Catalytic activity:ATP + a protein = ADP + a phosphoprotein. ,cofactor:Binds 3 calcium ions per subunit. The ions are bound to the C2 domain. ,Function:This is a calcium-activated , phospholipid-dependent , serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters , a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking. ,PTM:Phosphorylation on Thr-500 of isoform beta-I , within the activation loop , renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence , and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly , isoform beta-II is autophosphorylated on 'Thr-640' and 'Ser-659' , subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on PKC activity. ,similarity:Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. ,similarity:Contains 1 AGC-kinase C-terminal domain. ,similarity:Contains 1 C2 domain. ,similarity:Contains 1 protein kinase domain. ,similarity:Contains 2 phorbol-ester/DAG-type zinc fingers. ,subunit:Interacts with PDK1 (By similarity) . Interacts in vitro with PRKCBP1. ,
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