Abstract：
:Protein function is often regulated by posttranslational modifications (PTMs), and recent advances in mass spectrometry have resulted in an exponential increase in PTM identification. However, the functional significance of the vast majority of these modifications remains unknown. To address this problem, we compiled nearly 200,000 phosphorylation, acetylation, and ubiquitination sites from 11 eukaryotic species, including 2,500 newly identified ubiquitylation sites for Saccharomyces cerevisiae. We developed methods to prioritize the functional relevance of these PTMs by predicting those that likely participate in cross-regulatory events, regulate domain activity, or mediate protein-protein interactions. PTM conservation within domain families identifies regulatory "hot spots" that overlap with functionally important regions, a concept that we experimentally validated on the HSP70 domain family. Finally, our analysis of the evolution of PTM regulation highlights potential routes for neutral drift in regulatory interactions and suggests that only a fraction of modification sites are likely to have a significant biological role.
journal_name
Celljournal_title
Cellauthors
Beltrao P,Albanèse V,Kenner LR,Swaney DL,Burlingame A,Villén J,Lim WA,Fraser JS,Frydman J,Krogan NJdoi
10.1016/j.cell.2012.05.036subject
Has Abstractpub_date
2012-07-20 00:00:00pages
413-25issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(12)00706-4journal_volume
150pub_type
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