Deciphering a global network of functionally associated post-translational modifications
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...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2012 Jul 17
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| In: |
Molecular systems biology
Year: 2012, Volume: 8 |
| ISSN: | 1744-4292 |
| DOI: | 10.1038/msb.2012.31 |
| Online Access: | Verlag, Volltext: http://dx.doi.org/10.1038/msb.2012.31 Verlag, Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3421446/ 
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| Author Notes: | Pablo Minguez, Luca Parca, Francesca Diella, Daniel R Mende, Runjun Kumar, Manuela Helmer-Citterich, Anne-Claude Gavin, Vera van Noort and Peer Bork |
| Summary: | 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. |
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| Item Description: | Gesehen am 23.10.2018 |
| Physical Description: | Online Resource |
| ISSN: | 1744-4292 |
| DOI: | 10.1038/msb.2012.31 |