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Proper Citation: PTMcode (RRID:SCR_002046)
Description: Database of known and predicted functional associations between protein posttranslational modifications (PTMs) within proteins. In its first release it contains 13 different PTM types. PTM types are abbreviated in a two letter code as: Ph (phosphorylation), NG (N-linked glycosylation), Ac (acetylation), OG (O-linked glycosylation), Ub (ubiquitination), Me (methylation), SM (SUMOylation), Hy (hydroxylation), Ca (carboxylation), Pa (palmitoylation), Su (sulfation), Ni (nitrosylation) and CG (C-linked glycosylation). These PTMs are present in 25,765 proteins of 8 different eukaryotes. The database is focused on the exploration of the global post-translational regulation of proteins, not only by describing the set of its modifications, but by identifying the functional associations among the PTMs present in the protein. To do that, they combine five different evidence channels based on a literature survey, the modified residue co-evolution, their structural proximity, their competition for the same residue and the location within PTM highly-enriched protein regions (hotspots) and show the functional associations within the context of the protein architecture.
Abbreviations: PTMCode
Resource Type: database, data or information resource
Defining Citation: PMID:23193284
Keywords: protein posttranslational modification, protein, function, phosphorylation, n-linked glycosylation, acetylation, o-linked glycosylation, ubiquitination, methylation, sumoylation, hydroxylation, carboxylation, palmitoylation, sulfation, nitrosylation, c-linked glycosylation
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