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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