMed#PubMed_1705009
RESID:AA0213
http://purl.org/obo/owl/RESID#RESID_AA0213
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O3-(phospho-5'-RNA)-L-serine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
O-(5'-phospho-RNA)-serine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-citrulline
This modification is not the result of deamidation, instead the guanidino group is replaced with an ureido group.
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N5-carbamylornithine
N5-carbamoylornithine
delta-ureidonorvaline
N5-(aminocarbonyl)ornithine
Deamidated
Deamidation
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-arginine residue to L-citrulline.
PubMed:2466844
http://purl.org/obo/owl/PubMed#PubMed_2466844
RESID:AA0214
http://purl.org/obo/owl/RESID#RESID_AA0214
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:7
http://purl.org/obo/owl/UniMod#UniMod_7
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Citrulline
Citrulline
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
alpha-amino-delta-ureidovaleric acid
2-amino-5-(aminocarbonyl)aminopentanoic acid
(S)-2-amino-5-(carbamoylamino)pentanoic acid
4-hydroxy-L-arginine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
4-hydroxylated L-arginine
4HyArg
2-amino-5-guanidino-4-hydroxypentanoic acid
4-hydroxyarginine
C(gamma)-hydroxyarginine
(2S,4Xi)-2-amino-5-carbamimidamido-4-hydroxypentanoic acid
gamma-hydroxyarginine
A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine.
RESID:AA0215
http://purl.org/obo/owl/RESID#RESID_AA0215
PubMed:7650037
http://purl.org/obo/owl/PubMed#PubMed_7650037
PubMed:10966817
http://purl.org/obo/owl/PubMed#PubMed_10966817
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-(L-isoaspartyl)-L-cysteine
Cross-link 2.
PSI-MOD
2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid
(S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-isoaspartyl cysteine
A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine.
PubMed:8286361
http://purl.org/obo/owl/PubMed#PubMed_8286361
RESID:AA0216
http://purl.org/obo/owl/RESID#RESID_AA0216
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Isoaspartyl cysteine isopeptide (Cys-Asn)
N-beta-aspartylcysteine
2'-alpha-mannosyl-L-tryptophan
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
C-linked (Man)
2'-tryptophan C-mannoside
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-(1H-2-alpha-mannopyranosyl-indol-3-yl)propanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Hexose
C2'ManTrp
Hex
A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.
PubMed:7947762
http://purl.org/obo/owl/PubMed#PubMed_7947762
PubMed:7547911
http://purl.org/obo/owl/PubMed#PubMed_7547911
UniMod:41
http://purl.org/obo/owl/UniMod#UniMod_41
RESID:AA0217
http://purl.org/obo/owl/RESID#RESID_AA0217
PubMed:15279557
http://purl.org/obo/owl/PubMed#PubMed_15279557
N6-mureinyl-L-lysine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine
N6-murein peptidoglycan lysine
modification from RESID
PubMed:4261992
http://purl.org/obo/owl/PubMed#PubMed_4261992
RESID:AA0218
http://purl.org/obo/owl/RESID#RESID_AA0218
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
1-chondroitin sulfate-L-aspartic acid ester
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
modification from RESID
RESID:AA0219
http://purl.org/obo/owl/RESID#RESID_AA0219
PubMed:1898736
http://purl.org/obo/owl/PubMed#PubMed_1898736
1-aspartic acid ester with 6-chondroitin 4-sulfate
Chondroitin 4-sulfate (covalent)
poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose)
protein-glycosaminoglycan-protein cross-link
S-(6-FMN)-L-cysteine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
modification from RESID
PubMed:1551870
http://purl.org/obo/owl/PubMed#PubMed_1551870
PubMed:620783
http://purl.org/obo/owl/PubMed#PubMed_620783
RESID:AA0220
http://purl.org/obo/owl/RESID#RESID_AA0220
UniMod:409
http://purl.org/obo/owl/UniMod#UniMod_409
PubMed:10869173
http://purl.org/obo/owl/PubMed#PubMed_10869173
6-[S-cysteinyl]flavin mononucleotide
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid
FMNH
S-6-FMN cysteine
6-[S-cysteinyl]FMN
flavin mononucleotide
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S6FMNCys
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
1'-(8alpha-FAD)-L-histidine
From DeltaMass: Average Mass: 784
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
modification from RESID
PubMed:4339951
http://purl.org/obo/owl/PubMed#PubMed_4339951
PubMed:1396672
http://purl.org/obo/owl/PubMed#PubMed_1396672
PubMed:10585424
http://purl.org/obo/owl/PubMed#PubMed_10585424
PubMed:9261083
http://purl.org/obo/owl/PubMed#PubMed_9261083
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0221
http://purl.org/obo/owl/RESID#RESID_AA0221
UniMod:50
http://purl.org/obo/owl/UniMod#UniMod_50
Tele-8alpha-FAD histidine
Ntele8aFADHis
tele-(8alpha-FAD)-histidine
tau-(8alpha-FAD)-histidine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Flavin adenine dinucleotide
N theta and N pi-(8alpha-Flavin) (on Histidine)
8alpha-N3-histidyl FAD [misnomer]
FAD
8alpha-(N(epsilon)-histidyl)FAD
8alpha-(N1'-histidyl)FAD
(S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
omega-N-phospho-L-arginine
PSI-MOD
Phosphorylation
Phosphoarginine
Phospho
PhosArg
modification from RESID
PubMed:8300603
http://purl.org/obo/owl/PubMed#PubMed_8300603
RESID:AA0222
http://purl.org/obo/owl/RESID#RESID_AA0222
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-5-[imino(phosphonoamino)methyl]aminopentanoic acid
alpha-amino-delta-phosphonoguanidinovaleric acid
N5-[imino(phosphonoamino)methyl]-L-ornithine
S-diphytanylglycerol diether-L-cysteine
incidental to RESID:AA0043
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
S-diphytanylglycerol diether
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-archaeol cysteine
S-archaeol cysteine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
modification from RESID
UniMod:410
http://purl.org/obo/owl/UniMod#UniMod_410
PubMed:8195126
http://purl.org/obo/owl/PubMed#PubMed_8195126
RESID:AA0223
http://purl.org/obo/owl/RESID#RESID_AA0223
PubMed:7797461
http://purl.org/obo/owl/PubMed#PubMed_7797461
S-(1-2',3'-phytanyl glycerol)cysteine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Archaeol
(R)-2-amino-3-[(S)-2,3-(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanylpropanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
alpha-1-microglobulin-Ig alpha complex chromophore
Cross-link 2.
PSI-MOD
Multimeric 3-hydroxykynurenine chromophore (covalent)
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
modification from RESID
PubMed:7506257
http://purl.org/obo/owl/PubMed#PubMed_7506257
PubMed:11877257
http://purl.org/obo/owl/PubMed#PubMed_11877257
PubMed:11058759
http://purl.org/obo/owl/PubMed#PubMed_11058759
RESID:AA0224
http://purl.org/obo/owl/RESID#RESID_AA0224
PubMed:7535251
http://purl.org/obo/owl/PubMed#PubMed_7535251
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
bis-L-cysteinyl bis-L-histidino diiron disulfide
Cross-link 4.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts three L-cysteine residues and an L-histidine residue to bis-L-cysteinyl bis-L-histidino diiron disulfide.
RESID:AA0225
http://purl.org/obo/owl/RESID#RESID_AA0225
PubMed:9651245
http://purl.org/obo/owl/PubMed#PubMed_9651245
PubMed:2765515
http://purl.org/obo/owl/PubMed#PubMed_2765515
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Rieske iron-sulfur cofactor
di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
hexakis-L-cysteinyl hexairon hexasulfide
Cross-link 6.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
modification from RESID
RESID:AA0226
http://purl.org/obo/owl/RESID#RESID_AA0226
PubMed:1318833
http://purl.org/obo/owl/PubMed#PubMed_1318833
PubMed:1311311
http://purl.org/obo/owl/PubMed#PubMed_1311311
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
prismane iron-sulfur cofactor
hexa-mu3-sulfidohexakis(S-cysteinyliron)
N6-(phospho-5'-adenosine)-L-lysine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid
AMP Lysyl
epsilon-5'-adenylic-L-lysine
5'-adenylic-N6-L-lysine
AMP binding site
A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine.
RESID:AA0227
http://purl.org/obo/owl/RESID#RESID_AA0227
PubMed:4944632
http://purl.org/obo/owl/PubMed#PubMed_4944632
UniMod:405
http://purl.org/obo/owl/UniMod#UniMod_405
DeltaMass:316
http://purl.org/obo/owl/DeltaMass#DeltaMass_316
PubMed:3882425
http://purl.org/obo/owl/PubMed#PubMed_3882425
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Phosphoadenosine
L-lysine monoanhydride with 5'-adenylic acid
N6-L-lysine 5'-adenosine phosphoramidester
N(zeta)-5'-adenylic-L-lysine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N6-(phospho-5'-guanosine)-L-lysine
From DeltaMass: Average Mass: 345 Formula:C10H12O5N7P1 Monoisotopic Mass Change:345.047 Average Mass Change:345.209 References:PE Sciex
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
5'-guanylic-N6-L-lysine
(S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Phosphoguanosine
phospho-guanosine
N6-L-lysine 5'-guanosine phosphoramidester
modification from RESID
RESID:AA0228
http://purl.org/obo/owl/RESID#RESID_AA0228
UniMod:413
http://purl.org/obo/owl/UniMod#UniMod_413
PubMed:6092377
http://purl.org/obo/owl/PubMed#PubMed_6092377
PubMed:6264433
http://purl.org/obo/owl/PubMed#PubMed_6264433
DeltaMass:304
http://purl.org/obo/owl/DeltaMass#DeltaMass_304
N(zeta)-5'-guanylic-lysine
lysine guanosine-5'-monophosphate
L-lysine monoanhydride with 5'-guanylic acid
epsilon-5'-guanylic-L-lysine
5'phos Guanosyl
L-cysteine glutathione disulfide
From DeltaMass: Average Mass: 305
PSI-MOD
A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine.
PubMed:3083866
http://purl.org/obo/owl/PubMed#PubMed_3083866
PubMed:8344916
http://purl.org/obo/owl/PubMed#PubMed_8344916
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0229
http://purl.org/obo/owl/RESID#RESID_AA0229
UniMod:55
http://purl.org/obo/owl/UniMod#UniMod_55
ChEBI:21264
http://purl.org/obo/owl/ChEBI#ChEBI_21264
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N-(N-gamma-glutamyl-cystinyl)-glycine
S-glutathionyl cysteine
L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid
Glutathionation
cysteinyl glutathione
glutathione disulfide
Glutathione
S-nitrosyl-L-cysteine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
SNOCys
S-nitrosocysteine
S-nitrosylation
A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine.
PubMed:11562475
http://purl.org/obo/owl/PubMed#PubMed_11562475
PubMed:15688001
http://purl.org/obo/owl/PubMed#PubMed_15688001
PubMed:10442087
http://purl.org/obo/owl/PubMed#PubMed_10442087
RESID:AA0230
http://purl.org/obo/owl/RESID#RESID_AA0230
UniMod:275
http://purl.org/obo/owl/UniMod#UniMod_275
PubMed:8626764
http://purl.org/obo/owl/PubMed#PubMed_8626764
PubMed:8637569
http://purl.org/obo/owl/PubMed#PubMed_8637569
L-cysteine nitrite ester
(R)-2-amino-3-nitrososulfanyl-propanoic acid
S-nitrosocysteine
Nitrosyl
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N4-(ADP-ribosyl)-L-asparagine
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid
ADP Ribose addition
ADP-Ribosyl
ADP-ribosylasparagine
A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine.
PubMed:15842200
http://purl.org/obo/owl/PubMed#PubMed_15842200
PubMed:2498316
http://purl.org/obo/owl/PubMed#PubMed_2498316
RESID:AA0231
http://purl.org/obo/owl/RESID#RESID_AA0231
UniMod:213
http://purl.org/obo/owl/UniMod#UniMod_213
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-beta-methylthioaspartic acid
PSI-MOD
3-methylthio-aspartic acid
3-methylthioaspartic acid
(2R,3Xi)-2-amino-3-methylsulfanylbutanedioic acid
3-carboxy-S-methyl-cysteine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid.
DeltaMass:61
http://purl.org/obo/owl/DeltaMass#DeltaMass_61
PubMed:15473684
http://purl.org/obo/owl/PubMed#PubMed_15473684
PubMed:8844851
http://purl.org/obo/owl/PubMed#PubMed_8844851
UniMod:39
http://purl.org/obo/owl/UniMod#UniMod_39
RESID:AA0232
http://purl.org/obo/owl/RESID#RESID_AA0232
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Methylthio
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Beta-methylthiolation
beta-methylthio-aspartic acid
beta-Methylthio-aspartic acid
5'-(N6-L-lysine)-L-topaquinone
Cross-link 2; secondary to RESID:AA0147.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
modification from RESID
RESID:AA0233
http://purl.org/obo/owl/RESID#RESID_AA0233
PubMed:8688089
http://purl.org/obo/owl/PubMed#PubMed_8688089
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Lysine tyrosylquinone (Lys-Tyr)
lysyl oxidase cofactor
5'-(L-lysine)-L-tyrosylquinone
1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
S-methyl-L-cysteine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
SMeCys
S-methylcysteine
S-methylated L-cysteine
Methylation
Methyl
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-3-(methylthio)alanine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(R)-2-amino-3-(methylsulfanyl)propanoic acid
A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine.
RESID:AA0234
http://purl.org/obo/owl/RESID#RESID_AA0234
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:1339288
http://purl.org/obo/owl/PubMed#PubMed_1339288
PubMed:10660523
http://purl.org/obo/owl/PubMed#PubMed_10660523
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
4-hydroxy-L-lysine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine.
RESID:AA0235
http://purl.org/obo/owl/RESID#RESID_AA0235
PubMed:4005040
http://purl.org/obo/owl/PubMed#PubMed_4005040
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(2S,4R)-2,6-diamino-4-hydroxyhexanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-threo-gamma-hydroxylysine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
alpha,epsilon-diamino-gamma-hydroxycaproic acid
4HyLys
4-hydroxylated L-lysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N4-hydroxymethyl-L-asparagine
This modification has not been observed to occur naturally.
PSI-MOD
N4-hydroxymethylasparagine
Hydroxymethyl
beta-hydroxymethylasparagine
(S)-2-amino-N4-hydroxymethylbutanediamic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
hydroxymethyl
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N(gamma)-hydroxymethylasparagine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine.
RESID:AA0236
http://purl.org/obo/owl/RESID#RESID_AA0236
UniMod:414
http://purl.org/obo/owl/UniMod#UniMod_414
O-(ADP-ribosyl)-L-serine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
ADP-ribosylserine
O3-(ADP-ribosyl)-L-serine
O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine.
PubMed:15842200
http://purl.org/obo/owl/PubMed#PubMed_15842200
PubMed:3141412
http://purl.org/obo/owl/PubMed#PubMed_3141412
RESID:AA0237
http://purl.org/obo/owl/RESID#RESID_AA0237
UniMod:213
http://purl.org/obo/owl/UniMod#UniMod_213
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid
ADP-Ribosyl
ADP Ribose addition
L-cysteine oxazole-4-carboxylic acid
Cross-link 2.
PSI-MOD
(R)-2-(1-amino-2-sulfanylethyl)-4-oxazolecarboxylic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Oxazole-4-carboxylic acid (Cys-Ser)
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
PubMed:8183941
http://purl.org/obo/owl/PubMed#PubMed_8183941
PubMed:8895467
http://purl.org/obo/owl/PubMed#PubMed_8895467
RESID:AA0238
http://purl.org/obo/owl/RESID#RESID_AA0238
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
L-cysteine oxazoline-4-carboxylic acid
Cross-link 2.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid.
RESID:AA0239
http://purl.org/obo/owl/RESID#RESID_AA0239
PubMed:1880060
http://purl.org/obo/owl/PubMed#PubMed_1880060
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Oxazoline-4-carboxylic acid (Cys-Ser)
(S)-2-((R)-1-amino-2-sulfanylethyl)-4-oxazolinecarboxylic acid
glycine oxazole-4-carboxylic acid
Cross-link 2.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid.
PubMed:8895467
http://purl.org/obo/owl/PubMed#PubMed_8895467
RESID:AA0240
http://purl.org/obo/owl/RESID#RESID_AA0240
PubMed:8183941
http://purl.org/obo/owl/PubMed#PubMed_8183941
Oxazole-4-carboxylic acid (Gly-Ser)
2-aminomethyl-4-oxazolecarboxylic acid
glycine thiazole-4-carboxylic acid
Cross-link 2.
PSI-MOD
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid.
RESID:AA0241
http://purl.org/obo/owl/RESID#RESID_AA0241
PubMed:8895467
http://purl.org/obo/owl/PubMed#PubMed_8895467
PubMed:8183941
http://purl.org/obo/owl/PubMed#PubMed_8183941
ChEBI:21276
http://purl.org/obo/owl/ChEBI#ChEBI_21276
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Thiazole-4-carboxylic acid (Gly-Cys)
2-aminomethyl-4-thiazolecarboxylic acid
L-serine thiazole-4-carboxylic acid
Cross-link 2.
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid.
PubMed:8895467
http://purl.org/obo/owl/PubMed#PubMed_8895467
RESID:AA0242
http://purl.org/obo/owl/RESID#RESID_AA0242
PubMed:8183941
http://purl.org/obo/owl/PubMed#PubMed_8183941
(R)-2-(1-amino-2-hydroxyethyl)-4-thiazolecarboxylic acid
Thiazole-4-carboxylic acid (Ser-Cys)
L-phenylalanine thiazole-4-carboxylic acid
Cross-link 2.
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid.
RESID:AA0243
http://purl.org/obo/owl/RESID#RESID_AA0243
PubMed:1880060
http://purl.org/obo/owl/PubMed#PubMed_1880060
Thiazole-4-carboxylic acid (Phe-Cys)
(R)-2-(1-amino-2-phenylethyl)-4-thiazolecarboxylic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-cysteine thiazole-4-carboxylic acid
Cross-link 2.
PSI-MOD
Thiazole-4-carboxylic acid (Cys-Cys)
(S)-2-(1-amino-2-sulfanylethyl)-4-thiazolecarboxylic acid
A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid.
RESID:AA0244
http://purl.org/obo/owl/RESID#RESID_AA0244
PubMed:1880060
http://purl.org/obo/owl/PubMed#PubMed_1880060
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-lysine thiazole-4-carboxylic acid
Cross-link 2. Lysine is now thought not to be encoded in the peptide sequence modified to produce GE2270. See RESID:AA0470.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(R)-2-(1,5-diaminopentyl)-4-thiazolecarboxylic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid.
PubMed:1880060
http://purl.org/obo/owl/PubMed#PubMed_1880060
RESID:AA0245
http://purl.org/obo/owl/RESID#RESID_AA0245
O-(phospho-5'-DNA)-L-serine
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine.
PubMed:7265205
http://purl.org/obo/owl/PubMed#PubMed_7265205
PubMed:7142163
http://purl.org/obo/owl/PubMed#PubMed_7142163
RESID:AA0246
http://purl.org/obo/owl/RESID#RESID_AA0246
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
O-(5'-phospho-DNA)-serine
O3-(phospho-5'-DNA)-L-serine
O3-L-serine 5'-DNA phosphodiester
keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
modification from RESID
PubMed:3472204
http://purl.org/obo/owl/PubMed#PubMed_3472204
RESID:AA0247
http://purl.org/obo/owl/RESID#RESID_AA0247
PubMed:1417734
http://purl.org/obo/owl/PubMed#PubMed_1417734
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
O-linked (Xyl...) (keratan sulfate)
poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
keratosulfate
O4'-(phospho-5'-RNA)-L-tyrosine
PSI-MOD
(S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid
O-(5'-phospho-RNA)-tyrosine
A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine.
PubMed:1702164
http://purl.org/obo/owl/PubMed#PubMed_1702164
PubMed:217003
http://purl.org/obo/owl/PubMed#PubMed_217003
PubMed:209034
http://purl.org/obo/owl/PubMed#PubMed_209034
RESID:AA0249
http://purl.org/obo/owl/RESID#RESID_AA0249
PubMed:6264310
http://purl.org/obo/owl/PubMed#PubMed_6264310
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
O4'-L-tyrosine 5'-RNA phosphodiester
3-(3'-L-histidyl)-L-tyrosine
Cross-link 2.
PSI-MOD
modification from RESID
PubMed:9144772
http://purl.org/obo/owl/PubMed#PubMed_9144772
RESID:AA0250
http://purl.org/obo/owl/RESID#RESID_AA0250
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(2S,3R)-2-amino-3-[3-((S)-2-amino-2-carboxy-1-(4-hydoxyphenyl)ethyl)imidazol-4-yl]propanoic acid
3'-histidyl-3-tyrosine (His-Tyr)
3-(pi-histidyl)tyrosine
3-(N3'-histidyl)tyrosine
beta-(N(delta)-histidyl)tyrosine
3-(pros-histidyl)tyrosine
beta-(N3'-histidyl)tyrosine
L-methionine sulfone
DeltaMass gives the formula C 5 H 9 N 3 O 1 S 1 with mass 163
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S)-2-amino-4-(methylsulfonyl)butanoic acid
Dioxidation
dihydroxy
S,S-dioxymethionine
Oxidation of Methionine (to Sulphone)
A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone.
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
DeltaMass:205
http://purl.org/obo/owl/DeltaMass#DeltaMass_205
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
PubMed:7786407
http://purl.org/obo/owl/PubMed#PubMed_7786407
PubMed:7791219
http://purl.org/obo/owl/PubMed#PubMed_7791219
PubMed:9252331
http://purl.org/obo/owl/PubMed#PubMed_9252331
RESID:AA0251
http://purl.org/obo/owl/RESID#RESID_AA0251
L-methionine S,S-dioxide
Methionine sulfone
MethionylSulphone
MetO2
dipyrrolylmethanemethyl-L-cysteine
PSI-MOD
dipyrrolylmethanemethyl
Dipyrrolylmethanemethyl
dipyrromethane cofactor
dipyrrolylmethyl-L-cysteine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
pyrromethane cofactor
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
dipyrrole cofactor
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid
Pyrromethane cofactor (covalent)
modification from RESID
PubMed:3042456
http://purl.org/obo/owl/PubMed#PubMed_3042456
PubMed:3421931
http://purl.org/obo/owl/PubMed#PubMed_3421931
PubMed:3196304
http://purl.org/obo/owl/PubMed#PubMed_3196304
RESID:AA0252
http://purl.org/obo/owl/RESID#RESID_AA0252
UniMod:416
http://purl.org/obo/owl/UniMod#UniMod_416
PubMed:8727319
http://purl.org/obo/owl/PubMed#PubMed_8727319
S-(2-aminovinyl)-3-methyl-D-cysteine
Cross-link 2.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys)
decarboxylated methyllanthionine
(2S,3S)-2-amino-3-[((Z)-2-aminovinyl)sulfanyl]butanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine.
RESID:AA0253
http://purl.org/obo/owl/RESID#RESID_AA0253
PubMed:9119018
http://purl.org/obo/owl/PubMed#PubMed_9119018
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
O4'-(phospho-5'-DNA)-L-tyrosine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O4'-L-tyrosine 5'-DNA phosphodiester
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
O-(5'-phospho-DNA)-tyrosine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine.
RESID:AA0254
http://purl.org/obo/owl/RESID#RESID_AA0254
PubMed:1861973
http://purl.org/obo/owl/PubMed#PubMed_1861973
PubMed:3684578
http://purl.org/obo/owl/PubMed#PubMed_3684578
PubMed:2940511
http://purl.org/obo/owl/PubMed#PubMed_2940511
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
O-(phospho-5'-DNA)-L-threonine
PSI-MOD
O3-(phospho-5'-DNA)-L-threonine
O3-L-threonine 5'-DNA phosphodiester
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine.
RESID:AA0255
http://purl.org/obo/owl/RESID#RESID_AA0255
PubMed:3081736
http://purl.org/obo/owl/PubMed#PubMed_3081736
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
O4'-(phospho-5'-uridine)-L-tyrosine
From DeltaMass: Average Mass: 306.
PSI-MOD
PhosphoUridine
O-Uridinylylation (of Tyrosine)
O4'-L-tyrosine 5'-uridine phosphodiester
A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine.
PubMed:11467524
http://purl.org/obo/owl/PubMed#PubMed_11467524
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:417
http://purl.org/obo/owl/UniMod#UniMod_417
PubMed:2885322
http://purl.org/obo/owl/PubMed#PubMed_2885322
RESID:AA0256
http://purl.org/obo/owl/RESID#RESID_AA0256
hydrogen 5'-uridylate tyrosine ester
O-UMP-tyrosine
(S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid
5'-uridylic-O-tyrosine
uridine phosphodiester
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-(L-glutamyl)-L-tyrosine
Cross-link 2.
PSI-MOD
(S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
modification from RESID
PubMed:8093886
http://purl.org/obo/owl/PubMed#PubMed_8093886
PubMed:6387372
http://purl.org/obo/owl/PubMed#PubMed_6387372
ChEBI:21477
http://purl.org/obo/owl/ChEBI#ChEBI_21477
RESID:AA0257
http://purl.org/obo/owl/RESID#RESID_AA0257
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
S-phycoviolobilin-L-cysteine
PSI-MOD
S-phycobiliviolin-L-cysteine
phycocyanobilin
Phycocyanobilin
cryptoviolobilin
cryptoviolin
cryptobiliviolin
(4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin.
UniMod:387
http://purl.org/obo/owl/UniMod#UniMod_387
PubMed:2106585
http://purl.org/obo/owl/PubMed#PubMed_2106585
RESID:AA0258
http://purl.org/obo/owl/RESID#RESID_AA0258
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
phycoerythrobilin-bis-L-cysteine
Cross-link 2.
PSI-MOD
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin.
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
RESID:AA0259
http://purl.org/obo/owl/RESID#RESID_AA0259
PubMed:3838747
http://purl.org/obo/owl/PubMed#PubMed_3838747
(2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione
phycoerythrobilin biscysteine adduct
3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
phycourobilin-bis-L-cysteine
Cross-link 2.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
phycourobilin biscysteine adduct
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin.
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
PubMed:3838665
http://purl.org/obo/owl/PubMed#PubMed_3838665
PubMed:3838747
http://purl.org/obo/owl/PubMed#PubMed_3838747
PubMed:8876649
http://purl.org/obo/owl/PubMed#PubMed_8876649
RESID:AA0260
http://purl.org/obo/owl/RESID#RESID_AA0260
3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione
3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid
N-L-glutamyl-poly-L-glutamic acid
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
modification from RESID
PubMed:328274
http://purl.org/obo/owl/PubMed#PubMed_328274
RESID:AA0261
http://purl.org/obo/owl/RESID#RESID_AA0261
PubMed:2570347
http://purl.org/obo/owl/PubMed#PubMed_2570347
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-cysteine sulfinic acid
"Hyun Ae Woo, et. al., Science 300 (5619), 653-656"
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-amino-3-sulfinopropanoic acid
(R)-2-amino-2-carboxyethanesulfinic acid
A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
ChEBI:16345
http://purl.org/obo/owl/ChEBI#ChEBI_16345
RESID:AA0262
http://purl.org/obo/owl/RESID#RESID_AA0262
PubMed:9586994
http://purl.org/obo/owl/PubMed#PubMed_9586994
PubMed:9252331
http://purl.org/obo/owl/PubMed#PubMed_9252331
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-cysteinesulfinic acid
S-sulfinocysteine
dihydroxy
Dioxidation
Cysteine sulfinic acid (-SO2H)
cysteine-S,S-dioxide
3-sulfinoalanine
CysO2H
L-3',4',5'-trihydroxyphenylalanine
From DeltaMass: Average Mass: 32
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA)
A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine.
PubMed:9252331
http://purl.org/obo/owl/PubMed#PubMed_9252331
PubMed:9434739
http://purl.org/obo/owl/PubMed#PubMed_9434739
PubMed:12771378
http://purl.org/obo/owl/PubMed#PubMed_12771378
PubMed:8554314
http://purl.org/obo/owl/PubMed#PubMed_8554314
RESID:AA0263
http://purl.org/obo/owl/RESID#RESID_AA0263
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
(S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
35Hy2Tyr
dihydroxy
Dioxidation
L-3,4,5-TOPA
O-(sn-1-glycerophosphoryl)-L-serine
PSI-MOD
Glycerophospho
alpha-glycerophosphoryl serine
(S)-2-amino-3-[(Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
glycerophosphoserine
O-(sn-1-glycerophosphoryl)serine
O3-(sn-1-glycerophosphoryl)-L-serine
O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester
modification from RESID
RESID:AA0264
http://purl.org/obo/owl/RESID#RESID_AA0264
UniMod:419
http://purl.org/obo/owl/UniMod#UniMod_419
PubMed:8645220
http://purl.org/obo/owl/PubMed#PubMed_8645220
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
glycerophospho
O3-L-serine glyceryl-1-phosphodiester
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
1-thioglycine
This modification occurs naturally in two forms. At an interior peptide location it exists as aminoethanethionic acid (or aminoethanethioic O-acid). At the carboxyl-terminal it exists as aminoethanethiolic acid (or aminoethanethioic S-acid).
PSI-MOD
1-thioglycine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
thiocarboxylic acid
A protein modification that effectively converts a glycine residue to 1-thioglycine.
RESID:AA0265
http://purl.org/obo/owl/RESID#RESID_AA0265
PubMed:9367957
http://purl.org/obo/owl/PubMed#PubMed_9367957
UniMod:420
http://purl.org/obo/owl/UniMod#UniMod_420
PubMed:11463785
http://purl.org/obo/owl/PubMed#PubMed_11463785
aminoethanethioic acid
2-amino-1-sulfanylethanone
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
aminoethanethioic S-acid
aminoethanethioic O-acid
aminoethanethionic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
aminoethanethiolic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Carboxy->Thiocarboxy
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
aminothioacetic acid
S(O)Gly
heme P460-bis-L-cysteine-L-tyrosine
Cross-link 3.
PSI-MOD
Heme (covalent; via 3 links)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
biscysteinyl-tyrosinyl-heme
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:8325841
http://purl.org/obo/owl/PubMed#PubMed_8325841
RESID:AA0266
http://purl.org/obo/owl/RESID#RESID_AA0266
PubMed:9095195
http://purl.org/obo/owl/PubMed#PubMed_9095195
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
O-(phospho-5'-adenosine)-L-threonine
PSI-MOD
AMP binding site
5'-adenylic-O3-L-threonine
(2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid
O3-(phospho-5'-adenosine)-L-threonine
O(gamma)-5'-adenylic-L-threonine
L-threonine monoanhydride with 5'-adenylic acid
beta-5'-adenylic-L-threonine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine.
RESID:AA0267
http://purl.org/obo/owl/RESID#RESID_AA0267
PubMed:8917428
http://purl.org/obo/owl/PubMed#PubMed_8917428
UniMod:405
http://purl.org/obo/owl/UniMod#UniMod_405
PubMed:2989287
http://purl.org/obo/owl/PubMed#PubMed_2989287
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Phosphoadenosine
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
O3-L-threonine 5'-adenosine phosphodiester
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide
Cross-link 7; secondary to RESID:AA0269.
PSI-MOD
modification from RESID
RESID:AA0268
http://purl.org/obo/owl/RESID#RESID_AA0268
PubMed:12764602
http://purl.org/obo/owl/PubMed#PubMed_12764602
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
4Fe-2S-3O cluster
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron)
hybrid four iron cluster 2
prismane iron-sulfur cofactor [misnomer]
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-cysteine persulfide
PSI-MOD
persulfide
Cysteine persulfide
3-(thiosulfeno)-alanine
2-amino-3-persulfhydrylpropanoic acid
A protein modification that effectively converts an L-cysteine residue to L-cysteine persulfide.
RESID:AA0269
http://purl.org/obo/owl/RESID#RESID_AA0269
UniMod:421
http://purl.org/obo/owl/UniMod#UniMod_421
PubMed:8161529
http://purl.org/obo/owl/PubMed#PubMed_8161529
PubMed:4276457
http://purl.org/obo/owl/PubMed#PubMed_4276457
PubMed:15096637
http://purl.org/obo/owl/PubMed#PubMed_15096637
ChEBI:28839
http://purl.org/obo/owl/ChEBI#ChEBI_28839
2-amino-3-hydropersulfidopropanoic acid
2-amino-3-hydrodisulfidopropanoic acid
2-amino-3-disulfanylpropanoic acid
(R)-2-amino-3-disulfanylpropanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-sulfanylcysteine
thiocysteine
Sulfide
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
3'-(1'-L-histidyl)-L-tyrosine
Cross-link 2.
PSI-MOD
(2S)-2-amino-3-[1-(1-((S)-2-amino-2-carboxyethyl)-4-hydoxyphen-3-yl)imidazol-4-yl]propanoic acid
3'-(N1'-histidyl)tyrosine
3'-(N(epsilon)-histidyl)tyrosine
1'-histidyl-3'-tyrosine (His-Tyr)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
3'-(pi-histidyl)tyrosine
3'-(pros-histidyl)tyrosine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine.
PubMed:10338009
http://purl.org/obo/owl/PubMed#PubMed_10338009
RESID:AA0270
http://purl.org/obo/owl/RESID#RESID_AA0270
ChEBI:19837
http://purl.org/obo/owl/ChEBI#ChEBI_19837
heme P460-bis-L-cysteine-L-lysine
Cross-link 3.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
RESID:AA0271
http://purl.org/obo/owl/RESID#RESID_AA0271
PubMed:9237682
http://purl.org/obo/owl/PubMed#PubMed_9237682
PubMed:12709052
http://purl.org/obo/owl/PubMed#PubMed_12709052
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Heme (covalent; via 3 links)
bis-S-cysteinyl-N6-lysino-heme
5-methyl-L-arginine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
C5MeArg
5-methylated L-arginine
Methyl
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
delta-methylarginine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-amino-5-guanidinohexanoic acid
(2S,5S)-2-amino-5-carbamimidamidohexanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
5-methylarginine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
4-methylarginine [misnomer]
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine.
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0272
http://purl.org/obo/owl/RESID#RESID_AA0272
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:9367957
http://purl.org/obo/owl/PubMed#PubMed_9367957
PubMed:10660523
http://purl.org/obo/owl/PubMed#PubMed_10660523
Methylation
2-methyl-L-glutamine
PSI-MOD
Methylation
Methyl
A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine.
PubMed:10660523
http://purl.org/obo/owl/PubMed#PubMed_10660523
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:9367957
http://purl.org/obo/owl/PubMed#PubMed_9367957
RESID:AA0273
http://purl.org/obo/owl/RESID#RESID_AA0273
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
C2MeGln
alpha-methylglutamine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-methylated L-glutamine
2-methylglutamine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-methylglutamine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-2-amino-2-methylpentanediamic acid
N-pyruvic acid 2-iminyl-L-cysteine
PSI-MOD
PyruvicAcidIminyl
(R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid
N-pyruvate 2-iminyl-cysteine
N-pyruvic acid 2-iminyl
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an Lcysteline residue to N-pyruvic acid 2-iminyl-L-cysteine.
UniMod:422
http://purl.org/obo/owl/UniMod#UniMod_422
RESID:AA0274
http://purl.org/obo/owl/RESID#RESID_AA0274
PubMed:1388164
http://purl.org/obo/owl/PubMed#PubMed_1388164
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-pyruvic acid 2-iminyl-L-valine
PSI-MOD
A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine.
RESID:AA0275
http://purl.org/obo/owl/RESID#RESID_AA0275
UniMod:422
http://purl.org/obo/owl/UniMod#UniMod_422
PubMed:2071591
http://purl.org/obo/owl/PubMed#PubMed_2071591
N-pyruvic acid 2-iminyl
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
PyruvicAcidIminyl
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-2-(1-carboxy-2-methylpropanimino)propanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-pyruvate 2-iminyl-valine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
3'-heme-L-histidine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
pros-histidyl heme
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:12486054
http://purl.org/obo/owl/PubMed#PubMed_12486054
PubMed:9712585
http://purl.org/obo/owl/PubMed#PubMed_9712585
PubMed:12429096
http://purl.org/obo/owl/PubMed#PubMed_12429096
PubMed:12119398
http://purl.org/obo/owl/PubMed#PubMed_12119398
RESID:AA0276
http://purl.org/obo/owl/RESID#RESID_AA0276
[7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
2-[1-(N3'-histidyl)ethyl]protoporphyrin IX
N(delta)-histidyl heme
Heme (covalent; via 1 link)
pi-histidyl heme
N3'-histidyl heme
S-selenyl-L-cysteine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine.
PubMed:10430865
http://purl.org/obo/owl/PubMed#PubMed_10430865
PubMed:10966817
http://purl.org/obo/owl/PubMed#PubMed_10966817
UniMod:423
http://purl.org/obo/owl/UniMod#UniMod_423
RESID:AA0277
http://purl.org/obo/owl/RESID#RESID_AA0277
PubMed:14594807
http://purl.org/obo/owl/PubMed#PubMed_14594807
PubMed:12716131
http://purl.org/obo/owl/PubMed#PubMed_12716131
PubMed:11827487
http://purl.org/obo/owl/PubMed#PubMed_11827487
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
selenyl
S-selenylcysteine
S-selanylcysteine
S-selanylcysteine
Delta:Se(1)
cysteine perselenide [misnomer]
2-amino-3-hydroselenylthiopropanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-amino-3-hydroselenylsulfidopropanoic acid
(R)-2-amino-3-(selanylsulfanyl)propanoic acid
2-amino-3-hydroselenosulfidopropanoic acid
N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
lysine derivative Lys(x)
N6-[3-(N(omega)-dimethylaminopropyl-poly[3-(methylamino)propyl]amino)propyl]lysine
N6-poly(methylaminopropyl)lysine
silaffin polycationic lysine derivative
A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine.
RESID:AA0278
http://purl.org/obo/owl/RESID#RESID_AA0278
PubMed:11349130
http://purl.org/obo/owl/PubMed#PubMed_11349130
PubMed:10550045
http://purl.org/obo/owl/PubMed#PubMed_10550045
(S)-2-amino-N6-(dimethylaminoprop-3-yl-poly[N-(methyl)aminoprop-3-yl]aminoprop-3-yl)aminohexanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
dihydroxyheme-L-aspartate ester-L-glutamate ester
Cross-link 2.
PSI-MOD
A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
RESID:AA0279
http://purl.org/obo/owl/RESID#RESID_AA0279
PubMed:10447690
http://purl.org/obo/owl/PubMed#PubMed_10447690
Heme (covalent; via 2 links)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
[13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
peroxidase heme cofactor
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium
Cross-link 3.
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Heme (covalent; via 3 links)
myeloperoxidase heme cofactor
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium
[13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
RESID:AA0280
http://purl.org/obo/owl/RESID#RESID_AA0280
PubMed:7840679
http://purl.org/obo/owl/PubMed#PubMed_7840679
PubMed:1320128
http://purl.org/obo/owl/PubMed#PubMed_1320128
PubMed:10480885
http://purl.org/obo/owl/PubMed#PubMed_10480885
PubMed:10447690
http://purl.org/obo/owl/PubMed#PubMed_10447690
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
PSI-MOD
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-molybdenum
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
molybdenum bis(molybdopterin guanine dinucleotide)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MolybdopterinGD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
modification from RESID
UniMod:424
http://purl.org/obo/owl/UniMod#UniMod_424
RESID:AA0281
http://purl.org/obo/owl/RESID#RESID_AA0281
(2S,3R,4S)-3,4-dihydroxyproline
From DeltaMass: Average Mass: 32.
PSI-MOD
A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline.
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
RESID:AA0282
http://purl.org/obo/owl/RESID#RESID_AA0282
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
trans-2,3-cis-3,4-dihydroxy-L-proline
Dioxidation
dihydroxy
34Hy2Pro
3,4-Dihydroxylation (of Proline)
3,4-dihydroxylated L-proline
2-alpha-3-beta-4-beta-3,4-dihydroxyproline
(3R,4S)-3,4-dihydroxyproline
pyrroloquinoline quinone
Cross-link 2.
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
methoxatin
coenzyme PQQ
Pyrroloquinoline quinone (Glu-Tyr)
2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone
4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid
2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
modification from RESID
ChEBI:18315
http://purl.org/obo/owl/ChEBI#ChEBI_18315
PubMed:1310505
http://purl.org/obo/owl/PubMed#PubMed_1310505
RESID:AA0283
http://purl.org/obo/owl/RESID#RESID_AA0283
PubMed:7665488
http://purl.org/obo/owl/PubMed#PubMed_7665488
tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide
Cross-link 4.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron)
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts three L-cysteine residues and an L-histidine residue to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide.
RESID:AA0284
http://purl.org/obo/owl/RESID#RESID_AA0284
PubMed:9836629
http://purl.org/obo/owl/PubMed#PubMed_9836629
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide
Cross-link 4.
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts three L-cysteine residues and an L-histidine residue to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide.
PubMed:7854413
http://purl.org/obo/owl/PubMed#PubMed_7854413
RESID:AA0285
http://purl.org/obo/owl/RESID#RESID_AA0285
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
tris-L-cysteinyl L-aspartato tetrairon tetrasulfide
Cross-link 4.
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron)
modification from RESID
PubMed:7819255
http://purl.org/obo/owl/PubMed#PubMed_7819255
PubMed:9283079
http://purl.org/obo/owl/PubMed#PubMed_9283079
RESID:AA0286
http://purl.org/obo/owl/RESID#RESID_AA0286
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N6-pyruvic acid 2-iminyl-L-lysine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine.
RESID:AA0287
http://purl.org/obo/owl/RESID#RESID_AA0287
PubMed:9047371
http://purl.org/obo/owl/PubMed#PubMed_9047371
UniMod:422
http://purl.org/obo/owl/UniMod#UniMod_422
PubMed:1463470
http://purl.org/obo/owl/PubMed#PubMed_1463470
PubMed:7853400
http://purl.org/obo/owl/PubMed#PubMed_7853400
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
PyruvicAcidIminyl
N-pyruvic acid 2-iminyl
(S)-2-amino-6-(1-carboxy-ethylimino)hexanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
tris-L-cysteinyl L-serinyl tetrairon tetrasulfide
Cross-link 4.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
modification from RESID
RESID:AA0288
http://purl.org/obo/owl/RESID#RESID_AA0288
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron)
bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide
Cross-link 4.
PSI-MOD
tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modification from RESID
RESID:AA0289
http://purl.org/obo/owl/RESID#RESID_AA0289
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
O-octanoyl-L-serine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
OOctSer
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Octanoyl
octanoyl
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
O3-octanoyl-L-serine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-serine octanoate ester
(2S)-2-amino-3-(octanoyloxy)propanoic acid
O-octanoylated L-serine
O-octanoyl serine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine.
UniMod:426
http://purl.org/obo/owl/UniMod#UniMod_426
PubMed:10604470
http://purl.org/obo/owl/PubMed#PubMed_10604470
RESID:AA0290
http://purl.org/obo/owl/RESID#RESID_AA0290
PubMed:12716131
http://purl.org/obo/owl/PubMed#PubMed_12716131
O-D-glucuronosyl-L-serine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
modification from RESID
UniMod:54
http://purl.org/obo/owl/UniMod#UniMod_54
RESID:AA0291
http://purl.org/obo/owl/RESID#RESID_AA0291
PubMed:10858503
http://purl.org/obo/owl/PubMed#PubMed_10858503
PubMed:7398618
http://purl.org/obo/owl/PubMed#PubMed_7398618
PubMed:12716131
http://purl.org/obo/owl/PubMed#PubMed_12716131
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O3-D-glucuronosyl-L-serine
O-linked (HexA)
N-glucuronylation
Glucuronyl
(2S)-2-amino-3-glucuronosylpropanoic acid
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide
Cross-link 7; secondary to RESID:AA0269.
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
modification from RESID
RESID:AA0292
http://purl.org/obo/owl/RESID#RESID_AA0292
hybrid nickel-triiron cluster
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron)
carbon monoxide dehydrogenase nickel-iron cofactor
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Ni-3Fe-2S-3O cluster
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide
Cross-link 7; secondary to RESID:AA0269.
PSI-MOD
Ni-3Fe-2S-3O cluster
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron)
hybrid nickel-triiron cluster
carbon monoxide dehydrogenase nickel-iron cofactor
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modification from RESID
RESID:AA0293
http://purl.org/obo/owl/RESID#RESID_AA0293
PubMed:2550436
http://purl.org/obo/owl/PubMed#PubMed_2550436
N6-(L-isoaspartyl)-L-lysine
Cross-link 2.
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S,S)-2-amino-6-[(3-amino-3-carboxypropanoyl)amino]hexanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoaspartyl)-L-lysine.
ChEBI:21862
http://purl.org/obo/owl/ChEBI#ChEBI_21862
PubMed:11000116
http://purl.org/obo/owl/PubMed#PubMed_11000116
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0294
http://purl.org/obo/owl/RESID#RESID_AA0294
PubMed:6503713
http://purl.org/obo/owl/PubMed#PubMed_6503713
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Isoaspartyl lysine isopeptide (Lys-Asn) (interchain with N-...)
beta-(N6-lysyl)aspartyl acid
N-(beta-Aspartyl)-Lysine (Crosslink)
isoaspartyl N6-lysine
L-glutamyl-5-poly(ADP-ribose)
From DeltaMass: Average Mass: 541.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-ADP-ribosylation (on Glutamate or C terminus)
L-isoglutamyl-poly(ADP-ribose)
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
PolyADP-ribosyl glutamic acid
(S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid
A protein modification that effectively converts an L-glutamic acid residue to an L-glutamyl-5-poly(ADP-ribose).
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:213
http://purl.org/obo/owl/UniMod#UniMod_213
RESID:AA0295
http://purl.org/obo/owl/RESID#RESID_AA0295
PubMed:8533153
http://purl.org/obo/owl/PubMed#PubMed_8533153
PubMed:15842200
http://purl.org/obo/owl/PubMed#PubMed_15842200
PubMed:11246023
http://purl.org/obo/owl/PubMed#PubMed_11246023
ADP-Ribosyl
ADP Ribose addition
O-(N-acetylglucosamine-1-phosphoryl)-L-serine
From DeltaMass: Average Mass: 266
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
modification from RESID
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0296
http://purl.org/obo/owl/RESID#RESID_AA0296
UniMod:428
http://purl.org/obo/owl/UniMod#UniMod_428
PubMed:6438439
http://purl.org/obo/owl/PubMed#PubMed_6438439
PubMed:6993483
http://purl.org/obo/owl/PubMed#PubMed_6993483
PubMed:8631906
http://purl.org/obo/owl/PubMed#PubMed_8631906
PhosphoHexNAc
O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester
O3-(N-acetylglucosamine-1-phosphoryl)-L-serine
O-linked (P-GlcNAc)
O-GlcNAc-1-phosphorylation (of Serine)
O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine
N-acetylglucosamine-1-phosphoryl
(S)-2-amino-3-(2-acetamido-2-deoxy-D-glucopyranose alpha1-phosphonoxy)propanoic acid
O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
phosphoglycosyl-D-mannose-1-phosphoryl
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modification from RESID
UniMod:429
http://purl.org/obo/owl/UniMod#UniMod_429
RESID:AA0297
http://purl.org/obo/owl/RESID#RESID_AA0297
PubMed:15649890
http://purl.org/obo/owl/PubMed#PubMed_15649890
PubMed:10037765
http://purl.org/obo/owl/PubMed#PubMed_10037765
PhosphoHex
O-(alpha-D-mannosyl-1-phosphoryl)-L-serine
O3-L-serine alpha-D-mannopyranose 1-phosphodiester
O3-(D-mannose-1-phosphoryl)-L-serine
O-linked (P-Man)
O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine
heptakis-L-histidino tetracopper mu4-sulfide hydroxide
Cross-link 7.
PSI-MOD
modification from RESID
PubMed:11041839
http://purl.org/obo/owl/PubMed#PubMed_11041839
RESID:AA0298
http://purl.org/obo/owl/RESID#RESID_AA0298
PubMed:11024061
http://purl.org/obo/owl/PubMed#PubMed_11024061
pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide
mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper)
nitrous oxide reductase nosZ CuZ cluster
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-leucine methyl ester
incidental to RESID:AA0039
PSI-MOD
methyl L-leucinate
Methylation
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-amino-4-methylpentanoic methyl ester
alpha-aminoisocaproic methyl ester
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
methyl (S)-2-amino-4-methylpentanoate
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
methyl esterified L-leucine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Leucine methyl ester
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Methyl
A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester.
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0299
http://purl.org/obo/owl/RESID#RESID_AA0299
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:8206937
http://purl.org/obo/owl/PubMed#PubMed_8206937
PubMed:10191253
http://purl.org/obo/owl/PubMed#PubMed_10191253
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
OMeLeu
hexakis-L-cysteinyl L-serinyl octairon heptasulfide
Cross-link 7; incidental to RESID:AA0141.
PSI-MOD
modification from RESID
PubMed:9063865
http://purl.org/obo/owl/PubMed#PubMed_9063865
PubMed:12215645
http://purl.org/obo/owl/PubMed#PubMed_12215645
PubMed:10525412
http://purl.org/obo/owl/PubMed#PubMed_10525412
RESID:AA0300
http://purl.org/obo/owl/RESID#RESID_AA0300
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Cys6Ser-[8Fe7S]
nitrogenase P-cluster
L-aspartimide
From DeltaMass: Average Mass: -17 Average Mass Change:-17 References:Clarke, S., Lability of Aspargine and Aspartic Acid Residues in Protein and Peptides, in: Stability of Protein Pharmaceuticals : Chemical and Physical Paths of Protein Degradation, Part A (T.J. Ahern and M.C. Manning, eds.), 1992,Plenum Press, New York, pp.1-29Xie, M.; Vander Velde, D.; Morton, M.; Borchardt, R.T.; Schowen,R.L.: pH-Induced Change in the Rate-Determining Step for the Hydrolysis of the Asp/Asn-Derived Cyclic-Imide Intermediate in Protein Degradation. (1996) J. Am. Chem. Soc. 118: 8955-8956.
PSI-MOD
Succinimide formation from asparagine
A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide.
DeltaMass:18
http://purl.org/obo/owl/DeltaMass#DeltaMass_18
PubMed:7988548
http://purl.org/obo/owl/PubMed#PubMed_7988548
PubMed:9309583
http://purl.org/obo/owl/PubMed#PubMed_9309583
RESID:AA0302
http://purl.org/obo/owl/RESID#RESID_AA0302
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
PubMed:2378679
http://purl.org/obo/owl/PubMed#PubMed_2378679
PubMed:7662664
http://purl.org/obo/owl/PubMed#PubMed_7662664
PubMed:12771378
http://purl.org/obo/owl/PubMed#PubMed_12771378
Dehydration
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-3-amino-2,5-pyrrolidinedione
2-amino-butanimide
alpha-aminosuccinimide
Dehydrated
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
L-glutamimide
PSI-MOD
A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide.
PubMed:12771378
http://purl.org/obo/owl/PubMed#PubMed_12771378
PubMed:14593103
http://purl.org/obo/owl/PubMed#PubMed_14593103
RESID:AA0303
http://purl.org/obo/owl/RESID#RESID_AA0303
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Dehydration
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Dehydrated
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
alpha-aminoglutarimide
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-aminopentanimide
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(S)-3-amino-2,6-piperidinedione
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-beta-carboxyaspartic acid
PSI-MOD
Carboxy
2-amino-1,1,2-ethanetricarboxylic acid
3-carboxyaspartic acid
(S)-2-amino-3-carboxybutanedioic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Carboxylation
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid.
PubMed:6390094
http://purl.org/obo/owl/PubMed#PubMed_6390094
PubMed:7138832
http://purl.org/obo/owl/PubMed#PubMed_7138832
PubMed:7457858
http://purl.org/obo/owl/PubMed#PubMed_7457858
PubMed:8135347
http://purl.org/obo/owl/PubMed#PubMed_8135347
RESID:AA0304
http://purl.org/obo/owl/RESID#RESID_AA0304
UniMod:299
http://purl.org/obo/owl/UniMod#UniMod_299
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N5-methyl-L-arginine
PSI-MOD
(S)-2-amino-5-[(amino-iminomethyl)(methyl)amino]pentanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
delta-N-methylarginine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine.
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:9792625
http://purl.org/obo/owl/PubMed#PubMed_9792625
PubMed:9873020
http://purl.org/obo/owl/PubMed#PubMed_9873020
RESID:AA0305
http://purl.org/obo/owl/RESID#RESID_AA0305
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
Methyl
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Methylation
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N5-methylated L-arginine
N5MeArg
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N5-methylarginine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-cysteine coenzyme A disulfide
DeltaMass gives no formula with mass as 454.
PSI-MOD
(2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate)
coenzyme A L-cysteine mixed disulfide
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
CoenzymeA
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from RESID
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:281
http://purl.org/obo/owl/UniMod#UniMod_281
RESID:AA0306
http://purl.org/obo/owl/RESID#RESID_AA0306
PubMed:1734967
http://purl.org/obo/owl/PubMed#PubMed_1734967
SCoACys
Cysteine modified Coenzyme A
S-myristoyl-L-cysteine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine.
PubMed:8824274
http://purl.org/obo/owl/PubMed#PubMed_8824274
PubMed:10080938
http://purl.org/obo/owl/PubMed#PubMed_10080938
PubMed:10026218
http://purl.org/obo/owl/PubMed#PubMed_10026218
UniMod:45
http://purl.org/obo/owl/UniMod#UniMod_45
RESID:AA0307
http://purl.org/obo/owl/RESID#RESID_AA0307
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
tetradecanoate cysteine thioester
SMyrCys
S-myristoylated L-cysteine
(R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid
Myristoyl
Myristoylation
S-palmitoleyl-L-cysteine
PSI-MOD
palmitoleyl
cis-9-hexadecenoate cysteine thioester
Palmitoleyl
(R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine.
UniMod:431
http://purl.org/obo/owl/UniMod#UniMod_431
RESID:AA0308
http://purl.org/obo/owl/RESID#RESID_AA0308
PubMed:8294460
http://purl.org/obo/owl/PubMed#PubMed_8294460
SPamD1Cys
S-palmitoleylated L-cysteine
glycine cholesterol ester
Incidental to RESID:AA0060. UniMod origin corrected. [JSG]
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
cholesterol ester
Cholesterol
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts a glycine residue to glycine cholesterol ester.
PubMed:11111088
http://purl.org/obo/owl/PubMed#PubMed_11111088
RESID:AA0309
http://purl.org/obo/owl/RESID#RESID_AA0309
PubMed:8824192
http://purl.org/obo/owl/PubMed#PubMed_8824192
UniMod:432
http://purl.org/obo/owl/UniMod#UniMod_432
Cholesterol glycine ester
pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide
Cross-link 6.
PSI-MOD
modification from RESID
RESID:AA0310
http://purl.org/obo/owl/RESID#RESID_AA0310
PubMed:2550436
http://purl.org/obo/owl/PubMed#PubMed_2550436
PubMed:11509720
http://purl.org/obo/owl/PubMed#PubMed_11509720
mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron)
carbon monoxide dehydrogenase nickel-iron cofactor
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Ni-4Fe-5S cluster
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N4,N4-dimethyl-L-asparagine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine.
PubMed:8783012
http://purl.org/obo/owl/PubMed#PubMed_8783012
PubMed:14570711
http://purl.org/obo/owl/PubMed#PubMed_14570711
UniMod:36
http://purl.org/obo/owl/UniMod#UniMod_36
RESID:AA0311
http://purl.org/obo/owl/RESID#RESID_AA0311
PubMed:12964758
http://purl.org/obo/owl/PubMed#PubMed_12964758
N4Me2Asn
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
di-Methylation
beta-dimethylasparagine [misnomer]
(S)-2-amino-N4,N4-dimethylbutanediamic acid
N4,N4-dimethylated L-asparagine
N4,N4-dimethylasparagine
N(gamma),N(gamma)-dimethylasparagine
Dimethyl
N6-3,4-didehydroretinylidene-L-lysine
PSI-MOD
modification from RESID
UniMod:433
http://purl.org/obo/owl/UniMod#UniMod_433
RESID:AA0312
http://purl.org/obo/owl/RESID#RESID_AA0312
PubMed:4056688
http://purl.org/obo/owl/PubMed#PubMed_4056688
PubMed:10717661
http://purl.org/obo/owl/PubMed#PubMed_10717661
PubMed:3257009
http://purl.org/obo/owl/PubMed#PubMed_3257009
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N6-3-dehydroretinyl-lysine
N6-3-dehydroretinal-L-lysine
Didehydroretinylidene
3,4-didehydroretinylidene
(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
4'-(S-L-cysteinyl)-L-tryptophyl quinone
Cross-link 2; secondary to RESID:AA0148.
PSI-MOD
A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone.
PubMed:11717396
http://purl.org/obo/owl/PubMed#PubMed_11717396
PubMed:11555656
http://purl.org/obo/owl/PubMed#PubMed_11555656
RESID:AA0313
http://purl.org/obo/owl/RESID#RESID_AA0313
cysteine tryptophylquinone
4-(S-cysteinyl)tryptophan-6,7-dione
4'-cysteinyl-tryptophylquinone (Cys-Trp)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(S)-3-(2-amino-2-carboxyethyl)-4-[(R)-2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
3-(S-L-cysteinyl)-L-aspartic acid
Cross-link 2.
PSI-MOD
(2S,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(2S,3S)-2-amino-3-[(R)-2-amino-2-carboxyethyl]sulfanylbutanedioic acid
3-cysteinyl-aspartic acid (Cys-Asp)
3-carboxy-L-lanthionine
A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid.
PubMed:11555656
http://purl.org/obo/owl/PubMed#PubMed_11555656
PubMed:11717396
http://purl.org/obo/owl/PubMed#PubMed_11717396
RESID:AA0314
http://purl.org/obo/owl/RESID#RESID_AA0314
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
4-(S-L-cysteinyl)-L-glutamic acid
Cross-link 2.
PSI-MOD
4-cysteinyl-glutamic acid (Cys-Glu)
(2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid
(2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid.
ChEBI:20293
http://purl.org/obo/owl/ChEBI#ChEBI_20293
PubMed:11717396
http://purl.org/obo/owl/PubMed#PubMed_11717396
PubMed:11555656
http://purl.org/obo/owl/PubMed#PubMed_11555656
RESID:AA0315
http://purl.org/obo/owl/RESID#RESID_AA0315
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester
PSI-MOD
modification from RESID
PubMed:7949339
http://purl.org/obo/owl/PubMed#PubMed_7949339
UniMod:434
http://purl.org/obo/owl/UniMod#UniMod_434
RESID:AA0316
http://purl.org/obo/owl/RESID#RESID_AA0316
PubMed:11435437
http://purl.org/obo/owl/PubMed#PubMed_11435437
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester
(7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid
barley lipid transfer protein modification
CHDH
Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
1'-methyl-L-histidine
PSI-MOD
tau-methylhistidine
tele-methylated L-histidine
N(epsilon)-methylhistidine
NteleMeHis
Methylation
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
tele-methylhistidine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Tele-methylhistidine
A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine.
PubMed:11474090
http://purl.org/obo/owl/PubMed#PubMed_11474090
PubMed:10601317
http://purl.org/obo/owl/PubMed#PubMed_10601317
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:8076
http://purl.org/obo/owl/PubMed#PubMed_8076
PubMed:8645219
http://purl.org/obo/owl/PubMed#PubMed_8645219
RESID:AA0317
http://purl.org/obo/owl/RESID#RESID_AA0317
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Methyl
4-methyl-histidine [misnomer]
3-methylhistidine [misnomer]
(S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid
L-lysine methyl ester
PSI-MOD
Lysine methyl ester
alpha,epsilon-diaminocaproic methyl ester
methyl (S)-2,6-diaminohexanoate
Methyl
2,6-diaminohexanoic methyl ester
methyl L-lysinate
methyl esterified L-lysine
OMeLys
Methylation
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester.
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0318
http://purl.org/obo/owl/RESID#RESID_AA0318
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
PubMed:10973948
http://purl.org/obo/owl/PubMed#PubMed_10973948
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)
PSI-MOD
modification from RESID
RESID:AA0319
http://purl.org/obo/owl/RESID#RESID_AA0319
PubMed:8658132
http://purl.org/obo/owl/PubMed#PubMed_8658132
PubMed:8658134
http://purl.org/obo/owl/PubMed#PubMed_8658134
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-beta-methylthioasparagine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
beta-methylthio-asparagine
Beta-methylthiolation
Methylthio
A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine.
UniMod:39
http://purl.org/obo/owl/UniMod#UniMod_39
RESID:AA0320
http://purl.org/obo/owl/RESID#RESID_AA0320
(2R,3Xi)-2-amino-3-methylsulfanylbutanedioic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
3-methylthio-asparagine
3-carboxamido-S-methyl-cysteine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
L-pyrrolysine (Lys)
This entry is for the artifactual formation of L-pyrrolysine from lysine. For encoded L-pyrrolysine, use PSI-MOD:01187.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process).
PubMed:16096277
http://purl.org/obo/owl/PubMed#PubMed_16096277
PubMed:15314242
http://purl.org/obo/owl/PubMed#PubMed_15314242
PubMed:12029132
http://purl.org/obo/owl/PubMed#PubMed_12029132
PubMed:12029131
http://purl.org/obo/owl/PubMed#PubMed_12029131
UniMod:435
http://purl.org/obo/owl/UniMod#UniMod_435
RESID:AA0321
http://purl.org/obo/owl/RESID#RESID_AA0321
PubMed:11435424
http://purl.org/obo/owl/PubMed#PubMed_11435424
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Pyl(Lys)
Pyrrolysine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
3-hydroxy-L-tryptophan
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
beta-hydroxytryptophan
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan.
PubMed:10024453
http://purl.org/obo/owl/PubMed#PubMed_10024453
RESID:AA0322
http://purl.org/obo/owl/RESID#RESID_AA0322
PubMed:11457355
http://purl.org/obo/owl/PubMed#PubMed_11457355
3HyTrp
3-hydroxytryptophan
3-hydroxytryptophan
3-hydroxylated L-tryptophan
O4'-(phospho-3'-DNA)-L-tyrosine
PSI-MOD
A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine.
RESID:AA0323
http://purl.org/obo/owl/RESID#RESID_AA0323
PubMed:2211714
http://purl.org/obo/owl/PubMed#PubMed_2211714
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
O4'-L-tyrosine 3'-DNA phosphodiester
O-(3'-phospho-DNA)-tyrosine
(S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
hydroxyheme-L-glutamate ester
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
hydroxyheme
Hydroxyheme
A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
UniMod:436
http://purl.org/obo/owl/UniMod#UniMod_436
PubMed:11139583
http://purl.org/obo/owl/PubMed#PubMed_11139583
PubMed:11821421
http://purl.org/obo/owl/PubMed#PubMed_11821421
PubMed:11980497
http://purl.org/obo/owl/PubMed#PubMed_11980497
RESID:AA0324
http://purl.org/obo/owl/RESID#RESID_AA0324
Heme (covalent; via 1 link)
cytochrome P450 CYP4A family heme cofactor
[3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
5-hydroxymethyl protoporphyrin IX 5-glutamate ester
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(phospho-5'-guanosine)-L-histidine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine.
RESID:AA0325
http://purl.org/obo/owl/RESID#RESID_AA0325
UniMod:413
http://purl.org/obo/owl/UniMod#UniMod_413
PubMed:10869342
http://purl.org/obo/owl/PubMed#PubMed_10869342
PubMed:7559521
http://purl.org/obo/owl/PubMed#PubMed_7559521
PubMed:10529169
http://purl.org/obo/owl/PubMed#PubMed_10529169
Phosphoguanosine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
phospho-guanosine
L-histidine monoanhydride with 5'-guanylic acid
L-histidine 5'-guanosine phosphoramidester
guanylylated histidine
5'-guanylic-L-histidine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-3-(5'-guanosine phosphono-imidazol-4-yl)propanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
tetrakis-L-cysteinyl triiron tetrasulfide
Cross-link 4.
PSI-MOD
tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron
tetrakis-L-cysteinyl linear [3Fe-4S] cluster
tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
bis[bis-L-cysteinyl iron disulfido]iron
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron)
modification from RESID
PubMed:2511202
http://purl.org/obo/owl/PubMed#PubMed_2511202
PubMed:6094558
http://purl.org/obo/owl/PubMed#PubMed_6094558
PubMed:11941493
http://purl.org/obo/owl/PubMed#PubMed_11941493
RESID:AA0326
http://purl.org/obo/owl/RESID#RESID_AA0326
PubMed:11592901
http://purl.org/obo/owl/PubMed#PubMed_11592901
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
omega-N-glucosyl-L-arginine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Hexose
A protein modification that effectively forms an N4-glucosyl-arginine.
PubMed:8521968
http://purl.org/obo/owl/PubMed#PubMed_8521968
PubMed:9536051
http://purl.org/obo/owl/PubMed#PubMed_9536051
RESID:AA0327
http://purl.org/obo/owl/RESID#RESID_AA0327
UniMod:41
http://purl.org/obo/owl/UniMod#UniMod_41
PubMed:15279557
http://purl.org/obo/owl/PubMed#PubMed_15279557
Hex
(S)-2-amino-5-[beta-glucopyranosyl(imino(methylamino)methyl)amino]pentanoic acid
omega-N-glycosyl-L-arginine
omega-N-(beta-D-glucosyl)-L-arginine
NG-beta-D-glucosylarginine
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine
UniMod origin corrected. [JSG]
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine.
UniMod:437
http://purl.org/obo/owl/UniMod#UniMod_437
PubMed:8183363
http://purl.org/obo/owl/PubMed#PubMed_8183363
RESID:AA0328
http://purl.org/obo/owl/RESID#RESID_AA0328
PubMed:7559516
http://purl.org/obo/owl/PubMed#PubMed_7559516
PubMed:7835418
http://purl.org/obo/owl/PubMed#PubMed_7835418
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine
MicrocinC7
1'-heme-L-histidine
PSI-MOD
tele-histidyl heme
tau-histidyl heme
N1'-histidyl heme
N(epsilon)-histidyl heme
Heme (covalent; via 1 link)
heme
Heme
2-[1-(N1'-histidyl)ethyl]protoporphyrin IX
(S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:12033922
http://purl.org/obo/owl/PubMed#PubMed_12033922
UniMod:390
http://purl.org/obo/owl/UniMod#UniMod_390
RESID:AA0329
http://purl.org/obo/owl/RESID#RESID_AA0329
PubMed:12121092
http://purl.org/obo/owl/PubMed#PubMed_12121092
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
3-methyl-L-lanthionine sulfoxide
Cross-link 2.
PSI-MOD
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyl-L-lanthionine sulfoxide.
RESID:AA0330
http://purl.org/obo/owl/RESID#RESID_AA0330
PubMed:7737178
http://purl.org/obo/owl/PubMed#PubMed_7737178
PubMed:9219543
http://purl.org/obo/owl/PubMed#PubMed_9219543
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
3-methyl-L-lanthionine S-oxide
(2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid
(2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid
S-oxy-3-methyllanthionine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Beta-methyllanthionine sulfoxide (Thr-Cys)
tris-L-cysteinyl L-aspartato diiron disulfide
Cross-link 4
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
modification from RESID
PubMed:7947772
http://purl.org/obo/owl/PubMed#PubMed_7947772
RESID:AA0331
http://purl.org/obo/owl/RESID#RESID_AA0331
PubMed:1312028
http://purl.org/obo/owl/PubMed#PubMed_1312028
PubMed:10968624
http://purl.org/obo/owl/PubMed#PubMed_10968624
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-carbamoyl-L-cysteine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine.
PubMed:12586941
http://purl.org/obo/owl/PubMed#PubMed_12586941
PubMed:240389
http://purl.org/obo/owl/PubMed#PubMed_240389
RESID:AA0332
http://purl.org/obo/owl/RESID#RESID_AA0332
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-cysteinyl carbamate ester
S-carbamylcysteine
S-carbamoylcysteine
S-(aminocarbonyl)cysteine
beta-carbamylthioalanine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
2-amino-3-(aminocarbonyl)sulfanylpropanoic acid
2-amino-3-(aminocarbonyl)thiopropanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
alpha-amino-beta-carbamylthiopropionic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(R)-2-amino-3-(carbamoylsulfanyl)propanoic acid
S-cyano-L-cysteine
PSI-MOD
serine thiocyanic acid ester
beta-thiocyanatoalanine
Cyano
cyano
S-cyanocysteine
(R)-2-amino-3-thiocyanatopropanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine.
UniMod:438
http://purl.org/obo/owl/UniMod#UniMod_438
PubMed:4808702
http://purl.org/obo/owl/PubMed#PubMed_4808702
RESID:AA0333
http://purl.org/obo/owl/RESID#RESID_AA0333
PubMed:12586941
http://purl.org/obo/owl/PubMed#PubMed_12586941
alpha-amino-beta-thiocyanatopropionic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
L-cysteinyl hydrogenase diiron subcluster
incidental to RESID:AA0140
PSI-MOD
Diironsubcluster
hydrogenase diiron subcluster
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
modification from RESID
UniMod:439
http://purl.org/obo/owl/UniMod#UniMod_439
PubMed:10694885
http://purl.org/obo/owl/PubMed#PubMed_10694885
RESID:AA0334
http://purl.org/obo/owl/RESID#RESID_AA0334
PubMed:9836629
http://purl.org/obo/owl/PubMed#PubMed_9836629
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-amidino-L-cysteine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine.
PubMed:9148748
http://purl.org/obo/owl/PubMed#PubMed_9148748
RESID:AA0335
http://purl.org/obo/owl/RESID#RESID_AA0335
UniMod:440
http://purl.org/obo/owl/UniMod#UniMod_440
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
beta-(S-isothiourea)alanine
beta-amidinothioalanine
S-amidinocysteine
amidino
(R)-2-amino-3-amidinosulfanylpropanoic acid
2-amino-3-amidinothiopropanoic acid
alpha-amino-beta-thiocyanatopropionic acid
Amidino
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N-methyl-L-isoleucine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Methylation
Methyl
N-methylated L-isoleucine
(2S,3S)-2-methylamino-3-methylpentanoic acid
N-methylisoleucine
N-methylisoleucine
NMeIle
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine.
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0336
http://purl.org/obo/owl/RESID#RESID_AA0336
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N-methyl-L-leucine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine.
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
RESID:AA0337
http://purl.org/obo/owl/RESID#RESID_AA0337
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-methylleucine
NMeLeu
N-methylleucine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Methyl
(S)-2-methylamino-4-methylpentanoic acid
N-methylated L-leucine
Methylation
N-methyl-L-tyrosine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-methyltyrosine
N-methyl Tyrosinyl [misnomer]
(S)-2-methylamino-3-(4-hydoxyphenyl)propanoic acid
N-methyltyrosine
N-methylated L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine.
RESID:AA0338
http://purl.org/obo/owl/RESID#RESID_AA0338
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
NMeTyr
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-palmitoylglycine
incidental to RESID:AA0060
PSI-MOD
N-palmitoyl glycine
N-palmitoylated glycine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
NPamGly
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts a glycine residue to N-palmitoylglycine.
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
RESID:AA0339
http://purl.org/obo/owl/RESID#RESID_AA0339
PubMed:12574119
http://purl.org/obo/owl/PubMed#PubMed_12574119
2-(S-L-cysteinyl)-L-phenylalanine
Cross-link 2.
PSI-MOD
A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine.
PubMed:12696888
http://purl.org/obo/owl/PubMed#PubMed_12696888
PubMed:3936839
http://purl.org/obo/owl/PubMed#PubMed_3936839
RESID:AA0340
http://purl.org/obo/owl/RESID#RESID_AA0340
alpha-(S-L-cysteinyl)-L-phenylalanine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
(R)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylethanoic acid
2-cysteinyl-L-phenylalanine (Cys-Phe)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
2-(S-L-cysteinyl)-D-phenylalanine
Cross-link 2.
PSI-MOD
(S)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylethanoic acid
2-cysteinyl-D-phenylalanine (Cys-Phe)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine.
PubMed:12696888
http://purl.org/obo/owl/PubMed#PubMed_12696888
PubMed:3936839
http://purl.org/obo/owl/PubMed#PubMed_3936839
RESID:AA0341
http://purl.org/obo/owl/RESID#RESID_AA0341
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
alpha-(S-L-cysteinyl)-D-phenylalanine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-(S-L-cysteinyl)-D-allo-threonine
Cross-link 2.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid
(2S,3R)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine.
PubMed:12696888
http://purl.org/obo/owl/PubMed#PubMed_12696888
RESID:AA0342
http://purl.org/obo/owl/RESID#RESID_AA0342
PubMed:3936839
http://purl.org/obo/owl/PubMed#PubMed_3936839
2-cysteinyl-D-allo-threonine (Cys-Thr)
alpha-(S-L-cysteinyl)-D-allo-threonine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-carbamoyl-L-alanine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine.
RESID:AA0343
http://purl.org/obo/owl/RESID#RESID_AA0343
PubMed:12203680
http://purl.org/obo/owl/PubMed#PubMed_12203680
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-ureidopropanoic acid
(S)-2-(carbamoylamino)propanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-carbamylalanine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
4-amino-3-isothiazolidinone-L-serine
Cross-link 2.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
(4R)-2-((S)-1-carboxy-2-hydroxyethyl)-4-amino-3(2H)-isothiazolidinone
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid
4-amino-3-isothiazolidinone serine (Cys-Ser)
cysteine sulfenyl amide cross-link
N,N-(L-cystein-sulphen-1,S-diyl)-L-serine
modification from RESID
PubMed:12802338
http://purl.org/obo/owl/PubMed#PubMed_12802338
RESID:AA0344
http://purl.org/obo/owl/RESID#RESID_AA0344
PubMed:12802339
http://purl.org/obo/owl/PubMed#PubMed_12802339
cysteine sulphenyl amide cross-link
L-threonyl-pentaglycyl-murein peptidoglycan
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
modification from RESID
PubMed:10754567
http://purl.org/obo/owl/PubMed#PubMed_10754567
PubMed:1638631
http://purl.org/obo/owl/PubMed#PubMed_1638631
RESID:AA0345
http://purl.org/obo/owl/RESID#RESID_AA0345
(2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine
Pentaglycyl murein peptidoglycan amidated threonine
N-glycyl-1-(phosphatidyl)ethanolamine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Phosphatidylethanolamine amidated glycine
N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine.
RESID:AA0346
http://purl.org/obo/owl/RESID#RESID_AA0346
PubMed:11100732
http://purl.org/obo/owl/PubMed#PubMed_11100732
(R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-glutamyl 5-omega-hydroxyceramide ester
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine
Omega-hydroxyceramide glutamate ester
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester.
PubMed:9651377
http://purl.org/obo/owl/PubMed#PubMed_9651377
RESID:AA0347
http://purl.org/obo/owl/RESID#RESID_AA0347
PubMed:10411887
http://purl.org/obo/owl/PubMed#PubMed_10411887
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium
Cross-link 3.
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-...)
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-tryptophan residue, an L-tyrosine residue, and an L-methionine residue to S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium.
PubMed:12172540
http://purl.org/obo/owl/PubMed#PubMed_12172540
RESID:AA0348
http://purl.org/obo/owl/RESID#RESID_AA0348
PubMed:16285713
http://purl.org/obo/owl/PubMed#PubMed_16285713
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
O-(riboflavin phosphoryl)-L-threonine
PSI-MOD
A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine.
UniMod:442
http://purl.org/obo/owl/UniMod#UniMod_442
RESID:AA0349
http://purl.org/obo/owl/RESID#RESID_AA0349
PubMed:11248234
http://purl.org/obo/owl/PubMed#PubMed_11248234
PubMed:11163785
http://purl.org/obo/owl/PubMed#PubMed_11163785
PubMed:10587447
http://purl.org/obo/owl/PubMed#PubMed_10587447
O3-(riboflavin phosphoryl)
FMN phosphoryl threonine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
FMN
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
OFMNThr
O3-threonyl flavin mononucleotide
O3-threonyl FMN
(R,)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid
O-(riboflavin phosphoryl)-L-serine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine.
UniMod:442
http://purl.org/obo/owl/UniMod#UniMod_442
RESID:AA0350
http://purl.org/obo/owl/RESID#RESID_AA0350
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
FMN
FMN phosphoryl serine
(R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid
O3-(riboflavin phosphoryl)
O3-seryl FMN
O3-seryl flavin mononucleotide
OFMNSer
S-(4a-FMN)-L-cysteine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine.
PubMed:12668455
http://purl.org/obo/owl/PubMed#PubMed_12668455
UniMod:443
http://purl.org/obo/owl/UniMod#UniMod_443
RESID:AA0351
http://purl.org/obo/owl/RESID#RESID_AA0351
PubMed:7692961
http://purl.org/obo/owl/PubMed#PubMed_7692961
PubMed:12846567
http://purl.org/obo/owl/PubMed#PubMed_12846567
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid
S4aFMNCys
S-4a-FMN cysteine
4a-(S-cysteinyl)flavin mononucleotide
4a-(S-cysteinyl)FMN
FMNC
S-(4a-FMN)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
1'-(8alpha-FMN)-L-histidine
PSI-MOD
(S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
8alpha-(N(epsilon)-histidyl)FMN
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
flavin mononucleotide
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
8alpha-(N1'-histidyl)FMN
Ntele8aFMNHis
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
FMNH
tele-(8alpha-FMN)-histidine
tau-(8alpha-FMN)-histidine
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine.
PubMed:11902668
http://purl.org/obo/owl/PubMed#PubMed_11902668
PubMed:8611516
http://purl.org/obo/owl/PubMed#PubMed_8611516
RESID:AA0352
http://purl.org/obo/owl/RESID#RESID_AA0352
UniMod:409
http://purl.org/obo/owl/UniMod#UniMod_409
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Tele-8alpha-FMN histidine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
3'-(8alpha-FMN)-L-histidine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine.
PubMed:12417325
http://purl.org/obo/owl/PubMed#PubMed_12417325
RESID:AA0353
http://purl.org/obo/owl/RESID#RESID_AA0353
UniMod:409
http://purl.org/obo/owl/UniMod#UniMod_409
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
FMNH
flavin mononucleotide
8alpha-(N3'-histidyl)FMN
8alpha-(N(delta)-histidyl)FMN
pros-(8alpha-FMN)-histidine
pi-(8alpha-FMN)-histidine
Npros8aFMNHis
(S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
N2-acetyl-L-arginine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N(alpha)-acetylarginine
alpha-acetylamino-delta-guanidinovaleric acid
acetylarginine
AcArg
2-acetylamino-5-guanidinopentanoic acid
2-acetamido-5-guanidinopentanoic acid
(S)-2-acetamido-5-carbamimidamidopentanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine.
PubMed:1894641
http://purl.org/obo/owl/PubMed#PubMed_1894641
PubMed:12883043
http://purl.org/obo/owl/PubMed#PubMed_12883043
RESID:AA0354
http://purl.org/obo/owl/RESID#RESID_AA0354
N2-acetylarginine
N2-acetylated L-arginine
L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
copper sulfido molybdopterin cytosine dinuncleotide
CuSMo
[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide
modification from RESID
PubMed:12475995
http://purl.org/obo/owl/PubMed#PubMed_12475995
UniMod:444
http://purl.org/obo/owl/UniMod#UniMod_444
RESID:AA0355
http://purl.org/obo/owl/RESID#RESID_AA0355
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide
Cross-link 3.
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
modification from RESID
PubMed:14704425
http://purl.org/obo/owl/PubMed#PubMed_14704425
RESID:AA0356
http://purl.org/obo/owl/RESID#RESID_AA0356
PubMed:11222759
http://purl.org/obo/owl/PubMed#PubMed_11222759
tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron)
tris-L-cysteinyl L-arginyl diiron disulfide
Cross-link 4.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron)
modification from RESID
RESID:AA0357
http://purl.org/obo/owl/RESID#RESID_AA0357
PubMed:14704425
http://purl.org/obo/owl/PubMed#PubMed_14704425
L-cysteinyl-L-selenocysteine (Cys-Sec)
Cross-link 2.
PSI-MOD
A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine.
RESID:AA0358
http://purl.org/obo/owl/RESID#RESID_AA0358
PubMed:12911312
http://purl.org/obo/owl/PubMed#PubMed_12911312
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid
Cysteinyl-selenocysteine (Sec-Cys)
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
5-hydroxy-N6,N6,N6-trimethyl-L-lysine
Incidental to RESID:AA0278; secondary to RESID:AA0028; secondary to RESID:AA0074.
PSI-MOD
5-hydroxylated N6,N6,N6-trimethylated L-lysine
5-hydroxy-N6,N6,N6-trimethyl
5-hydroxy-N(zeta)-trimethyllysine
(2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium
(2S,5Xi)-2-amino-5-hydroxy-6-(trimethylammonio)hexanoic acid
delta-hydroxy-epsilon-N,N,N-trimethyllysine
Hydroxytrimethyl
5HyN6Me3Lys
A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine.
UniMod:445
http://purl.org/obo/owl/UniMod#UniMod_445
PubMed:14661085
http://purl.org/obo/owl/PubMed#PubMed_14661085
RESID:AA0359
http://purl.org/obo/owl/RESID#RESID_AA0359
PubMed:11349130
http://purl.org/obo/owl/PubMed#PubMed_11349130
alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
lysine derivative Lys(z)
FormalCharge:NULL
http://purl.org/obo/owl/FormalCharge#FormalCharge_NULL
N6,N6,N6-trimethyl-5-hydroxylysine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-(L-isoglutamyl)-glycine
Cross-link 2.
PSI-MOD
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine.
PubMed:14531691
http://purl.org/obo/owl/PubMed#PubMed_14531691
RESID:AA0360
http://purl.org/obo/owl/RESID#RESID_AA0360
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Isoglutamyl glycine isopeptide (Gly-Glu)
isoglutamyl glycine
2-amino-N5-(carboxymethyl)-pentanediamic acid
(S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid
N-gamma-glutamylglycine
O-sulfo-L-serine
PSI-MOD
serine sulfate ester
O3-sulfoserine
Sulfoserine
Sulfo
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
O3-sulfonoserine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
O-Sulfonation
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine.
RESID:AA0361
http://purl.org/obo/owl/RESID#RESID_AA0361
UniMod:40
http://purl.org/obo/owl/UniMod#UniMod_40
PubMed:14752058
http://purl.org/obo/owl/PubMed#PubMed_14752058
(S)-2-amino-3-hydroxypropanoic acid 3-sulfate
O-sulfo-L-threonine
PSI-MOD
O-Sulfonation
A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine.
UniMod:40
http://purl.org/obo/owl/UniMod#UniMod_40
RESID:AA0362
http://purl.org/obo/owl/RESID#RESID_AA0362
PubMed:14752058
http://purl.org/obo/owl/PubMed#PubMed_14752058
O3-sulfothreonine
O3-sulfonothreonine
threonine sulfate ester
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Sulfo
Sulfothreonine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(2S,3R)-2-amino-3-hydroxybutanoic acid 3-sulfate
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-carboxy-L-methionine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-carboxymethionine
Carboxylation
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Carboxy
2-carbamic-4-(methylthio)butanoic acid
A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine.
PubMed:12595263
http://purl.org/obo/owl/PubMed#PubMed_12595263
PubMed:11120890
http://purl.org/obo/owl/PubMed#PubMed_11120890
PubMed:8312270
http://purl.org/obo/owl/PubMed#PubMed_8312270
PubMed:10368287
http://purl.org/obo/owl/PubMed#PubMed_10368287
RESID:AA0363
http://purl.org/obo/owl/RESID#RESID_AA0363
UniMod:299
http://purl.org/obo/owl/UniMod#UniMod_299
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
2-carbamic-4-(methylsulfanyl)butanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
O-acetyl-L-serine
incidental to RESID:AA0051
PSI-MOD
Acetylation
O-acetylated L-serine
Acetyl
OAcSer
serine acetate ester
O-acetylserine
O-acetylserine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-3-acetyloxypropanoic acid
A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine.
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
UniMod:1
http://purl.org/obo/owl/UniMod#UniMod_1
RESID:AA0364
http://purl.org/obo/owl/RESID#RESID_AA0364
PubMed:7309355
http://purl.org/obo/owl/PubMed#PubMed_7309355
ChEBI:17981
http://purl.org/obo/owl/ChEBI#ChEBI_17981
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
PubMed:16731519
http://purl.org/obo/owl/PubMed#PubMed_16731519
PubMed:489587
http://purl.org/obo/owl/PubMed#PubMed_489587
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
(E)-2,3-didehydrotyrosine
incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381
PSI-MOD
trans-dehydrotyrosine
E-dHTyr
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively converts L-tyrosine to (E)-2,3-didehydrotyrosine.
RESID:AA0365
http://purl.org/obo/owl/RESID#RESID_AA0365
UniMod:401
http://purl.org/obo/owl/UniMod#UniMod_401
PubMed:12623015
http://purl.org/obo/owl/PubMed#PubMed_12623015
amino-(para-hydroxybenzylidenyl)acetic acid
2-amino-3-oxo-butanoic_acid
Didehydro
blue non-fluorescent pocilloporin chromophore
(E)-2,3-didehydrogenated tyrosine
(E)-2-amino-3-(4-hydoxyphenyl)propenoic acid
(E)-2,3-didehydrotyrosine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide
Cross-link 6.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
modification from RESID
PubMed:14764885
http://purl.org/obo/owl/PubMed#PubMed_14764885
RESID:AA0366
http://purl.org/obo/owl/RESID#RESID_AA0366
4Mn-Ca-4O cluster
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
photosystem II catalytic cluster
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
3'-(3'-L-tyrosinyl)-L-tyrosine
Cross-link 2; From DeltaMass: Average Mass: -2.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively cross-links L-tyrosine residues to form 3'-(3'-L-tyrosinyl)-L-tyrosine.
PubMed:8702710
http://purl.org/obo/owl/PubMed#PubMed_8702710
PubMed:8937563
http://purl.org/obo/owl/PubMed#PubMed_8937563
PubMed:14249161
http://purl.org/obo/owl/PubMed#PubMed_14249161
PubMed:637884
http://purl.org/obo/owl/PubMed#PubMed_637884
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
RESID:AA0367
http://purl.org/obo/owl/RESID#RESID_AA0367
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
o,o-dityrosine
6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid)
3,3'-BiTyr (Crosslink)
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
bityrosine
alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid
(2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid)
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
3'-(O4'-L-tyrosinyl)-L-tyrosine
Cross-link 2; secondary to RESID:AA0146; From DeltaMass: Average Mass: -2.
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine
IsodiTyr (Crosslink)
2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid
Isodityrosine (Tyr-Tyr)
isodityrosine
(2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid
A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine,
RESID:AA0368
http://purl.org/obo/owl/RESID#RESID_AA0368
PubMed:8702710
http://purl.org/obo/owl/PubMed#PubMed_8702710
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:7115340
http://purl.org/obo/owl/PubMed#PubMed_7115340
PubMed:12719529
http://purl.org/obo/owl/PubMed#PubMed_12719529
3,4-dihydroxy-L-arginine
PSI-MOD
beta,gamma-dihydroxyarginine
34Hy2Arg
3,4-dihydroxylated L-arginine
3,4-dihydroxyarginine
2-amino-5-guanidino-3,4-dihydroxypentanoic acid
(2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid
Dioxidation
dihydroxy
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine.
PubMed:10978343
http://purl.org/obo/owl/PubMed#PubMed_10978343
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
RESID:AA0369
http://purl.org/obo/owl/RESID#RESID_AA0369
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
4,5-dihydroxy-L-lysine
PSI-MOD
(2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
4,5-dihydroxylated L-lysine
4,5-dihydroxylysine
45Hy2Lys
alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid
A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine.
PubMed:10978343
http://purl.org/obo/owl/PubMed#PubMed_10978343
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
RESID:AA0370
http://purl.org/obo/owl/RESID#RESID_AA0370
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
delta,gamma-dihydroxylysine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
dihydroxy
Dioxidation
1'-(phospho-5'-adenosine)-L-histidine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine.
PubMed:9323207
http://purl.org/obo/owl/PubMed#PubMed_9323207
RESID:AA0371
http://purl.org/obo/owl/RESID#RESID_AA0371
PubMed:15182206
http://purl.org/obo/owl/PubMed#PubMed_15182206
UniMod:405
http://purl.org/obo/owl/UniMod#UniMod_405
AMP binding site
(S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid
L-histidine monoanhydride with 5'-adenylic acid
L-histidine 5'-adenosine phosphoramidester
Phosphoadenosine
tau-5'-adenylic-L-histidine
N1'-adenylylated histidine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
tele-5'-adenylic-L-histidine
1'-(phospho-5'-uridine)-L-histidine
PSI-MOD
A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine.
UniMod:417
http://purl.org/obo/owl/UniMod#UniMod_417
PubMed:11467524
http://purl.org/obo/owl/PubMed#PubMed_11467524
PubMed:8794735
http://purl.org/obo/owl/PubMed#PubMed_8794735
RESID:AA0372
http://purl.org/obo/owl/RESID#RESID_AA0372
PubMed:321007
http://purl.org/obo/owl/PubMed#PubMed_321007
PubMed:380639
http://purl.org/obo/owl/PubMed#PubMed_380639
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-histidine 5'-uridine phosphoramidester
L-histidine monoanhydride with 5'-uridylic acid
N1'-uridylylated histidine
PhosphoUridine
tau-5'-uridylic-L-histidine
tele-5'-uridylic-L-histidine
uridine phosphodiester
(S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-aspartyl aldehyde
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-beta-formylalanine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
reduction
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl aldehyde.
UniMod:447
http://purl.org/obo/owl/UniMod#UniMod_447
PubMed:1093385
http://purl.org/obo/owl/PubMed#PubMed_1093385
PubMed:14235557
http://purl.org/obo/owl/PubMed#PubMed_14235557
PubMed:15237995
http://purl.org/obo/owl/PubMed#PubMed_15237995
RESID:AA0373
http://purl.org/obo/owl/RESID#RESID_AA0373
Deoxy
Aspartyl aldehyde
(S)-2-amino-4-oxobutanoic acid
L-aspartic beta-semialdehyde
L-aspartate-beta-semialdehyde
L-aminosuccinic acid semialdehyde
L-aminosuccinaldehydic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
L-serine microcin E492 siderophore ester
UniMod origin corrected. [JSG]
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from RESID
PubMed:15102848
http://purl.org/obo/owl/PubMed#PubMed_15102848
RESID:AA0374
http://purl.org/obo/owl/RESID#RESID_AA0374
UniMod:448
http://purl.org/obo/owl/UniMod#UniMod_448
Serine microcin E492 siderophore ester
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Microcin
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
microcin E492 siderophore ester from serine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide)
PSI-MOD
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide).
PubMed:14725769
http://purl.org/obo/owl/PubMed#PubMed_14725769
PubMed:12910261
http://purl.org/obo/owl/PubMed#PubMed_12910261
RESID:AA0375
http://purl.org/obo/owl/RESID#RESID_AA0375
UniMod:424
http://purl.org/obo/owl/UniMod#UniMod_424
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester
nitrate reductase A aspartyl Mo-bisMGD cofactor
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
carboxamidine; cross-link 1
PSI-MOD
L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine
GFP-like chromoprotein asFP595 chromophore
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol
3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
modification from RESID
RESID:AA0377
http://purl.org/obo/owl/RESID#RESID_AA0377
PubMed:15491166
http://purl.org/obo/owl/PubMed#PubMed_15491166
PubMed:11259412
http://purl.org/obo/owl/PubMed#PubMed_11259412
PubMed:10852900
http://purl.org/obo/owl/PubMed#PubMed_10852900
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-imino-glutamic acid 5-imidazolinone glycine
Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
2-iminomethyl-5-imidazolinone (Glu-Gly)
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
2-imino-glutamyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
[2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine.
RESID:AA0378
http://purl.org/obo/owl/RESID#RESID_AA0378
PubMed:11682051
http://purl.org/obo/owl/PubMed#PubMed_11682051
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
2,N-didehydroglutamyl-5-imidazolinone glycine
2-imino-methionine 5-imidazolinone glycine
Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein eqFP611 chromophore
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.
PubMed:10852900
http://purl.org/obo/owl/PubMed#PubMed_10852900
PubMed:12185250
http://purl.org/obo/owl/PubMed#PubMed_12185250
PubMed:12909624
http://purl.org/obo/owl/PubMed#PubMed_12909624
PubMed:15542608
http://purl.org/obo/owl/PubMed#PubMed_15542608
RESID:AA0379
http://purl.org/obo/owl/RESID#RESID_AA0379
2-imino-methionyl-5-imidazolinone glycine
2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one
GFP-like chromoprotein asFP595 chromophore
2-iminomethyl-5-imidazolinone (Met-Gly)
2,N-didehydromethionyl-5-imidazolinone glycine
(2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-asparagine 5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine.
PubMed:10504696
http://purl.org/obo/owl/PubMed#PubMed_10504696
RESID:AA0380
http://purl.org/obo/owl/RESID#RESID_AA0380
Zoanthus sp. fluorescent protein FP506 chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
asparaginyl-5-imidazolinone glycine
[2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
5-imidazolinone (Asn-Gly)
2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
L-lysine 5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine.
PubMed:10504696
http://purl.org/obo/owl/PubMed#PubMed_10504696
RESID:AA0381
http://purl.org/obo/owl/RESID#RESID_AA0381
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Anemonia majano fluorescent protein FP486 chromophore
[2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
para-hydroxybenzylidene-imidazolidinone chromophore
lysyl-5-imidazolinone glycine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one
5-imidazolinone (Lys-Gly)
2-tetrahydropyridinyl-5-imidazolinone glycine
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one
2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine
2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
[5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
para-hydroxybenzylidene-imidazolidinone chromophore
Zoanthus sp. fluorescent protein zFP538 chromophore
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine.
RESID:AA0382
http://purl.org/obo/owl/RESID#RESID_AA0382
PubMed:15628861
http://purl.org/obo/owl/PubMed#PubMed_15628861
PubMed:10504696
http://purl.org/obo/owl/PubMed#PubMed_10504696
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-alanyl-pentaglycyl-murein peptidoglycan
PSI-MOD
Pentaglycyl murein peptidoglycan amidated alanine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
modification from RESID
RESID:AA0383
http://purl.org/obo/owl/RESID#RESID_AA0383
PubMed:8163519
http://purl.org/obo/owl/PubMed#PubMed_8163519
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-formyl-L-proline
CAUTION - observations of this modification can be attributed to unintended artifactual production, or to spurious peptide MS identification. This modification is probably not a natural post-translational modification [JSG].
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
1-formylpyrrolidine-2-carboxylic acid
N-formylated L-proline
A protein modification that effectively converts an L-proline residue to N-formyl-L-proline.
RESID:AA0384
http://purl.org/obo/owl/RESID#RESID_AA0384
PubMed:5464655
http://purl.org/obo/owl/PubMed#PubMed_5464655
PubMed:12051774
http://purl.org/obo/owl/PubMed#PubMed_12051774
NFoPro
1-formylproline
(S)-1-formyl-2-pyrrolidinecarboxylic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
O-decanoyl-L-serine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-serine decanoate ester
lipid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O3-decanoyl-L-serine
ODecSer
O-decanoyl serine
O-decanoylated L-serine
A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine.
RESID:AA0385
http://purl.org/obo/owl/RESID#RESID_AA0385
UniMod:449
http://purl.org/obo/owl/UniMod#UniMod_449
PubMed:12630926
http://purl.org/obo/owl/PubMed#PubMed_12630926
Decanoyl
(2S)-2-amino-3-(decanoyloxy)propanoic acid
O-octanoyl-L-threonine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
octanoyl
Octanoyl
O3-octanoyl-L-threonine
O-octanoylated L-threonine
O-octanoyl threonine
L-threonine octanoate ester
(2S)-2-amino-3-(octanoyloxy)propanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
OOctThr
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine.
PubMed:11546772
http://purl.org/obo/owl/PubMed#PubMed_11546772
RESID:AA0386
http://purl.org/obo/owl/RESID#RESID_AA0386
PubMed:12716131
http://purl.org/obo/owl/PubMed#PubMed_12716131
UniMod:426
http://purl.org/obo/owl/UniMod#UniMod_426
O-decanoyl-L-threonine
PSI-MOD
A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine.
RESID:AA0387
http://purl.org/obo/owl/RESID#RESID_AA0387
PubMed:11546772
http://purl.org/obo/owl/PubMed#PubMed_11546772
UniMod:449
http://purl.org/obo/owl/UniMod#UniMod_449
Decanoyl
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-threonine decanoate ester
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(2S)-2-amino-3-(decanoyloxy)propanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
O-decanoylated L-threonine
O3-decanoyl-L-threonine
lipid
O-decanoyl threonine
ODecThr
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
O-methylated residue
PSI-MOD
OMeRes
A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
acetylated residue
Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). From DeltaMass: Average Mass: 42
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
AcRes
Acetylation
Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Acetyl
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively replaces a hydrogen atom with an acetyl group.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:12175151
http://purl.org/obo/owl/PubMed#PubMed_12175151
PubMed:14730666
http://purl.org/obo/owl/PubMed#PubMed_14730666
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
PubMed:11999733
http://purl.org/obo/owl/PubMed#PubMed_11999733
PubMed:15350136
http://purl.org/obo/owl/PubMed#PubMed_15350136
UniMod:1
http://purl.org/obo/owl/UniMod#UniMod_1
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
thioester crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
O-glycosylated residue
PSI-MOD
a protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
OGlycoRes
carbamylated residue by cyanate or urea derivatization
From DeltaMass: Average Mass: 43 Formula: -NH2 to -NHCONH2 Monoisotopic Mass Change:43.006 Average Mass Change: 43.025 Notes: Generally the result of the reaction of cyanate (from sources such as old or impure urea) with primary amines. Cyanylated lysine is no longer a substrate for trypsin.
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Carbamyl
Carbamylation
Carbamylation
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that is produced by hydrogen cyanate, as a reagent or as released by urea degradation, reaction with a reactive hydrogen to form a carbamyl group or, in the case of an amine, to form a ureido group.
DeltaMass:56
http://purl.org/obo/owl/DeltaMass#DeltaMass_56
PubMed:12203680
http://purl.org/obo/owl/PubMed#PubMed_12203680
UniMod:5
http://purl.org/obo/owl/UniMod#UniMod_5
PubMed:10978403
http://purl.org/obo/owl/PubMed#PubMed_10978403
deamidated residue
From DeltaMass: References:Vish Katta.
PSI-MOD
Deamidated
Deamidation
Deamidation of Asparagine and Glutamine to Aspartate and Glutamate
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
dNRes
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and a loss of nitrogen.
DeltaMass:32
http://purl.org/obo/owl/DeltaMass#DeltaMass_32
UniMod:7
http://purl.org/obo/owl/UniMod#UniMod_7
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-acetylated residue
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-Acetyl
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N-Acetylation
NAcRes
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-formylated residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively replaces a residue amino group with a formamido group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
NFoRes
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
monomethylated L-arginine
From DeltaMass: formula incorrect, N and O reversed
PSI-MOD
A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group.
DeltaMass:215
http://purl.org/obo/owl/DeltaMass#DeltaMass_215
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N-methyl Arginyl
Me1Arg
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
phosphorylation of an hydroxyl amino acid with prompt loss of phosphate
O4-phosphotyrosine does not lose phosphate by this mechanism.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Dehydration
Dehydrated
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment.
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
2-pyrrolidone-5-carboxylic acid (Glu)
From DeltaMass: References: The conversion of glutamic acid to pyroglutamic was reported for the beta-amiloid protein. Miller et.al. Arch. Biochem. Biophy. (1993) 301, 41-52 [DeltaMass]. This is an artifact of treatment with strong acid under anhydrous conditions [JSG].
PSI-MOD
A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid.
UniMod:27
http://purl.org/obo/owl/UniMod#UniMod_27
PubMed:3473473
http://purl.org/obo/owl/PubMed#PubMed_3473473
PubMed:8382902
http://purl.org/obo/owl/PubMed#PubMed_8382902
PubMed:10214721
http://purl.org/obo/owl/PubMed#PubMed_10214721
PubMed:1836357
http://purl.org/obo/owl/PubMed#PubMed_1836357
DeltaMass:16
http://purl.org/obo/owl/DeltaMass#DeltaMass_16
(S)-5-oxo-2-pyrrolidinecarboxylic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Glu->pyro-Glu
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
PyrGlu(Glu)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Pyrrolidone carboxylic acid (Glu)
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Pyroglutamic Acid formed from Glutamic Acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
pyroglutamic acid
Pyro-glu from E
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
C-glycosylated residue
PSI-MOD
CGlycoRes
A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
monohydroxylated residue
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Hy1Res
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Oxidation or Hydroxylation
Oxidation
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively replaces one hydrogen atom with a hydroxyl group.
UniMod:35
http://purl.org/obo/owl/UniMod#UniMod_35
S-glycosylated residue
PSI-MOD
SGlycoRes
a protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
methylated residue
From DeltaMass: Average Mass: 14 Average Mass Change:14 References:Methylation of Asparagine (found in phycobiliproteins) Klotz and Glazer (1987) J. Biol. Chem. 262; 17350-17355
PSI-MOD
Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine)
MeRes
A protein modification that effectively replaces a hydrogen atom with a methyl group.
DeltaMass:36
http://purl.org/obo/owl/DeltaMass#DeltaMass_36
dihydroxylated residue
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Hy2Res
Dioxidation
dihydroxy
A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups.
PubMed:12686488
http://purl.org/obo/owl/PubMed#PubMed_12686488
UniMod:425
http://purl.org/obo/owl/UniMod#UniMod_425
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
dimethylated residue
For amino-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts only for dimethylation and not protonation. The alternative Me2+Res process accounts for both protonation and dimethylation. From DeltaMass: Average Mass: 28.
PSI-MOD
di-Methylation
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Dimethyl
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N,N dimethylation (of Arginine or Lysine)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Me2Res
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively replaces two hydrogen atoms with two methyl group.
UniMod:36
http://purl.org/obo/owl/UniMod#UniMod_36
PubMed:14570711
http://purl.org/obo/owl/PubMed#PubMed_14570711
PubMed:12964758
http://purl.org/obo/owl/PubMed#PubMed_12964758
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
trimethylated residue
For amino acids residues, trimethylation can effectively only be accomplished with a protonated primary amino group. This process accounts only for trimethylation and not protonation. The alternative Me3+Res process accounts for both protonation and trimethylation.
PSI-MOD
a protein modification that effectively replaces three hydrogen atoms with three methyl group
UniMod:37
http://purl.org/obo/owl/UniMod#UniMod_37
PubMed:8453381
http://purl.org/obo/owl/PubMed#PubMed_8453381
PubMed:7093227
http://purl.org/obo/owl/PubMed#PubMed_7093227
PubMed:6778808
http://purl.org/obo/owl/PubMed#PubMed_6778808
PubMed:4304194
http://purl.org/obo/owl/PubMed#PubMed_4304194
PubMed:3145979
http://purl.org/obo/owl/PubMed#PubMed_3145979
PubMed:12590383
http://purl.org/obo/owl/PubMed#PubMed_12590383
Trimethyl
Me3Res
tri-Methylation
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
modified residue with a secondary neutral loss
PSI-MOD
NLModRes
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified residue with neutral loss of phosphate
PSI-MOD
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
dPhosModRes
glucosylated residue
PSI-MOD
GlcRes
a protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
hexosylated residue
From DeltaMass: Average Mass: 162 Formula:C6 H10 05 Monoisotopic Mass Change:162.053 Average Mass Change:162.143 References:PE Sciex.
PSI-MOD
Hexose
Hex
O-Glycosyl-
Hexoses (Fru, Gal, Glc, Man)
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Hex
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond.
DeltaMass:203
http://purl.org/obo/owl/DeltaMass#DeltaMass_203
PubMed:15279557
http://purl.org/obo/owl/PubMed#PubMed_15279557
UniMod:41
http://purl.org/obo/owl/UniMod#UniMod_41
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
farnesylated residue
From DeltaMass: Average Mass: 204
PSI-MOD
Farnesylation
FarnRes
A protein modification that effectively replaces a hydrogen atom with a farnesyl group.
UniMod:44
http://purl.org/obo/owl/UniMod#UniMod_44
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:15609361
http://purl.org/obo/owl/PubMed#PubMed_15609361
Farnesyl
Farnesylation
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
myristoylated residue
From DeltaMass: Average Mass: 210
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively replaces a hydrogen atom with a myristoyl group.
UniMod:45
http://purl.org/obo/owl/UniMod#UniMod_45
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Myristoyl
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MyrRes
Myristoylation
Myristoylation
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
palmitoylated residue
From DeltaMass: Average Mass: 238
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Palmitoyl
Palmitoylation
Palmitoylation
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively replaces a hydrogen atom with a palmitoyl group.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:47
http://purl.org/obo/owl/UniMod#UniMod_47
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
PamRes
geranylgeranylated residue
From DeltaMass: Average Mass: 272
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
GergerRes
Geranylgeranylation
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
GeranylGeranyl
A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group.
UniMod:48
http://purl.org/obo/owl/UniMod#UniMod_48
PubMed:15609361
http://purl.org/obo/owl/PubMed#PubMed_15609361
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
Geranyl-geranyl
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine
PSI-MOD
N-acyl diglyceride cysteine
Tripalmitate
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
UniMod:51
http://purl.org/obo/owl/UniMod#UniMod_51
PubMed:10356335
http://purl.org/obo/owl/PubMed#PubMed_10356335
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-glucuronylated residue
From DeltaMass: Average Mass: 176
PSI-MOD
modification from UniMod Post-translational
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:54
http://purl.org/obo/owl/UniMod#UniMod_54
PubMed:7398618
http://purl.org/obo/owl/PubMed#PubMed_7398618
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N-glucuronylation
N-Glucuronyl (N terminus)
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Glucuronyl
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-acetylaminoglucosylated residue
PSI-MOD
a protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
GlcNAcRes
glycosylsphingolipidinositolated residue
PSI-MOD
GSIRes
A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
PubMed:12626404
http://purl.org/obo/owl/PubMed#PubMed_12626404
PubMed:8404891
http://purl.org/obo/owl/PubMed#PubMed_8404891
galactosylated residue
PSI-MOD
GalRes
a protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
formylated residue
From DeltaMass: Average Mass: 28
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
FoRes
Formyl
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formylation
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formylation (CHO)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively replaces a hydrogen atom with a formyl group.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:15799070
http://purl.org/obo/owl/PubMed#PubMed_15799070
UniMod:122
http://purl.org/obo/owl/UniMod#UniMod_122
fluorinated residue
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Fluoro
fluorophenylalanine replacement of phenylalanine
Fluorophenylalanyl
FRes
A protein modification that effectively substitutes a fluorine atom for a hydrogen atom.
PubMed:1093385
http://purl.org/obo/owl/PubMed#PubMed_1093385
UniMod:127
http://purl.org/obo/owl/UniMod#UniMod_127
triiodinated residue
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
tri-Iodination
Triiodo
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively substitutes three iodine atoms of a residue for three hydrogen atoms
PubMed:15627961
http://purl.org/obo/owl/PubMed#PubMed_15627961
PubMed:2026710
http://purl.org/obo/owl/PubMed#PubMed_2026710
UniMod:131
http://purl.org/obo/owl/UniMod#UniMod_131
I3Res
N-acetylaminogalactosylated residue
PSI-MOD
GalNAcRes
a protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
mannosylated residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
a protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ManRes
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
monomethylated residue
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively replaces one hydrogen atom with one methyl group.
PubMed:11875433
http://purl.org/obo/owl/PubMed#PubMed_11875433
UniMod:34
http://purl.org/obo/owl/UniMod#UniMod_34
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Methylation
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Methyl
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Me1Res
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
cyclized residue
PSI-MOD
A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or alpha carboxyl group, possibly breaking the peptide chain.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
CycRes
N-methylated residue
PSI-MOD
NMeRes
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
O-acetylated residue
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
OAcRes
A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
S-acetylated residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
SAcRes
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
acetylated L-cysteine
PSI-MOD
AcCys
A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
acetylated L-serine
PSI-MOD
AcSer
A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
acylated residue
PSI-MOD
AcylRes
A protein modification that effectively replaces a hydrogen atom with an acyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
N-myristoylated residue
PSI-MOD
A protein modification that effectively replaces a residue amino group with a myristoylamino group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
NMyrRes
N-palmitoylated residue
PSI-MOD
NPamRes
A protein modification that effectively replaces a residue amino group with a palmitoylamino group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
O-palmitoylated residue
PSI-MOD
A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
OPamRes
S-palmitoylated residue
PSI-MOD
SPamRes
A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
S-methylated residue
PSI-MOD
a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
SMeRes
S-myristoylated residue
PSI-MOD
SMyrRes
A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
C-methylated residue
PSI-MOD
A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
CMeRes
L-glutamic acid 5-methyl ester (Gln)
PSI-MOD
Deamidation followed by a methylation
deamidated 5-methyl esterified glutamine
Methyl+Deamidated
Glutamate methyl ester (Gln)
O5MeGlu(Gln)
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester.
PubMed:6300110
http://purl.org/obo/owl/PubMed#PubMed_6300110
PubMed:16888
http://purl.org/obo/owl/PubMed#PubMed_16888
UniMod:528
http://purl.org/obo/owl/UniMod#UniMod_528
RESID:AA0072
http://purl.org/obo/owl/RESID#RESID_AA0072
methylated arginine
PSI-MOD
MeArg
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
methylated glutamine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-metylated glutamine, or methyl esterified deamidated glutamine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MeGln
methylated cysteine
PSI-MOD
A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MeCys
methylated histidine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MeHis
Methylhistidine
methylated leucine
PSI-MOD
A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MeLeu
methylated lysine
PSI-MOD
A protein modification that effectively converts an L-lysine residue to a methylated lysine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MeLys
stereoisomerized residue
PSI-MOD
D-Res
A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
methylated alanine
PSI-MOD
MeAla
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
octanoylated residue
PSI-MOD
OctRes
A protein modification that effectively replaces a hydrogen atom with an octanoyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
decanoylated residue
PSI-MOD
A protein modification that effectively replaces a hydrogen atom with a decanoyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
DecRes
O-decanoylated residue
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group.
UniMod:449
http://purl.org/obo/owl/UniMod#UniMod_449
lipid
Decanoyl
ODecRes
O-octanoylated residue
PSI-MOD
Octanoyl
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group.
UniMod:426
http://purl.org/obo/owl/UniMod#UniMod_426
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
OOctRes
octanoyl
N-acylated residue
PSI-MOD
A protein modification that effectively replaces a residue amino group with a acylamino group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
NAcylRes
O-acylated residue
PSI-MOD
A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
OAcylRes
S-acylated residue
PSI-MOD
A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
SAcylRes
methylated asparagine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MeAsn
A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
amidated residue
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively replaces a carboxyl group with a carboxamido group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
oxidized residue
PSI-MOD
OxRes
A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
oxygenated residue
PSI-MOD
A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
OxyRes
hydroxylated residue
From DeltaMass: Average Mass: 16
PSI-MOD
A protein modification that effectively replaces a hydrogen atom with an hydroxyl group.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
HyRes
Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate)
hydroxylated proline
PSI-MOD
HyPro
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
carbon oxygenated residue
PSI-MOD
COxyRes
A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
sulfur oxygenated residue
PSI-MOD
A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
SOxyRes
hydroxylated lysine
PSI-MOD
HyLys
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
hydroxylated arginine
PSI-MOD
A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
HyArg
dehydrogenated residue
PSI-MOD
dHRes
A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue.
UniMod:401
http://purl.org/obo/owl/UniMod#UniMod_401
deamidated L-asparagine
incidental to RESID:AA0059
PSI-MOD
dNAsn
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Deamidated asparagine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid.
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:8089117
http://purl.org/obo/owl/PubMed#PubMed_8089117
PubMed:9521123
http://purl.org/obo/owl/PubMed#PubMed_9521123
PubMed:9582379
http://purl.org/obo/owl/PubMed#PubMed_9582379
PubMed:339692
http://purl.org/obo/owl/PubMed#PubMed_339692
PubMed:4399050
http://purl.org/obo/owl/PubMed#PubMed_4399050
PubMed:5764436
http://purl.org/obo/owl/PubMed#PubMed_5764436
UniMod:7
http://purl.org/obo/owl/UniMod#UniMod_7
RESID:AA0004
http://purl.org/obo/owl/RESID#RESID_AA0004
PubMed:1097438
http://purl.org/obo/owl/PubMed#PubMed_1097438
deamidated L-glutamine
PSI-MOD
Deamidated glutamine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid.
PubMed:4922541
http://purl.org/obo/owl/PubMed#PubMed_4922541
PubMed:4565668
http://purl.org/obo/owl/PubMed#PubMed_4565668
PubMed:1881881
http://purl.org/obo/owl/PubMed#PubMed_1881881
UniMod:7
http://purl.org/obo/owl/UniMod#UniMod_7
RESID:AA0006
http://purl.org/obo/owl/RESID#RESID_AA0006
PubMed:957425
http://purl.org/obo/owl/PubMed#PubMed_957425
PubMed:9192900
http://purl.org/obo/owl/PubMed#PubMed_9192900
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
dNGln
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
thioether crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
isopeptide crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
disulfide crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues by formation of a disulfide bond with two cysteine thiols.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
oxazole/thiazole ring crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
5-imidazolinone ring crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
uncategorized crosslinked residues
PSI-MOD
A protein crosslink modification that is not chemically categorized.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
glycosylated residue
PSI-MOD
A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
GlycoRes
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
halogen containing residue
PSI-MOD
A protein modification that effectively substitutes a halogen atom for a hydrogen atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
HalRes
halogenated residue
sulfated residue
From DeltaMass: Average Mass: 80.
PSI-MOD
A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:14752058
http://purl.org/obo/owl/PubMed#PubMed_14752058
UniMod:40
http://purl.org/obo/owl/UniMod#UniMod_40
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Sulphonation (SO3H) (of PMC group)
SulfRes
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Sulfo
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-Sulfonation
phosphorylated residue
From DeltaMass: Average Mass: 80.
PSI-MOD
PhosRes
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively replaces a hydrogen atom with a phosphate group.
UniMod:21
http://purl.org/obo/owl/UniMod#UniMod_21
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine)
Phosphorylation
Phospho
flavin modified residue
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
FlavRes
A protein modification that effectively results from forming an adduct with a compound containing a flavin group.
UniMod:50
http://purl.org/obo/owl/UniMod#UniMod_50
FAD
Flavin adenine dinucleotide
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
metal or metal cluster containing residue
PSI-MOD
A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MetalRes
porphyrin modified residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
PorphRes
tetrapyrrole modified residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TetrapyrRes
nucleotide or nucleic acid modified residue
PSI-MOD
NucRes
A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
isoprenylated residue
PSI-MOD
IpRes
A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
dehydrated residue
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively forms a double bond by removing a molecule of water from a residue.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Dehydrated
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Dehydration
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
D-valine
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-valine residue to D-valine.
PubMed:15853325
http://purl.org/obo/owl/PubMed#PubMed_15853325
RESID:AA0200
http://purl.org/obo/owl/RESID#RESID_AA0200
ChEBI:30016
http://purl.org/obo/owl/ChEBI#ChEBI_30016
D-valine
D-Val
alpha-aminoisovaleric acid
alpha-amino-beta-methylbutyric acid
(R)-2-amino-3-methylbutanoic acid
dehydrogenated tyrosine
PSI-MOD
dHTyr
A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
hydroxylated tyrosine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
HyTyr
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
sulfur oxygenated L-cysteine
PSI-MOD
SOxyCys
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
sulfur oxygenated L-methionine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
a protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
SOxyMet
protonated-dimethylated residue
For N-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts for both protonation and dimethylation. The alternative Me2Res process accounts only for dimethylation and not protonation.
PSI-MOD
A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Me2+Res
protonated-trimethylated residue
For amino acids residues, trimethylation can effectively only be accomplished with a protonated primary amino group. This process accounts for both protonation and trimethylation. The alternative Me3Res process accounts only for trimethylation and not protonation.
PSI-MOD
A protein modification that effectively adds a proton to an amino group, and replaces three hydrogen atoms with three methyl groups.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Me3+Res
methylated proline
PSI-MOD
A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MePro
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
methylated glycine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MeGly
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
methylated isoleucine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MeIle
methylated methionine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MeMet
methylated phenylalanine
PSI-MOD
MePhe
a protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
methylated tyrosine
PSI-MOD
A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MeTyr
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
monomethylated L-glutamine
PSI-MOD
a protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Me1Gln
N-acetylated L-lysine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
NAcLys
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N-methylated L-histidine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
NMeHis
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
iron containing modified residue
PSI-MOD
FeRes
A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
iron-sulfur cluster containing modification
PSI-MOD
A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
FeSRes
manganese containing modified residue
PSI-MOD
MnRes
A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
nickel containing modified residue
PSI-MOD
A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
NiRes
copper containing modified residue
PSI-MOD
CuRes
A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
molybdenum containing modified residue
PSI-MOD
MoRes
A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
molybdenum pterin containing modification
PSI-MOD
MoPterRes
A protein modification containing a molybdenum atom in a pterin ring system.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
selenium containing residue
PSI-MOD
A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
SeRes
pterin modified residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a pterin group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
PterRes
sulfur substitution for oxygen
PSI-MOD
A protein modification that effectively substitutes a sulfur atom for an oxygen atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
S(O)Res
deoxyribonucleic acid linked residue
PSI-MOD
A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
DNARes
ribonucleic acid linked residue
PSI-MOD
a protein modification
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
RNARes
adenosine diphosphoribosyl (ADP-ribosyl) modified residue
From DeltaMass: Average Mass: 541.
PSI-MOD
A protein modification that effectively results from forming an adduct with ADP-ribose through formation of a glycosidic bond.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ADPRRes
ADP-rybosylation (from NAD)
chlorinated residue
PSI-MOD
ClRes
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively substitutes a chlorine atom for a hydrogen atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
brominated residue
PSI-MOD
BrRes
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively substitutes a bromine atom for a hydrogen atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
iodinated residue
PSI-MOD
IRes
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
4-hydroxy-D-valine
PSI-MOD
D-4-hydroxyvaline
(2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid
D-gamma-hydroxyvaline
D-4HyVal
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine.
PubMed:15853325
http://purl.org/obo/owl/PubMed#PubMed_15853325
RESID:AA0388
http://purl.org/obo/owl/RESID#RESID_AA0388
O4-galactosyl-L-hydroxyproline
secondary to RESID:AA0030
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
beta-galactopyranosyl-4-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline.
RESID:AA0389
http://purl.org/obo/owl/RESID#RESID_AA0389
4-(galactosyloxy)proline
O4-glycosyl-hydroxyproline
4-(beta-D-galactopyranosyloxy)proline
(2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid
O4-(N-acetylamino)glucosyl-L-hydroxyproline
secondary to RESID:AA0030
PSI-MOD
O4-glycosyl-hydroxyproline
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline
4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline.
RESID:AA0390
http://purl.org/obo/owl/RESID#RESID_AA0390
PubMed:9660787
http://purl.org/obo/owl/PubMed#PubMed_9660787
PubMed:15238247
http://purl.org/obo/owl/PubMed#PubMed_15238247
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
4-(N-acetylglucosaminyloxy)proline
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
glycoconjugated residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through formation of a glycosidic bond or through glycation formation of a 1-deoxy-2-keto-1-yl bond.
PubMed::3743566
http://purl.org/obo/owl/PubMed#PubMed_:3743566
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
vanadium containing modified residue
PSI-MOD
A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
VRes
dimethylated L-arginine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
NNMe2Arg
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
PSI-MOD
a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
PubMed:4696757
http://purl.org/obo/owl/PubMed#PubMed_4696757
RESID:AA0391
http://purl.org/obo/owl/RESID#RESID_AA0391
PubMed:8664284
http://purl.org/obo/owl/PubMed#PubMed_8664284
PubMed:7999765
http://purl.org/obo/owl/PubMed#PubMed_7999765
phospholactoyl cysteine adduct
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
phosphoenolpyruvate cysteine adduct
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
SPEPCys
S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine
(R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid
Phosphoenolpyruvate (covalent)
cysteinyl pyruvate O-phosphothioketal
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S-galactosyl-L-cysteine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively forms an S-beta-galactosylated L-cysteine.
PubMed:11945907
http://purl.org/obo/owl/PubMed#PubMed_11945907
RESID:AA0392
http://purl.org/obo/owl/RESID#RESID_AA0392
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
S-(beta-D-galactopyranosyl)cysteine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(R)-2-amino-3-(beta-D-galactopyranosylsulfanyl)propanoic acid
SGalCys
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
S-glycosyl-cysteine
L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide
Cross-link 2; incidental to RESID:AA0300.
PSI-MOD
a protein modification that effectively converts an L-cysteine residue and an L-histidine residue to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide
PubMed:2345152
http://purl.org/obo/owl/PubMed#PubMed_2345152
RESID:AA0393
http://purl.org/obo/owl/RESID#RESID_AA0393
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
nitrogenase iron-vanadium cofactor
CysHis-[V7Fe9S]
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
L-cysteinyl-L-histidino-homocitryl octairon nonasulfide
Cross-link 2; incidental to RESID:AA0300.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-cysteine residue and an L-histidine residue to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide.
RESID:AA0394
http://purl.org/obo/owl/RESID#RESID_AA0394
PubMed:8392330
http://purl.org/obo/owl/PubMed#PubMed_8392330
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
nitrogenase iron-iron cofactor
CysHis-[8Fe9S]
L-histidino vanadium tetraoxide
PSI-MOD
(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium
1'-vanadato-L-histidine
a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide
PubMed:10543953
http://purl.org/obo/owl/PubMed#PubMed_10543953
RESID:AA0395
http://purl.org/obo/owl/RESID#RESID_AA0395
PubMed:8552646
http://purl.org/obo/owl/PubMed#PubMed_8552646
PubMed:16494433
http://purl.org/obo/owl/PubMed#PubMed_16494433
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
tele-vanadatohistidine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
haloperoxidase vanadium cofactor
histidine-1-vanadate
chloroperoxidase vanadium cofactor
dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate
NtauH2VO4His
tau-vanadatohistidine
histidine-N(epsilon)-vanadate
histidine-N1'-vanadate
bromoperoxidase vanadium cofactor
3-(S-L-cysteinyl)-L-tyrosine
Cross-link 2.
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine.
RESID:AA0396
http://purl.org/obo/owl/RESID#RESID_AA0396
PubMed:15342250
http://purl.org/obo/owl/PubMed#PubMed_15342250
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
XLNKSCys3Tyr
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
S-(3-tyrosinyl)cysteine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
3-(S-cysteinyl)-tyrosine (Cys-Tyr)
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid
(S,R)-2-amino-3-(2-amino-2-carboxyethylsulfanyl)-3-(4-hydroxyphenyl)propanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-glucosyl-L-serine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
O3-glucosylserine
OGlcSer
a protein modification that effectively forms a O3-beta-glucosylated L-serine
RESID:AA0397
http://purl.org/obo/owl/RESID#RESID_AA0397
PubMed:2511201
http://purl.org/obo/owl/PubMed#PubMed_2511201
PubMed:2105311
http://purl.org/obo/owl/PubMed#PubMed_2105311
PubMed:10734111
http://purl.org/obo/owl/PubMed#PubMed_10734111
(S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid
O-glycosylserine
O-(N-acetylaminoglucosyl)-L-serine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
O3-(N-acetylglucosaminyl)serine
OGlcNAcSer
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid
O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine
O-(N-acetylglucosaminyl)serine
O-linked (GlcNAc)
a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)serine
RESID:AA0398
http://purl.org/obo/owl/RESID#RESID_AA0398
PubMed:8404891
http://purl.org/obo/owl/PubMed#PubMed_8404891
O-glycosylserine
O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine
O-seryl-beta-N-acetylglucosaminide
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O-(N-acetylaminoglucosyl)-L-threonine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid
O-(N-acetylglucosaminyl)-L-threonine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
O-glycosylthreonine
O-linked (GlcNAc)
O3-(N-acetylglucosaminyl)threonine
OGlcNAcThr
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)threonine
RESID:AA0399
http://purl.org/obo/owl/RESID#RESID_AA0399
PubMed:8404891
http://purl.org/obo/owl/PubMed#PubMed_8404891
pyruvic acid (Ser)
DeltaMass gives mass 70 and difference mass -16 with no formula
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-serine residue to pyruvic acid.
DeltaMass:23
http://purl.org/obo/owl/DeltaMass#DeltaMass_23
PubMed:10085076
http://purl.org/obo/owl/PubMed#PubMed_10085076
PubMed:3042771
http://purl.org/obo/owl/PubMed#PubMed_3042771
PubMed:8464063
http://purl.org/obo/owl/PubMed#PubMed_8464063
RESID:AA0127
http://purl.org/obo/owl/RESID#RESID_AA0127
UniMod:385
http://purl.org/obo/owl/UniMod#UniMod_385
Pyruvic acid (Ser)
Pyruvoyl- (Serine)
Pyruvate
O-galactosyl-L-serine
PSI-MOD
(S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid
O-glycosylserine
O-linked (Gal)
O3-galactosylserine
OGalSer
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
a protein modification that effectively forms a O3-galactosylserine
RESID:AA0400
http://purl.org/obo/owl/RESID#RESID_AA0400
PubMed:666730
http://purl.org/obo/owl/PubMed#PubMed_666730
O-galactosyl-L-threonine
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
a protein modification that effectively forms a O3-galactosylthreonine
PubMed:2673008
http://purl.org/obo/owl/PubMed#PubMed_2673008
RESID:AA0401
http://purl.org/obo/owl/RESID#RESID_AA0401
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid
O-glycosylthreonine
O-linked (Gal)
O3-galactosylthreonine
OGalThr
O-mannosyl-L-serine
PSI-MOD
O-mannopyranosylserine
O3-mannosylserine
O-glycosylserine
O-linked (Man)
OManSer
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
a protein modification that effectively forms a O3-mannosylserine
PubMed:391559
http://purl.org/obo/owl/PubMed#PubMed_391559
RESID:AA0402
http://purl.org/obo/owl/RESID#RESID_AA0402
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid
O-mannosyl-L-threonine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-linked (Man)
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
O-glycosylthreonine
(2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid
OManThr
O3-mannosylthreonine
a protein modification that effectively forms a O3-mannosylthreonine
PubMed:391559
http://purl.org/obo/owl/PubMed#PubMed_391559
RESID:AA0403
http://purl.org/obo/owl/RESID#RESID_AA0403
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
O-fucosyl-L-serine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
OFucSer
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O3-fucosylserine
O-glycosylserine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Fucose
dHex
(S)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)propanoic acid
A protein modification that effectively converts an serine residue to an O-fucosylserine.
RESID:AA0404
http://purl.org/obo/owl/RESID#RESID_AA0404
PubMed:3578767
http://purl.org/obo/owl/PubMed#PubMed_3578767
PubMed:1517205
http://purl.org/obo/owl/PubMed#PubMed_1517205
PubMed:12096136
http://purl.org/obo/owl/PubMed#PubMed_12096136
PubMed:1904059
http://purl.org/obo/owl/PubMed#PubMed_1904059
UniMod:295
http://purl.org/obo/owl/UniMod#UniMod_295
PubMed:15189151
http://purl.org/obo/owl/PubMed#PubMed_15189151
PubMed:10734111
http://purl.org/obo/owl/PubMed#PubMed_10734111
PubMed:11344537
http://purl.org/obo/owl/PubMed#PubMed_11344537
PubMed:11067851
http://purl.org/obo/owl/PubMed#PubMed_11067851
PubMed:3311742
http://purl.org/obo/owl/PubMed#PubMed_3311742
O-fucosyl-L-threonine
PSI-MOD
Fucose
O-glycosylthreonine
dHex
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(2S,3R)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)butanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.
PubMed:11857757
http://purl.org/obo/owl/PubMed#PubMed_11857757
PubMed:11344537
http://purl.org/obo/owl/PubMed#PubMed_11344537
UniMod:295
http://purl.org/obo/owl/UniMod#UniMod_295
PubMed:1900431
http://purl.org/obo/owl/PubMed#PubMed_1900431
RESID:AA0405
http://purl.org/obo/owl/RESID#RESID_AA0405
PubMed:15189151
http://purl.org/obo/owl/PubMed#PubMed_15189151
PubMed:1740125
http://purl.org/obo/owl/PubMed#PubMed_1740125
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
OFucThr
O3-fucosylthreonine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
O-linked (Fuc)
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
O-xylosyl-L-serine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
a protein modification that effectively forms a O3-xylosylserine
RESID:AA0406
http://purl.org/obo/owl/RESID#RESID_AA0406
PubMed:8747463
http://purl.org/obo/owl/PubMed#PubMed_8747463
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
OXylSer
O-glycosylserine
O3-xylosylserine
(S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid
O-(beta-D-xylopyranosyl)-L-serine
S-stearoyl-L-cysteine
From DeltaMass: Average Mass: 266
PSI-MOD
SSteCys
Stearoylation
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
S-stearoyl cysteine
cysteine stearate thioester
cysteine octadecanoate thioester
2-amino-3-(octadecanoylthio)propanoic acid
(R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine.
PubMed:3143715
http://purl.org/obo/owl/PubMed#PubMed_3143715
PubMed:8761467
http://purl.org/obo/owl/PubMed#PubMed_8761467
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:2371783
http://purl.org/obo/owl/PubMed#PubMed_2371783
RESID:AA0407
http://purl.org/obo/owl/RESID#RESID_AA0407
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
PubMed:8168130
http://purl.org/obo/owl/PubMed#PubMed_8168130
PubMed:16407988
http://purl.org/obo/owl/PubMed#PubMed_16407988
ChEBI:35304
http://purl.org/obo/owl/ChEBI#ChEBI_35304
RESID:AA0408
http://purl.org/obo/owl/RESID#RESID_AA0408
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
3'Ger2'N2cycTrp
3'-geranyl-2',N2-cyclotryptophan
(2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
glycosylphosphatidylinositolated residue
PSI-MOD
GPIanchor
GPIRes
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
GPI-anchor amidated carboxyl end
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
glycosylphosphatidylinositol
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated.
UniMod:394
http://purl.org/obo/owl/UniMod#UniMod_394
PubMed:12643538
http://purl.org/obo/owl/PubMed#PubMed_12643538
L-2-aminobutanoic acid (Glu)
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Abu
A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid.
RESID:AA0409
http://purl.org/obo/owl/RESID#RESID_AA0409
PubMed:11740505
http://purl.org/obo/owl/PubMed#PubMed_11740505
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ChEBI:35619
http://purl.org/obo/owl/ChEBI#ChEBI_35619
(S)-2-aminobutanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-2-amino-n-butyric acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
dCbxGlu
L-alpha-amino-n-butyric acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-2-aminobutyric acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
L-butyrine
L-alpha-aminobutyric acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
2-imino-alanine 5-imidazolinone glycine
Cross-link 2; carboxamidine.
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2,N-didehydroalanyl-5-imidazolinone glycine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
alanyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
2-imino-alanyl-5-imidazolinone glycine
[2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
red fluorescent protein zRFP574 chromophore
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine.
RESID:AA0410
http://purl.org/obo/owl/RESID#RESID_AA0410
PubMed:16627946
http://purl.org/obo/owl/PubMed#PubMed_16627946
S-(L-alanyl)-L-cysteine
Cross-link 2.
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
XLNK1AlaSCys
S-(2-aminopropanoyl)cysteine
A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine.
RESID:AA0411
http://purl.org/obo/owl/RESID#RESID_AA0411
PubMed:11807079
http://purl.org/obo/owl/PubMed#PubMed_11807079
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(R)-2-amino-3-[(S)-2-amino-1-oxopropyl]sulfanylpropanoic acid
alanine cysteine thioester
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-(L-leucyl)-L-cysteine
Cross-link 2.
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine.
RESID:AA0412
http://purl.org/obo/owl/RESID#RESID_AA0412
PubMed:12591958
http://purl.org/obo/owl/PubMed#PubMed_12591958
S-(2-amino-4-methylpentanoyl)cysteine
XLNK1LeuSCys
(R)-2-amino-3-[(S)-2-amino-4-methyl-1-oxopentyl]sulfanylpropanoic acid
leucine cysteine thioester
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-(L-methionyl)-L-cysteine
Cross-link 2.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine.
PubMed:12146974
http://purl.org/obo/owl/PubMed#PubMed_12146974
RESID:AA0413
http://purl.org/obo/owl/RESID#RESID_AA0413
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
methionine cysteine thioester
S-(2-amino-4-methylthiobutanoyl)cysteine
(R)-2-amino-3-[(S)-2-amino-4-methylsulfanyl-1-oxobutyl]sulfanylpropanoic acid
XLNK1MetSCys
S-(L-phenylalanyl)-L-cysteine
Cross-link 2.
PSI-MOD
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine.
PubMed:12591958
http://purl.org/obo/owl/PubMed#PubMed_12591958
RESID:AA0414
http://purl.org/obo/owl/RESID#RESID_AA0414
phenylalanine cysteine thioester
(R)-2-amino-3-[(S)-2-amino-3-phenyl-1-oxopropyl]sulfanylpropanoic acid
XLNK1PheSCys
S-(2-amino-3-phenylpropanoyl)cysteine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-(L-threonyl)-L-cysteine
Cross-link 2.
PSI-MOD
S-(2-amino-3-hydroxybutanoyl)cysteine
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(R)-2-amino-3-[(2S,3R)-2-amino-3-hydroxy-1-oxobutyl]sulfanylpropanoic acid
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine.
RESID:AA0415
http://purl.org/obo/owl/RESID#RESID_AA0415
PubMed:15268951
http://purl.org/obo/owl/PubMed#PubMed_15268951
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
threonine cysteine thioester
XLNK1ThrSCys
S-(L-tyrosyl)-L-cysteine
Cross-link 2.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
XLNK1TyrSCys
tyrosine cysteine thioester
A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine.
RESID:AA0416
http://purl.org/obo/owl/RESID#RESID_AA0416
PubMed:11807079
http://purl.org/obo/owl/PubMed#PubMed_11807079
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(R)-2-amino-3-[(S)-2-amino-3-(4-hydoxyphenyl)-1-oxopropyl]sulfanylpropanoic acid
S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
S-(L-tryptophanyl)-L-cysteine
Cross-link 2.
PSI-MOD
XLNK1TrpSCys
S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine
tryptophan cysteine thioester
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
(R)-2-amino-3-[(S)-2-amino-3-(1H-indol-3-yl)-1-oxopropyl]sulfanylpropanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine.
PubMed:16030216
http://purl.org/obo/owl/PubMed#PubMed_16030216
RESID:AA0417
http://purl.org/obo/owl/RESID#RESID_AA0417
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
O-(L-phenylalanyl)-L-serine
Cross-link 2.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O-(2-amino-3-phenylpropanoyl)serine
(R)-2-amino-3-[(S)-2-amino-3-phenyl-1-oxopropyl]oxypropanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
XLNK1PheOSer
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
phenylalanine serine ester
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine.
RESID:AA0418
http://purl.org/obo/owl/RESID#RESID_AA0418
PubMed:12591958
http://purl.org/obo/owl/PubMed#PubMed_12591958
N-methyl-L-proline
PSI-MOD
N-methylproline
A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline.
RESID:AA0419
http://purl.org/obo/owl/RESID#RESID_AA0419
PubMed:3127388
http://purl.org/obo/owl/PubMed#PubMed_3127388
1-methylpyrrolidine-2-carboxylic acid
N-methylated L-proline
(S)-1-methylpyrrolidine-2-carboxylic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
NMePro
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N4-(N-acetylamino)galactosyl-L-asparagine
PSI-MOD
N4-glycosylasparagine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N4GalNAcAsn
(S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid
N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine
N4-asparagine-beta-N-acetylgalactosaminide
N4-glycosyl-L-asparagine
N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine
N4-(N-acetylgalactosaminyl)asparagine
A protein modification that effectively converts an L-asparagine residue to an N4-(N-acetamino)galactosyl-asparagine.
PubMed:8262914
http://purl.org/obo/owl/PubMed#PubMed_8262914
RESID:AA0420
http://purl.org/obo/owl/RESID#RESID_AA0420
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
N4-glucosyl-L-asparagine
PSI-MOD
(S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid
N4-(D-glucopyranosyl)-L-asparagine
N4-asparagine-glucoside
N4-glycosyl-L-asparagine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N4-glucosylasparagine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
N4-glycosylasparagine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N4GlcAsn
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts an L-asparagine residue to an N4-glucosyl-asparagine.
PubMed:3410849
http://purl.org/obo/owl/PubMed#PubMed_3410849
RESID:AA0421
http://purl.org/obo/owl/RESID#RESID_AA0421
PubMed:1569073
http://purl.org/obo/owl/PubMed#PubMed_1569073
O-(N-acetylamino)fucosyl-L-serine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
OFucNAcSer
O-seryl-beta-N-acetylfucosaminide
O-(N-acetylfucosaminyl)serine
O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine
(S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
O3-(N-acetylfucosaminyl)serine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
a protein modification that effectively forms an O3-(N-acetamino)fucosylserine
PubMed:11342554
http://purl.org/obo/owl/PubMed#PubMed_11342554
PubMed:12010970
http://purl.org/obo/owl/PubMed#PubMed_12010970
RESID:AA0422
http://purl.org/obo/owl/RESID#RESID_AA0422
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
L-3-oxoalanine (Ser)
PSI-MOD
3-oxoalanine (Ser)
2-amino-3-oxopropionic acid
L-amino-malonic acid semialdehyde
formylglycine (from serine)
L-serinesemialdehyde
L-aminomalonaldehydic acid
dehydrogenated serine residue
C(alpha)-formylglycine
formylglycine
A protein modification that effectively converts an L-serine residue to L-oxoalanine.
UniMod:401
http://purl.org/obo/owl/UniMod#UniMod_401
RESID:AA0185
http://purl.org/obo/owl/RESID#RESID_AA0185
PubMed:9478923
http://purl.org/obo/owl/PubMed#PubMed_9478923
PubMed:9276974
http://purl.org/obo/owl/PubMed#PubMed_9276974
PubMed:8681943
http://purl.org/obo/owl/PubMed#PubMed_8681943
PubMed:7628016
http://purl.org/obo/owl/PubMed#PubMed_7628016
PubMed:14563551
http://purl.org/obo/owl/PubMed#PubMed_14563551
DeltaMass:349
http://purl.org/obo/owl/DeltaMass#DeltaMass_349
Didehydro
(S)-2-amino-3-oxopropanoic acid
oxoalanine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
reagent derivatized residue
PSI-MOD
A protein modification that is produced by formation of an adduct with a particular compound used as a reagent.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
D-alanine (Ser)
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
D-Ala(Ser)
D-alanine (Ser)
A protein modification that effectively converts an L-serine residue to D-alanine.
RESID:AA0191
http://purl.org/obo/owl/RESID#RESID_AA0191
PubMed:7961627
http://purl.org/obo/owl/PubMed#PubMed_7961627
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modified residue that can arise from different natural residues
PSI-MOD
A protein modification that can be derived from different natural residues by different chemical processes.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
sulfur containing residue
PSI-MOD
A protein modification that produces an amino acid residue containing a sulfur atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
phosphorus containing residue
PSI-MOD
A protein modification that produces an amino acid residue containing a phosphorus atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
D-alanine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(R)-2-aminopropanoic acid
A protein modification that effectively converts a source amino acid residue to D-alanine.
RESID:AA0191
http://purl.org/obo/owl/RESID#RESID_AA0191
ChEBI:29949
http://purl.org/obo/owl/ChEBI#ChEBI_29949
PubMed:7287302
http://purl.org/obo/owl/PubMed#PubMed_7287302
PubMed:7961627
http://purl.org/obo/owl/PubMed#PubMed_7961627
D-allo-threonine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-threonine residue to D-allo-threonine.
PubMed:6893271
http://purl.org/obo/owl/PubMed#PubMed_6893271
RESID:AA0199
http://purl.org/obo/owl/RESID#RESID_AA0199
ChEBI:32826
http://purl.org/obo/owl/ChEBI#ChEBI_32826
PubMed:18025465
http://purl.org/obo/owl/PubMed#PubMed_18025465
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
D-threonine
D-Thr
D-allo-threonine
(2R,3R)-2-amino-3-hydroxybutanoic acid
tris-L-cysteinyl L-histidino diiron disulfide
Cross-link 4.
PSI-MOD
A protein modification that effectively converts three L-cysteine residues and an L-histidine residue to tris-L-cysteinyl L-histidino diiron disulfide.
PubMed:17766439
http://purl.org/obo/owl/PubMed#PubMed_17766439
RESID:AA0438
http://purl.org/obo/owl/RESID#RESID_AA0438
PubMed:17766440
http://purl.org/obo/owl/PubMed#PubMed_17766440
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
CDGSH domain iron-sulfur cluster
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron)
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-aspartyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
GSIAsp
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine.
RESID:AA0439
http://purl.org/obo/owl/RESID#RESID_AA0439
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
GPI-like-anchor amidated aspartate
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
dihydroxylated proline
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Hy2Pro
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
natural, non-standard encoded residue
These are produced exclusively by modification of amino acids acylated to special tRNA before incorporation by ribosomes into proteins. For this reason, they have also been referred to as pre-translational modifications.
PSI-MOD
A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
L-alanine residue (Asp)
This has been reported to occur by a natural process of beta-decarboxylation.
PSI-MOD
Beta-decarboxylated aspartate
Asp(Ala)
A protein modification that effectively converts an L-aspartic acid residue to L-alanine.
PubMed:17138938
http://purl.org/obo/owl/PubMed#PubMed_17138938
RESID:AA0001
http://purl.org/obo/owl/RESID#RESID_AA0001
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
alpha-amidated residue
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Amide formation (C terminus)
Amidation
A protein modification that effectively replaces an alpha-carboxyl group with a carboxamido group.
UniMod:2
http://purl.org/obo/owl/UniMod#UniMod_2
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
ResN
Amidated
ester crosslinked residues
PSI-MOD
A protein modification that crosslinks two residues by formation of an ester bond.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
L-6'-chlorotryptophan
PSI-MOD
6'-ClTrp
(S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid
6'-chlorotryptophan
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
A protein modification that effectively converts an L-tryptophan residue to L-6'-chlorotryptophan.
RESID:AA0180
http://purl.org/obo/owl/RESID#RESID_AA0180
UniMod:340
http://purl.org/obo/owl/UniMod#UniMod_340
PubMed:9033387
http://purl.org/obo/owl/PubMed#PubMed_9033387
phosphorylated L-histidine
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
D-serine
PSI-MOD
(R)-2-amino-3-hydroxypropanoic acid
D-Ser
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts a source amino acid residue to D-serine.
ChEBI:29998
http://purl.org/obo/owl/ChEBI#ChEBI_29998
RESID:AA0195
http://purl.org/obo/owl/RESID#RESID_AA0195
PubMed:7973665
http://purl.org/obo/owl/PubMed#PubMed_7973665
PubMed:6893271
http://purl.org/obo/owl/PubMed#PubMed_6893271
D-serine (Cys)
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts an L-cysteine residue to D-serine.
PubMed:18025465
http://purl.org/obo/owl/PubMed#PubMed_18025465
RESID:AA0195
http://purl.org/obo/owl/RESID#RESID_AA0195
PubMed:6893271
http://purl.org/obo/owl/PubMed#PubMed_6893271
D-serine (Cys)
FAD modified residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
FMN modified residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
N-palmitoyl-S-diacylglycerol-L-cysteine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modified L-alanine residue
PSI-MOD
ModAla
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Alanine derivative
A protein modification that modifies an L-alanine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-arginine residue
PSI-MOD
Arginine derivative
ModArg
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-arginine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-asparagine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModAsn
A protein modification that modifies an L-asparagine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-aspartic acid residue
PSI-MOD
A protein modification that modifies an L-aspartic acid residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModAsp
modified L-cysteine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-cysteine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
ModCys
Cysteine derivative
modified L-glutamic acid residue
PSI-MOD
A protein modification that modifies an L-glutamic acid residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModGlu
modified L-glutamine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Glutamine derivative
ModGln
A protein modification that modifies an L-glutamine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified glycine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies a glycine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
ModGly
modified L-histidine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModHis
A protein modification that modifies an L-histidine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-isoleucine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-isoleucine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Isoleucine derivative
ModIle
modified L-leucine residue
PSI-MOD
ModLeu
A protein modification that modifies an L-leucine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modified L-lysine residue
PSI-MOD
A protein modification that modifies an L-lysine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModLys
Lysine derivative
modified L-methionine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-methionine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
ModMet
Methionine derivative
modified L-phenylalanine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-phenylalanine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
ModPhe
modified L-proline residue
PSI-MOD
A protein modification that modifies an L-proline residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
ModPro
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
modified L-serine residue
PSI-MOD
ModSer
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-serine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-threonine residue
PSI-MOD
A protein modification that modifies an L-threonine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModThr
modified L-tryptophan residue
PSI-MOD
Tryptophan derivative
ModTrp
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-tryptophan residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-tyrosine residue
PSI-MOD
A protein modification that modifies an L-tyrosine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModTyr
modified L-valine residue
PSI-MOD
A protein modification that modifies an L-valine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ModVal
N6-(L-threonyl)-L-lysine
Cross-link 2.
PSI-MOD
A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine.
PubMed:18063774
http://purl.org/obo/owl/PubMed#PubMed_18063774
RESID:AA0440
http://purl.org/obo/owl/RESID#RESID_AA0440
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
(2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
N6-threonyl-lysine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
crosslinked residues with loss of ammonia
PSI-MOD
A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
(2-aminosuccinimidyl)acetic acid
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue with the alpha-amido of the following residue.
PSI-MOD
(3-amino-2,5-dioxopyrrolidin-1-yl)acetic acid
A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid.
PubMed:10801322
http://purl.org/obo/owl/PubMed#PubMed_10801322
RESID:AA0441
http://purl.org/obo/owl/RESID#RESID_AA0441
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid
N-(2-aminosuccinyl)glycine
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
crosslinked residues with loss of water
PSI-MOD
A protein modification that crosslinks two residues with a covalent bond and the loss of water.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
monobrominated L-phenylalanine
From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Br1Phe
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
bromination
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Bromo
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
halogenated tyrosine
PSI-MOD
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
HalTyr
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
iodinated tyrosine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
ITyr
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
monohydroxylated proline
From DeltaMass: Average Mass: 131
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Hydroxyproline
Hyp
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Hy1Pro
A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline.
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
Hydroxyproline
monohydroxylated lysine
From DeltaMass: Average Mass: 144 Abbreviation:-Hyl- Formula:C6H12N2O2 Monoisotopic Mass Change:144.09 Average Mass Change:144.174.
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Hydroxy Lysyl (-Hyl-)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Hy1Lys
A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine.
DeltaMass:168
http://purl.org/obo/owl/DeltaMass#DeltaMass_168
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
2-pyrrolidone-5-carboxylic acid
From DeltaMass: Average Mass: -18 Average Mass Change:-18.01 References:The conversion of glutamic acid to pyroglutamic was reported for the beta-amiloid protein.Miller et.al. Arch. Biochem. Biophy. (1993) 301, 41-52.
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Pyrrolidone carboxylic acid
PyrGlu
isoprenylated cysteine
PSI-MOD
IpCys
A protein modification that effectively replaces a hydrogen atom of an L-cysteine residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20).
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
S-farnesyl-L-cysteine methyl ester
PSI-MOD
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester.
PubMed:15609361
http://purl.org/obo/owl/PubMed#PubMed_15609361
RESID:AA0102
http://purl.org/obo/owl/RESID#RESID_AA0102
SFarnOMeCys
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic methyl ester
(R,E,E)-2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylsulfanyl)propanoic methyl ester
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
S-geranylgeranyl-L-cysteine methyl ester
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester.
PubMed:1483450
http://purl.org/obo/owl/PubMed#PubMed_1483450
PubMed:15609361
http://purl.org/obo/owl/PubMed#PubMed_15609361
RESID:AA0104
http://purl.org/obo/owl/RESID#RESID_AA0104
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
SGergerOMeCys
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
(R,E,E,E)-2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylsulfanyl)propanoic methyl ester
2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic methyl ester
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
S-12-hydroxyfarnesyl-L-cysteine methyl ester
PSI-MOD
(R,E,E,Z)-2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylsulfanyl)propanoic methyl ester
2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic methyl ester
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester.
PubMed:17790543
http://purl.org/obo/owl/PubMed#PubMed_17790543
RESID:AA0103
http://purl.org/obo/owl/RESID#RESID_AA0103
S12HyFarnOMeCys
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
S-(sn-1-2,3-dipalmitoylglycerol)-L-cysteine
From DeltaMass: Average Mass: 524
PSI-MOD
S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine)
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
PubMed:9056182
http://purl.org/obo/owl/PubMed#PubMed_9056182
RESID:AA0107
http://purl.org/obo/owl/RESID#RESID_AA0107
PubMed:10896212
http://purl.org/obo/owl/PubMed#PubMed_10896212
PubMed:4575979
http://purl.org/obo/owl/PubMed#PubMed_4575979
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
ubiquitinylated lysine
PSI-MOD
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin.
PubMed:11125103
http://purl.org/obo/owl/PubMed#PubMed_11125103
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
sumoylated lysine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
PubMed:12612601
http://purl.org/obo/owl/PubMed#PubMed_12612601
neddylated lysine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein.
PubMed:11125103
http://purl.org/obo/owl/PubMed#PubMed_11125103
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
PubMed:12612601
http://purl.org/obo/owl/PubMed#PubMed_12612601
carboxylated residue
PSI-MOD
Carboxy
A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group.
UniMod:299
http://purl.org/obo/owl/UniMod#UniMod_299
Carboxylation
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
methylthiolated residue
PSI-MOD
A protein modification that effectively replaces a hydrogen atom with an sulfanylmethyl group (thiomethyl group).
UniMod:39
http://purl.org/obo/owl/UniMod#UniMod_39
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Beta-methylthiolation
Methylthio
pyruvic acid
PSI-MOD
2-oxopropanoic acid
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts a source amino acid to pyruvic acid.
PubMed:10085076
http://purl.org/obo/owl/PubMed#PubMed_10085076
PubMed:8464063
http://purl.org/obo/owl/PubMed#PubMed_8464063
PubMed:3042771
http://purl.org/obo/owl/PubMed#PubMed_3042771
RESID:AA0127
http://purl.org/obo/owl/RESID#RESID_AA0127
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
lipoconjugated residue
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
protein modification categorized by chemical process
PSI-MOD
Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
protein modification categorized by amino acid modified
PSI-MOD
A protein modification considered either as modified amino acid residues derived from natural amino acids, as a replacement by another natural amino acid, or as a replacement by an unnatural amino acid.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
modified L-selenocysteine residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that modifies an L-selenocysteine residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
peptidoglycanated residue
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively attaches a residue to murein peptidoglycan by a pentaglycine linker peptide.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
deaminated residue
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Ammonia-loss
Loss of ammonia
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively results in the loss of an ammonia, usually by a process of vicinal dehydration, rearrangement, and rehydration with release of ammonia, resulting in a loss of nitrogen with no gain of oxygen.
UniMod:385
http://purl.org/obo/owl/UniMod#UniMod_385
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
deoxygenated residue
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms.
UniMod:447
http://purl.org/obo/owl/UniMod#UniMod_447
PubMed:14235557
http://purl.org/obo/owl/PubMed#PubMed_14235557
Deoxy
reduction
dOxyRes
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
guanylated residue
From DeltaMass: (formula incorrect, N and O reversed) Average Mass: 345 Formula: C10H12O5N7P1 Monoisotopic Mass Change: 345.047 Average Mass Change: 345.209.
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond.
UniMod:413
http://purl.org/obo/owl/UniMod#UniMod_413
DeltaMass:304
http://purl.org/obo/owl/DeltaMass#DeltaMass_304
Phosphoguanosine
phospho-guanosine
5'phos Guanosyl
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
riboflavin-phosphoryl
PSI-MOD
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through a phosphodiester bond.
UniMod:442
http://purl.org/obo/owl/UniMod#UniMod_442
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
FMN
O3-(riboflavin phosphoryl)
adenylated residue
From DeltaMass: (name misspelled "5'phos adenosinyl") Average Mass: 329
PSI-MOD
AMP binding site
5'phos Adenosinyl
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond.
UniMod:405
http://purl.org/obo/owl/UniMod#UniMod_405
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
Phosphoadenosine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
uridylated residue
From DeltaMass: (name misspelled "5'phos Uridinyl" and formula incorrect, N and O reversed) Average Mass: 306 Formula: C9H11O2N8P1 Monoisotopic Mass Change: 306.025 Average Mass Change: 306.17
PSI-MOD
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
5'phos Uridinyl
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond.
DeltaMass:292
http://purl.org/obo/owl/DeltaMass#DeltaMass_292
UniMod:417
http://purl.org/obo/owl/UniMod#UniMod_417
PhosphoUridine
uridine phosphodiester
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
molybdopterin guanine dinucleotide
PSI-MOD
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MolybdopterinGD
modification from UniMod
UniMod:424
http://purl.org/obo/owl/UniMod#UniMod_424
molybdenum bis(molybdopterin guanine dinucleotide)
dehydroalanine
incidental to RESID:AA0178
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
A protein modification that effectively converts a source amino acid residue to dehydroalanine.
PubMed:10220322
http://purl.org/obo/owl/PubMed#PubMed_10220322
PubMed:2914619
http://purl.org/obo/owl/PubMed#PubMed_2914619
PubMed:1547888
http://purl.org/obo/owl/PubMed#PubMed_1547888
PubMed:1815586
http://purl.org/obo/owl/PubMed#PubMed_1815586
PubMed:7947813
http://purl.org/obo/owl/PubMed#PubMed_7947813
PubMed:6838602
http://purl.org/obo/owl/PubMed#PubMed_6838602
RESID:AA0181
http://purl.org/obo/owl/RESID#RESID_AA0181
PubMed:8239649
http://purl.org/obo/owl/PubMed#PubMed_8239649
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
anhydroserine
4-methylidene-imidazole-5-one active site
2-aminopropenoic acid
2,3-didehydroalanine
dHAla
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
L-3-oxoalanine
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts a source amino acid residue to L-oxoalanine.
PubMed:14563551
http://purl.org/obo/owl/PubMed#PubMed_14563551
RESID:AA0185
http://purl.org/obo/owl/RESID#RESID_AA0185
PubMed:9478923
http://purl.org/obo/owl/PubMed#PubMed_9478923
PubMed:8681943
http://purl.org/obo/owl/PubMed#PubMed_8681943
PubMed:7628016
http://purl.org/obo/owl/PubMed#PubMed_7628016
DeltaMass:349
http://purl.org/obo/owl/DeltaMass#DeltaMass_349
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
L-aminomalonaldehydic acid
L-serinesemialdehyde [misnomer]
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
C(alpha)-formylglycine [misnomer]
L-amino-malonic acid semialdehyde
pyruvic acid iminylated residue
PSI-MOD
PyruvicAcidIminyl
A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group.
UniMod:422
http://purl.org/obo/owl/UniMod#UniMod_422
N-pyruvic acid 2-iminyl
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
O-acetyl-L-threonine
PSI-MOD
O-acetylthreonine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Acetylation
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
(S)-2-amino-3-acetyloxypropanoic acid
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
OAcThr
threonine acetate ester
A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine.
PubMed:16728640
http://purl.org/obo/owl/PubMed#PubMed_16728640
UniMod:1
http://purl.org/obo/owl/UniMod#UniMod_1
RESID:AA0423
http://purl.org/obo/owl/RESID#RESID_AA0423
N-alanyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine.
RESID:AA0424
http://purl.org/obo/owl/RESID#RESID_AA0424
PubMed:12626404
http://purl.org/obo/owl/PubMed#PubMed_12626404
GSIAla
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
GPI-like-anchor amidated alanine
N-asparaginyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
GSIAsn
GPI-like-anchor amidated asparagine
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine.
PubMed:12626404
http://purl.org/obo/owl/PubMed#PubMed_12626404
RESID:AA0425
http://purl.org/obo/owl/RESID#RESID_AA0425
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine
PSI-MOD
(5Z,9Xi,12E,14Z)-9-([(2R)-2-amino-3-carboxyethyl]sulfanyl)-11-oxoprosta-5,12,14-trien-1-oic acid
(2R)-2-amino-3-([(5Z,9Xi,12E,14Z)-1-hydroxy-1,11-oxoprosta-5,12,14-trien-9-yl]sulfanyl)propanoic acid
PG-J2Cys
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine.
PubMed:11466314
http://purl.org/obo/owl/PubMed#PubMed_11466314
ChEBI:27485
http://purl.org/obo/owl/ChEBI#ChEBI_27485
RESID:AA0426
http://purl.org/obo/owl/RESID#RESID_AA0426
PubMed:12684535
http://purl.org/obo/owl/PubMed#PubMed_12684535
S-phycourobilin-L-cysteine
PSI-MOD
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
18-ethenyl-3-[1-(2-amino-2-carboxyethylsulfanyl)ethyl]-2,3,15,16-dihydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(2S,3R,16R)-18-ethenyl-3-[(1R)-1-([(R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydrobiline-1,19(21H,22H,24H)-dione
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
PUBCys
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin.
PubMed:1903388
http://purl.org/obo/owl/PubMed#PubMed_1903388
PubMed:3838747
http://purl.org/obo/owl/PubMed#PubMed_3838747
PubMed:3208761
http://purl.org/obo/owl/PubMed#PubMed_3208761
RESID:AA0427
http://purl.org/obo/owl/RESID#RESID_AA0427
phycourobilin cysteine adduct
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
L-dehydrolysinonorleucine
Cross-link 2.
PSI-MOD
modification from RESID
RESID:AA0430
http://purl.org/obo/owl/RESID#RESID_AA0430
PubMed:16929109
http://purl.org/obo/owl/PubMed#PubMed_16929109
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
L-6,N6-didehydrolysino-L-norleucine
didehydrolysinonorleucine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(2R)-6-[(5R)-5-amino-5-carboxypentyl]imino-2-aminohexanoic acid
dehydrolysinorleucine [misspelling]
dehydrolysylnorleucine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
N6-[(S)-5-amino-5-carboxypentylidene]-L-lysine
XLNK6NleN6Lys
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine
PSI-MOD
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
tele-(1,2,3-trihydroxypropan-2-yl)histidine
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
tau-(1,2,3-trihydroxypropan-2-yl)histidine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
modification from RESID
PubMed:16760471
http://purl.org/obo/owl/PubMed#PubMed_16760471
RESID:AA0431
http://purl.org/obo/owl/RESID#RESID_AA0431
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
N(epsilon)-histidine dihydroxyacetone adduct
NtauDHAHis
(S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine
S-(aspart-4-yloxy) thiocarbonate
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
4-aspartyloxysulfanylcarbonate
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
(2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
O-carboxysulfanyl-4-oxo-L-homoserine
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
AspOSCO2H
a protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate
RESID:AA0432
http://purl.org/obo/owl/RESID#RESID_AA0432
PubMed:16627948
http://purl.org/obo/owl/PubMed#PubMed_16627948
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
N,N-dimethyl-L-alanine
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
N,N-dimethylalanine
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
NMe2Ala
(S)-1-carboxy-N,N-dimethylaminoethane
A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine.
PubMed:387091
http://purl.org/obo/owl/PubMed#PubMed_387091
PubMed:17691833
http://purl.org/obo/owl/PubMed#PubMed_17691833
RESID:AA0433
http://purl.org/obo/owl/RESID#RESID_AA0433
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
(S)-2-(dimethylamino)propanoic acid
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
2-hydroxyglycine observational artifact
CAUTION - peptides of 2-hydroxyglycine are known to be unstable, decaying to break the peptide backbone or to form peptidyl amides [see J. Am. Chem. Soc. 111, 1933-1934, 1989, and J. Org. Chem. 57, 3916-3921, 1992]. If computer analysis of tandem mass-spectrometric results predicts this modification, then it is most probable that there are multiple isobaric peptides differing in the location of multiple hydroxylation modifications [JSG].
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
alpha-hydroxyglycine
amino(hydroxy)acetic acid
aminohydroxyacetic acid
A protein modification that effectively converts a glycine residue to 2-hydroxyglycine.
ChEBI:38048
http://purl.org/obo/owl/ChEBI#ChEBI_38048
PubMed:17431180
http://purl.org/obo/owl/PubMed#PubMed_17431180
PubMed:16178056
http://purl.org/obo/owl/PubMed#PubMed_16178056
RESID:AA0434
http://purl.org/obo/owl/RESID#RESID_AA0434
PubMed:17823333
http://purl.org/obo/owl/PubMed#PubMed_17823333
2HyGly
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
4-amidated L-aspartic acid
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
Amidated aspartic acid
4NAsp
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively converts an L-aspartic acid residue to L-asparagine.
PubMed:17962566
http://purl.org/obo/owl/PubMed#PubMed_17962566
RESID:AA0003
http://purl.org/obo/owl/RESID#RESID_AA0003
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
acetylated L-threonine
PSI-MOD
AcThr
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
L-pyrrolysine residue
PSI-MOD
A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification.
PubMed:12029131
http://purl.org/obo/owl/PubMed#PubMed_12029131
PubMed:11435424
http://purl.org/obo/owl/PubMed#PubMed_11435424
ChEBI:21860
http://purl.org/obo/owl/ChEBI#ChEBI_21860
PubMed:16096277
http://purl.org/obo/owl/PubMed#PubMed_16096277
PubMed:15314242
http://purl.org/obo/owl/PubMed#PubMed_15314242
PubMed:12029132
http://purl.org/obo/owl/PubMed#PubMed_12029132
RESID:AA0321
http://purl.org/obo/owl/RESID#RESID_AA0321
UniMod:435
http://purl.org/obo/owl/UniMod#UniMod_435
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Pyl
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
nitrotyrosine
One or more isobaric isomers produced by nitration with peroxynitrite reagent. [JSG]
PSI-MOD
Nitro
Oxidation to nitro
Nitrated tyrosine
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
modification from UniMod Chemical derivative -
PubMed:8839040
http://purl.org/obo/owl/PubMed#PubMed_8839040
PubMed:9252331
http://purl.org/obo/owl/PubMed#PubMed_9252331
PubMed:14678012
http://purl.org/obo/owl/PubMed#PubMed_14678012
UniMod:354
http://purl.org/obo/owl/UniMod#UniMod_354
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
monomethylated proline
PSI-MOD
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Me1Pro
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
A protein modification that effectively converts an L-proline residue to a monomethylated proline.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
thiazole/thiazoline ring croslinked residues
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
A protein modification that crosslinks two residues by condensation of a cysteine thiol with the carbonyl of the preceding residue to form a thiazole or thiazoline ring.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
natural, standard, encoded residue
PSI-MOD
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that inserts or replaces a residue with a natural, standard, encoded residue.
PubMed:6692818
http://purl.org/obo/owl/PubMed#PubMed_6692818
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
L-glutamic acid 5-methyl ester
PSI-MOD
A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester.
RESID:AA0072
http://purl.org/obo/owl/RESID#RESID_AA0072
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
O5MeGlu
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
5-methyl esterified L-glutamic acid
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
O-methyl Glutamyl
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
Glutamate methyl ester (Glu)
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
N-alpha-methylated proline
PSI-MOD
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
(E)-dehydrobutyrine
PSI-MOD
Dehydroamino butyric acid
dHyThr
Dehydration
methyl-dehydroalanine
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
(E)-2-amino-butenoic acid
2,3-didehydrobutyrine
2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
Dehydrated
A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine.
PubMed:1547888
http://purl.org/obo/owl/PubMed#PubMed_1547888
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
RESID:AA0182
http://purl.org/obo/owl/RESID#RESID_AA0182
PubMed:3769923
http://purl.org/obo/owl/PubMed#PubMed_3769923
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
(Z)-dehydrobutyrine
PSI-MOD
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine
RESID:AA0182
http://purl.org/obo/owl/RESID#RESID_AA0182
UniMod:23
http://purl.org/obo/owl/UniMod#UniMod_23
DeltaMass:NULL
http://purl.org/obo/owl/DeltaMass#DeltaMass_NULL
PubMed:1547888
http://purl.org/obo/owl/PubMed#PubMed_1547888
PubMed:3769923
http://purl.org/obo/owl/PubMed#PubMed_3769923
2,3-didehydrobutyrine
Dehydroamino butyric acid
Dehydration
methyl-dehydroalanine
dHyThr
alpha,beta-dehydroaminobutyric acid
(Z)-2-amino-butenoic acid
2,3-didehydrobutyrine
Dehydrated
anhydrothreonine
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
reduced residue
PSI-MOD
RedRes
A protein modification that effectively either adds neutral hydrogen atoms (proton and electron), or removes oxygen atoms from a residue with or without the addition of hydrogen atoms.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
hydrogenated residue
PSI-MOD
HRes
A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
calcium containing modified residue
PSI-MOD
A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
CaRes
O-formylated residue
PSI-MOD
A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group.
PubMed:18688235
http://purl.org/obo/owl/PubMed#PubMed_18688235
Source:NULL
http://purl.org/obo/owl/Source#Source_NULL
Origin:NULL
http://purl.org/obo/owl/Origin#Origin_NULL
DiffFormula:NULL
http://purl.org/obo/owl/DiffFormula#DiffFormula_NULL
TermSpec:NULL
http://purl.org/obo/owl/TermSpec#TermSpec_NULL
DiffAvg:NULL
http://purl.org/obo/owl/DiffAvg#DiffAvg_NULL
Formula:NULL
http://purl.org/obo/owl/Formula#Formula_NULL
DiffMono:NULL
http://purl.org/obo/owl/DiffMono#DiffMono_NULL
MassMono:NULL
http://purl.org/obo/owl/MassMono#MassMono_NULL
MassAvg:NULL
http://purl.org/obo/owl/MassAvg#MassAvg_NULL
OFoRes
Drugable Genome Project
Subset of PSI-MI
subset of protein modifications