Purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using a non-phosphopeptide corresponding to the phosphorylation site.
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.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.
The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor. The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner.
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.