title: PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins.
abstract: Post-translational modifications (PTMs) are involved in the regulation and structural stabilization of eukaryotic proteins. The combination of individual PTM states is a key to modulate cellular functions as became evident in a few well-studied proteins. This combinatorial setting, dubbed the PTM code, has been proposed to be extended to whole proteomes in eukaryotes. Although we are still far from deciphering such a complex language, thousands of protein PTM sites are being mapped by high-throughput technologies, thus providing sufficient data for comparative analysis. PTMcode (http://ptmcode.embl.de) aims to compile known and predicted PTM associations to provide a framework that would enable hypothesis-driven experimental or computational analysis of various scales. In its first release, PTMcode provides PTM functional associations of 13 different PTM types within proteins in 8 eukaryotes. They are based on five evidence channels: a literature survey, residue co-evolution, structural proximity, PTMs at the same residue and location within PTM highly enriched protein regions (hotspots). PTMcode is presented as a protein-based searchable database with an interactive web interface providing the context of the co-regulation of nearly 75 000 residues in >10 000 proteins.
authors.affiliation: European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
authors.forename: Pablo
authors.initials: P
authors.lastname: Minguez
authors.forename: Ivica
authors.initials: I
authors.lastname: Letunic
authors.forename: Luca
authors.initials: L
authors.lastname: Parca
authors.forename: Peer
authors.initials: P
authors.lastname: Bork
mesh_terms: D000818:Animals; D002417:Cattle; D030562:Databases, Protein; D019143:Evolution, Molecular; D006801:Humans; D020407:Internet; D051379:Mice; D046188:Protein Modification, Translational; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D051381:Rats; D014584:User-Computer Interface
chemical_list: D011506:Proteins