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Description

Calcium/calmodulin-dependent protein kinase type II subunit beta (UniProt: P08413, also known as EC: 2.7.11.17, CaM kinase II subunit beta, CaMK-II subunit beta) is encoded by the Camk2b gene (Gene ID: 24245) in rat. CaM kinase II is one of the most widely studied multi-functional enzyme. It is found in high concentrations in the brain and in some regions it may constitute up to 2% of the total protein content. CaM kinase II is a complex of about 12 subunits, which exist in four differentially expressed forms (alpha, beta, gamma, and delta). CaMKII beta contains an auto-inhibitory domain (aa 283-293), a calmodulin-binding domain (aa 291-301) and a unique C-terminal association domain responsible for oligomerization. It is activated Ca2+/calmodulin and binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-287 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity that persists even after withdrawal of calcium. Phosphorylation of Thr-287 locks the kinase into an activated state. CaM Kinase II typically recognizes the phosphorylation site sequence Arg-X-X-Ser/Thr. It prefers arginine in the P3 position, which is reported to make an electrostatic contact with Glu96 in the catalytic core.