Classical Protein Kinase C beta, catalytic domain (IPR034664)

Short name: cPKC_beta

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]. Conventional PKCs (cPKCs) have functional C1A and C1B domains, and a C2 domain. PKCs undergo three phosphorylations in order to take mature forms [PMID: 8749392, PMID: 19934406]. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine for activation. There are three conventional PKC isoenzymes (alpha, beta, and gamma).

The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function [PMID: 16799396, PMID: 17084284, PMID: 17160912, PMID: 17245085]. PKC-beta is also being explored as a therapeutic target in cancer [PMID: 16797377, PMID: 17671157]. It contributes to tumour formation and is involved in the tumour host mechanisms of inflammation and angiogenesis [PMID: 17548205].

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.