Protein kinase C (PKC) is a family of
serine- and threonine-specific protein kinases that can be activated by the second messenger
diacylglycerol. PKC family members
phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for
phorbol esters, a class of
tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play distinct roles in cells. The protein encoded by this gene is one of the PKC family members. Studies both in human and mice demonstrate that this kinase is involved in
B cell signaling and in the regulation of
growth,
apoptosis, and
differentiation of a variety of cell types. Protein kinase C delta is also regulated by phosphorylation on various serine/threonine (e.g. T50, T141, S304, T451, T505, S506, T507, S643, S664) and tyrosine residues including Y311 (by
SRC). == Interactions ==