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Information on EC 2.7.11.13 - protein kinase C and Organism(s) Rattus norvegicus

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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:
Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
C1Bbeta
-
C1 domain of PKC
Calcium-dependent protein kinase C
-
-
-
-
delta protein kinase C
-
epsilonPKC
-
-
-
-
PKC delta
-
isoform
PKC-zeta
isozyme
PKCalpha
PKCbetaI
-
isoform
PKCbetaII
-
isoform
PKCdelta
PKCepsilon
-
isoform
PKCgamma
-
isoform
protein kinase C
-
-
-
-
protein kinase C betaII
-
-
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, zeta type
-
protein kinase C-delta
-
protein kinase C-eta
-
protein kinase C-like 1
-
protein kinase C-zeta
isozyme
protein kinase Calpha
-
-
protein kinase Cdelta
-
protein kinase epsilon
-
isoform
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 + phosphorylated protein
show the reaction diagram
-
-
-
-
?
ATP + Akt
ADP + phosphorylated Akt
show the reaction diagram
-
phosphorylation on Ser473 by isozyme PKCbetaII
-
-
?
ATP + Bcl-xL
ADP + phosphorylated Bcl-xL
show the reaction diagram
-
recombinant human substrate, recombinant isozyme PKCdelta
-
-
?
ATP + calcium-activated potassium channel alpha subunit Slo1
ADP + phosphorylated calcium-activated potassium channel alpha subunit Slo1
show the reaction diagram
-
-
-
-
?
ATP + glycine transporter 2
ADP + phosphorylated glycine transporter 2
show the reaction diagram
-
-
-
-
?
ATP + hematopoietic-specific G-protein Galpha15
ADP + phosphorylated hematopoietic-specific G-protein Galpha15
show the reaction diagram
-
recombinant substrate expressed in COS-7 cells, phosphorylation at Ser334, mutant G-protein Galpha15 S334A is inactive as substrate for PKC
-
-
?
ATP + hematopoietic-specific G-protein Galpha15 peptide
ADP + phosphorylated hematopoietic-specific G-protein Galpha15 peptide
show the reaction diagram
-
the PKC phosphorylation site peptide sequence RKGSR includes Ser334
-
-
?
ATP + hematopoietic-specific G-protein Galpha16
ADP + phosphorylated hematopoietic-specific G-protein Galpha16
show the reaction diagram
-
substrate from HL-60 cells, phosphorylation at Ser336, mutant G-protein Galpha16 S336A is inactive as substrate for PKC
-
-
?
ATP + hematopoietic-specific G-protein Galpha16 peptide
ADP + phosphorylated hematopoietic-specific G-protein Galpha16 peptide
show the reaction diagram
-
the PKC phosphorylation site peptide sequence KKGARSRR includes Ser336
-
-
?
ATP + histone
ADP + phosphorylated histone
show the reaction diagram
ATP + histone H1
ADP + phosphorylated histone H1
show the reaction diagram
-
-
-
-
?
ATP + histone III-SS
ADP + phosphorylated histone III-SS
show the reaction diagram
-
commercial substrate
-
-
?
ATP + histone IIIS
ADP + phosphorylated histone IIIS
show the reaction diagram
poor substrate
-
-
?
ATP + hyperpolarization-activated cyclic nucleotide-gated channel 1 protein
ADP + phosphorylated hyperpolarization-activated cyclic nucleotide-gated channel 1 protein
show the reaction diagram
-
-
-
-
?
ATP + insulin receptor
ADP + phosphorylated insulin receptor
show the reaction diagram
-
isozyme PKCalpha
-
-
?
ATP + insulin receptor substrate 1
ADP + phosphorylated insulin receptor substrate 1
show the reaction diagram
ATP + insulin receptor substrate-1
ADP + phosphorylated insulin receptor substrate-1
show the reaction diagram
ATP + insulin receptor substrate-3
ADP + phosphorylated insulin receptor substrate-3
show the reaction diagram
-
-
-
?
ATP + insulin receptor substrate-4
ADP + phosphorylated insulin receptor substrate-4
show the reaction diagram
-
-
-
?
ATP + IRS
ADP + phosphorylated IRS
show the reaction diagram
-
isozymes PKCalpha and PKCdelta, phosphorylation on Ser307
-
-
?
ATP + LC3
ADP + phosphorylated LC3
show the reaction diagram
-
-
-
-
?
ATP + Na,K-ATPase
ADP + phosphorylated Na,K-ATPase
show the reaction diagram
ATP + pyruvate dehydrogenase kinase
ADP + phosphorylated pyruvate dehydrogenase kinase
show the reaction diagram
-
-
-
?
ATP + RalB
ADP + phosphorylated RalB
show the reaction diagram
-
PKCalpha phosphorylates RalB on Ser-192 and Ser-198 in the hypervariable sequence and Ser-198 phosphorylation promotes activation of RalB and causes RalB relocalization from the plasma membrane to late endosomes
-
-
?
ATP + ribosomal protein S6-(229-239) peptide analogue
ADP + phosphorylated ribosomal protein S6-(229-239) peptide analogue
show the reaction diagram
-
-
-
?
ATP + S6-(229-239) peptide
ADP + phosphorylated S6-(229-239) peptide
show the reaction diagram
-
-
-
?
ATP + serine racemase
ADP + phosphorylated serine racemase
show the reaction diagram
-
-
-
-
?
ATP + serotonin N-acetyltransferase
ADP + phosphorylated serotonin N-acetyltransferase
show the reaction diagram
ATP + sodium channel
ADP + phosphorylated sodium channel
show the reaction diagram
ATP + [low density lipoprotein receptor-related protein]
ADP + phosphorylated [low density lipoprotein receptor-related protein]
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 + phosphorylated protein
show the reaction diagram
-
-
-
-
?
ATP + hyperpolarization-activated cyclic nucleotide-gated channel 1 protein
ADP + phosphorylated hyperpolarization-activated cyclic nucleotide-gated channel 1 protein
show the reaction diagram
-
-
-
-
?
ATP + insulin receptor substrate 1
ADP + phosphorylated insulin receptor substrate 1
show the reaction diagram
-
phosphorylation of insulin receptor substrate proteins on serine residues is an important posttranslational modification that is linked to insulin resistance, overview
-
-
?
ATP + Na,K-ATPase
ADP + phosphorylated Na,K-ATPase
show the reaction diagram
-
-
-
-
?
ATP + pyruvate dehydrogenase kinase
ADP + phosphorylated pyruvate dehydrogenase kinase
show the reaction diagram
-
-
-
?
ATP + serotonin N-acetyltransferase
ADP + phosphorylated serotonin N-acetyltransferase
show the reaction diagram
-
PKC regulates the activity and stability of serotonin N-acetyltransferase in vivo, recombinant enzyme expressed in COS-7 cells
-
-
?
ATP + sodium channel
ADP + phosphorylated sodium channel
show the reaction diagram
-
PKC mediates inhibition of sodium channels and tetrodotoxin-sensitive transient sodium current by phosphorylation by topiramate, overview
-
-
?
ATP + [low density lipoprotein receptor-related protein]
ADP + phosphorylated [low density lipoprotein receptor-related protein]
show the reaction diagram
-
involved in regulation of endocytosis and association with adaptor molecules, e.g. Shc, Dab1, or CED-6/GULP
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
the C1 domain of PKC requires two Zn2+ ions for proper folding and stability
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ALSTER
psi pyruvate dehydrogenase kinase peptide, selective inhibitor of deltaPKC-mediated pyruvate dehydrogenase kinase phosphorylation
-
angiotensin II type 2-receptor
-
inhibits isozyme PKCalpha
-
bisindolylmaleimide I
-
PKC inhibitors induce LC3 processing and autophagosome formation. Inhibition of protein kinase C increased autophagy
CG53353
-
inhibitor of isozyme PKCbetaII
cheletrytrine
-
complete inhibition at 0.05 mM
curcumin
-
inhibits or activates PKC dependent on Ca2+ and the presence of membranes or phosphatidylserine, respectively, in presence of phosphatidylserine curcumin activates PKC, in presence of membranes with phosphatidylserine the enzyme is inhibited, Ca2+ competes with curcumin at the regulatory domainbinding site, overview, effects on different isozymes, overview
GF109203X
Gö 6976
-
-
G-6976
G6976
Gö6983
-
an inhibitor of isozyme PKCbeta, but not of PKCmy
H-7
-
specific PKC inhibitor
LY333531
-
specific inhibition of PKCbeta
LY379196
-
highly specific for PKCbeta, inhibits amphetamine-stimulated dopamine efflux in striatum in vivo
phorbol 12,13-dibutyrate
-
activates Na+,K+-ATPase activity at low concentration, but inhibits it at high concentration, the inhibitory effect can be reversed by preincubation with ethoxyresorufin, 17-octadecynoic acid, wortmannin, LY294002, cytochlasin D, or latrunculin B
Ro 31-8220
-
i.e., 2-[1-[3-(amidinothio)propyl]-1H-indol-3-yl]-3-(1-methylindol-3-yl)-maleimide
Ro-32-0432
Ro318220
-
-
rottlerin
staurosporine
-
inhibits all PKC isozymes
thymeleatoxin
-
activates Na+,K+-ATPase activity at low concentration, but inhibits it at high concentration
YGRKKRRQRRR-GSG-ALSTER
psi pyruvate dehydrogenase kinase 1 peptide, inhibits the phosphorylation of pyruvate dehydrogenase kinase but not the phosphorylation of HSP, MARCKS, STAT, GAPDH, and troponin I
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-oleoyl-2-acetyl-sn-glycerol
-
-
12-O-Tetradecanoylphorbol 13-acetate
-
activates PKC
12-O-tetradecanoylphorbol-13-acetate
-
-
cardiolipin
activates
curcumin
-
inhibits or activates PKC dependent on Ca2+ and the presence of membranes or phosphatidylserine, respectively, in presence of phosphatidylserine curcumin activates PKC, in presence of membranes with phosphatidylserine the enzyme is inhibited, Ca2+ competes with curcumin at the regulatory domainbinding site, overview, effects on different isozymes, overview
diacylglycerol
Epidermal growth factor
-
EGF, activates isozyme PKCalpha in the fetal lung during signaling involved in lung maturation, overview
fatty acids
-
activation mechanism, isozyme PKCdelta is involved in fatty acid-induced hepatic insulin resistance
hydrogen peroxide
-
-
Insulin
-
activates PKC isozymes alpha, betaII, delta, and zeta in several cell types, activation mechanism, isozyme PKCdelta is involved in fatty acid-induced hepatic insulin resistance
-
mezerein
-
stimulates classical, but not novel PKC isozymes
palmitate
-
activates isozyme PKCtheta, but not isozymes PKCalpha and PKCepsilon
phorbol 12,13-diacetate
-
-
phorbol 12,13-dibutyrate
phorbol 12-myristate 13-acetate
phorbol 12-myristate-13-acetate
-
activation of protein kinase C significantly attenuates starvation- or rapamycin-induced LC3 processing. Activation of protein kinase C inhibits autophagy
phosphatidylserine
-
activation mechanism
phosphatidylserine-diolein
-
-
Phospholipid
R59949
-
increases isofom PKCdelta and PKCepsilon activities in both membrane and cytosolic fractions
thymeleatoxin
transforming growth factor alpha
-
TGFalpha, activates isozyme PKCalpha in the fetal lung during signaling involved in lung maturation, overview
-
zileuton
-
zileuton acts as a PKC delta activator, causing it to translocate from the cytosol to nucleus, the activation is inhibited by rottlerin
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036
S6-(229-239) peptide
enzyme activated by cardiolipin
-
additional information
additional information
-
binding kinetics of phorbol 12-myristate 13-acetate and diacylglycerol
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000023 - 0.0000079
Gö-6976
Rattus norvegicus
-
IC50 of 2.3-7.9 nM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
24
-
assay at
36
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
pulmonary
Manually annotated by BRENDA team
-
arterial pulmonary
Manually annotated by BRENDA team
-
expression of several isozymes
Manually annotated by BRENDA team
-
purified PKC from brain
Manually annotated by BRENDA team
-
constitutively active isozyme PKCdelta
Manually annotated by BRENDA team
-
isozyme PKCbetaII
Manually annotated by BRENDA team
-
pulmonary arterial
Manually annotated by BRENDA team
-
pulmonary cell line
Manually annotated by BRENDA team
-
increased expresison of isozyme PKCtheta in insulin-resistant rats
Manually annotated by BRENDA team
additional information
-
developmental expression patterns of isozymes PKCalpha, PKCepsilon, PKCmy, and PKCzeta
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
PKC activity controls serine racemase phosphorylation and D-serine levels both in vitro and in vivo
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPCB_RAT
671
0
76751
Swiss-Prot
other Location (Reliability: 2)
KPCD1_RAT
918
0
102043
Swiss-Prot
Secretory Pathway (Reliability: 2)
KPCD2_RAT
875
0
96497
Swiss-Prot
other Location (Reliability: 2)
KPCD_RAT
673
0
77520
Swiss-Prot
other Location (Reliability: 2)
KPCA_RAT
672
0
76792
Swiss-Prot
other Location (Reliability: 2)
KPCE_RAT
737
0
83478
Swiss-Prot
other Location (Reliability: 4)
KPCG_RAT
697
0
78358
Swiss-Prot
other Location (Reliability: 3)
KPCI_RAT
596
0
68276
Swiss-Prot
other Location (Reliability: 3)
KPCL_RAT
683
0
77947
Swiss-Prot
Mitochondrion (Reliability: 4)
KPCT_RAT
707
0
81750
Swiss-Prot
other Location (Reliability: 2)
PKN1_RAT
946
0
104468
Swiss-Prot
other Location (Reliability: 3)
PKN2_RAT
985
0
112069
Swiss-Prot
other Location (Reliability: 1)
KPCZ_RAT
592
0
67733
Swiss-Prot
other Location (Reliability: 2)
D4A0U0_RAT
569
0
65819
TrEMBL
other Location (Reliability: 1)
A0A8I5ZVA4_RAT
682
0
78469
TrEMBL
other Location (Reliability: 3)
A0A0G2K928_RAT
876
0
98680
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8I5XW57_RAT
629
0
72015
TrEMBL
other Location (Reliability: 2)
A0A0G2K5Q0_RAT
652
0
74531
TrEMBL
other Location (Reliability: 5)
F1LM10_RAT
707
0
81777
TrEMBL
other Location (Reliability: 2)
A0A8I5ZMR6_RAT
688
0
78766
TrEMBL
other Location (Reliability: 2)
A0A8I6AM65_RAT
633
0
71858
TrEMBL
other Location (Reliability: 2)
F1LPA4_RAT
983
0
111729
TrEMBL
other Location (Reliability: 1)
B5DFC4_RAT
672
0
76792
TrEMBL
other Location (Reliability: 2)
A0A8I6G952_RAT
609
0
69746
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8I6ABU2_RAT
667
0
76406
TrEMBL
other Location (Reliability: 5)
F1LS98_RAT
672
0
76780
TrEMBL
other Location (Reliability: 2)
A0A8I5ZUY0_RAT
631
0
72158
TrEMBL
other Location (Reliability: 2)
F1LS42_RAT
672
0
76715
TrEMBL
other Location (Reliability: 2)
A0A8I5ZZZ3_RAT
722
0
81680
TrEMBL
other Location (Reliability: 4)
A0A8I6GEN7_RAT
948
0
104651
TrEMBL
other Location (Reliability: 2)
D4A229_RAT
890
0
100156
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I5ZK64_RAT
940
0
106978
TrEMBL
other Location (Reliability: 1)
A0A8I5ZN16_RAT
646
0
72963
TrEMBL
other Location (Reliability: 3)
A0A8I6G5U2_RAT
795
0
90395
TrEMBL
other Location (Reliability: 2)
A0A8I6AR64_RAT
844
0
92913
TrEMBL
other Location (Reliability: 2)
A0A0G2K6J2_RAT
870
0
98946
TrEMBL
other Location (Reliability: 2)
F1M2P8_RAT
636
0
72783
TrEMBL
other Location (Reliability: 2)
A0A0G2JZ66_RAT
879
0
98132
TrEMBL
other Location (Reliability: 2)
A0A8I6A9E1_RAT
910
0
101242
TrEMBL
Secretory Pathway (Reliability: 2)
F1LS36_RAT
615
0
69810
TrEMBL
other Location (Reliability: 2)
A0A8I6G981_RAT
951
0
105090
TrEMBL
other Location (Reliability: 2)
A0A8I5Y861_RAT
635
0
72580
TrEMBL
other Location (Reliability: 2)
A0A8I5ZQ41_RAT
951
0
108200
TrEMBL
other Location (Reliability: 1)
A0A140UHX0_RAT
673
0
77506
TrEMBL
other Location (Reliability: 2)
Q6DUV1_RAT
737
0
83576
TrEMBL
other Location (Reliability: 4)
A0A8I5ZQS9_RAT
667
0
76141
TrEMBL
other Location (Reliability: 2)
A0A8I6AMW9_RAT
676
0
76954
TrEMBL
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116000
x * 116000
64000
x * 64000, SDS-PAGE
78000
-
SDS-PAGE
82000
-
x * 82000, isozyme PKCalpha, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
isozymes alpha, delta, and epsilon require trans- and autophosphorylation for activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of full-length protein kinase C bII is determined at 4.0 A. The C1B domain clamps the NFD helix in a low activity conformation, which is reversed upon membrane binding. A low-resolution solution structure of the closed conformation of PKCbII is derived from small-angle X-ray scattering
-
crystal structure of PKC-delta C2 domain. Structural elements unique to this C2 domain include a helix and a protruding beta hairpin which may contribute basic sequences to a membrane-interaction site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D116A
-
site-directed mutagenesis, isozyme PKCgamma domain C1B mutant shows unaltered activity
D55A
-
site-directed mutagenesis, isozyme PKCalpha and PKCgamma mutants show unaltered activity and ligand binding, isozyme PKCalpha shows enhanced activation by phospholipids
DELTA621-622
-
deletion of two residues in the AGC linker that passes through the cleft of the C1B domain (DELTA621–622) results in a 2fold decrease in the concentration of phorbol 12-myristate 13-acetate required to mediate half-maximal translocation
F629D
-
within the NFD helix, mutant F629D and mutant F633D lead to 2- to 5fold decrease in EC50 for phorbol 12-myristate 13-acetate induced translocation
F633D
-
within the NFD helix, mutant F629D and mutant F633D lead to 2- to 5fold decrease in EC50 for phorbol 12-myristate 13-acetate induced translocation
K368A
-
a dominant-negative mutant of PKCalpha
L125D
-
mutation of Leu125 in the C1B domain, which is part of the C1B clamp interface, increases EC50 for phorbol 12-myristate 13-acetate induced translocation more than 10fold
L358D
-
mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation
L367D
-
mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation
W58A
-
site-directed mutagenesis, isozyme PKCgamma domain C1A mutant shows impaired binding of phorbol 12-myristate 13-acetate and diacylglycerol
Y123A
-
site-directed mutagenesis, isozyme PKCgamma domain C1B mutant shows impaired binding of phorbol 12-myristate 13-acetate and diacylglycerol
Y123W
-
the mutation in the C1 domain of PKC leads to measurable changes upon membrane binding
Y422D
-
mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation
Y430D
-
mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation
additional information
-
specific modulation of apoptosis and Bcl-xL phosphorylation in recombinant yeast by isozymes PKCepsilon and PKCzeta
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anion-exchange chromatography and gel filtration
-
HisTrap Ni2+ affinity column chromatography and Superdex 200 gel filtration
-
isozyme PKC betaII from jejunal loops
-
isozymes partially from primary cerebellar granule cells, Tris buffer leads to degradation of the proteins
-
protein A Sepharose column chromatography
-
recombinant full-length isozymes PKCalpha and PKCgamma from Sf9 cells by ion exchange chromatography, recombinant His-tagged isolated isozymes PKCalpha and PKCgamma domains C1 from Escherichia coli strain BL21(DE3) inclusion bodies by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloning of an alternative splicing variant of protein kinase C delta, expression of truncated form of PKC deltaIII fused to green fluorescent protein in CHO-K1 cells
co-expression of PKC isozymes and insulin in HEK-293 or CHO cells, interaction analysis, overview
-
expressed in COS 7 cells
expressed in COS-7 cells
expressed in Escherichia coli
-
expressed in Escherichia coli Rosetta 2(DE3)pLysS cells
-
expressed in HEK-293 cells
-
expressed in Sf9 cells as a GST-fusion protein
-
expression in COS cells
expression of full-length isozymes PKCalpha and PKCgamma in Spodoptera frugiperda Sf9 cells using the baculovirus infection system, expression of His-tagged isolated isozymes PKCalpha and PKCgamma domains C1 in Escherichia coli strain BL21(DE3)
-
expression of isozyme PKCbetaI in HEK-293 cells, and co-expression with dopamine transporter significantly enhancing the amphetamine-stimulated dopamine efflux
-
expression of isozyme PKCdelta in Saccharomyces cerevisiae, subcloning in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mitochondrial reactive oxygen species production activates PKCepsilon
-
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
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
Kikkawa, U.; Ogita, K.; Ono, Y.; Asaoka, Y.; Shearman, M.S.; Fujii, T.; Ase, K.; Sekiguchi, K.; Igarashi, K.; Nishizuka, Y.
The common structure and activities of four subspecies of rat brain protein kinase C family
FEBS Lett.
223
212-216
1987
Rattus norvegicus (P05696)
Manually annotated by BRENDA team
Ueyama, T.; Ren, Y.; Ohmori, S.; Sakai, K.; Tamaki, N.; Saito, N.
cDNA cloning of an alternative splicing variant of protein kinase C delta (PKC deltaIII), a new truncated form of PKCdelta, in rats
Biochem. Biophys. Res. Commun.
269
557-563
2000
Rattus norvegicus (P09215)
Manually annotated by BRENDA team
Kurkinen, K.M.; Keinanen, R.A.; Karhu, R.; Koistinaho, J.
Genomic structure and chromosomal localization of the rat protein kinase Cdelta-gene
Gene
242
115-123
2000
Rattus norvegicus (P09215)
Manually annotated by BRENDA team
Pappa, H.; Murray-Rust, J.; Dekker, L.V.; Parker, P.J.; McDonald, N.Q.
Crystal structure of the C2 domain from protein kinase C-delta
Structure
6
885-894
1998
Rattus norvegicus (P09215)
Manually annotated by BRENDA team
Garcia-Paramio, P.; Cabrerizo, Y.; Bornancin, F.; Parker, P.J.
The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation
Biochem. J.
333
631-636
1998
Rattus norvegicus (P09215)
-
Manually annotated by BRENDA team
Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; Nishizuka, Y.
The structure, expression, and properties of additional members of the protein kinase C family
J. Biol. Chem.
263
6927-6932
1988
Rattus norvegicus (P09215), Rattus norvegicus (P09216), Rattus norvegicus (P09217)
Manually annotated by BRENDA team
Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; Nishizuka, Y.
Identification of three additional members of rat protein kinase C family: delta-, epsilon- and zeta-subspecies
FEBS Lett.
226
125-128
1987
Rattus norvegicus (P09215), Rattus norvegicus (P09216), Rattus norvegicus (P09217)
Manually annotated by BRENDA team
Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; Nishizuka, Y.
Protein kinase C zeta subspecies from rat brain: its structure, expression, and properties
Proc. Natl. Acad. Sci. USA
86
3099-3103
1989
Rattus norvegicus (P09217)
Manually annotated by BRENDA team
Mukai, H.; Ono, Y.
A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C
Biochem. Biophys. Res. Commun.
199
897-904
1994
Homo sapiens (Q16512), Homo sapiens, Rattus norvegicus (Q63433)
Manually annotated by BRENDA team
Morrice, N.A.; Gabrielli, B.; Kemp, B.E.; Wettenhall, R.E.
A cardiolipin-activated protein kinase from rat liver structurally distinct from the protein kinases C
J. Biol. Chem.
269
20040-20046
1994
Rattus norvegicus (Q63433)
Manually annotated by BRENDA team
Dekker, L.V.; Parker, P.J.; McIntyre, P.
Biochemical properties of rat protein kinase C-eta expressed in COS cells
FEBS Lett.
312
195-199
1992
Rattus norvegicus (Q64617)
Manually annotated by BRENDA team
Choi, B.H.; Chae, H.D.; Park, T.J.; Oh, J.; Lim, J.; Kang, S.S.; Ha, H.; Kim, K.T.
Protein kinase C regulates the activity and stability of serotonin N-acetyltransferase
J. Neurochem.
90
442-454
2004
Rattus norvegicus
Manually annotated by BRENDA team
Beltowski, J.; Marciniak, A.; Jamroz-Wisniewska, A.; Borkowska, E.; Wojcicka, G.
Bidirectional regulation of renal cortical Na+,K+-ATPase by protein kinase C
Acta Biochim. Pol.
51
757-772
2004
Rattus norvegicus
Manually annotated by BRENDA team
Barman, S.A.; Zhu, S.; White, R.E.
Protein kinase C inhibits BKCa channel activity in pulmonary arterial smooth muscle
Am. J. Physiol.
286
L149-155
2004
Rattus norvegicus
Manually annotated by BRENDA team
Duran, M.J.; Pierre, S.V.; Carr, D.L.; Pressley, T.A.
The isoform-specific region of the Na,K-ATPase catalytic subunit: role in enzyme kinetics and regulation by protein kinase C
Biochemistry
43
16174-16183
2004
Rattus norvegicus
Manually annotated by BRENDA team
Yang, J.H.; Derr-Yellin, E.C.; Kodavanti, P.R.
Alterations in brain protein kinase C isoforms following developmental exposure to a polychlorinated biphenyl mixture
Brain Res. Mol. Brain Res.
111
123-135
2003
Rattus norvegicus
Manually annotated by BRENDA team
Hung, A.C.; Chu, Y.J.; Lin, Y.H.; Weng, J.Y.; Chen, H.B.; Au, Y.C.; Sun, S.H.
Roles of protein kinase C in regulation of P2X7 receptor-mediated calcium signalling of cultured type-2 astrocyte cell line, RBA-2
Cell. Signal.
17
1384-1396
2005
Rattus norvegicus
Manually annotated by BRENDA team
Geeraert, V.; Dupont, J.L.; Grant, N.J.; Huvet, C.; Chasserot-Golaz, S.; Janoshazi, A.; Procksch, O.; de Barry, J.
F-actin does not modulate the initial steps of the protein kinase C activation process in living nerve cells
Exp. Cell Res.
289
222-236
2003
Rattus norvegicus
Manually annotated by BRENDA team
Helliwell, P.A.; Rumsby, M.G.; Kellett, G.L.
Intestinal sugar absorption is regulated by phosphorylation and turnover of protein kinase C betaII mediated by phosphatidylinositol 3-kinase- and mammalian target of rapamycin-dependent pathways
J. Biol. Chem.
278
28644-28650
2003
Rattus norvegicus
Manually annotated by BRENDA team
Ananthanarayanan, B.; Stahelin, R.V.; Digman, M.A.; Cho, W.
Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains
J. Biol. Chem.
278
46886-46894
2003
Rattus norvegicus
Manually annotated by BRENDA team
Ranganathan, S.; Liu, C.X.; Migliorini, M.M.; Von Arnim, C.A.; Peltan, I.D.; Mikhailenko, I.; Hyman, B.T.; Strickland, D.K.
Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules
J. Biol. Chem.
279
40536-40544
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Johnson, L.A.; Guptaroy, B.; Lund, D.; Shamban, S.; Gnegy, M.E.
Regulation of amphetamine-stimulated dopamine efflux by protein kinase C beta
J. Biol. Chem.
280
10914-10919
2005
Rattus norvegicus
Manually annotated by BRENDA team
Tsuda, K.; Tsuda, S.; Nishio, I.
Role of protein kinase C in the regulation of acetylcholine release in the central nervous system of spontaneously hypertensive rats
J. Cardiovasc. Pharmacol.
41 Suppl 1
S57-60
2003
Rattus norvegicus
Manually annotated by BRENDA team
Gu, J.L.; Lu, W.; Xia, C.; Wu, X.; Liu, M.
Regulation of hematopoietic-specific G-protein Galpha15 and Galpha16 by protein kinase C
J. Cell. Biochem.
88
1101-1111
2003
Rattus norvegicus
Manually annotated by BRENDA team
Bayer, A.L.; Heidkamp, M.C.; Patel, N.; Porter, M.; Engman, S.; Samarel, A.M.
Alterations in protein kinase C isoenzyme expression and autophosphorylation during the progression of pressure overload-induced left ventricular hypertrophy
Mol. Cell. Biochem.
242
145-152
2003
Rattus norvegicus
Manually annotated by BRENDA team
Larsen, G.A.; Berg-Johnsen, J.; Moe, M.C.; Vinje, M.L.
Calcium-dependent protein kinase C activation in acutely isolated neurons during oxygen and glucose deprivation
Neurochem. Res.
29
1931-1937
2004
Rattus norvegicus
Manually annotated by BRENDA team
Mahmmoud, Y.A.
Modulation of protein kinase C by curcumin; inhibition and activation switched by calcium ions
Br. J. Pharmacol.
150
200-208
2007
Rattus norvegicus
Manually annotated by BRENDA team
Curia, G.; Aracri, P.; Colombo, E.; Scalmani, P.; Mantegazza, M.; Avanzini, G.; Franceschetti, S.
Phosphorylation of sodium channels mediated by protein kinase-C modulates inhibition by topiramate of tetrodotoxin-sensitive transient sodium current
Br. J. Pharmacol.
150
792-797
2007
Rattus norvegicus
Manually annotated by BRENDA team
Popp, R.L.; Velasquez, O.; Bland, J.; Hughes, P.
Characterization of protein kinase C isoforms in primary cultured cerebellar granule cells
Brain Res.
1083
70-84
2006
Rattus norvegicus
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
Villanueva-Garcia, D.; Wang, K.T.; Nielsen, H.C.; Ramadurai, S.M.
Expression of specific protein kinase C (PKC) isoforms and ligand-specific activation of PKCalpha in late gestation fetal lung
Exp. Lung Res.
33
185-196
2007
Rattus norvegicus
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
Nawaratne, R.; Gray, A.; Jorgensen, C.H.; Downes, C.P.; Siddle, K.; Sethi, J.K.
Regulation of insulin receptor substrate 1 pleckstrin homology domain by protein kinase C: role of serine 24 phosphorylation
Mol. Endocrinol.
20
1838-1852
2006
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
Kim, J.Y.; Park, C.S.
Potentiation of large-conductance calcium-activated potassium (BK(Ca)) channels by a specific isoform of protein kinase C
Biochem. Biophys. Res. Commun.
365
459-465
2008
Rattus norvegicus
Manually annotated by BRENDA team
Fornes, A.; Nunez, E.; Alonso-Torres, P.; Aragon, C.; Lopez-Corcuera, B.
Trafficking properties and activity regulation of the neuronal glycine transporter GLYT2 by protein kinase C
Biochem. J.
412
495-506
2008
Rattus norvegicus
Manually annotated by BRENDA team
Lee, S.; Lynn, E.G.; Kim, J.A.; Quon, M.J.
Protein kinase C-zeta phosphorylates insulin receptor substrate-1, -3, and -4 but not -2: isoform specific determinants of specificity in insulin signaling
Endocrinology
149
2451-2458
2008
Rattus norvegicus (P09217)
Manually annotated by BRENDA team
Waraich, R.S.; Weigert, C.; Kalbacher, H.; Hennige, A.M.; Lutz, S.Z.; Haering, H.U.; Schleicher, E.D.; Voelter, W.; Lehmann, R.
Phosphorylation of Ser357 of rat insulin receptor substrate-1 mediates adverse effects of protein kinase C-delta on insulin action in skeletal muscle cells
J. Biol. Chem.
283
11226-11233
2008
Rattus norvegicus (P09215)
Manually annotated by BRENDA team
Dries, D.R.; Newton, A.C.
Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy
J. Biol. Chem.
283
7885-7893
2008
Rattus norvegicus
Manually annotated by BRENDA team
Weng, J.Y.; Hsu, T.T.; Sun, S.H.
Functional characterization of P2Y1 versus P2X receptors in RBA-2 astrocytes: elucidate the roles of ATP release and protein kinase C
J. Cell. Biochem.
104
554-567
2008
Rattus norvegicus
Manually annotated by BRENDA team
Jajoo, S.; Mukherjea, D.; Brewer, G.J.; Ramkumar, V.
Pertussis toxin B-oligomer suppresses human immunodeficiency virus-1 Tat-induced neuronal apoptosis through feedback inhibition of phospholipase C-beta by protein kinase C
Neuroscience
151
525-532
2008
Rattus norvegicus
Manually annotated by BRENDA team
Baldanzi, G.; Alchera, E.; Imarisio, C.; Gaggianesi, M.; Dal Ponte, C.; Nitti, M.; Domenicotti, C.; van Blitterswijk, W.J.; Albano, E.; Graziani, A.; Carini, R.
Negative regulation of diacylglycerol kinase theta mediates adenosine-dependent hepatocyte preconditioning
Cell Death Differ.
17
1059-1068
2010
Rattus norvegicus
Manually annotated by BRENDA team
Kwak, H.J.; Park, K.M.; Choi, H.E.; Lim, H.J.; Park, J.H.; Park, H.Y.
The cardioprotective effects of zileuton, a 5-lipoxygenase inhibitor, are mediated by COX-2 via activation of PKC delta
Cell. Signal.
22
80-87
2010
Rattus norvegicus
Manually annotated by BRENDA team
Nakamura, K.; Yokotani, K.
Presynaptic BK type Ca(2+)-activated K(+) channels are involved in prostanoid TP receptor-mediated inhibition of noradrenaline release from the rat gastric sympathetic nerves
Eur. J. Pharmacol.
629
111-117
2010
Rattus norvegicus
Manually annotated by BRENDA team
Hansson, M.J.; Morota, S.; Teilum, M.; Mattiasson, G.; Uchino, H.; Elmer, E.
Increased potassium conductance of brain mitochondria induces resistance to permeability transition by enhancing matrix volume
J. Biol. Chem.
285
741-750
2010
Rattus norvegicus
Manually annotated by BRENDA team
Parrales, A.; Palma-Nicolas, J.P.; Lopez, E.; Lopez-Colome, A.M.
Thrombin stimulates RPE cell proliferation by promoting c-Fos-mediated cyclin D1 expression
J. Cell. Physiol.
222
302-312
2010
Rattus norvegicus
Manually annotated by BRENDA team
Jiang, H.; Cheng, D.; Liu, W.; Peng, J.; Feng, J.
Protein kinase C inhibits autophagy and phosphorylates LC3
Biochem. Biophys. Res. Commun.
395
471-476
2010
Rattus norvegicus
Manually annotated by BRENDA team
Leonard, T.A.; Rozycki, B.; Saidi, L.F.; Hummer, G.; Hurley, J.H.
Crystal structure and allosteric activation of protein kinase C betaII
Cell
144
55-66
2011
Rattus norvegicus
Manually annotated by BRENDA team
Martin, T.D.; Mitin, N.; Cox, A.D.; Yeh, J.J.; Der, C.J.
Phosphorylation by protein kinase Calpha regulates RalB small GTPase protein activation, subcellular localization, and effector utilization
J. Biol. Chem.
287
14827-14836
2012
Rattus norvegicus
Manually annotated by BRENDA team
Vargas-Lopes, C.; Madeira, C.; Kahn, S.A.; Albino do Couto, I.; Bado, P.; Houzel, J.C.; De Miranda, J.; de Freitas, M.S.; Ferreira, S.T.; Panizzutti, R.
Protein kinase C activity regulates D-serine availability in the brain
J. Neurochem.
116
281-290
2011
Rattus norvegicus
Manually annotated by BRENDA team
Williams, A.D.; Jung, S.; Poolos, N.P.
Protein kinase C bidirectionally modulates Ih and hyperpolarization-activated cyclic nucleotide-gated (HCN) channel surface expression in hippocampal pyramidal neurons
J. Physiol.
593
2779-2792
2015
Rattus norvegicus
Manually annotated by BRENDA team
Cole, T.R.; Igumenova, T.I.
Expression and purification of the N-terminal regulatory domain of protein kinase C for biophysical studies
Protein Expr. Purif.
110
14-21
2015
Rattus norvegicus
Manually annotated by BRENDA team
Qvit, N.; Disatnik, M.H.; Sho, E.; Mochly-Rosen, D.
Selective phosphorylation inhibitor of delta protein kinase C-pyruvate dehydrogenase kinase protein-protein interactions Application for myocardial injury in vivo
J. Am. Chem. Soc.
138
7626-7635
2016
Rattus norvegicus (P09215)
Manually annotated by BRENDA team