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The PKC family of serine/threonine kinases, including PRKCD (PKC delta), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II, and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent. Protein kinase C (PKC) can be activated by calcium and 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. Alternatively spliced transcript variants encoding the same protein have been observed.
1-May; AI385711; ALPS3; CVID9; D14Ertd420e; kinase nPKC-delta; KPCD; MAY1; nPKC-delta; PKC[d]; Pkcd; PKCdelta; Prkcd; protein kinase C delta; protein kinase C delta type; Protein kinase C delta type catalytic subunit; Protein kinase C delta type regulatory subunit; protein kinase C delta variant IX; protein kinase C delta VIII; protein kinase C, delta; protein kinase C, delta IV; protein kinase C, delta V; protein kinase C[d]; SDK1; Sphingosine-dependent protein kinase-1; Tyrosine-protein kinase PRKCD
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