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Deciphering a global network of functionally associated post-translational modifications

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Item Type:Article
Title:Deciphering a global network of functionally associated post-translational modifications
Creators Name:Minguez, P. and Parca, L. and Diella, F. and Mende, D.R. and Kumar, R. and Helmer-Citterich, M. and Gavin, A.C. and van Noort, V. and Bork, P.
Abstract:Various post-translational modifications (PTMs) fine-tune the functions of almost all eukaryotic proteins, and co-regulation of different types of PTMs has been shown within and between a number of proteins. Aiming at a more global view of the interplay between PTM types, we collected modifications for 13 frequent PTM types in 8 eukaryotes, compared their speed of evolution and developed a method for measuring PTM co-evolution within proteins based on the co-occurrence of sites across eukaryotes. As many sites are still to be discovered, this is a considerable underestimate, yet, assuming that most co-evolving PTMs are functionally associated, we found that PTM types are vastly interconnected, forming a global network that comprise in human alone >50,000 residues in about 6000 proteins. We predict substantial PTM type interplay in secreted and membrane-associated proteins and in the context of particular protein domains and short-linear motifs. The global network of co-evolving PTM types implies a complex and intertwined post-translational regulation landscape that is likely to regulate multiple functional states of many if not all eukaryotic proteins.
Keywords:Post-Translational Modifications, Protein Regulation, Proteomics, PTM Code, PTM Crosstalk
Source:Molecular Systems Biology
Publisher:Nature Publishing Group
Page Range:599
Date:17 July 2012
Official Publication:https://doi.org/10.1038/msb.2012.31
PubMed:View item in PubMed

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