Ontology highlight
ABSTRACT:
SUBMITTER: Aubol BE
PROVIDER: S-EPMC5056641 | biostudies-literature | 2014 Aug
REPOSITORIES: biostudies-literature
Aubol Brandon E BE Plocinik Ryan M RM Keshwani Malik M MM McGlone Maria L ML Hagopian Jonathan C JC Ghosh Gourisankar G Fu Xiang-Dong XD Adams Joseph A JA
The Biochemical journal 20140801 1
SR proteins are essential splicing factors that are regulated through multisite phosphorylation of their RS (arginine/serine-rich) domains by two major families of protein kinases. The SRPKs (SR-specific protein kinases) efficiently phosphorylate the arginine/serine dipeptides in the RS domain using a conserved docking groove in the kinase domain. In contrast, CLKs (Cdc2-like kinases) lack a docking groove and phosphorylate both arginine/serine and serine-proline dipeptides, modifications that g ...[more]