Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase
STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Comment:includes ATP binding and substrate binding sites
Comment:based on the structures of human CDK2 and DYRK1A bound with ATP or inhibitor and substrate peptides, and on the structures of other CMGC kinases, bound with ATP or ATP analogs
Jiyao W et al.(2023). "The conserved domain database in 2023.",