Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins

[img] PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
2MB

Item Type:Article
Title:PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins
Creators Name:Minguez, P. and Letunic, I. and Parca, L. and Garcia-Alonso, L. and Dopazo, J. and Huerta-Cepas, J. and Bork, P.
Abstract:The post-translational regulation of proteins is mainly driven by two molecular events, their modification by several types of moieties and their interaction with other proteins. These two processes are interdependent and together are responsible for the function of the protein in a particular cell state. Several databases focus on the prediction and compilation of protein-protein interactions (PPIs) and no less on the collection and analysis of protein post-translational modifications (PTMs), however, there are no resources that concentrate on describing the regulatory role of PTMs in PPIs. We developed several methods based on residue co-evolution and proximity to predict the functional associations of pairs of PTMs that we apply to modifications in the same protein and between two interacting proteins. In order to make data available for understudied organisms, PTMcode v2 (http://ptmcode.embl.de) includes a new strategy to propagate PTMs from validated modified sites through orthologous proteins. The second release of PTMcode covers 19 eukaryotic species from which we collected more than 300 000 experimentally verified PTMs (>1 300 000 propagated) of 69 types extracting the post-translational regulation of >100 000 proteins and >100 000 interactions. In total, we report 8 million associations of PTMs regulating single proteins and over 9.4 million interplays tuning PPIs.
Keywords:Internet, Post-Translational Protein Processing, Protein Databases, Protein Interaction Mapping
Source:Nucleic Acids Research
ISSN:0305-1048
Publisher:Oxford University Press
Volume:43
Number:Database issue
Page Range:D494-D502
Date:28 January 2015
Official Publication:https://doi.org/10.1093/nar/gku1081
PubMed:View item in PubMed

Repository Staff Only: item control page

Downloads

Downloads per month over past year

Open Access
MDC Library