Protein kinase C, epsilon (IPR027274)

Short name: PKC_epsilon

Overlapping homologous superfamilies


Family relationships


Protein kinase C, epsilon is a novel type of protein kinase C (nPKC). PKC epsilon plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion [PMID: 15949469], motility, migration [PMID: 15355962] and cell cycle, functions in neuron growth [PMID: 18637121, PMID: 17971128, PMID: 21681677] and ion channel regulation [PMID: 17875639, PMID: 11884385], and is involved in immune response [PMID: 14643884], cancer cell invasion and regulation of apoptosis [PMID: 19228372, PMID: 17537614].

The N-terminal regulatory domain of nPKC consists of a C2 domain follows by a double C1 domain (C1A and C1B). The C2 domain does not respond to calcium which makes nPKC diacylglycerol-sensitive but calcium-independent [PMID: 19033211, PMID: 1411571, PMID: 12359062].

PKC is a family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol [PMID: 199594, PMID: 7358670]. Members of this family play key regulatory roles in various cellular processes. Currently, there are ten isoforms of PKC which can be classified into classical (alpha, beta I, beta II, gamma), novel (delta, epsilon, eta, theta) and atypical (zeta, iota/lambda) types based on their primary structure and biochemical characteristics [PMID: 9601053, PMID: 17661083, PMID: 9792904]. All PKCs contain a C-terminal kinase domain and an N-terminal regulatory domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004699 calcium-independent 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.