An atlas of substrate specificities for the human serine/threonine kinome
Cornell University · Weill Cornell Medicine · +22 more institutions
Abstract
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 responsible 3 . 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.…
Citation impact
- FWCI
- 95.75
- Percentile
- 100%
- References
- 97
Authors
40- JLJared L. JohnsonCorresponding
Cornell University, Weill Cornell Medicine
- TMTomer M. Yaron
Cornell University, Tri-Institutional PhD Program in Chemical Biology, Weill Cornell Medicine
- EMEmily M. Huntsman
Cornell University, Weill Cornell Medicine
- AKAlexander Kerelsky
Cornell University, Weill Cornell Medicine
- JSJunho Song
Cornell University, Weill Cornell Medicine
Topics & keywords
- Kinome
- Phosphorylation
- Serine
- Kinase
- Phosphoproteomics
- Threonine
- Biology
- Protein phosphorylation