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Information on EC 2.7.11.13 - protein kinase C and Organism(s) Homo sapiens and UniProt Accession P05129

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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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Homo sapiens
UNIPROT: P05129
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
PKCgamma
isozyme
protein kinase C, gamma type
-
aPKCzeta
-
-
Calcium-dependent protein kinase C
-
-
-
-
epsilonPKC
-
-
-
-
PKC alpha
-
-
PKC beta II
-
-
PKC beta-II
-
-
PKC beta1
-
-
PKC delta
-
-
PKC epsilon
-
-
PKC eta
-
-
PKC theta
-
-
PKC-alpha/beta
-
isozyme
PKC-betaII
isozyme
PKC-delta
-
PKC-zeta
PKCalpha
PKCbeta
-
isoform
PKCbeta1
PKCbeta2
isozyme
PKCbetaII
PKCdelta
PKCepsilon
PKCeta
PKCgamma
-
isoform
PKCiota/lambda
isozyme
PKCtheta
PKCzeta
protein kinase C
protein kinase C alpha
protein kinase C delta
protein kinase C theta
-
protein kinase C, alpha type
-
protein kinase C, beta type
-
protein kinase C, D2 type
-
protein kinase C, delta type
-
protein kinase C, epsilon type
-
protein kinase C, eta type
-
protein kinase C, iota type
-
protein kinase C, mu type
-
protein kinase C, nu type
-
protein kinase C, theta type
-
protein kinase C, zeta type
-
protein kinase C-alpha
-
protein kinase C-epsilon
-
protein kinase C-like 1
-
protein kinase C-like 2
-
protein kinase Calpha
protein kinase D2
-
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 + 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 + PKC-alpha-derived peptide
ADP + phosphorylated PKC-alpha-derived peptide
show the reaction diagram
in the presence of the classical PKC activators phosphatidylserine/diacylglycerol, PKC alpha phosphorylates a PKC-alpha pseudosubstrate-derived peptide, an epidermal-growth-factor-receptor-derived peptide, histone III-S and myelin basic protein to an equal extent, whilst PKC zeta phosphorylates only the PKC-alpha-derived peptide
-
-
?
alphatomega peptide + ATP
ADP + phosphorylated-alphatomega peptide
show the reaction diagram
-
an improved PKCalpha-responsive polyion complex (PIC) to measure PKCalpha activity is reported. The polycation molecule is the poly(amidoamine) (PAMAM) dendrimer modified with both cationic PKCalpha-specific peptide substrates (alphatomega, FKKQGSFAKKK-NH2) and near infrared (NIR) fluorophores (Cy5.5), and the polyanion molecule is the quencher (BHQ-3)-modified chondroitin sulfate
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + AAKIQASFRGHMARKK
ADP + AAKIQApSFRGHMARKK
show the reaction diagram
-
-
-
-
?
ATP + ADAM17
ADP + phosphorylated ADAM17
show the reaction diagram
-
-
-
?
ATP + ADKRRSVRIGA
ADP + ADKRRpSVRIGA
show the reaction diagram
-
-
-
-
?
ATP + Akt
ADP + phosphorylated Akt
show the reaction diagram
ATP + alpha1D Ca channel
ADP + phosphorylated alpha1D Ca channel
show the reaction diagram
-
-
-
-
?
ATP + ARKRERTYSFGHHA
ADP + ARKRERTYpSFGHHA
show the reaction diagram
-
-
-
-
?
ATP + ASQKRPSQRH
ADP + ASQKRPpSQRH
show the reaction diagram
-
-
-
-
?
ATP + beta-catenin
ADP + phosphorylated beta-catenin
show the reaction diagram
-
-
-
?
ATP + calcium-independent phospholipase A2
ADP + phosphorylated calcium-independent phospholipase A2
show the reaction diagram
ATP + casein kinase 1delta
ADP + phosphorylated casein kinase 1delta
show the reaction diagram
ATP + CREB1 protein
ADP + phosphorylated CREB1 protein
show the reaction diagram
-
-
-
-
?
ATP + CTP:phosphoethanolamine cytidylyltransferase
ADP + phosphorylated CTP:phosphoethanolamine cytidylyltransferase
show the reaction diagram
-
phosphorylation at Ser215 and Ser223
-
-
?
ATP + diacylglycerol kinase-zeta
ADP + phosphorylated diacylglycerol kinase-zeta
show the reaction diagram
ATP + EF factor 1
ADP + phosphorylated EF factor 1
show the reaction diagram
-
i.e. eukaryotic translation elongation factor 1-alpha1, in vitro phosphorylation
-
-
?
ATP + extracellular signal-regulated kinase 2
ADP + phosphorylated extracellular signal-regulated kinase 2
show the reaction diagram
-
-
-
-
?
ATP + extracellular signal-related kinase
ADP + phosphorylated extracellular signal-related kinase
show the reaction diagram
-
-
-
-
?
ATP + FAFKKSFKLAG
ADP + FAFKKpSFKLAG
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 + FKLKRKGSFKKFA
ADP + FKLKRKGpSFKKFA
show the reaction diagram
-
-
-
-
?
ATP + Fyn
ADP + phosphorylated Fyn
show the reaction diagram
-
Fyn is a tyrosine protein kinase of the Src family, phosphorylation at a serine residue
-
-
?
ATP + Galpha-interacting, vesicle-associated protein
ADP + phosphorylated-Galpha-interacting, vesicle-associated protein
show the reaction diagram
-
PKCtheta, down-regulates Galpha-interacting, vesicle-associated protein (GIV's) guanine exchange factor, GEF function by phosphorylating Ser-1689 located within GIV's GEF motif. PKCtheta specifically binds and phosphorylates GIV at S1689, and this phosphoevent abolishes GIV's ability to bind and activate trimeric G proteins Galphai
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
show the reaction diagram
PKD2 activated by phorbol esters efficiently phosphorylate the exogenous substrate histone H1
-
-
?
ATP + histone H2
ADP + phosphorylated histone H2
show the reaction diagram
-
in vitro phosphorylation
-
-
?
ATP + histone H3
ADP + phosphorylated histone H3
show the reaction diagram
-
in vitro phosphorylation
-
-
?
ATP + inhibitory killer cell Ig-like receptor
ADP + phosphorylated inhibitory killer cell Ig-like receptor
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 + IRS
ADP + phosphorylated IRS
show the reaction diagram
-
isozymes PKCalpha and PKCdelta, phosphorylation on Ser307
-
-
?
ATP + IVRKATLRRLL
ADP + IVRKApTLRRLL
show the reaction diagram
-
-
-
-
?
ATP + KFKRPTLRRVR
ADP + KFKRPpTLRRVR
show the reaction diagram
-
-
-
-
?
ATP + KKKRFSFKKAF
ADP + KKKRFpSFKKAF
show the reaction diagram
-
-
-
-
?
ATP + KLAGFSFKKNK
ADP + KLAGFpSFKKNK
show the reaction diagram
-
-
-
-
?
ATP + KPCB protein
ADP + phosphorylated KPCB protein
show the reaction diagram
-
-
-
-
?
ATP + lamin A
ADP + phosphorylated lamin A
show the reaction diagram
-
a nuclear membrane protein, isozyme PKCalpha
-
-
?
ATP + lamin C
ADP + phosphorylated lamin C
show the reaction diagram
-
a nuclear membrane protein, isozyme PKCalpha, phosphorylation at Ser572
-
-
?
ATP + LLRMFSFKAPA
ADP + LLRMFpSFKAPA
show the reaction diagram
-
-
-
-
?
ATP + metabotropic glutamate receptor 5
ADP + phosphorylated metabotropic glutamate receptor 5
show the reaction diagram
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
show the reaction diagram
-
-
-
?
ATP + myristoylated alanine-rich C kinase substrate
ADP + phosphorylated myristoylated alanine-rich C kinase substrate
show the reaction diagram
-
a major PKC substrate
-
-
?
ATP + myristoylated alanine-rich C-kinase (152-164)
ADP + phosphorylated myristoylated alanine-rich C-kinase (152-164)
show the reaction diagram
-
-
-
-
?
ATP + NADPH oxidase
ADP + phosphorylated NADPH oxidase
show the reaction diagram
-
-
-
-
?
ATP + NRFARKGSLRQKNV
ADP + NRFARKGpSLRQKNV
show the reaction diagram
-
-
-
-
?
ATP + phosphoinositide-dependent kinase
ADP + phosphorylated phosphoinositide-dependent kinase
show the reaction diagram
ATP + phospholipase D1
ADP + phosphorylated phospholipase D1
show the reaction diagram
-
phosphorylation by PKC
-
-
?
ATP + phospholipase D2
ADP + phosphorylated phospholipase D2
show the reaction diagram
-
phosphorylation by PKCalpha
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
ATP + protein kinase CK2alpha
ADP + phosphorylated protein kinase CK2alpha
show the reaction diagram
-
phosphorylation at serines 194 and 277
-
-
?
ATP + protein kinase CK2beta
ADP + phosphorylated protein kinase CK2beta
show the reaction diagram
-
phosphorylation at serine 148
-
-
?
ATP + RFARKGSLRQKNV
ADP + phoshorylated RFARKGSLRQKNV
show the reaction diagram
-
a commercially available peptide substrate
-
-
?
ATP + RFARKGSLRQKNV
ADP + phosphorylated RFARKGSLRQKNV
show the reaction diagram
-
-
-
-
?
ATP + RFARKGSLRQKNV
ADP + RFARKGphosphoSLRQKNV
show the reaction diagram
-
synthetic peptide substrate
-
-
?
ATP + RRFKRQGSFFYFF
ADP + RRFKRQGpSFFYFF
show the reaction diagram
-
-
-
-
?
ATP + RRRRSIIFI
ADP + RRRRpSIIFI
show the reaction diagram
-
-
-
-
?
ATP + RVVGGSLRGAQ
ADP + RVVGGpSLRGAQ
show the reaction diagram
-
-
-
-
?
ATP + transient receptor potential protein V4
ADP + phosphorylated transient receptor potential protein vanilloid 4
show the reaction diagram
-
-
-
-
?
ATP + transient receptor potential protein vanilloid 1
ADP + phosphorylated transient receptor potential protein vanilloid 1
show the reaction diagram
-
-
-
-
?
ATP + vascular endothelial growth factor receptor 2
ADP + phosphorylated vascular endothelial growth factor receptor 2
show the reaction diagram
-
phosphorylation at Ser1188 and Ser 1191
-
-
?
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
-
-
?
ATP + [low density lipoprotein receptor-related protein]
ADP + phosphorylated [low density lipoprotein receptor-related protein]
show the reaction diagram
N6-phenyl-ATP + RFARKGSLRQKNV
N6-phenyl-ADP + RFARKGphosphoSLRQKNV
show the reaction diagram
-
synthetic peptide substrate, recombinant isozyme PKCalpha mutant M417A
-
-
?
Rab11 + ATP
ADP + phosphorylated Rab11
show the reaction diagram
-
Rab11 is differentially phosphorylated in vitro by several purified PKC isoenzymes. Ser 177 is identified as the single PKC-phosphorylated residue in Rab11
-
-
?
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 + beta-catenin
ADP + phosphorylated beta-catenin
show the reaction diagram
-
-
-
?
ATP + calcium-independent phospholipase A2
ADP + phosphorylated calcium-independent phospholipase A2
show the reaction diagram
-
PKC regulates membrane-associated, calcium-independent phospholipase A2 in coronary artery endothelial cells in competition to thrombin, overview
-
-
?
ATP + casein kinase 1delta
ADP + phosphorylated casein kinase 1delta
show the reaction diagram
-
phosphorylation at Ser328, Thr329, and Ser370
-
-
?
ATP + CTP:phosphoethanolamine cytidylyltransferase
ADP + phosphorylated CTP:phosphoethanolamine cytidylyltransferase
show the reaction diagram
-
phosphorylation at Ser215 and Ser223
-
-
?
ATP + diacylglycerol kinase-zeta
ADP + phosphorylated diacylglycerol kinase-zeta
show the reaction diagram
-
the enzyme, especially isozyme PKCalpha, inhibits binding of diacylglycerol kinase-zeta to the retinoblastoma protein
-
-
?
ATP + inhibitory killer cell Ig-like receptor
ADP + phosphorylated inhibitory killer cell Ig-like receptor
show the reaction diagram
-
the enzyme regulates expression and function of inhibitory killer cell Ig-like receptors in NK cells, KIR negatively regulate NK cell cytotoxicity by activating Src homology 2 domain-containing protein tyrsine phospatase 1 and 2, overview
-
-
?
ATP + metabotropic glutamate receptor 5
ADP + phosphorylated metabotropic glutamate receptor 5
show the reaction diagram
-
isozyme-specific phosphorylation of metabotropic glutamate receptor 5 by PKCdelta blocks Ca2+ oscillation and oscillatory translocation of Ca2+-dependent PKCgamma
-
-
?
ATP + NADPH oxidase
ADP + phosphorylated NADPH oxidase
show the reaction diagram
-
-
-
-
?
ATP + phosphoinositide-dependent kinase
ADP + phosphorylated phosphoinositide-dependent kinase
show the reaction diagram
-
phosphoinositide-dependent kinases are conserved substrates of PKC
-
-
?
ATP + protein kinase CK2alpha
ADP + phosphorylated protein kinase CK2alpha
show the reaction diagram
-
phosphorylation at serines 194 and 277
-
-
?
ATP + protein kinase CK2beta
ADP + phosphorylated protein kinase CK2beta
show the reaction diagram
-
phosphorylation at serine 148
-
-
?
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
-
-
?
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
N6-phenyl-ATP
-
preferred by PKCalpha mutant M417A to phosphorylate peptide and protein substrates, no activity with the wild-type PKCalpha
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activity is independent of Ca2+
Cd2+
-
cell exposure to 0.020 mM cadmium for 24 h results in PKC activation
Mn2+
-
-
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-2-[(2S)-4-[5-chloro-6-(1H-pyrazolo[3,4-b]pyridin-3-yl)pyridin-2-yl]piperazin-2-yl]-3-methylbutan-2-ol
-
(2R)-N1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
-
-
1,1'-(1,10-decanediyl)bis[1-amino isoquinolinium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[2-amino-1-methylbenzimidazolium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[2-methylbenzothiazolium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[2-methylbenzoxazolium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[2-methylquinolinium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[4-amino-2-methyl quinolinium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[4-aminoquinolinium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[4-N,N,dimethylaminoquinolinium] diiodide
-
-
1,1'-(1,10-decanediyl)bis[quinolinium] diiodide
-
-
1,1'-decane-1,10-diylbis(4-aminopyridinium) diiodide
-
-
1,1'-decane-1,10-diylbis[4-(dimethylamino)pyridinium]
-
-
1,6-bis[N-(1-methylquinolinium-2-methyl)amino]-hexane diiodide
-
-
1-(1,4-diazepan-1-yl)-3-(pyridin-4-yl)-2,6-naphthyridine
-
-
1-(piperazin-1-yl)-3-(pyridin-4-yl)-2,6-naphthyridine
-
-
1-methoxypropan-2-yl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 49%
1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]piperidin-3-amine
-
-
1-[3-chloro-6-(1,4-diazepan-1-yl)pyridin-2-yl]-7-ethoxy-1,3-dihydro-2H-imidazo[4,5-b]pyridin-2-one
-
15-chloro-11-methyl-8,9,10,11-tetrahydro-7H-16,12-(azeno)-6-oxa-2,3,11,16a-tetraazacyclotetradeca[1,2,3-cd]inden-1(2H)-one
-
2,7,11-triamino-3,6,13-trihydroxy-5-methyl-6,7,8,9,15,16-hexahydro-5H,14H-5,9-epoxy-4b,9a,15-triazadibenzo[b,h]cyclonona[1,2,3,4-jkl]cyclopenta[e]-as-indacen-14-one
-
-
2,7,11-triamino-3,6-dihydroxy-5-methyl-6,7,8,9,15,16-hexahydro-5H,14H-5,9-epoxy-4b,9a,15-triazadibenzo[b,h]cyclonona[1,2,3,4-jkl]cyclopenta[e]-as-indacen-14-one
-
-
2,7-diamino-3,6,13-trihydroxy-5-methyl-6,7,8,9,15,16-hexahydro-5H,14H-5,9-epoxy-4b,9a,15-triazadibenzo[b,h]cyclonona[1,2,3,4-jkl]cyclopenta[e]-as-indacen-14-one
-
-
2,7-diamino-3,6-dihydroxy-5-methyl-6,7,8,9,15,16-hexahydro-5H,14H-5,9-epoxy-4b,9a,15-triazadibenzo[b,h]cyclonona[1,2,3,4-jkl]cyclopenta[e]-as-indacen-14-one
-
-
2-(2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-1-yl)-6-(2-phenylpiperazin-1-yl)pyridine-3-carbonitrile
-
2-([3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]amino)ethanol
-
-
2-([3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]oxy)ethanamine
-
-
2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carbonitrile
-
0.03 mM, inhibition: 87%
2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylic acid
-
0.03 mM, inhibition: 65%
2-fluorobenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
2-methoxyethyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 57%
2-methyl-6-(phenylethynyl)-pyridine
-
complete inhibition of PKCgamma oscillation at 0.05 mM
2-methyl-N1-[3-(3-methylpyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
-
-
2-methyl-N1-[3-(pyridin-3-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
-
-
2-methyl-N1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
-
-
2-methylbenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 64%
3-(1-(3-(dimethylamino)propyl)-2-methyl-1H-indol-3-yl)-4-(2-methyl-1H-indol-3-yl)-1H-pyrrole-2,5-dione
-
a bisindolylmaleimide analogue of BIM-1 inhibitor
3-cyanobenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 70%
3-methoxybenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
3-methylbenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 67%
3-phenyl-N1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
-
-
3-[1-[3-(dimethylamino)propyl]-5-methoxy-1H-indol-3-yl]-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dione
-
Go6983, PKC-specific inhibitor, complete inhibition at 500 nM
4-amino-1,2-dimethylquinolinium
-
-
4-amino-1-decyl-2-methylquinolinium iodide
-
-
4-cyanobenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 10%
4-fluorobenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 2%
4-methylbenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 50%
4-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]piperazin-2-one
-
-
alsterpaullone
-
7% inhibition of PKCalpha at 0.01 mM
arachidonoyl fluoromethylketone
-
inhibition of PKCgamma oscillation at 0.1 mM
AVGPRPQT
-
-
benzyl 2-amino-4-(1,3-benzodioxol-5-yl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 85%
benzyl 2-amino-4-(2-fluoro-4-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 78%
benzyl 2-amino-4-(2-fluorophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 57%
benzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
benzyl 2-amino-4-(3-cyanophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 25%
benzyl 2-amino-4-(3-fluorophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 53%
benzyl 2-amino-4-(3-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 57%
benzyl 2-amino-4-(3-methylphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 68%
benzyl 2-amino-4-(4-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 86%
benzyl 2-amino-4-(4-methylphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 60%
benzyl 2-amino-4-[3-(trifluoromethyl)phenyl]thiophene-3-carboxylate
-
0.03 mM, inhibition: 29%
benzyl 2-amino-4-[4-(trifluoromethyl)phenyl]thiophene-3-carboxylate
-
0.03 mM, inhibition: 21%
bisindolylmaleimide
-
strong inhibition of PKCalpha
bisindolylmaleimide derivatives
-
-
bisindolylmaleimide I
bromoerol lactone
-
slight inhibition of PKCgamma oscillation at 0.1 mM
calphostin C
-
PKC-specific inhibitor
CG53353
-
inhibitor of isozyme PKCbetaII
compound 48/80
-
complete inhibition of PKCgamma oscillation at 0.1 mM
CRLVLASC
-
targets isozyme PKCgamma, blocks formalin-induced pain response
cytochalasine D
-
inhibition of PKCgamma oscillation at 0.01 mM
EAVSLKPT
-
targets isozyme PKCepsilon, reverses psi epsilonRACK-mediated protection, and decreases formalin-induced pain response
enzastaurin
-
oral serine/threonine kinase inhibitor
ethanol
-
0.03%, inhibition of PKCgamma oscillation at 0.1 mM
ethyl 2-(carbamoylamino)-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 14%
ethyl 2-amino-4-(1,3-benzodioxol-5-yl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 2-amino-4-(2-fluoro-4-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 2-amino-4-(2-fluorophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 62%
ethyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 2-amino-4-(3-cyanophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 32%
ethyl 2-amino-4-(3-fluoro-4-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 2-amino-4-(3-fluorophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 38%
ethyl 2-amino-4-(3-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 82%
ethyl 2-amino-4-(3-methylphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 77%
ethyl 2-amino-4-(4-aminophenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 2-amino-4-(4-methoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 2-amino-4-(4-methylphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 80%
ethyl 2-amino-4-[3-(trifluoromethyl)phenyl]thiophene-3-carboxylate
ethyl 2-amino-4-[4-(dimethylamino)phenyl]thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
ethyl 4-(3,4-dimethoxyphenyl)-2-(dimethylamino)thiophene-3-carboxylate
-
0.03 mM, inhibition: 60%
ethyl 4-(3,4-dimethoxyphenyl)-2-(methylamino)thiophene-3-carboxylate
-
0.03 mM, inhibition: 32%
ethyl 4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 3%
FLLDPY
-
-
FNGLLKIKI
-
protects from cardiac ischaemic injury
FTRKRQRAMRRVHQ
-
autoregulatory pseudosubstrate sequence, residues 24-40, lung enzyme
GF 109203X
GF109203X
Go-6983
-
isoform PKCalpha-specific inhibitor
Goe6976
-
-
Goe6983
-
-
Gö 6976
-
slight inhibition of PKCalpha
Gö 6983
-
-
Gö6976
-
-
HDAPIGYD
-
protects from cardiac ischaemic injury, from graft coronary artery disease, and activates potassium current, inhibits sodium current
indirubin-3'-monoxime
-
32% inhibition of PKCalpha at 0.01 mM
K-252a
-
strong inhibition
KGDYEKILVALCGGN
-
targets isozyme PKCbeta
KLFIMNL
-
targets isozyme PKCbetaI, inhibits cardiomyocyte hypertrophy
KQKTKTIK T
-
targets isozyme PKCbeta
LEPEGK
-
-
MDPNGLSDPYVKL
-
targets isozyme PKCbeta, blocks Ca2+ current
MRAAEDPM
-
increased injury from cardiac ischaemia
myr-PKC 19-27
-
specific protein kinase C inhibitor
N,N,N,N',N',N'-hexaethyldecane-1,10-diaminium
-
-
N-(5'-([(3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-4',5'-dihydro-1'H-spiro[cyclopropane-1,6'-pyrrolo[3,4-c]pyrazol]-3'-yl)pyridine-2-carboxamide
-
-
N-(5-([(2S)-2-benzyl-4-methylpiperazin-1-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)-3-phenoxybenzamide
-
-
N-(5-([(2S)-2-benzyl-4-methylpiperazin-1-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)benzamide
-
-
N-(5-([(3S,7S,8aS)-7-fluoro-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-(5-([(3S,8aS)-3-ethylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-(5-([(3S,8aS)-7,7-difluoro-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-(5-([(8aS)-3,3-dimethylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-(6,6-dimethyl-5-([(3R,8aR)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
0.001 mM, 13% inhibition
N-(6,6-dimethyl-5-([(3R,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
0.001 mM, 24% inhibition
N-(6,6-dimethyl-5-([(3S,8aR)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-(6,6-dimethyl-5-([(3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-(6,6-dimethyl-5-[(4-methylpiperazin-1-yl)carbonyl]-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)benzamide
-
-
N-(6-ethyl-6-methyl-5-([(3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
-
N-cyclohexa-1,3-dien-1-yl-N,N,N',N',N'-pentaphenyldecane-1,10-diaminium
-
-
N-methyl-N'-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]ethane-1,2-diamine
-
-
N-methyl-N-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]ethane-1,2-diamine
-
-
N-[2-(pyridin-4-yl)pyrido[3,4-d]pyrimidin-4-yl]ethane-1,2-diamine
-
-
N-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]ethane-1,2-diamine
-
-
N-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,3-diamine
-
-
N-[3-(pyridin-4-yl)-2,7-naphthyridin-1-yl]ethane-1,2-diamine
-
-
N-[3-(pyridin-4-yl)isoquinolin-1-yl]ethane-1,2-diamine
-
-
N-[5-(hexahydropyrrolo[1,2-a]pyrazin-2(1H)-ylcarbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl]benzamide
-
-
N-[7-(pyridin-4-yl)-1,6-naphthyridin-5-yl]ethane-1,2-diamine
-
-
N-[7-(pyridin-4-yl)isoquinolin-5-yl]ethane-1,2-diamine
-
-
N1-(3-[2-(propan-2-ylamino)pyridin-4-yl]-2,6-naphthyridin-1-yl)-2-methylpropane-1,2-diamine
-
-
N1-[3-(2-aminopyridin-4-yl)-2,6-naphthyridin-1-yl]-2-methylpropane-1,2-diamine
-
-
N1-[3-(3-chloropyridin-4-yl)-2,6-naphthyridin-1-yl]-2-methylpropane-1,2-diamine
-
-
N1-[3-(3-fluoropyridin-4-yl)-2,6-naphthyridin-1-yl]-2-methylpropane-1,2-diamine
-
-
NGRKI
-
-
PAWHD
-
-
phenyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 48%
propan-2-yl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 100%
propidiumiodide
-
-
PYIALNVD
-
-
pyridin-4-ylmethyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
-
0.03 mM, inhibition: 53%
QEVIRNN
-
targets isozyme PKCbetaII, inhibits cardiomyocyte hypertrophy and activates potassium channels
RACK1 peptide I homologue
-
-
-
Ro-31-7549
specific inhibitor for isozyme PKCalpha
Ro-31-8220
-
strong inhibition of PKCalpha
Ro-31-8425
-
-
rottlerin
safranine O
-
-
SFNSYELGSL
-
targets isozyme PKCdelta, protects from cardiac ischaemic injury, from cerebral injury, from graft coronary artery disease, and increases fibroblast proliferation
SIKIWD
-
targets isozyme PKCbeta
SIYRRGARRWRKLYRAN
-
targets isozyme PKCzeta, which leads to inhibition of fibroblast proliferation
SLNPEWNE
-
targets isozyme PKCbeta
SRIGQ
-
-
staurosporine
thapsigargin
-
complete inhibition of PKCgamma oscillation at 0.005 mM
Tween 80
-
inhibits the enzyme at high concentration
[2-amino-4-(3,4-dimethoxyphenyl)thiophen-3-yl][(benzylamino)oxy]methanone
-
0.03 mM, inhibition: 43%
[2-amino-4-(3,4-dimethoxyphenyl)thiophen-3-yl][(ethylamino)oxy]methanone
-
0.03 mM, inhibition: 50%
[2-amino-4-(3,4-dimethoxyphenyl)thiophen-3-yl]{[(2-methoxyethyl)amino]oxy}methanone
-
0.03 mM, inhibition: 55%
[2-amino-4-(3,4-dimethoxyphenyl)thiophen-3-yl]{[(pyridin-4-ylmethyl)amino]oxy}methanone
-
0.03 mM, inhibition: 3%
{3-[5-amino-4-(ethoxycarbonyl)thiophen-3-yl]phenyl}carbamate
-
0.03 mM, inhibition: 89%
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arachidonic acid
alone or a combination of gamma-linolenic acid and phosphatidylserine slightly enhances PKC zeta activity
diacylglycerol
plus phosphatidylserine, activates
phosphatidylserine
plus diacylglycerol, activates
1,2-diacyl-sn-glycerol
-
-
1,2-dioleoyl-sn-glycerol
-
activates
12-O-Tetradecanoylphorbol 13-acetate
12-O-tetradecanoylphorbol-13-acetate
-
-
4beta-phorbol 12-myristate 13-acetate
arachidonic acid
slightly enhances PKC zeta activity
CSF-1
-
CSF-1 increases PKCgamma Thr 410 phosphorylation and kinase activity in 32D.R cells
-
diacylglycerol
fatty acids
-
activation mechanism
gamma-linolenic acid
a combination of gamma-linolenic acid and phosphatidylserine slightly enhances PKC zeta activity
gastrin
physiological activator of PKD2 in human AGS-B cells stably transfected with the CCK(B)/gastrin receptor
hypericin
-
competes with 12-O-tetradecanoylphorbol 13-acetate for binding to the regulatory domain of PKC, localization of PKC isozymes alpha, delta, and gamma, high affinty binding and interaction witht he C1B domain of PKC, molecular modeling
Insulin
-
activates PKC isozymes alpha, betaII, delta, and zeta in several cell types, activation mechanism
-
ionomycin
-
-
kenpaullone
-
20% activation of PKCalpha at 0.01 mM
phorbol 12,13-dibutyrate
-
-
phorbol 12-myristate 13-acetate
Phorbol esters
bind to and stimulate the kinase activity of PKC-L
phorbol-ester-12-13-dibutyrate
-
phosphatidylserine
Phospholipids
-
regulatory function for isozymes alpha, betaI, betaII, gamma, delta, epsilon, eta, and theta
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0347
FKKQGSFAKKK
isozyme PKCgamma, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C
0.00009141 - 0.0828
ATP
0.01561
casein kinase 1delta
at pH 7.5 and 30°C
-
0.0166 - 0.0599
FKKQGSFAKKK
0.0124
N6-phenyl-ATP
-
pH 7.4, 37°C, recombinant isozyme PKCalpha mutant M417A
additional information
additional information
-
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000338
N-(5'-([(3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-4',5'-dihydro-1'H-spiro[cyclopropane-1,6'-pyrrolo[3,4-c]pyrazol]-3'-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000541
N-(5-([(2S)-2-benzyl-4-methylpiperazin-1-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)-3-phenoxybenzamide
-
pH and temperature not specified in the publication
0.000189
N-(5-([(2S)-2-benzyl-4-methylpiperazin-1-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)benzamide
-
pH and temperature not specified in the publication
0.000109
N-(5-([(3S,7S,8aS)-7-fluoro-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000046
N-(5-([(3S,8aS)-3-ethylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.01
N-(5-([(3S,8aS)-7,7-difluoro-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000125
N-(5-([(8aS)-3,3-dimethylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000092
N-(6,6-dimethyl-5-([(3S,8aR)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000029
N-(6,6-dimethyl-5-([(3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000541
N-(6,6-dimethyl-5-[(4-methylpiperazin-1-yl)carbonyl]-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)benzamide
-
pH and temperature not specified in the publication
0.000062
N-(6-ethyl-6-methyl-5-([(3S,8aS)-3-methylhexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]carbonyl)-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl)pyridine-2-carboxamide
-
pH and temperature not specified in the publication
0.000131
N-[5-(hexahydropyrrolo[1,2-a]pyrazin-2(1H)-ylcarbonyl)-6,6-dimethyl-1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazol-3-yl]benzamide
-
pH and temperature not specified in the publication
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000002 - 0.000829
(2R)-N1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
0.03
1,1'-(1,10-decanediyl)bis[1-amino isoquinolinium] diiodide
Homo sapiens
-
pH 7.4
0.014
1,1'-(1,10-decanediyl)bis[2-amino-1-methylbenzimidazolium] diiodide
Homo sapiens
-
pH 7.4
0.017
1,1'-(1,10-decanediyl)bis[2-methylbenzothiazolium] diiodide
Homo sapiens
-
pH 7.4
0.036
1,1'-(1,10-decanediyl)bis[2-methylbenzoxazolium] diiodide
Homo sapiens
-
pH 7.4
0.022
1,1'-(1,10-decanediyl)bis[2-methylquinolinium] diiodide
Homo sapiens
-
pH 7.4
0.007
1,1'-(1,10-decanediyl)bis[4-amino-2-methyl quinolinium] diiodide
Homo sapiens
-
pH 7.4
0.03
1,1'-(1,10-decanediyl)bis[4-aminoquinolinium] diiodide
Homo sapiens
-
pH 7.4
0.029
1,1'-(1,10-decanediyl)bis[4-N,N,dimethylaminoquinolinium] diiodide
Homo sapiens
-
pH 7.4
0.072
1,1'-(1,10-decanediyl)bis[quinolinium] diiodide
Homo sapiens
-
pH 7.4
0.112
1,1'-decane-1,10-diylbis(4-aminopyridinium) diiodide
Homo sapiens
-
pH 7.4
0.231
1,1'-decane-1,10-diylbis[4-(dimethylamino)pyridinium]
Homo sapiens
-
pH 7.4
0.03
1,6-bis[N-(1-methylquinolinium-2-methyl)amino]-hexane diiodide
Homo sapiens
-
pH 7.4
0.000004 - 0.000661
1-(1,4-diazepan-1-yl)-3-(pyridin-4-yl)-2,6-naphthyridine
0.000006 - 0.001
1-(piperazin-1-yl)-3-(pyridin-4-yl)-2,6-naphthyridine
0.000008 - 0.000865
1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]piperidin-3-amine
0.000000086
1-[3-chloro-6-(1,4-diazepan-1-yl)pyridin-2-yl]-7-ethoxy-1,3-dihydro-2H-imidazo[4,5-b]pyridin-2-one
Homo sapiens
pH and temperature not specified in the publication
0.00000087
15-chloro-11-methyl-8,9,10,11-tetrahydro-7H-16,12-(azeno)-6-oxa-2,3,11,16a-tetraazacyclotetradeca[1,2,3-cd]inden-1(2H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0000063
2-(2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-1-yl)-6-(2-phenylpiperazin-1-yl)pyridine-3-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.000081 - 0.001
2-([3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]amino)ethanol
0.000082 - 0.001
2-([3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]oxy)ethanamine
0.000052 - 0.001
2-methyl-N1-[3-(3-methylpyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
0.001
2-methyl-N1-[3-(pyridin-3-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
Homo sapiens
-
value higher than, pH and temperature not specified in the publication
0.000009 - 0.000967
2-methyl-N1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
0.005
3-methoxybenzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000403 - 0.001
3-phenyl-N1-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,2-diamine
3.59
4-amino-1,2-dimethylquinolinium
Homo sapiens
-
pH 7.4
0.117
4-amino-1-decyl-2-methylquinolinium iodide
Homo sapiens
-
pH 7.4
0.000735 - 0.001
4-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]piperazin-2-one
0.006
benzyl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0075
bisindolylmaleimide I
Homo sapiens
-
pH not specified in the publication, 30°C
0.002
ethyl 2-amino-4-(1,3-benzodioxol-5-yl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.004
ethyl 2-amino-4-(2-fluoro-4-methoxyphenyl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.001
ethyl 2-amino-4-(4-aminophenyl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.002
ethyl 2-amino-4-(4-methoxyphenyl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0025
Gö 6983
Homo sapiens
-
pH not specified in the publication, 30°C
0.25
N,N,N,N',N',N'-hexaethyldecane-1,10-diaminium
Homo sapiens
-
pH 7.4
0.094
N-cyclohexa-1,3-dien-1-yl-N,N,N',N',N'-pentaphenyldecane-1,10-diaminium
Homo sapiens
-
pH 7.4
0.000079 - 0.001
N-methyl-N'-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]ethane-1,2-diamine
0.000024 - 0.001
N-methyl-N-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]ethane-1,2-diamine
0.000027 - 0.001
N-[2-(pyridin-4-yl)pyrido[3,4-d]pyrimidin-4-yl]ethane-1,2-diamine
0.000005 - 0.0009
N-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]ethane-1,2-diamine
0.00001 - 0.000779
N-[3-(pyridin-4-yl)-2,6-naphthyridin-1-yl]propane-1,3-diamine
0.001
N-[3-(pyridin-4-yl)-2,7-naphthyridin-1-yl]ethane-1,2-diamine
Homo sapiens
-
value higher than, pH and temperature not specified in the publication
0.000743 - 0.001
N-[3-(pyridin-4-yl)isoquinolin-1-yl]ethane-1,2-diamine
0.000401 - 0.001
N-[7-(pyridin-4-yl)-1,6-naphthyridin-5-yl]ethane-1,2-diamine
0.000044 - 0.001
N-[7-(pyridin-4-yl)isoquinolin-5-yl]ethane-1,2-diamine
0.000862 - 0.001
N1-(3-[2-(propan-2-ylamino)pyridin-4-yl]-2,6-naphthyridin-1-yl)-2-methylpropane-1,2-diamine
0.00006 - 0.001
N1-[3-(2-aminopyridin-4-yl)-2,6-naphthyridin-1-yl]-2-methylpropane-1,2-diamine
0.000015 - 0.001
N1-[3-(3-chloropyridin-4-yl)-2,6-naphthyridin-1-yl]-2-methylpropane-1,2-diamine
0.000018 - 0.001
N1-[3-(3-fluoropyridin-4-yl)-2,6-naphthyridin-1-yl]-2-methylpropane-1,2-diamine
0.006
propan-2-yl 2-amino-4-(3,4-dimethoxyphenyl)thiophene-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.016
propidiumiodide
Homo sapiens
-
pH 7.4
0.000008
Ro-31-8425
Homo sapiens
-
pH 7.3, 25°C
0.048
safranine O
Homo sapiens
-
pH 7.4
0.00023
staurosporine
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.3
-
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
assay at room temperature
22
-
assay at room temperature
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
AGS-B cell
Manually annotated by BRENDA team
shows higher levels of PKCalpha than normal breast tissue
Manually annotated by BRENDA team
-
high expression of isozyme PKCalpha in most cell lines, overview
Manually annotated by BRENDA team
-
isozyme PKCgamma
Manually annotated by BRENDA team
-
recombinant PKCalpha
Manually annotated by BRENDA team
-
from normal sigmoid colon
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
follicular lymphoma cell line
Manually annotated by BRENDA team
-
follicular lymphoma cell line
Manually annotated by BRENDA team
-
diffuse large B-cell lymphoma cell line
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
myeloma cell line
Manually annotated by BRENDA team
-
diffuse large B-cell lymphoma cell line
Manually annotated by BRENDA team
-
precursor T-lymphoblastic leukemia cell line
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
diffuse large B-cell lymphoma cell line
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
shows higher levels of PKCalpha than normal liver tissue
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
myeloid progenitor cell line 32D.R
Manually annotated by BRENDA team
-
isozyme PKCbetaII
Manually annotated by BRENDA team
-
Burkitt lymphoma cell line
Manually annotated by BRENDA team
-
isozyme PKCalpha
Manually annotated by BRENDA team
-
fibroblast cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
activated PKCbetaII and PKCbetaI are translocated from cytosol, juxtanuclear location, isozyme-specific translocation of PKCbetaII and not PKCbetaI to a juxtanuclear subset of recycling endosomes, involvement of phospholipase D
Manually annotated by BRENDA team
-
localization of PKC isozymes alpha, delta, and gamma, is influenced by hypericin, high affinity binding and interaction with the C1B domain of PKC, molecular modeling
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPCG_HUMAN
697
0
78448
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103925
x * 103925, calculation from nucleotide sequence
105000
x * 105000, SDS-PAGE
120000
x * 120000, SDS-PAGE
65000
x * 65000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
PKC domain composition
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant isozyme PKCbetaII catalytic domain, residues 321-673, hanging drop vapour diffusion method, 8 mg/ml protein in 0.1 M acetamidoiminodiacetic acid, pH 6.5, and 1.7-2.3 M sodium acetate, 19°C, X-ray diffraction structure determination and analysis at 3.2 A resolution, molecular replacement, modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K368D
-
site-directed mutagenesis of isozyme PKCalpha ATP-binding site, a dominant-negative mutant
K371R
-
site-directed mutagenesis, inactive isozyme PKCbetaII mutant
M417A
-
site-directed mutagenesis, utilizes the alternate cofactor N6-phenyl-ATP
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of the PKC-zeta isoenzyme
FLAG M2 affinity resin column chromatography
recombinant full-length enzyme by nickel affinity chromatography, proteolytic clevage of the recombinant full-length enzyme to obtain the catalytic domain, followed by anion exchange chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in recombinant baculovirus-infected insect cells
co-expression of PKC isozymes and insulin in HEK-293 or CHO cells, interaction analysis, overview
-
expressed in COS-7 cells
expressed in HEK-293 cells and human-derived rhabdhomyosarcoma cells
expressed in HeLa cells
-
expressed in Sf9 insect cells
expression in COS cells
expression in COS1 cells
expression in COS7 cells
expression in recombinant baculovirus-infected insect cells, overexpression in NIH 3T3 cells or insect cells
expression in the baculovirus insect-cell expression system
expression of FLAG-tagged wild-type and mutant isozyme PLCalpha in MCF-10A human breast epithelial cells
-
expression of full-length His-tagged isoform PKCbetaII in Spodoptera frugiperda Sf21 cells
-
expression of GFP-tagged PKC
-
expression of GFP-tagged wild-type PKC isozymes in HEK-293 cells, and of GFP-tagged PKCgamma wild-type and mutants lacking the C1 or C2 domain in HEK-293 cells
-
expression of wild-type and mutant isoyzem PKCalpha in COS-7 cells, co-expression of PKCalpha with diacylglycerol kinase-zeta and retinoblastoma protein in COS-7 cells
-
isolation of cDNA
isozymes PKCbetaII and PKCbetaI are products of alternative splicing of gene PKCbeta, expression of GFP- or HA-tagged isozymes PKCbetaII, wild-type and mutant, and PKCbetaI in HEK-293 or HeLa cells
-
protein kinase C-epsilon E1 and E2, expression in Sf9 cells, the recombinant protein displays protein kinase C activity and phorbol ester binding activity
the 5' segment of the gene for protein kinase C beta is cloned from a human leukocyte genomic library in EMBL3 bacteriophage
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
knockdown of diacylglycerol kinase delta enhances PKCalpha activity
-
prolonged PKC activation by phorbol esters is downregulates PKC for at least 24 h
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
a phase II trial of enzastaurin is conducted to determine the 6-month progression-free survival rate in advanced non-small-cell lung cancer using Enzaustaurin: 13% of the patients have a progression-free survival for more than 6 months
molecular biology
-
a technique is developed to detect PKCalpha activity in a cancerous cell lysate through the simple measurement of fluorescence intensity. The principle of this methodology is based on a fluorescence increase associated with polyion complex dissociation due to phosphorylation by PKCalpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kemp, B.E.; Pearson, R.B.; House, M.
Pseudosubstrate-based peptide inhibitors
Methods Enzymol.
201
287-304
1991
Saccharomyces cerevisiae, Drosophila melanogaster, eukaryota, Homo sapiens
Manually annotated by BRENDA team
Sturany, S.; Van Lint, J.; Muller, F.; Wilda, M.; Hameister, H.; Hocker, M.; Brey, A.; Gern, U.; Vandenheede, J.; Gress, T.; Adler, G.; Seufferlein, T.
Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases
J. Biol. Chem.
276
3310-3318
2001
Homo sapiens (Q9BZL6), Homo sapiens
Manually annotated by BRENDA team
Zhang, Q.H.; Ye, M.; Wu, X.Y.; et al.
Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells
Genome Res.
10
1546-1560
2000
Homo sapiens (Q9BZL6)
Manually annotated by BRENDA team
Hayashi, A.; Seki, N.; Hattori, A.; Kozuma, S.; Saito, T.
PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu
Biochim. Biophys. Acta
1450
99-106
1999
Homo sapiens (O94806), Homo sapiens
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
Dryja, T.P.; McEvoy, J.; McGee, T.L.; Berson, E.L.
No mutations in the coding region of the PRKCG gene in three families with retinitis pigmentosa linked to the RP11 locus on chromosome 19q
Am. J. Hum. Genet.
65
926-928
1999
Homo sapiens (P05129)
Manually annotated by BRENDA team
Al-Maghtheh, M.; Vithana, E.N.; Inglehearn, C.F.; Moore, T.; Bird, A.C.; Bhattacharya, S.S.
Segregation of a PRKCG mutation in two RP11 families
Am. J. Hum. Genet.
62
1248-1252
1998
Homo sapiens (P05129)
Manually annotated by BRENDA team
Kochs, G.; Hummel, R.; Meyer, D.; Hug, H.; Marme, D.; Sarre, T.F.
Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes
Eur. J. Biochem.
216
597-606
1993
Homo sapiens (P05129), Homo sapiens (Q05513), Homo sapiens
Manually annotated by BRENDA team
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
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
Palmer, R.H.; Ridden, J.; Parker, P.J.
Identification of multiple, novel, protein kinase C-related gene products
FEBS Lett.
356
5-8
1994
Homo sapiens (P24723), Homo sapiens (Q16512), Homo sapiens (Q16513)
Manually annotated by BRENDA team
Bacher, N.; Zisman, Y.; Berent, E.; Livneh, E.
Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart
Mol. Cell. Biol.
12
1404
1992
Homo sapiens (P24723)
Manually annotated by BRENDA team
Bacher, N.; Zisman, Y.; Berent, E.; Livneh, E.
Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart
Mol. Cell. Biol.
11
126-133
1991
Homo sapiens (P24723), Homo sapiens
Manually annotated by BRENDA team
Mazzarella, R.; Ciccodicola, A.; Esposito, T.; Arcucci, A.; Migliaccio, C.; Jones, C.; Schlessinger, D.; D'Urso, M.; D'Esposito, M.
Human protein kinase C iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3
Genomics
26
629-631
1995
Homo sapiens (P41743), Homo sapiens
Manually annotated by BRENDA team
Selbie, L.A.; Schmitz-Peiffer, C.; Sheng, Y.; Biden, T.J.
Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells
J. Biol. Chem.
268
24296-24302
1993
Homo sapiens (P41743), Homo sapiens
Manually annotated by BRENDA team
Basta, P.; Strickland, M.B.; Holmes, W.; Loomis, C.R.; Ballas, L.M.; Burns, D.J.
Sequence and expression of human protein kinase C-epsilon
Biochim. Biophys. Acta
1132
154-160
1992
Homo sapiens (Q02156), Homo sapiens
Manually annotated by BRENDA team
Chang, J.D.; Xu, Y.; Raychowdhury, M.K.; Ware, J.A.
Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets
J. Biol. Chem.
268
14208-14214
1993
Homo sapiens (Q04759), Homo sapiens
Manually annotated by BRENDA team
Baier, G.; Telford, D.; Giampa, L.; Coggeshall, K.M.; Baier-Bitterlich, G.; Isakov, N.; Altman, A.
Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells
J. Biol. Chem.
268
4997-5004
1993
Homo sapiens (Q04759), Homo sapiens
Manually annotated by BRENDA team
Barbee, J.L.; Deutscher, S.L.; Loomis, C.R.; Burns, D.J.
The cDNA sequence encoding human protein kinase C-zeta
Gene
132
305-306
1993
Homo sapiens (Q05513), Homo sapiens
Manually annotated by BRENDA team
Nomoto, S.; Watanabe, Y.; Ninomiya-Tsuji, J.; Yang, L.X.; Nagai, Y.; Kiuchi, K.; Hagiwara, M.; Hidaka, H.; Matsumoto, K.; Irie, K.
Functional analyses of mammalian protein kinase C isozymes in budding yeast and mammalian fibroblasts
Genes Cells
2
601-614
1997
Homo sapiens (Q05655), Homo sapiens
Manually annotated by BRENDA team
Aris, J.P.; Basta, P.V.; Holmes, W.D.; Ballas, L.M.; Moomaw, C.; Rankl, N.B.; Blobel, G.; Loomis, C.R.; Burns, D.J.
Molecular and biochemical characterization of a recombinant human PKC-delta family member
Biochim. Biophys. Acta
1174
171-181
1993
Homo sapiens (Q05655), Homo sapiens
Manually annotated by BRENDA team
Johannes, F.J.; Prestle, J.; Eis, S.; Oberhagemann, P.; Pfizenmaier, K.
PKCu is a novel, atypical member of the protein kinase C family
J. Biol. Chem.
269
6140-6148
1994
Homo sapiens (Q15139), Homo sapiens
Manually annotated by BRENDA team
Palmer, R.H.; Ridden, J.; Parker, P.J.
Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family
Eur. J. Biochem.
227
344-351
1995
Homo sapiens (Q16512), Homo sapiens (Q16513)
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
Meyer, M.C.; Kell, P.J.; Creer, M.H.; McHowat, J.
Calcium-independent phospholipase A2 is regulated by a novel protein kinase C in human coronary artery endothelial cells
Am. J. Physiol.
288
C475-482
2005
Homo sapiens
Manually annotated by BRENDA team
Bain, J.; McLauchlan, H.; Elliott, M.; Cohen, P.
The specificities of protein kinase inhibitors: an update
Biochem. J.
371
199-204
2003
Homo sapiens
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
Crosby, D.; Poole, A.W.
Physical and functional interaction between protein kinase C delta and Fyn tyrosine kinase in human platelets
J. Biol. Chem.
278
24533-24541
2003
Homo sapiens
Manually annotated by BRENDA team
Chen, J.S.; Exton, J.H.
Regulation of phospholipase D2 activity by protein kinase Calpha
J. Biol. Chem.
279
22076-22083
2004
Homo sapiens
Manually annotated by BRENDA team
Uchino, M.; Sakai, N.; Kashiwagi, K.; Shirai, Y.; Shinohara, Y.; Hirose, K.; Iino, M.; Yamamura, T.; Saito, N.
Isoform-specific phosphorylation of metabotropic glutamate receptor 5 by protein kinase C (PKC) blocks Ca2+ oscillation and oscillatory translocation of Ca2+-dependent PKC
J. Biol. Chem.
279
2254-2261
2004
Homo sapiens
Manually annotated by BRENDA team
Becker, K.P.; Hannun, Y.A.
Isoenzyme-specific translocation of protein kinase C (PKC)betaII and not PKCbetaI to a juxtanuclear subset of recycling endosomes: involvement of phospholipase D
J. Biol. Chem.
279
28251-28256
2004
Homo sapiens
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
Nozawa, Y.; Nishihara, K.; Akizawa, Y.; Orimoto, N.; Nakano, M.; Uji, T.; Ajioka, H.; Kanda, A.; Matsuura, N.; Kiniwa, M.
Protein kinase C activation by Helicobacter pylori in human gastric epithelial cells limits interleukin-8 production through suppression of extracellular signal-regulated kinase
J. Pharmacol. Sci.
94
233-239
2004
Homo sapiens
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
Kamimura, K.; Hojo, H.; Abe, M.
Characterization of expression of protein kinase C isozymes in human B-cell lymphoma: Relationship between its expression and prognosis
Pathol. Int.
54
224-230
2004
Homo sapiens
Manually annotated by BRENDA team
Budas, G.R.; Koyanagi, T.; Churchill, E.N.; Mochly-Rosen, D.
Competitive inhibitors and allosteric activators of protein kinase C isoenzymes: a personal account and progress report on transferring academic discoveries to the clinic
Biochem. Soc. Trans.
35
1021-1026
2007
Homo sapiens, Xenopus laevis
Manually annotated by BRENDA team
Grodsky, N.; Li, Y.; Bouzida, D.; Love, R.; Jensen, J.; Nodes, B.; Nonomiya, J.; Grant, S.
Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor
Biochemistry
45
13970-13981
2006
Homo sapiens
Manually annotated by BRENDA team
Abeyweera, T.P.; Rotenberg, S.A.
Design and characterization of a traceable protein kinase Calpha
Biochemistry
46
2364-2370
2007
Homo sapiens
Manually annotated by BRENDA team
Los, A.P.; de Widt, J.; Topham, M.K.; van Blitterswijk, W.J.; Divecha, N.
Protein kinase C inhibits binding of diacylglycerol kinase-zeta to the retinoblastoma protein
Biochim. Biophys. Acta
1773
352-357
2007
Homo sapiens
Manually annotated by BRENDA team
Abeywickrama, C.; Rotenberg, S.A.; Baker, A.D.
Inhibition of protein kinase C by dequalinium analogues: structure-activity studies on head group variations
Bioorg. Med. Chem.
14
7796-7803
2006
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Qu, Y.; Zu, P.; Han, S.; Gao, G.; Xu, Q.; Fang, L.
Increased isoform-specific membrane translocation of conventional and novel protein kinase C in human neuroblastoma SH-SY5Y cells following prolonged hypoxia
Brain Res.
1093
25-32
2006
Homo sapiens
Manually annotated by BRENDA team
Chwae, Y.J.; Lee, J.M.; Kim, E.J.; Lee, S.T.; Soh, J.W.; Kim, J.
Activation-induced upregulation of inhibitory killer Ig-like receptors is regulated by protein kinase C
Immunol. Cell Biol.
85
220-228
2007
Homo sapiens
Manually annotated by BRENDA team
Alvarez-Arias, D.A.; Campbell, K.S.
Protein kinase C regulates expression and function of inhibitory killer cell Ig-like receptors in NK cells
J. Immunol.
179
5281-5290
2007
Homo sapiens
Manually annotated by BRENDA team
Bowley, K.A.; Linley, J.E.; Robins, G.G.; Kopanati, S.; Hunter, M.; Sandle, G.I.
Role of protein kinase C in aldosterone-induced non-genomic inhibition of basolateral potassium channels in human colonic crypts
J. Steroid Biochem. Mol. Biol.
104
45-52
2007
Homo sapiens
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
Cerda, S.R.; Mustafi, R.; Little, H.; Cohen, G.; Khare, S.; Moore, C.; Majumder, P.; Bissonnette, M.
Protein kinase C delta inhibits Caco-2 cell proliferation by selective changes in cell cycle and cell death regulators
Oncogene
25
3123-3138
2006
Homo sapiens
Manually annotated by BRENDA team
Kocanova, S.; Hornakova, T.; Hritz, J.; Jancura, D.; Chorvat, D.; Mateasik, A.; Ulicny, J.; Refregiers, M.; Maurizot, J.C.; Miskovsky, P.
Characterization of the interaction of hypericin with protein kinase C in U-87 MG human glioma cells
Photochem. Photobiol.
82
720-728
2006
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
Caunt, C.J.; Rivers, C.A.; Conway-Campbell, B.L.; Norman, M.R.; McArdle, C.A.
Epidermal growth factor receptor and protein kinase C signaling to ERK2: Spatiotemporal regulation of ERK2 by dual specificity phosphatases
J. Biol. Chem.
283
6241-6252
2008
Homo sapiens
Manually annotated by BRENDA team
Oh, Y.; Herbst, R.S.; Burris, H.; Cleverly, A.; Musib, L.; Lahn, M.; Bepler, G.
Enzastaurin, an oral serine/threonine kinase inhibitor, as second- or third-line therapy of non-small-cell lung cancer
J. Clin. Oncol.
26
1135-1141
2008
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
Chahine, M.; Qu, Y.; Mancarella, S.; Boutjdir, M.
Protein kinase C activation inhibits alpha1D L-type Ca channel: a single-channel analysis
Pflugers Arch.
455
913-919
2008
Homo sapiens
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
Peng, H.; Lewandrowski, U.; Mueller, B.; Sickmann, A.; Walz, G.; Wegierski, T.
Identification of a protein kinase C-dependent phosphorylation site involved in sensitization of TRPV4 channel
Biochem. Biophys. Res. Commun.
391
1721-1725
2010
Homo sapiens
Manually annotated by BRENDA team
Conner, M.T.; Conner, A.C.; Brown, J.E.; Bill, R.M.
Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity
Biochemistry
49
821-823
2010
Homo sapiens
Manually annotated by BRENDA team
Deyev, I.E.; Petrenko, A.G.
Regulation of CIRL-1 proteolysis and trafficking
Biochimie
92
418-422
2010
Homo sapiens
Manually annotated by BRENDA team
Freitas, M.; Porto, G.; Lima, J.L.; Fernandes, E.
Zinc activates neutrophils oxidative burst
Biometals
23
31-41
2010
Homo sapiens
Manually annotated by BRENDA team
Jokinen, J.; White, D.J.; Salmela, M.; Huhtala, M.; Kaepylae, J.; Sipilae, K.; Puranen, J.S.; Nissinen, L.; Kankaanpaeae, P.; Marjomaeki, V.; Hyypiae, T.; Johnson, M.S.; Heino, J.
Molecular mechanism of alpha2beta1 integrin interaction with human echovirus 1
EMBO J.
29
196-208
2010
Homo sapiens
Manually annotated by BRENDA team
Martin, P.; Pognonec, P.
ERK and cell death: cadmium toxicity, sustained ERK activation and cell death
FEBS J.
277
39-46
2010
Homo sapiens
Manually annotated by BRENDA team
Cai, J.; Crotty, T.M.; Reichert, E.; Carraway, K.L.; Stafforini, D.M.; Topham, M.K.
Diacylglycerol kinase (delta) and protein kinase Calpha modulate epidermal growth factor receptor abundance and degradation through ubiquitin-specific protease 8
J. Biol. Chem.
285
6952-6959
2010
Homo sapiens
Manually annotated by BRENDA team
Oyesanya, R.A.; Greenbaum, S.; Dang, D.; Lee, Z.; Mukherjee, A.; Wu, J.; Dent, P.; Fang, X.
Differential requirement of the epidermal growth factor receptor for G protein-mediated activation of transcription factors by lysophosphatidic acid
Mol. Cancer
9
8-8
2010
Homo sapiens
Manually annotated by BRENDA team
Bruns, A.F.; Herbert, S.P.; Odell, A.F.; Jopling, H.M.; Hooper, N.M.; Zachary, I.C.; Walker, J.H.; Ponnambalam, S.
Ligand-stimulated VEGFR2 signaling is regulated by co-ordinated trafficking and proteolysis
Traffic
11
161-174
2010
Homo sapiens
Manually annotated by BRENDA team
Toita, R.; Mori, T.; Naritomi, Y.; Kang, J.H.; Shiosaki, S.; Niidome, T.; Katayama, Y.
Fluorometric detection of protein kinase Calpha activity based on phosphorylation-induced dissociation of a polyion complex
Anal. Biochem.
424
130-136
2012
Homo sapiens
Manually annotated by BRENDA team
Raveh-Amit, H.; Hai, N.; Rotem-Dai, N.; Shahaf, G.; Gopas, J.; Livneh, E.
Protein kinase Ceta activates NF-kappaB in response to camptothecin-induced DNA damage
Biochem. Biophys. Res. Commun.
412
313-317
2011
Homo sapiens
Manually annotated by BRENDA team
Dumont, O.; Mylroie, H.; Bauer, A.; Calay, D.; Sperone, A.; Thornton, C.; Hamdulay, S.S.; Ali, N.; Boyle, J.J.; Choo, J.R.; Samarel, A.M.; Haskard, D.O.; Randi, A.M.; Evans, P.C.; Mason, J.C.
Protein kinase Cepsilon activity induces anti-inflammatory and anti-apoptotic genes via an ERK1/2- and NF-kappaB-dependent pathway to enhance vascular protection
Biochem. J.
447
193-204
2012
Homo sapiens
Manually annotated by BRENDA team
Vijayakumar, B.; Velmurugan, D.
Designing of Protein Kinase C beta-II Inhibitors against Diabetic complications: Structure Based Drug Design, Induced Fit docking and analysis of active site conformational changes
Bioinformation
8
568-573
2012
Homo sapiens
Manually annotated by BRENDA team
Pavarotti, M.; Capmany, A.; Vitale, N.; Colombo, M.I.; Damiani, M.T.
Rab11 is phosphorylated by classical and novel protein kinase C isoenzymes upon sustained phorbol ester activation
Biol. Cell
104
102-115
2012
Homo sapiens
Manually annotated by BRENDA team
Li, H.; Hong, Y.; Nukui, S.; Lou, J.; Johnson, S.; Scales, S.; Botrous, I.; Tompkins, E.; Yin, C.; Zhou, R.; He, M.; Jensen, J.; Bouzida, D.; Alton, G.; Lafontaine, J.; Grant, S.
Identification of novel pyrrolopyrazoles as protein kinase C beta II inhibitors
Bioorg. Med. Chem. Lett.
21
584-587
2011
Homo sapiens
Manually annotated by BRENDA team
van Eis, M.J.; Evenou, J.P.; Floersheim, P.; Gaul, C.; Cowan-Jacob, S.W.; Monovich, L.; Rummel, G.; Schuler, W.; Stark, W.; Strauss, A.; von Matt, A.; Vangrevelinghe, E.; Wagner, J.; Soldermann, N.
2,6-Naphthyridines as potent and selective inhibitors of the novel protein kinase C isozymes
Bioorg. Med. Chem. Lett.
21
7367-7372
2011
Homo sapiens
Manually annotated by BRENDA team
Titchenell, P.M.; Hollis Showalter, H.D.; Pons, J.F.; Barber, A.J.; Jin, Y.; Antonetti, D.A.
Synthesis and structure-activity relationships of 2-amino-3-carboxy-4-phenylthiophenes as novel atypical protein kinase C inhibitors
Bioorg. Med. Chem. Lett.
23
3034-3038
2013
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Song, R.; Gao, Y.; Li, Y.; Wang, S.; Liu, H.Y.; Wang, Y.; Hu, Y.H.; Shu, H.B.
Protein kinase C-delta negatively regulates T cell receptor-induced NF-?B activation by inhibiting the assembly of CARMA1 signalosome
J. Biol. Chem.
287
20081-20087
2012
Homo sapiens
Manually annotated by BRENDA team
Lee, A.
The role of atypical protein kinase C in CSF-1-dependent Erk activation and proliferation in myeloid progenitors and macrophages
PLoS ONE
6
e25580
2011
Homo sapiens
Manually annotated by BRENDA team
Lopez-Sanchez, I.; Garcia-Marcos, M.; Mittal, Y.; Aznar, N.; Farquhar, M.G.; Ghosh, P.
Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin
Proc. Natl. Acad. Sci. USA
110
5510-5515
2013
Homo sapiens
Manually annotated by BRENDA team
Van Wandelen, L.; Van Ameijde, J.; Ismail-Ali, A.; Van Ufford, H.; Vijftigschild, L.; Beekman, J.; Martin, N.; Ruijtenbeek, R.; Liskamp, R.
Cell-penetrating bisubstrate-based protein kinase C inhibitors
ACS Chem. Biol.
8
1479-1487
2013
Homo sapiens
Manually annotated by BRENDA team
Meng, Z.; Bischof, J.; Ianes, C.; Henne-Bruns, D.; Xu, P.; Knippschild, U.
CK1delta kinase activity is modulated by protein kinase C alpha (PKCalpha)-mediated site-specific phosphorylation
Amino Acids
48
1185-1197
2016
Homo sapiens
Manually annotated by BRENDA team
Lee, Y.H.; Park, J.W.; Bae, Y.S.
Regulation of protein kinase CK2 catalytic activity by protein kinase C and phospholipase D2
Biochimie
121
131-139
2016
Homo sapiens
Manually annotated by BRENDA team
Pavlovic, Z.; Zhu, L.; Pereira, L.; Singh, R.; Cornel, R.; Bakovic, M.
Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation
J. Biol. Chem.
289
9053-9064
2014
Homo sapiens
Manually annotated by BRENDA team
Sommese, R.; Sivaramakrishnan, S.
Substrate affinity differentially influences protein kinase C regulation and inhibitor potency
J. Biol. Chem.
291
21963-21970
2016
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
Katoh, T.; Tomata, Y.; Setoh, M.; Sasaki, S.; Takai, T.; Yoshitomi, Y.; Yukawa, T.; Nakagawa, H.; Fukumoto, S.; Tsukamoto, T.; Nakada, Y.
Practical application of 3-substituted-2,6-difluoropyridines in drug discovery Facile synthesis of novel protein kinase C theta inhibitors
Bioorg. Med. Chem. Lett.
27
2497-2501
2017
Homo sapiens (Q04759)
Manually annotated by BRENDA team
Holmgren, C.; Cornmark, L.; Lonne, G.K.; Masoumi, K.C.; Larsson, C.
Molecular characterization of protein kinase C delta (PKCdelta)-Smac interactions
BMC Biochem.
17
11
2016
Homo sapiens (Q05655)
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