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Information on EC 2.7.11.13 - protein kinase C and Organism(s) Bos taurus and UniProt Accession P04409

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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:
Bos taurus
UNIPROT: P04409
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected 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
protein kinase C, alpha type
-
Calcium-dependent protein kinase C
-
-
-
-
epsilonPKC
-
-
-
-
protein kinase C
-
-
-
-
protein kinase C, beta type
-
protein kinase-C
-
-
-
-
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 + calmodulin
ADP + phosphorylated calmodulin
show the reaction diagram
-
phosphorylation at Thr497 in the calmodulin-binding domain, binding is competitive to substrate endothelial nitric oxide synthase
-
-
?
ATP + endothelial nitric oxide synthase
ADP + phosphorylated endothelial nitric oxide synthase
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + endothelial nitric oxide synthase
ADP + phosphorylated endothelial nitric oxide synthase
show the reaction diagram
-
the enzyme is responsible for the negative regulation of endothelial nitric oxide synthase, a key enzyme in nitric oxide-mediated signal transduction, phosphorylation reduces the affinity of nitric oxide synthase for calmodulin
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
-
Mg2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dioleoylglycerol
-
-
phorbol 12-myristate 13-acetate
-
-
phosphatidylserine
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
aortic
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPCA_BOVIN
672
0
76837
Swiss-Prot
other Location (Reliability: 2)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishizuka, Y.
The molecular heterogeneity of protein kinase C and its implications for cellular regulation
Nature
334
661-665
1988
Bos taurus (P04409), Bos taurus (P05126), Rattus norvegicus (P05696), Oryctolagus cuniculus (P10102)
Manually annotated by BRENDA team
Parker, P.J.; Coussens, L.; Totty, N.; Rhee, L.; Young, S.; Chen, E.; Stabel, S.; Waterfield, M.D.; Ullrich, A.
The complete primary structure of protein kinase C - the major phorbol ester receptor
Science
233
853-859
1986
Bos taurus (P04409), Bos taurus
Manually annotated by BRENDA team
Coussens, L.; Parker, P.J.; Rhee, L.; Yang-Feng, T.L.; Chen, E.; Waterfield, M.D.; Francke, U.; Ullrich, A.
Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways
Science
233
859-866
1986
Bos taurus (P05126), Bos taurus, Homo sapiens (P05129), Homo sapiens
Manually annotated by BRENDA team
Matsubara, M.; Hayashi, N.; Jing, T.; Titani, K.
Regulation of endothelial nitric oxide synthase by protein kinase C
J. Biochem.
133
773-781
2003
Bos taurus
Manually annotated by BRENDA team