EC 2 - Transferases
EC 2.7 - Transferring phosphorus-containing groups
EC 2.7.11 - Protein-serine/threonine kinases
EC 2.7.11.13 - Protein kinase C
IntEnz view
ENZYME view
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
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)
Reaction
- ATP + a protein = ADP + a phosphoprotein
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
Protein domains and families:
PROSITE:PDOC00100
Gene Ontology:
GO:0004698
,
GO:0004697
References
-
Protein kinase C and tumor promoters.Curr. Opin. Cell Biol. 2 : 192-197 (1990). [PMID: 2194521]
-
Multiple pathways control protein kinase C phosphorylation.EMBO J. 19 : 496-503 (2000). [PMID: 10675318]
-
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]
-
Characterization and properties of protein kinase C from the filamentous fungus Trichoderma reesei.Biochem. J. 330 : 689-694 (1998). [PMID: 9480876]
-
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)]