Novel protein kinase C epsilon, catalytic domain (IPR034669)

Short name: nPKC_epsilon

Overlapping homologous superfamilies

Domain relationships



Protein kinases C (PKCs) constitute a family of Ser/Thr kinases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain [PMID: 12495431, PMID: 24766842]. Novel PKCs (nPKCs) comprise delta, epsilon, eta, and theta isoforms, which have tandem C1 domains and a C2 domain that does not bind calcium [PMID: 15851033]. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity.

PKC-epsilon has been shown to behave as an oncoprotein [PMID: 19228372, PMID: 17537614]. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumour invasion and metastasis [PMID: 21406403, PMID: 26023164]. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage [PMID: 14654063, PMID: 17576073]. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility [PMID: 18637120].

This entry also includes PKCs from invertebrates, such as Pkc98E from Drosophila, which exhibits sequence identity to PKC-epsilon [PMID: 12359065].

GO terms

Biological Process

GO:0006468 protein phosphorylation

Molecular Function

GO:0004697 protein kinase C activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.