The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Deciphering a global network of functionally associated post‐translational modifications
Open accessAbstract
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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Cites
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Systematic Discovery of New Recognition Peptides Mediating Protein Interaction Networks
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Metadata
- Authors
- Minguez, P., Parca, L., Diella, F., Mende, D. R., Kumar, R., Helmer‐Citterich, M., Gavin, A., van Noort, V., & Bork, P.
- Venue
- Molecular Systems Biology
- Published
- 2012-01
- Volume
- 8
- Issue
- 1
- Pages
- 599-599
- ISSN
- 1744-4292 (ISSN-L)
- OpenAlex
- W2118439154
- Cited by
- 233
- References
- 9
- FWCI
- 10.91
- Type
- journal article
- Language
- en
- Open access
- gold
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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