An atlas of substrate specificities for the human serine/threonine kinome.

ABSTRACT: Protein phosphorylation is one of the most widespread post-translational modifications in biology^1,2. With advances in mass-spectrometry-based phosphoproteomics, 90,000 sites of serine and threonine phosphorylation have so far been identified, and several thousand have been associated with human diseases and biological processes^3,4. For the vast majority of phosphorylation events, it is not yet known which of the more than 300 protein serine/threonine (Ser/Thr) kinases encoded in the human genome are responsible³. Here we used synthetic peptide libraries to profile the substrate sequence specificity of 303 Ser/Thr kinases, comprising more than 84% of those predicted to be active in humans. Viewed in its entirety, the substrate specificity of the kinome was

SUBMITTER: Johnson JL 

PROVIDER: S-EPMC9876800 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature