EC 2.7.11.13 - Protein kinase C

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IntEnz Enzyme Nomenclature
EC 2.7.11.13

Names

Accepted name:
protein kinase C
Other names:
calcium-dependent protein kinase C
calcium-independent protein kinase C
calcium/phospholipid dependent protein kinase
cPKCα
cPKCβ
cPKCγ
nPKCδ
nPKCε
nPKCη
nPKCθ
PKC
PKCα
PKCβ
PKCγ
PKCδ
PKCε
PKCζ
Pkc1p
protein kinase Cε
STK24
nPKC
cPKC
Systematic name:
ATP:protein phosphotransferase (diacylglycerol-dependent)

Reactions

Comments:

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. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signalling pathways. Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumour promoters. Formerly EC 2.7.1.37.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00100
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004697
UniProtKB/Swiss-Prot: (86) [show] [UniProt]

References

  1. Jaken, S.
    Protein kinase C and tumor promoters.
    Curr. Opin. Cell Biol. 2: 192-197 (1990). [PMID: 2194521]
  2. Parekh, D.B., Ziegler, W. and Parker, P. J.
    Multiple pathways control protein kinase C phosphorylation.
    EMBO J. 19: 496-503 (2000). [PMID: 10675318]
  3. Valledor, A.F., Xaus, J., Comalada, M., Soler, C. and Celada, A.
    Protein kinase Cε is required for the induction of mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages.
    J. Immunol. 164: 29-37 (2000). [PMID: 10604989]
  4. Lendenfeld, T. and Kubicek, C.P.
    Characterization and properties of protein kinase C from the filamentous fungus Trichoderma reesei.
    Biochem. J. 330: 689-694 (1998). [PMID: 9480876]
  5. Brooks, S.P. and Storey, K.B.
    Protein kinase C from rainbow trout brain: identification and characterization of three isozymes.
    Biochem. Mol. Biol. Int. 44: 259-267 (1998). [PMID: 9530509]

[EC 2.7.11.13 created 2005 (EC 2.7.1.37 part-incorporated 2005)]