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Nucleic Acids Res. 2013 Jan;41(Database issue):D306-11. doi: 10.1093/nar/gks1230. Epub 2012 Nov 28.

PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins.

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1
European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

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.

PMID:
23193284
PMCID:
PMC3531129
DOI:
10.1093/nar/gks1230
[Indexed for MEDLINE]
Free PMC Article
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