The Enzyme Database

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EC 2.7.11.13     
Accepted name: protein kinase C
Reaction: ATP + a protein = ADP + a phosphoprotein
Other name(s): calcium-dependent protein kinase C; calcium-independent protein kinase C; calcium/phospholipid dependent protein kinase; cPKCα; cPKCβ; cPKCγ; nPKCδ; nPKCε; nPKC; nPKC; PKC; PKCα; PKCβ; PKCγ; PKCδ; PKCε; PKCζ; Pkc1p; protein kinase Cε; STK24
Systematic name: ATP:protein phosphotransferase (diacylglycerol-dependent)
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Jaken, S. Protein kinase C and tumor promoters. Curr. Opin. Cell 2 (1990) 192–197. [PMID: 2194521]
2.  Parekh, D.B., Ziegler, W. and Parker, P.J. Multiple pathways control protein kinase C phosphorylation. EMBO J. 19 (2000) 496–503. [PMID: 10675318]
3.  Valledor, A.F., Xaus, J., Comalada, M., Soler, C. and Celada, A. Protein kinase Cepsilon is required for the induction of mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J. Immunol. 164 (2000) 29–37. [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 (1998) 689–694. [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 (1998) 259–267. [PMID: 9530509]
[EC 2.7.11.13 created 2005 (EC 2.7.1.37 part-incorporated 2005)]
 
 


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