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Information on EC 2.7.11.13 - protein kinase C and Organism(s) Mus musculus and UniProt Accession P68404

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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:
Mus musculus
UNIPROT: P68404
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
PKCbeta1
isozyme
PKCbeta2
isozyme
alpha-PKC
-
AS PKCdelta
-
-
ATP analog specific protein kinase Cdelta
-
-
Calcium-dependent protein kinase C
-
-
-
-
epsilonPKC
-
-
-
-
PKC deltaII
-
PKC lambda
-
PKC-beta1
-
-
PKC-epsilon
-
PKCalpha
PKCdelta
isozyme
PKCepsilon
PKCgamma
PKCthetaC1B
-
C1B subdomain
protein kinase C
protein kinase C delta
-
protein kinase C, alpha type
-
protein kinase C, delta type
-
protein kinase C, epsilon type
-
protein kinase C, eta type
-
protein kinase C, gamma type
-
protein kinase C, iota type
-
protein kinase C, zeta type
-
protein kinase Cdelta
-
protein kinase-C
-
-
-
-
additional information
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 + a protein
ADP + phosphorylated protein
show the reaction diagram
-
-
-
-
?
ATP + Akt
ADP + phosphorylated Akt
show the reaction diagram
ATP + Bcl-xL
ADP + phosphorylated Bcl-xL
show the reaction diagram
-
recombinant human substrate, recombinant isozymes PKCepsilon and PKCzeta
-
-
?
ATP + Btk
ADP + phosphorylated Btk
show the reaction diagram
ATP + GluR6 kainate receptor subunit
ADP + phosphorylated GluR6 kainate receptor subunit
show the reaction diagram
-
two specific residues on the GluR6 C terminus, Ser846 and Ser868, are phosphorylated by protein kinase C, PKC phosphorylation of GluR6 retains GluR6 in the endoplasmic reticulum
-
-
?
ATP + insulin receptor
ADP + phosphorylated insulin receptor
show the reaction diagram
-
isozyme PKCalpha
-
-
?
ATP + IRS
ADP + phosphorylated IRS
show the reaction diagram
-
isozymes PKCalpha and PKCdelta, phosphorylation on Ser307
-
-
?
ATP + myristoylated alanine-rich C kinase substrate
ADP + phosphorylated myristoylated alanine-rich C kinase substrate
show the reaction diagram
ATP + Par-3
ADP + phosphorylated Par-3
show the reaction diagram
-
-
-
?
ATP + phosphoinositide-dependent kinase
ADP + phosphorylated phosphoinositide-dependent kinase
show the reaction diagram
ATP + poly(ADP-ribose) polymerase-1
ADP + phosphorylated poly(ADP-ribose) polymerase-1
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
autophosphorylation
-
-
?
ATP + transient receptor potential vanilloid 5
ADP + phosphorylated transient receptor potential vanilloid 5
show the reaction diagram
-
-
-
-
?
ATP + vasodilator-stimulated phosphoprotein
ADP + phosphorylated vasodilator-stimulated phosphoprotein
show the reaction diagram
-
phosphorylation at Ser157
-
-
?
Nepsilon-(benzyl)-ATP + histone 3
ADP + phosphorylated histone 3
show the reaction diagram
-
-
-
-
?
Nepsilon-(benzyl)-ATP + RFARKGSLRQKNV
Nepsilon-(benzyl)-ADP + RFARKGpSLRQKNV
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 + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + a protein
ADP + phosphorylated protein
show the reaction diagram
-
-
-
-
?
ATP + Akt
ADP + phosphorylated Akt
show the reaction diagram
-
phosphorylation by PKC isozymes at Ser473, regulation of the phosphorylation activity by PKCbetaII in mast cells stimulated by stem cell factor or interaleukin-3, and in serum-stimulated fibroblasts, and in antigen-receptor stimulated T- or B-lymphocytes, overview
-
-
?
ATP + Btk
ADP + phosphorylated Btk
show the reaction diagram
-
specific phosphorylation leads to inhibition of Btk membrane translocation and activation and the downstream events that promote PKCbeta activation, mechanism, overview
-
-
?
ATP + myristoylated alanine-rich C kinase substrate
ADP + phosphorylated myristoylated alanine-rich C kinase substrate
show the reaction diagram
-
the substrate is involved in actincytoskeletal rearrangement in response to extra-cellular stimuli, phosphorylation of MARCKS is dramatically upregulated specifically in microglial cells after kainic acid-induced seizures, but not in other types of glial cells, overview
-
-
?
ATP + phosphoinositide-dependent kinase
ADP + phosphorylated phosphoinositide-dependent kinase
show the reaction diagram
-
phosphoinositide-dependent kinases are conserved substrates of PKC
-
-
?
ATP + vasodilator-stimulated phosphoprotein
ADP + phosphorylated vasodilator-stimulated phosphoprotein
show the reaction diagram
-
phosphorylation at Ser157
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
Ca2+-mediated interactions between the two domains could contribute to enzyme activation as well as to the creation of a positively charged phosphatidylserine-binding site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(5-isoquinolinesulfonyl)-2-methylpiperazine
-
1-(tert-butyl)-3-(1-naphthyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
inhibits ATP analog-specific PKCdelta isoform
1-(tert-butyl)-3-(2-methylbenzyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
inhibits ATP analog-specific PKCdelta isoform
angiotensin II type 2-receptor
-
inhibits isozyme PKCalpha
-
bisindolylmaleimide derivatives
-
-
bisindolylmaleimide I
-
-
CG53353
-
inhibitor of isozyme PKCbetaII
GF109203X
Go6976
Go6983
-
-
Gö6976
-
inhibits classical isozymes
quinolinic acid
-
inhibits the phosphorylation of the enzyme
rottlerin
staurosporine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dioctanoyl-sn-glycerol
-
-
1-oleoyl-acetyl-sn-glycerol
-
0.01 mM
1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
12-O-Tetradecanoylphorbol 13-acetate
-
activates isozyme PKCepsilon
13-O-acetylphorbol 12-myristate
-
-
Berberine
-
-
diacylglycerol
Diacylglycerols
-
activate PKC isozymes
fatty acids
-
activation mechanism
IGF-1
-
-
-
Insulin
-
activates PKC isozymes alpha, betaII, delta, and zeta in several cell types, activation mechanism
-
Kainic acid
-
phosphorylation of MARCKS by PKC isozymes is dramatically upregulated specifically in microglial cells after kainic acid-induced seizures, but not in other types of glial cells, overview, upregulation of isozymes PKCalpha, PKCbetaI, PKCbetaII, and PKCdelta
phorbol 12,13-dibutyrate
-
-
phorbol 12-myristate 13-acetate
phorbol dibutyrate
activates
phosphatidylserine
-
activation mechanism
Phospholipid
strict dependence on the presence of phospholipids
Phospholipids
-
regulatory function for isozymes alpha, betaI, betaII, gamma, delta, epsilon, eta, and theta
thymeleatoxin
-
activates Ca2+-dependent PKC isozymes, reversal by chronic thymeleatoxin pretreatment of the effects of carbachol on glucose-induced Ca2+ oscillations and pulsatile 5-HT release, overview
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000154
1-(tert-butyl)-3-(1-naphthyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
Mus musculus
-
ATP analog-specific PKCdelta isoform, at pH 7.4 and 27°C
0.0026
1-(tert-butyl)-3-(2-methylbenzyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
Mus musculus
-
ATP analog-specific PKCdelta isoform, at pH 7.4 and 27°C
0.000221
bisindolylmaleimide I
Mus musculus
-
ATP analog-specific PKCdelta isoform, at pH 7.4 and 27°C
0.00167
staurosporine
Mus musculus
-
ATP analog-specific PKCdelta isoform, at pH 7.4 and 27°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the PKCbeta1 isozymes is expressed prominently in the retinal growth cones, whilst the beta2 isozyme is barely detected, the beta1 isozyme is restricted largely in the core region of the growth cones
Manually annotated by BRENDA team
-
PKC isozyme expression patterns
Manually annotated by BRENDA team
-
recombinant isozymes
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
from fetal liver
Manually annotated by BRENDA team
ABPL-3 myeloid tumor
Manually annotated by BRENDA team
-
derived from bone marrow
Manually annotated by BRENDA team
-
isozyme PKCbetaII
Manually annotated by BRENDA team
-
a hybridomal cell line of a rat neuroblastoma and a mouse glioma, expression of isozymes PKCalpha, PKCepsilon, PKCjota, and PKCzeta, no expression of isozymes PKCbeta, PKCdelta, PKCgamma, PKCmy, and PKCtheta
Manually annotated by BRENDA team
-
virus-induced macrophage cell line
Manually annotated by BRENDA team
additional information
-
PKC isozymes are expressed in a wide range of tissues, some isozymes are tissue-specific
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozyme PKCepsilon in a perinuclear site is associated with the Golgi apparatus, phosphorylation of isozyme PKCepsilon at Ser279 is required for translocation to the nucleus during which the enzyme looses the phsophate group at Ser279, overview
Manually annotated by BRENDA team
-
isozymes PKC-beta and PKC-gamma are recruited to microtubules by LFA-1 signalling, i.e. lymphocyte-function-associated antigen-1 signalling
Manually annotated by BRENDA team
-
PKC is recruited by other kinases
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
PKC-beta1 and PKC-gamma are important for the development of retinal, as their absence completely inhibits rod differentiation
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPCB_MOUSE
671
0
76751
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
SDS-PAGE, full-length PKCtheta
7000
-
SDS-PAGE, PKCthetaC1B subdomain
78000
-
x * 78000, SDS-PAGE
82000
-
x * 82000, isozyme PKCalpha, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphoprotein
additional information
two types of complementary DNA clones for rat brain protein kinase C, these clones encode 671 and 673 amino acid sequences, which differ from each other only in the carboxyl-terminal regions of approximately 50 amino acid residues. This difference seems to result from alternative splicing
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of PKCioata is determined at 2.4 A. The structure of the PKCiota/Par-3 peptide complex reveals that the kinase domain adopts an active conformation even though Thr402 in the activation loop is not phosphorylated. The Par-3 peptide binds to the groove between the N- and C-lobes of the kinase via combined hydrophobic and charge-charge interactions
crystal structure of PKCthetaC1B is determined to 1.63 A resolution. It is shown that, Trp253 at the rim of the activator-binding pocket is orientated towards the membrane
-
crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T500E
expression as a catalytically active protein kinase C in COS cells
T500V
expression as a catalytically inactive protein kinase C in COS cells
K368A
-
a dominant-negative mutant of PKCalpha
L255G
-
mutated activator-binding site: mutation reduces affinity for both phorbol ester and diacylglycerol. Mutation causes significantly reduced membrane translocation by phorbol ester treatment
Q258G
-
mutated activator-binding site: mutation reduces affinity for both phorbol ester and diacylglycerol. Mutation causes significantly reduced membrane translocation by phorbol ester treatment
S279A
-
site-directed mutagenesis of the isozyme PKCepsilon phosphorylation site results in altered subcellular localization not in the perinulcear/Golgi site
S279E
-
site-directed mutagenesis of the isozyme PKCepsilon phosphorylation site results in altered subcellular localization not in the perinulcear/Golgi site
S279T
-
site-directed mutagenesis of the isozyme PKCepsilon phosphorylation site results in altered subcellular localization not in the perinulcear/Golgi site
T243A
-
mutated activator-binding site: mutation reduces affinity for both phorbol ester and diacylglycerol. Mutation causes significantly reduced membrane translocation by phorbol ester treatment
W253G
-
mutated activator-binding site: mutation reduces affinity for both phorbol ester and diacylglycerol. Mutation causes significantly reduced membrane translocation by phorbol ester treatment
Y239A
-
mutated activator-binding site: mutation reduces affinity for both phorbol ester and diacylglycerol. Mutation causes significantly reduced membrane translocation by phorbol ester treatment
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using affinity purification through glutathione-Sepharose 4B columns, subsequent cleavage of the GST tag, ammonium sulfate precipitation and gel filtration chromatography
-
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS cells
expression of mutant enzymes in COS cells
isolation of cDNA clones encoding protein kinase C
isolation of cloned mouse protein kinase C beta-II cDNA
wild-type and mutant enzymes overexpressed in COS cells
cDNA sequence encoding mouse PKC-gamma isolated from a C57BL/6 brain cDNA library
co-expression of PKC isozymes and insulin in HEK-293 or CHO cells, interaction analysis, overview
-
COS cells transfected with the PKC lambda expression plasmid
expressed in COS-7 and Neuro2A cells
-
expressed in Escherichia coli as a GST-fusion protein
-
expressed in insect cells via a baculovirus expression vector, a 75000 Da protein is synthesized which, unlike other PKC isoforms, does not bind phorbol ester, even at very high concentrations
expressed in Sf9 cells as a His-tagged fusion protein using the baculovirus system
expression in COS cells
expression of GFP-tagged PKC
-
expression of isozymes PKCepsilon and PKCzeta in Saccharomyces cerevisiae, subcloning in Escherichia coli
-
expression of wild-type and mutant isozyme PKCepsilon in NIH3T3 fibroblasts as GFP-tagged proteins
-
overexpression PKCdelta in NMuMG cells, a normal immortalized mammary cell line derived from NAMRU mice
-
PKCdeltaII expressed in COS-1 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saijo, K.; Mecklenbrauker, I.; Santana, A.; et al.
Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha
J. Exp. Med.
195
1647-1652
2002
Mus musculus (P68404)
Manually annotated by BRENDA team
Mecklenbrauker, I.; Saijo, K.; Zheng, N.Y.; Leitges, M.; Tarakhovsky, A.
Protein kinase C delta controls self-antigen-induced B-cell tolerance
Nature
416
860-865
2002
Mus musculus (P28867)
Manually annotated by BRENDA team
Sakurai, Y.; Onishi, Y.; Tanimoto, Y.; Kizaki, H.
Novel protein kinase C delta isoform insensitive to caspase-3
Biol. Pharm. Bull.
24
973-977
2001
Mus musculus (P28867), Mus musculus
Manually annotated by BRENDA team
Sutton, R.B.; Sprang, S.R.
Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+
Structure
6
1395-1405
1998
Mus musculus (P68404)
Manually annotated by BRENDA team
Keranen, L.M.; Dutil, E.M.; Newton, A.C.
Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
Curr. Biol.
5
1394-1403
1995
Mus musculus (P68404)
Manually annotated by BRENDA team
Zhang, J.; Wang, L.; Schwartz, J.; Bond, R.W.; Bishop, W.R.
Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C beta 1 and is essential for its activation
J. Biol. Chem.
269
19578-19584
1994
Mus musculus (P68404)
Manually annotated by BRENDA team
Orr, J.W.; Newton, A.C.
Requirement for negative charge on "activation loop" of protein kinase C
J. Biol. Chem.
269
27715-27718
1994
Mus musculus (P68404)
Manually annotated by BRENDA team
Zhang, J.; Wang, L.; Petrin, J.; Bishop, W.R.; Bond, R.W.
Characterization of site-specific mutants altered at protein kinase C beta 1 isozyme autophosphorylation sites
Proc. Natl. Acad. Sci. USA
90
6130-6134
1993
Mus musculus (P68404)
Manually annotated by BRENDA team
Tang, Y.M.; Ashendel, C.L.
Isolation of cloned mouse protein kinase C beta-II cDNA and its sequence
Nucleic Acids Res.
18
5310
1990
Mus musculus (P68404), Mus musculus
Manually annotated by BRENDA team
Housey, G.M.; Johnson, M.D.; Hsiao, W.L.; O'Brian, C.A.; Murphy, J.P.; Kirschmeier, P.; Weinstein, I.B.
Overproduction of protein kinase C causes disordered growth control in rat fibroblasts
Cell
52
343-354
1988
Mus musculus (P68404)
Manually annotated by BRENDA team
Housey, G.M.; O'Brian, C.A.; Johnson, M.D.; Kirschmeier, P.; Weinstein, I.B.
Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family
Proc. Natl. Acad. Sci. USA
84
1065-1069
1987
Mus musculus (P68404)
Manually annotated by BRENDA team
Ono, Y.; Kurokawa, T.; Kawahara, K.; Nishimura, O.; Marumoto, R.; Igarashi, K.; Sugino, Y.; Kikkawa, U.; Ogita, K.; Nishizuka, Y.
Cloning of rat brain protein kinase C complementary DNA
FEBS Lett.
203
111-115
1986
Mus musculus (P68404)
Manually annotated by BRENDA team
Ono, Y.; Kurokawa, T.; Fujii, T.; Kawahara, K.; Igarashi, K.; Kikkawa, U.; Ogita, K.; Nishizuka, Y.
Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing
FEBS Lett.
206
347-352
1986
Mus musculus (P68404)
Manually annotated by BRENDA team
Knopf, J.L.; Lee, M.H.; Sultzman, L.A.; Kriz, R.W.; Loomis, C.R.; Hewick, R.M.; Bell, R.M.
Cloning and expression of multiple protein kinase C cDNAs
Cell
46
491-502
1986
Mus musculus (P63318), Mus musculus (P68404)
Manually annotated by BRENDA team
Le Good, J.A.; Ziegler, W.H.; Parekh, D.B.; Alessi, D.R.; Cohen, P.; Parker, P.J.
Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
Science
281
2042-2045
1998
Mus musculus (P28867)
Manually annotated by BRENDA team
Zhang, G.; Kazanietz, M.G.; Blumberg, P.M.; Hurley, J.H.
Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester
Cell
81
917-924
1995
Mus musculus (P28867)
Manually annotated by BRENDA team
Mizuno, K.; Kubo, K.; Saido, T.C.; Akita, Y.; Osada, S.; Kuroki, T.; Ohno, S.; Suzuki, K.
Structure and properties of a ubiquitously expressed protein kinase C, nPKC delta
Eur. J. Biochem.
202
931-940
1991
Mus musculus (P28867), Mus musculus
Manually annotated by BRENDA team
Mischak, H.; Bodenteich, A.; Kolch, W.; Goodnight, J.; Hofer, F.; Mushinski, J.F.
Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns, and characterization of the protein
Biochemistry
30
7925-7931
1991
Mus musculus (P28867), Mus musculus
Manually annotated by BRENDA team
Ono, Y.; Fujii, T.; Igarashi, K.; Kikkawa, U.; Ogita, K.; Nishizuka, Y.
Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat brain protein kinase C
Nucleic Acids Res.
16
5199-5200
1988
Rattus norvegicus (P05696), Mus musculus (P63318)
Manually annotated by BRENDA team
Xu, R.X.; Pawelczyk, T.; Xia, T.H.; Brown, S.C.
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions
Biochemistry
36
10709-10717
1997
Mus musculus (P63318)
Manually annotated by BRENDA team
Bowers, B.J.; Parham, C.L.; Sikela, J.M.; Wehner, J.M.
Isolation and sequence of a mouse brain cDNA coding for protein kinase C-gamma isozyme
Gene
123
263-265
1993
Mus musculus (P63318), Mus musculus
Manually annotated by BRENDA team
Chen, K.H.; Widen, S.G.; Wilson, S.H.; Huang, K.P.
Characterization of the 5'-flanking region of the rat protein kinase C gamma gene
J. Biol. Chem.
265
19961-19965
1990
Mus musculus (P63318)
Manually annotated by BRENDA team
Wang, Q.J.; Acs, P.; Goodnight, J.; Blumberg, P.M.; Mischak, H.; Mushinski, J.F.
The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and -epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation
Oncogene
16
53-60
1998
Mus musculus (P16054), Mus musculus
Manually annotated by BRENDA team
Schaap, D.; Parker, P.J.; Bristol, A.; Kriz, R.; Knopf, J.
Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity
FEBS Lett.
243
351-357
1989
Mus musculus (P16054), Mus musculus
Manually annotated by BRENDA team
Staudinger, J.; Zhou, J.; Burgess, R.; Elledge, S.J.; Olson, E.N.
PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system
J. Cell Biol.
128
263-271
1995
Mus musculus (P20444), Mus musculus
Manually annotated by BRENDA team
Megidish, T.; Mazurek, N.
A mutant protein kinase C that can transform fibroblasts
Nature
342
807-811
1989
Mus musculus (P20444), Mus musculus
Manually annotated by BRENDA team
Rose-John, S.; Dietrich, A.; Marks, F.
Molecular cloning of mouse protein kinase C (PKC) cDNA from Swiss 3T3 fibroblasts
Gene
74
465-471
1988
Mus musculus (P20444), Mus musculus
Manually annotated by BRENDA team
Osada, S.; Mizuno, K.; Saido, T.C.; Akita, Y.; Suzuki, K.; Kuroki, T.; Ohno, S.
A phorbol ester receptor/protein kinase, nPKC eta, a new member of the protein kinase C family predominantly expressed in lung and skin
J. Biol. Chem.
265
22434-22440
1990
Mus musculus (P23298), Mus musculus
Manually annotated by BRENDA team
Goodnight, J.; Kazanietz, M.G.; Blumberg, P.M.; Mushinski, J.F.; Mischak, H.
The cDNA sequence, expression pattern and protein characteristics of mouse protein kinase C-zeta
Gene
122
305-311
1992
Mus musculus (Q02956), Mus musculus
Manually annotated by BRENDA team
Akimoto, K.; Mizuno, K.; Osada, S.; Hirai, S.; Tanuma, S.; Suzuki, K.; Ohno, S.
A new member of the third class in the protein kinase C family, PKC lambda, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells
J. Biol. Chem.
269
12677-12683
1994
Mus musculus (Q62074), Mus musculus
Manually annotated by BRENDA team
Tan, S.L.; Parker, P.J.
Emerging and diverse roles of protein kinase C in immune cell signalling
Biochem. J.
376
545-552
2003
Mus musculus
Manually annotated by BRENDA team
Guo, B.; Su, T.T.; Rawlings, D.J.
Protein kinase C family functions in B-cell activation
Curr. Opin. Immunol.
16
367-373
2004
Mus musculus
Manually annotated by BRENDA team
Violin, J.D.; Newton, A.C.
Pathway illuminated: visualizing protein kinase C signaling
IUBMB Life
55
653-660
2003
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Kawakami, Y.; Nishimoto, H.; Kitaura, J.; Maeda-Yamamoto, M.; Kato, R.M.; Littman, D.R.; Rawlings, D.J.; Kawakami, T.
Protein kinase C betaII regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion
J. Biol. Chem.
279
47720-47725
2004
Mus musculus
Manually annotated by BRENDA team
Spitaler, M.; Cantrell, D.A.
Protein kinase C and beyond
Nat. Immunol.
5
785-790
2004
Caenorhabditis elegans, Homo sapiens, Solanum lycopersicum, Mus musculus
Manually annotated by BRENDA team
Harper, M.T.; Poole, A.W.
Isoform-specific functions of protein kinase C: the platelet paradigm
Biochem. Soc. Trans.
35
1005-1008
2007
Mus musculus
Manually annotated by BRENDA team
Baldeiras, I.E.; Santos, R.M.; Rosario, L.M.
Protein kinase C isoform specificity of cholinergic potentiation of glucose-induced pulsatile 5-HT/insulin release from mouse pancreatic islets
Biol. Res.
39
531-539
2006
Mus musculus
Manually annotated by BRENDA team
Xu, T.R.; He, G.; Dobson, K.; England, K.; Rumsby, M.
Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKCepsilon) in 3T3 fibroblasts
Cell. Signal.
19
1986-1995
2007
Mus musculus
Manually annotated by BRENDA team
Grossoni, V.C.; Falbo, K.B.; Mauro, L.V.; Krasnapolski, M.A.; Kazanietz, M.G.; Bal De Kier Joffe, E.D.; Urtreger, A.J.
Protein kinase C delta inhibits the production of proteolytic enzymes in murine mammary cells
Clin. Exp. Metastasis
24
513-520
2007
Mus musculus
Manually annotated by BRENDA team
Beaudry, H.; Gendron, L.; Guimond, M.O.; Payet, M.D.; Gallo-Payet, N.
Involvement of protein kinase C alpha (PKC alpha) in the early action of angiotensin II type 2 (AT2) effects on neurite outgrowth in NG108-15 cells: AT2-receptor inhibits PKC alpha and p21ras activity
Endocrinology
147
4263-4272
2006
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Eun, S.Y.; Kim, E.H.; Kang, K.S.; Kim, H.J.; Jo, S.A.; Kim, S.J.; Jo, S.H.; Kim, S.J.; Blackshear, P.J.; Kim, J.
Cell type-specific upregulation of myristoylated alanine-rich C kinase substrate and protein kinase C-alpha, -beta I, -beta II, and -delta in microglia following kainic acid-induced seizures
Exp. Mol. Med.
38
310-319
2006
Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Saraiva, L.; Silva, R.D.; Pereira, G.; Goncalves, J.; Corte-Real, M.
Specific modulation of apoptosis and Bcl-xL phosphorylation in yeast by distinct mammalian protein kinase C isoforms
J. Cell Sci.
119
3171-3181
2006
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sampson, S.R.; Cooper, D.R.
Specific protein kinase C isoforms as transducers and modulators of insulin signaling
Mol. Genet. Metab.
89
32-47
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Cha, S.K.; Wu, T.; Huang, C.L.
Protein kinase C inhibits caveolae-mediated endocytosis of TRPV5
Am. J. Physiol. Renal Physiol.
294
F1212-F1221
2008
Mus musculus
Manually annotated by BRENDA team
Hegedus, C.; Lakatos, P.; Olah, G.; Toth, B.I.; Gergely, S.; Szabo, E.; Biro, T.; Szabo, C.; Virag, L.
Protein kinase C protects from DNA damage-induced necrotic cell death by inhibiting poly(ADP-ribose) polymerase-1
FEBS Lett.
582
1672-1678
2008
Mus musculus
Manually annotated by BRENDA team
Lam, J.S.; Wang, L.; Lin, L.; Chan, S.O.
Role of protein kinase C in selective inhibition of mouse retinal neurites during contacts with chondroitin sulfates
Neurosci. Lett.
434
150-154
2008
Mus musculus (P16054), Mus musculus (P20444), Mus musculus (P28867), Mus musculus (P63318), Mus musculus (P68404), Mus musculus
Manually annotated by BRENDA team
Fiorentino, L.; Vivanti, A.; Cavalera, M.; Marzano, V.; Ronci, M.; Fabrizi, M.; Menini, S.; Pugliese, G.; Menghini, R.; Khokha, R.; Lauro, R.; Urbani, A.; Federici, M.
Increased tumor necrosis factor alpha-converting enzyme activity induces insulin resistance and hepatosteatosis in mice
Hepatology
51
103-110
2010
Mus musculus
Manually annotated by BRENDA team
Nasu-Nishimura, Y.; Jaffe, H.; Isaac, J.T.; Roche, K.W.
Differential regulation of kainate receptor trafficking by phosphorylation of distinct sites on GluR6
J. Biol. Chem.
285
2847-2856
2010
Mus musculus
Manually annotated by BRENDA team
Rahman, G.M.; Shanker, S.; Lewin, N.E.; Kedei, N.; Hill, C.S.; Prasad, B.V.; Blumberg, P.M.; Das, J.
Identification of the activator-binding residues in the second cysteine-rich regulatory domain of protein kinase Ctheta (PKCtheta)
Biochem. J.
451
33-44
2013
Mus musculus
Manually annotated by BRENDA team
Pinzon-Guzman, C.; Zhang, S.S.; Barnstable, C.J.
Specific protein kinase C isoforms are required for rod photoreceptor differentiation
J. Neurosci.
31
18606-18617
2011
Mus musculus
Manually annotated by BRENDA team
Wang, C.; Shang, Y.; Yu, J.; Zhang, M.
Substrate recognition mechanism of atypical protein kinase Cs revealed by the structure of PKCiota in complex with a substrate peptide from Par-3
Structure
20
791-801
2012
Mus musculus (Q62074)
Manually annotated by BRENDA team
Kumar, V.; Weng, Y.C.; Geldenhuys, W.J.; Wang, D.; Han, X.; Messing, R.O.; Chou, W.H.
Generation and characterization of ATP analog-specific protein kinase Cdelta
J. Biol. Chem.
290
1936-1951
2015
Mus musculus
Manually annotated by BRENDA team
Liu, P.; Li, Y.; Qi, X.; Xu, J.; Liu, D.; Ji, X.; Chi, T.; Liu, H.; Zou, L.
Protein kinase C is involved in the neuroprotective effect of berberine against intrastriatal injection of quinolinic acid-induced biochemical alteration in mice
J. Cell. Mol. Med.
23
6343-6354
2019
Mus musculus
Manually annotated by BRENDA team
Goode, D.J.; Molliver, D.C.
Phospho-substrate profiling of Epac-dependent protein kinase C activity
Mol. Cell. Biochem.
456
167-178
2019
Mus musculus (P16054), Mus musculus (P20444), Mus musculus (P63318), Mus musculus
Manually annotated by BRENDA team