Catalytic activity:ATP + a protein = ADP + a phosphoprotein.,Domain:The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.,Domain:The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner.,enzyme regulation:Three specific sites; Thr-507 (activation loop of the kinase domain), Ser-645 (turn motif) and Ser-664 (hydrophobic region), need to be phosphorylated for its full activation.,Function:This is calcium-independent, 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 play a role in antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin.,PTM:Phosphorylated on Thr-507, within the activation loop. Autophosphorylated and/or phosphorylated. Although the Thr-507 phosphorylation occurs it is not a prerequisite for enzymatic 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, RAD9A, CDCP1 and MUC1.,
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