Conserved phosphorylation hotspots in eukaryotic protein domain families.

ABSTRACT: Protein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization. While the inventory for phosphorylation sites across different species has rapidly expanded, their functional role remains poorly investigated. Here, we combine 537,321 phosphosites from 40 eukaryotic species to identify highly conserved phosphorylation hotspot regions within domain families. Mapping these regions onto structural data reveals that they are often found at interfaces, near catalytic residues and tend to harbor functionally important phosphosites. Notably, functional studies of a phospho-deficient mutant in the C-terminal hotspot region within the riboso

SUBMITTER: Strumillo MJ 

PROVIDER: S-EPMC6488607 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature