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Information on EC 2.7.11.13 - protein kinase C

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IUBMB 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.
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This record set is specific for:
UNIPROT: P05771
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
protein kinase c, pkcalpha, pkc-alpha, pkc alpha, pkcepsilon, pkc-delta, pkczeta, pkc-epsilon, pkc delta, pkc-zeta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PKC-betaII
isozyme
PKCbeta1
isozyme
PKCbeta2
isozyme
protein kinase C, beta type
-
Calcium-dependent protein kinase C
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-
-
-
epsilonPKC
-
-
-
-
PKC
-
-
-
-
protein kinase C
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-
-
-
protein kinase-C
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (diacylglycerol-dependent)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
141436-78-4
calcium-dependent protein kinase C
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + FKKQGSFAKKK
ADP + phosphorylated FKKQGSFAKKK
show the reaction diagram
highly specific substrate for isozyme PKCalpha relative to other isozymes, 60% phosphorylation rate with isozyme PKCalpha, less than 20% phosphorylation rate with other PKC isozymes
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-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0356 - 0.0599
FKKQGSFAKKK
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPCB_HUMAN
671
0
76869
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the 5' segment of the gene for protein kinase C beta is cloned from a human leukocyte genomic library in EMBL3 bacteriophage
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loftus, B.J.; Kim, U.J.; Sneddon, V.P.; Kalush, F.; Brandon, R.; Fuhrmann, J.; Mason, T.; Crosby, M.L.; Barnstead, M.; Cronin, L.; Deslattes Mays, A.; Cao, Y.; Xu, R.X.; Kang, H.L.; Mitchell, S.; Eichler, E.E.; Harris, P.C.; Venter, J.C.; Adams, M.D.
Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q
Genomics
60
295-308
1999
Homo sapiens (P05771)
Manually annotated by BRENDA team
Mahajna, J.; King, P.; Parker, P.; Haley, J.
Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells
DNA Cell Biol.
14
213-222
1995
Homo sapiens (P05771), Homo sapiens
Manually annotated by BRENDA team
Obeid, L.M.; Blobe, G.C.; Karolak, L.A.; Hannun, Y.A.
Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters
J. Biol. Chem.
267
20804-20810
1992
Homo sapiens (P05771), Homo sapiens
Manually annotated by BRENDA team
Kubo, K.; Ohno, S.; Suzuki, K.
Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta I/beta II
Nucleic Acids Res.
15
7179-7180
1987
Homo sapiens (P05771), Homo sapiens
Manually annotated by BRENDA team
Kubo, K.; Ohno, S.; Suzuki, K.
Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences
FEBS Lett.
223
138-142
1987
Homo sapiens (P05771), Homo sapiens
Manually annotated by BRENDA team
Coussens, L.; Rhee, L.; Parker, P.J.; Ullrich, A.
Alternative splicing increases the diversity of the human protein kinase C family
DNA
6
389-394
1987
Homo sapiens (P05771), Homo sapiens
Manually annotated by BRENDA team
Baskar, R.; Balajee, A.S.; Geard, C.R.; Hande, M.P.
Isoform-specific activation of protein kinase C in irradiated human fibroblasts and their bystander cells
Int. J. Biochem. Cell Biol.
40
125-134
2008
Homo sapiens, Homo sapiens (P05771), Homo sapiens (Q05513)
Manually annotated by BRENDA team
Kang, J.H.; Asai, D.; Yamada, S.; Toita, R.; Oishi, J.; Mori, T.; Niidome, T.; Katayama, Y.
A short peptide is a protein kinase C (PKC) alpha-specific substrate
Proteomics
8
2006-2011
2008
Homo sapiens (P05129), Homo sapiens (P05771), Homo sapiens (P17252), Homo sapiens (P24723), Homo sapiens (P41743), Homo sapiens (Q02156), Homo sapiens (Q04759), Homo sapiens (Q05513), Homo sapiens (Q05655), Homo sapiens
Manually annotated by BRENDA team