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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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UNIPROT: P17252
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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
PKCalpha
protein kinase C alpha
-
protein kinase C, alpha type
-
protein kinase C-alpha
-
protein kinase Calpha
-
Calcium-dependent protein kinase C
-
-
-
-
epsilonPKC
-
-
-
-
PKC
-
-
-
-
protein kinase C
-
-
-
-
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 + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
?
ATP + ADAM17
ADP + phosphorylated ADAM17
show the reaction diagram
-
-
-
?
ATP + beta-catenin
ADP + phosphorylated beta-catenin
show the reaction diagram
-
-
-
?
ATP + casein kinase 1delta
ADP + phosphorylated casein kinase 1delta
show the reaction diagram
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
-
-
?
ATP + [casein kinase 1 delta]
ADP + phosphorylated casein kinase 1 delta
show the reaction diagram
casein kinase 1 delta is modulated by protein kinase C alpha by site-specific phosphorylation within the kinase domain of CK1delta
-
-
?
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 + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
?
ATP + beta-catenin
ADP + phosphorylated beta-catenin
show the reaction diagram
-
-
-
?
ATP + [casein kinase 1 delta]
ADP + phosphorylated casein kinase 1 delta
show the reaction diagram
casein kinase 1 delta is modulated by protein kinase C alpha by site-specific phosphorylation within the kinase domain of CK1delta
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
10 mM used in assay conditions
Zn2+
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bisindolylmaleimide I
highly selective PKCalpha inhibitor
GF109203X
inhibits all PKC isozymes, except PKCmu
Ro-31-7549
specific inhibitor for isozyme PKCalpha
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phorbol-ester-12-13-dibutyrate
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00009141 - 0.0000963
ATP
0.01561
casein kinase 1delta
at pH 7.5 and 30°C
-
0.0174
FKKQGSFAKKK
isozyme PKCalpha, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C
additional information
additional information
kinetic parameters of wild type and mutant full-length and truncated GST-CK1delta fusion proteins
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.136
casein kinase 1delta
at pH 7.5 and 30°C
-
additional information
additional information
kinetic parameters of wild type and mutant full-length and truncated GST-CK1delta fusion proteins
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
shows higher levels of PKCalpha than normal breast tissue
Manually annotated by BRENDA team
PR-17 cells and wild-type HL-60 cells
Manually annotated by BRENDA team
shows higher levels of PKCalpha than normal liver tissue
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
site-specific phosphorylation of casein kinase 1delta by the enzyme contributes to fine-tuning of casein kinase 1delta activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPCA_HUMAN
672
0
76750
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 80000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
casein kinase 1 delta is modulated by protein kinase C alpha (PKCalpha) by site-specific phosphorylation within the kinase domain of CK1delta
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FLAG M2 affinity resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells and human-derived rhabdhomyosarcoma cells
expressed in Sf9 insect cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McSwine-Kennick, R.L.; McKeegan, E.M.; Johnson, M.D.; Morin, M.J.
Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones
J. Biol. Chem.
266
15135-15143
1991
Homo sapiens (P17252)
Manually annotated by BRENDA team
Finkenzeller, G.; Marme, D.; Hug, H.
Sequence of human protein kinase C alpha
Nucleic Acids Res.
18
2183
1990
Homo sapiens (P17252), Homo sapiens
Manually annotated by BRENDA team
Alfa Cisse, M.; Louis, K.; Braun, U.; Mari, B.; Leitges, M.; Slack, B.E.; Fisher, A.; Auberger, P.; Checler, F.; Vincent, B.
Isoform-specific contribution of protein kinase C to prion processing
Mol. Cell. Neurosci.
39
400-410
2008
Homo sapiens (P17252), Homo sapiens (Q02156), Homo sapiens (Q05513), Homo sapiens (Q05655)
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
Ninsontia, C.; Phiboonchaiyanan, P.P.; Kiratipaiboon, C.; Chanvorachote, P.
Zinc suppresses stem cell properties of lung cancer cells through protein kinase C-mediated beta-catenin degradation
Am. J. Physiol. Cell Physiol.
312
C487-C499
2017
Homo sapiens (P17252)
Manually annotated by BRENDA team
Meng, Z.; B hm, T.; Xu, P.; Henne-Bruns, D.; Peifer, C.; Witt, L.; Knippschild, U.; Bischof, J.
Kinase activity of casein kinase 1 delta (CK1delta)is modulated by protein kinase C alpha (PKCalpha) by site-specific phosphorylation within the kinase domain of CK1delta
Biochim. Biophys. Acta
1867
710-721
2019
Homo sapiens (P17252)
Manually annotated by BRENDA team
Meng, Z.; Bhm, T.; Xu, P.; Henne-Bruns, D.; Peifer, C.; Witt, L.; Knippschild, U.; Bischof, J.
Kinase activity of casein kinase 1 delta (CK1delta) is modulated by protein kinase Calpha (PKCalpha) by site-specific phosphorylation within the kinase domain of CK1delta
Biochim. Biophys. Acta Proteins Proteom.
1867
710-721
2019
Homo sapiens (P17252)
Manually annotated by BRENDA team
Lee, S.; Devamani, T.; Song, H.D.; Sandhu, M.; Larsen, A.; Sommese, R.; Jain, A.; Vaidehi, N.; Sivaramakrishnan, S.
Distinct structural mechanisms determine substrate affinity and kinase activity of protein kinase Calpha
J. Biol. Chem.
292
16300-16309
2017
Homo sapiens (P17252)
Manually annotated by BRENDA team