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Information on EC 2.7.11.24 - mitogen-activated protein kinase and Organism(s) Mus musculus and UniProt Accession Q61532

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EC Tree
IUBMB Comments
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline . A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
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Select one or more organisms in this record:
This record set is specific for:
Mus musculus
UNIPROT: Q61532
Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
mapk, p38, erk1/2, p38 mapk, map kinase, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, p38 map kinase, p38mapk, mek1/2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
c-Jun amino-terminal kinase
266253
-
c-Jun N-terminal kinase
c-jun N-terminal kinase 1
244
-
cp38a
-
-
-
-
cp38b
-
-
-
-
CSAID binding protein
-
-
-
-
CSBP
-
-
-
-
Cytokine suppressive anti-inflammatory drug binding protein
-
-
-
-
ERK1
244
-
ERK1/2
244
-
ERK3
266281
-
ERK5
-
-
-
-
extracellular regulated kinase
244
-
extracellular-signal-regulated protein kinase 3
266281
-
JNK-1
266286
-
JNK-2
266296
-
JNK-3
266282
-
JNK3
244
-
MAP kinase MXI2
-
-
-
-
MAP kinase p38 beta
-
-
-
-
MAP kinase p38 delta
-
-
-
-
MAP kinase p38 gamma
-
-
-
-
MAP kinase p38a
-
-
-
-
MAP kinase p38alpha
-
-
-
-
MAP kinase p38b
-
-
-
-
MAPK1
266241
-
MAPK2
244
-
mitogen- and stress-activated kinase 1
244
-
mitogen-activated kinase
244
-
mitogen-activated protein kinase
-
-
-
-
mitogen-activated protein kinase 1
266241
-
mitogen-activated protein kinase 10
266282
-
mitogen-activated protein kinase 14
266253
-
mitogen-activated protein kinase 6
266281
-
mitogen-activated protein kinase 8
266286
-
mitogen-activated protein kinase 9
266296
-
Mitogen-activated protein kinase p38 beta
-
-
-
-
Mitogen-activated protein kinase p38 delta
-
-
-
-
Mitogen-activated protein kinase p38 gamma
-
-
-
-
Mitogen-activated protein kinase p38a
-
-
-
-
Mitogen-activated protein kinase p38alpha
-
-
-
-
Mitogen-activated protein kinase p38b
-
-
-
-
MSK1
244
-
p38 alpha mitogen-activated protein kinase
244
-
p38 MAP kinase
244
-
p38 MAP kinase alpha
244
-
p38 MAPKalpha
244
-
p38 mitogen-activated protein kinase
244
-
p38 mitogen-activated protein kinase alpha
244
-
p38 mitogen-activated protein MAP kinase
244
-
p38-MAPK
244
-
p38a MAP kinase
244
-
p38alpha
244
-
p38alpha MAP kinase
244
-
p38alpha MAPK
266253
-
p38alpha mitogen activated protein kinase
244
-
p38b
-
-
-
-
p493F12 kinase
266282
-
pp42/mitogen-activated protein kinase
266241
-
Prkm1
266241
-
SAPK
244
-
SAPK/JNK
244
-
SAPK2A
-
-
-
-
stress-activated protein kinase 2a
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a protein = ADP + a phosphoprotein
show the reaction diagram
the kinetics of p38 MAPK follow a rapid-equilibrium random-order ternary-complex mechanism, the enzyme is highly specific for Ser-Pro or Thr-Pro motifs
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (MAPKK-activated)
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline [6]. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
CAS REGISTRY NUMBER
COMMENTARY hide
142243-02-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
Ser/Thr kinase
-
-
-
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
show the reaction diagram
ATP + ATF-2
ADP + phosphorylated ATF-2
show the reaction diagram
-
substrate in kinase assay
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
show the reaction diagram
phosphorylation by p38 MAPK at threonine residues
-
-
?
ATP + ATF2DELTA109
ADP + phosphorylated ATF2DELTA109
show the reaction diagram
-
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
show the reaction diagram
-
-
-
-
?
ATP + EGF receptor peptide
ADP + phosphorylated EGF receptor peptide
show the reaction diagram
-
-
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
show the reaction diagram
-
an ETS family transcription factor
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
show the reaction diagram
-
recombinant GST-tagged Elk1, substrate of ERK2
-
-
?
ATP + MAPKAP-K2
ADP + phosphorylated MAPKAP-K2
show the reaction diagram
-
-
-
-
?
ATP + MAPKAP-K3
ADP + phosphorylated MAPKAP-K3
show the reaction diagram
-
-
-
-
?
ATP + MEF2
ADP + phosphorylated MEF2
show the reaction diagram
-
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
show the reaction diagram
-
substrate of ERK2
-
-
?
ATP + Net
ADP + phosphorylated Net
show the reaction diagram
-
an ETS family transcription factor
-
-
?
ATP + protein ATF2
ADP + phosphorylated protein ATF2
show the reaction diagram
-
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
show the reaction diagram
-
ATF2
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
show the reaction diagram
-
an ETS family transcription factor
-
-
?
ATP + MAPKAP-K2
ADP + phosphorylated MAPKAP-K2
show the reaction diagram
-
-
-
-
?
ATP + MAPKAP-K3
ADP + phosphorylated MAPKAP-K3
show the reaction diagram
-
-
-
-
?
ATP + MEF2
ADP + phosphorylated MEF2
show the reaction diagram
-
-
-
-
?
ATP + Net
ADP + phosphorylated Net
show the reaction diagram
-
an ETS family transcription factor
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
show the reaction diagram
-
substrate of MAPKs, e.g. ERK2
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)acrylamide
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methanesulfinyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methylsulfanyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
-
1-(2,6-dichloro-phenyl)-5-(2,4-difluoro-phenyl)-7-piperazin-1-yl-3,4-dihydro-1H-quinazolin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 3.2 nM, the IC50 for mutants G110A and G110D are 37 nM and 56 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-(2,6-dichloro-phenyl)-5-(2,4-difluoro-phenyl)-7-piperidin-4-yl-3,4-dihydro-1H-quinolin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 0.74 nM, the IC50 for mutants G110A and G110D are 26 nM and 67 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 4.3 nM, the IC50 for mutants G110A and G110D are 61 nM and 160 nM, respectively, no inhibition of JNK3, JNK2, and ERK
2-(4-fluorophenyl)-3-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
2-(4-fluorophenyl)-3-(pyridin-4-yl)quinoxaline
-
-
2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
-
-
2-(4-fluorophenyl)-6,7-dimethyl-3-pyridin-4-ylquinoxaline
-
-
2-(4-fluorophenyl)-6-methoxy-3-(pyridin-4-yl)quinoxaline
-
-
2-(4-fluorophenyl)-N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
-
3-(4-fluorophenyl)-2-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
3-(4-fluorophenyl)-2-(pyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine
-
-
3-(4-fluorophenyl)-6-methoxy-2-(pyridin-4-yl)quinoxaline
-
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(R)-phenylethyl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(S)-phenylethyl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-phenylethyl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(3-methylbutan-2-yl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isobutylpyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isopropylpyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(R)-3-methylbutan-2-yl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(S)-3-methylbutan-2-yl]pyridin-2-amine
-
-
4-[4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-ylamine]-cyclohexanol
-
-
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1,2-dimethylpropyl)pyridin-2-amine
-
-
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
-
-
6,7-dichloro-2-(4-fluorophenyl)-3-pyridin-4-ylquinoxaline
-
-
7-(6-N-phenylaminohexyl)amino-2H-anthra[1,9-cd]pyrazol-6-one
-
AV-7
adenylyl-beta,gamma-methylene diphosphonic acid
-
i.e. AMP-PCP, MgAMP-PCP shows a mixed inhibition pattern in the kinase reaction, and a competitive pattern in the ATPase reaction
ADP
-
MgADP- shows an uncompetitive inhibition pattern
alsterpaullone
-
36% inhibition of MAPK2/ERK2 at 0.01 mM
AMP-PCP
-
-
BIRB796
binding structure with isozyme p38alpha
II/SP600125
inhibits SAPK/JNK
kenpaullone
-
30% inhibition of MAPK2/ERK2 at 0.01 mM
lignocaine
-
the enzyme inhibition by lignocine may involve voltage-sensitive sodium channels, the enzyme attenuates the induction of MAPK activation by lipopolysaccharides, overview
N-(1,2-dimethylpropyl)-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)2-phenoxypropanamide
-
N-benzyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-sec-butyl-4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-amine
-
N-sec-butyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-sec-butyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
-
-
N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine
-
-
N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
-
purvalanol
-
74% inhibition of MAPK2/ERK2 at 0.01 mM
pyridinyl imidazole-type inhibitors
IC50 of 15-48 nM
-
roscovitine
-
19% inhibition of MAPK2/ERK2 at 0.01 mM
SB202190
SB203580
siRNA
-
-
-
skepinone-L
-
the specificity by which SCD-1 modulates the phospholipid composition and inhibits p38 MAPK signaling (among survival/stress pathways), thereby preventing endoplasmic reticulum stress (but not other SCD-1-dependent responses), suggests selective protein-lipid interactions
SP600125
trans-4-([4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
-
-
trans-4-([4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
-
-
U0126
-
specific inhibitor of ERK
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
highly selective for p38 isozyme alpha wild-type and mutants with IC50 of 0.10-0.14 nM, IC50 for JNK2 is 680 nM, for JNK3 970 nM and for ERK 660 nM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EGF
-
induces phosphorylation of Smad3
-
palmitate
-
activates p38 MAPK phosphorylation and activates it
Ras
-
Ras induces phosphorylation of c-Jun by JNKs
-
TNF-alpha
-
activates p38 MAPK mediated by protein kinases MKK3, MKK4, and MKK6, overview
-
UV radiation
-
activates p38 MAPK mediated by protein kinases, overview
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.02
ATF2DELTA109
-
0.048 - 0.096
ATP
0.656 - 2.8
EGF receptor peptide
additional information
additional information
-
steady-state kinetics, kinetic mechanism for p38 MAP kinase alpha kinase and ATPase activities, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.8 - 4.7
ATF2DELTA109
-
6.99 - 31.6
EGF receptor peptide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
ADP
-
above, pH 7.6, 27°C, recombinant p38 MAPK
0.187 - 0.242
AMP-PCP
0.000021
SB203580
-
ATPase reaction versus ATP, pH 7.6, 27°C, recombinant p38 MAPK
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00252
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
P47811
-
0.000041
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methanesulfinyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
P47811
-
0.000019
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methylsulfanyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
P47811
-
0.0000043 - 0.00016
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
0.000333
2-(4-fluorophenyl)-3-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00315
2-(4-fluorophenyl)-3-(pyridin-4-yl)quinoxaline
Mus musculus
-
-
0.0037
2-(4-fluorophenyl)-6,7-dimethyl-3-pyridin-4-ylquinoxaline
Mus musculus
-
-
0.00156
2-(4-fluorophenyl)-N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
Mus musculus
P47811
-
0.000038
3-(4-fluorophenyl)-2-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00319
3-(4-fluorophenyl)-2-(pyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00614
3-(4-fluorophenyl)-6-methoxy-2-(pyridin-4-yl)quinoxaline
Mus musculus
-
-
0.00045
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(R)-phenylethyl)pyridin-2-amine
Mus musculus
P47811
-
0.000006
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(S)-phenylethyl)pyridin-2-amine
Mus musculus
P47811
-
0.00006
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
Mus musculus
P47811
-
0.000238
4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
Mus musculus
-
-
0.00072
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-phenylethyl)pyridin-2-amine
Mus musculus
-
-
0.000794
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(3-methylbutan-2-yl)pyridin-2-amine
Mus musculus
-
-
0.000642
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isobutylpyridin-2-amine
Mus musculus
-
-
0.000081
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isopropylpyridin-2-amine
Mus musculus
-
-
0.00479
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
Mus musculus
-
-
0.000431
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
Mus musculus
-
-
0.00159
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(R)-3-methylbutan-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00576
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(S)-3-methylbutan-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000211
4-[4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-ylamine]-cyclohexanol
Mus musculus
-
-
0.00946
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1,2-dimethylpropyl)pyridin-2-amine
Mus musculus
-
-
0.000412
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
Mus musculus
-
-
0.00004 - 0.00009
II/SP600125
0.00138
N-(1,2-dimethylpropyl)-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00089
N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)2-phenoxypropanamide
Mus musculus
P47811
-
0.00153
N-benzyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00003
N-sec-butyl-4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-amine
Mus musculus
P47811
-
0.000595
N-sec-butyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000114
N-sec-butyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000522
N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
Mus musculus
-
mixture of N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine and N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
0.000522
N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine
Mus musculus
-
mixture of N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine and N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
0.0003
N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
Mus musculus
P47811
-
0.000015 - 0.000048
pyridinyl imidazole-type inhibitors
Mus musculus
P47811
IC50 of 15-48 nM
-
0.000025 - 0.00005
skepinone-L
Mus musculus
-
pH 7.4, 22°C
0.000259
trans-4-([4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
Mus musculus
-
-
0.000608
trans-4-([4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
Mus musculus
-
-
0.0000001 - 0.00097
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
additional information
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.5
-
assay at
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
assay at room temperature
22
-
assay at room temperature
27
-
assay at
additional information
-
using a relatively low induction temperature (21°C in comparison to 32°C) phosphorylation is almost completely prevented. Combining a short 5 h induction with a low expression temperature (21°C) results in highly homogeneous unphosphorylated protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activated ERK2
Manually annotated by BRENDA team
-
p38 MAPK is expressed predominantly in nestin-positive cells in the cerebral cortex in embryonic day 10 brain
Manually annotated by BRENDA team
-
mixed glial cultures
Manually annotated by BRENDA team
-
the MAPK family enzymes have regulatory function in the myocardium
Manually annotated by BRENDA team
additional information
-
CD4+ T cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
p38 alpha mitogen-activated protein kinase is a key component of the cascade leading to pro-inflammatory cytokines such as tumor necrosis factor-alpha and interleukin-1beta
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
MK06_MOUSE
720
0
82199
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
-
x * 64000, recombinant p38alpha MAP kinase, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 64000, recombinant p38alpha MAP kinase, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
purified recombinant p38alpha MAP kinase free or in complex with inhibitor SB203580, sitting or hanging drop vapour diffusion method at 16-20°C, 16 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgCl2, 10 mM DTT, and 5% glycerol is mixed with reservoir solution containing 10-20% PEG 4000, 18% ethylene glycol, 0.1 M cacodylic acid, pH 6.0, at a volume ratio of 3:2, X-ray diffraction structure determination and analysis at 1.9-2.7 A resolution
-
purified p38 isozyme alpha bound to several inhibitors pyridinyl imidazole-type inhibitors, X-ray diffraction structure determination and analysis at 2.1-2.5 A resolution
p38alpha active mutants crystallized by sitting-drop vapour-diffusion method, mutant D176A/F327L to 1.45 A resolution, crystals of the three p38alpha mutants belong to the orthorhombic space group P212121, with one molecule in the asymmetric unit
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G110A
site-directed mutagenesis of isozyme alpha, the mutant shows a slightly decreased Km value for ATP, but unaltered activity compared to the wild-type enzyme, decreased sensitivity for inhibitors compared to the wild-type enzyme
G110D
site-directed mutagenesis of isozyme alpha, the mutant shows a decreased Km value for ATP, but unaltered activity compared to the wild-type enzyme, decreased sensitivity for inhibitors compared to the wild-type enzyme
D176A
-
active p38alpha mutant, crystals do not appear spontaneously, cross-seeding approaches using crystals of mutant D176A+F327L as the source of microseeds results in crystals suitable for X-ray analysis
D176A/F327L
-
most active p38alpha mutant, improvement of crystallization assays, obtained with abolishing phosporylation completely by reducing both the temperature and duration of induction and by significantly shortening the N-terminal hexahistidine spacer, facilitating the growth of well diffracting crystals
D176A/F327S
-
active p38alpha mutant, crystals do not appear spontaneously, cross-seeding approaches using crystals of mutant D176A+F327L as the source of microseeds results in crystals suitable for X-ray analysis
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 100 mM NaCl, 50 mM Tris-HCl buffer, pH 7.4, 10 mM DTT, 10 mM MgCl2, 5% glycerol
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
p38alpha active mutants, by gel filtration, on Ni2+-column
-
recombinant GST-tagged p38 isozyme alpha from Escherichia coli strain BL21(DE3) by two steps of ion exchange chromatography to homogeneity, the recombinant enzyme is detagged
-
recombinant His-tagged p38alpha from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography to homogeneity
-
recombinant His-tagged p38alpha MAP kinase from Escherichia coli strain BL21(DE3) by nickel chelate affinity chromatohgraphy, dialysis, and ion exchange chromatography to homogeneity, the His-tag is cleaved off by thrombin
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
expression of GST-tagged p38 isozyme alpha in Escherichia coli strain BL21(DE3)
-
expression of His-tagged p38alpha in Escherichia coli strain BL21(DE3)
-
expression of His-tagged wild-type and mutant p38 isozyme alpha
p38alpha active mutants subcloned into vector pET-28a and expressed in Rosetta strain of Escherichia coli
-
p38alpha MAP kinase expression in Escherichia coli strain BL21(DE3) as His-tagged protein with a thrombin cleavage site
-
quantitative RT-PCR enzyme expression analysis
-
recombinant expression of GST-tagged enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
MAPKs are targets for drug development
medicine
pharmacology
-
MAPKs are targets for inhibitors and pharmacological drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ershler, M.; Nagorskaya, T.V.; Visser, J.W.; Belyavsky, A.V.
Novel CDC2-related protein kinases produced in murine hematopoietic stem cells
Gene
124
305-306
1993
Mus musculus (P47811), Mus musculus (P63085), Mus musculus (Q61532)
Manually annotated by BRENDA team
Canagarajah, B.J.; Khokhlatchev, A.; Cobb, M.H.; Goldsmith, E.J.
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Cell
90
859-869
1997
Mus musculus (P63085)
Manually annotated by BRENDA team
Zhang, F.; Strand, A.; Robbins, D.; Cobb, M.H.; Goldsmith, E.J.
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Nature
367
704-711
1994
Mus musculus (P63085)
Manually annotated by BRENDA team
Payne, D.M.; Rossomando, A.J.; Martino, P.; Erickson, A.K.; Her, J.H.; Shabanowitz, J.; Hunt, D.F.; Weber, M.J.; Sturgill, T.W.
Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase)
EMBO J.
10
885-892
1991
Mus musculus (P63085)
Manually annotated by BRENDA team
Her, J.H.; Wu, J.; Rall, T.B.; Sturgill, T.W.; Weber, M.J.
Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation
Nucleic Acids Res.
19
3743
1991
Mus musculus (P63085)
Manually annotated by BRENDA team
Boulton, T.G.; Nye, S.H.; Robbins, D.J.; Ip, N.Y.; Radziejewska, E.; Morgenbesser, S.D.; DePinho, R.A.; Panayotatos, N.; Cobb, M.H.; Yancopoulos, G.D.
ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
Cell
65
663-675
1991
Mus musculus (P63085), Rattus norvegicus (P27704)
Manually annotated by BRENDA team
Derijard, B.; Raingeaud, J.; Barrett, T.; Wu, I.H.; Han, J.; Ulevitch, R.J.; Davis, R.J.
Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
Science
267
682-685
1995
Homo sapiens, Homo sapiens (P45983), Mus musculus (P47811)
Manually annotated by BRENDA team
Wang, Z.; Harkins, P.C.; Ulevitch, R.J.; Han, J.; Cobb, M.H.; Goldsmith, E.J.
The structure of mitogen-activated protein kinase p38 at 2.1-A resolution
Proc. Natl. Acad. Sci. USA
94
2327-2332
1997
Mus musculus (P47811)
Manually annotated by BRENDA team
Han, J.; Lee, J.D.; Bibbs, L.; Ulevitch, R.J.
A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
Science
265
808-811
1994
Mus musculus (P47811)
Manually annotated by BRENDA team
Turgeon, B.; Saba-El-Leil, M.K.; Meloche, S.
Cloning and characterization of mouse extracellular-signal-regulated protein kinase 3 as a unique gene product of 100 kDa
Biochem. J.
346
169-175
2000
Mus musculus (Q61532)
-
Manually annotated by BRENDA team
Ito, M.; Yoshioka, K.; Akechi, M.; Yamashita, S.; Takamatsu, N.; Sugiyama, K.; Hibi, M.; Nakabeppu, Y.; Shiba, T.; Yamamoto, K.I.
JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway
Mol. Cell. Biol.
19
7539-7548
1999
Mus musculus, Mus musculus (Q61831), Mus musculus (Q91Y86), Mus musculus (Q9WTU6)
Manually annotated by BRENDA team
Yang, D.D.; Kuan, C.Y.; Whitmarsh, A.J.; Rincon, M.; Zheng, T.S.; Davis, R.J.; Rakic, P.; Flavell, R.A.
Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
Nature
389
865-870
1997
Mus musculus (Q61831)
Manually annotated by BRENDA team
Martin, J.H.; Mohit, A.A.; Miller, C.A.
Developmental expression in the mouse nervous system of the p493F12 SAP kinase
Brain Res. Mol. Brain Res.
35
47-57
1996
Mus musculus, Mus musculus (Q61831)
Manually annotated by BRENDA team
Whitmarsh, A.J.; Kuan, C.Y.; Kennedy, N.J.; Kelkar, N.; Haydar, T.F.; Mordes, J.P.; Appel, M.; Rossini, A.A.; Jones, S.N.; Flavell, R.A.; Rakic, P.; Davis, R.J.
Requirement of the JIP1 scaffold protein for stress-induced JNK activation
Genes Dev.
15
2421-2432
2001
Mus musculus (Q91Y86)
Manually annotated by BRENDA team
Dong, C.; Yang, D.D.; Tournier, C.; Whitmarsh, A.J.; Xu, J.; Davis, R.J.; Flavell, R.A.
JNK is required for effector T-cell function but not for T-cell activation
Nature
405
91-94
2000
Mus musculus (Q91Y86)
Manually annotated by BRENDA team
Yang, D.; Tournier, C.; Wysk, M.; Lu, H.T.; Xu, J.; Davis, R.J.; Flavell, R.A.
Targeted disruption of the MKK4 gene causes embryonic death, inhibition of c-Jun NH2-terminal kinase activation, and defects in AP-1 transcriptional activity
Proc. Natl. Acad. Sci. USA
94
3004-3009
1997
Mus musculus (Q91Y86)
Manually annotated by BRENDA team
Tournier, C.; Whitmarsh, A.J.; Cavanagh, J.; Barrett, T.; Davis, R.J.
Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase
Proc. Natl. Acad. Sci. USA
94
7337-7342
1997
Mus musculus (Q91Y86)
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, Mus musculus
Manually annotated by BRENDA team
Matsuura, I.; Wang, G.; He, D.; Liu, F.
Identification and characterization of ERK MAP kinase phosphorylation sites in Smad3
Biochemistry
44
12546-12553
2005
Mus musculus
Manually annotated by BRENDA team
Otsuka, M.; Goto, K.; Tsuchiya, S.; Aramaki, Y.
Phosphatidylserine-specific receptor contributes to TGF-beta production in macrophages through a MAP kinase, ERK
Biol. Pharm. Bull.
28
1707-1710
2005
Mus musculus
Manually annotated by BRENDA team
Szafranska, A.E.; Dalby, K.N.
Kinetic mechanism for p38 MAP kinase alpha. A partial rapid-equilibrium random-order ternary-complex mechanism for the phosphorylation of a protein substrate
FEBS J.
272
4631-4645
2005
Mus musculus
Manually annotated by BRENDA team
Brancho, D.; Tanaka, N.; Jaeschke, A.; Ventura, J.J.; Kelkar, N.; Tanaka, Y.; Kyuuma, M.; Takeshita, T.; Flavell, R.A.; Davis, R.J.
Mechanism of p38 MAP kinase activation in vivo
Genes Dev.
17
1969-1978
2003
Mus musculus
Manually annotated by BRENDA team
Ravingerova, T.; Barancik, M.; Strniskova, M.
Mitogen-activated protein kinases: a new therapeutic target in cardiac pathology
Mol. Cell. Biochem.
247
127-138
2003
Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Fitzgerald, C.E.; Patel, S.B.; Becker, J.W.; Cameron, P.M.; Zaller, D.; Pikounis, V.B.; O'Keefe, S.J.; Scapin, G.
Structural basis for p38alpha MAP kinase quinazolinone and pyridol-pyrimidine inhibitor specificity
Nat. Struct. Biol.
10
764-769
2003
Mus musculus (P47811)
Manually annotated by BRENDA team
Bukhtiyarova, M.; Northrop, K.; Chai, X.; Casper, D.; Karpusas, M.; Springman, E.
Improved expression, purification, and crystallization of p38alpha MAP kinase
Protein Expr. Purif.
37
154-161
2004
Mus musculus
Manually annotated by BRENDA team
Diskin, R.; Engelberg, D.; Livnah, O.
High-resolution diffracting crystals of intrinsically active p38alpha MAP kinase: a case study for low-throughput approaches
Acta Crystallogr. Sect. D
63
260-265
2007
Mus musculus
Manually annotated by BRENDA team
Hedrick, M.N.; Olson, C.M.; Conze, D.B.; Bates, T.C.; Rincon, M.; Anguita, J.
Control of Borrelia burgdorferi-specific CD4+-T-cell effector function by interleukin-12- and T-cell receptor-induced p38 mitogen-activated protein kinase activity
Infect. Immun.
74
5713-5717
2006
Mus musculus, Mus musculus C3H/HEN
Manually annotated by BRENDA team
Kawasaki, T.; Choudhry, M.A.; Schwacha, M.G.; Fujimi, S.; Lederer, J.A.; Bland, K.I.; Chaudry, I.H.
Trauma-hemorrhage inhibits splenic dendritic cell proinflammatory cytokine production via a mitogen-activated protein kinase process
Am. J. Physiol. Cell Physiol.
294
C754-C764
2008
Mus musculus, Mus musculus (Q61831), Mus musculus (Q91Y86), Mus musculus (Q9WTU6)
Manually annotated by BRENDA team
Lee, P.Y.; Tsai, P.S.; Huang, Y.H.; Huang, C.J.
Inhibition of toll-like receptor-4, nuclear factor-kappaB and mitogen-activated protein kinase by lignocaine may involve voltage-sensitive sodium channels
Clin. Exp. Pharmacol. Physiol.
35
1052-1058
2008
Mus musculus
Manually annotated by BRENDA team
Heinrichsdorff, J.; Luedde, T.; Perdiguero, E.; Nebreda, A.R.; Pasparakis, M.
p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure
EMBO Rep.
9
1048-1054
2008
Mus musculus (P47811), Mus musculus C57BL/6 (P47811)
Manually annotated by BRENDA team
Zhang, Y.Y.; Mei, Z.Q.; Wu, J.W.; Wang, Z.X.
Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states
J. Biol. Chem.
283
26591-26601
2008
Mus musculus
Manually annotated by BRENDA team
Abidi, P.; Zhang, H.; Zaidi, S.M.; Shen, W.J.; Leers-Sucheta, S.; Cortez, Y.; Han, J.; Azhar, S.
Oxidative stress-induced inhibition of adrenal steroidogenesis requires participation of p38 mitogen-activated protein kinase signaling pathway
J. Endocrinol.
198
193-207
2008
Mus musculus, Mus musculus (Q91Y86), Mus musculus (Q9WTU6)
Manually annotated by BRENDA team
Sato, K.; Hamanoue, M.; Takamatsu, K.
Inhibitors of p38 mitogen-activated protein kinase enhance proliferation of mouse neural stem cells
J. Neurosci. Res.
86
2179-2189
2008
Mus musculus
Manually annotated by BRENDA team
Pocivavsek, A.; Rebeck, G.W.
Inhibition of c-Jun N-terminal kinase increases apoE expression in vitro and in vivo
Biochem. Biophys. Res. Commun.
387
516-520
2009
Mus musculus
Manually annotated by BRENDA team
Beck, I.M.; Berghe, W.V.; Gerlo, S.; Bougarne, N.; Vermeulen, L.; De Bosscher, K.; Haegeman, G.
Glucocorticoids and mitogen- and stress-activated protein kinase 1 inhibitors: possible partners in the combat against inflammation
Biochem. Pharmacol.
77
1194-1205
2009
Mus musculus
Manually annotated by BRENDA team
Lin, H.Y.; Shen, S.C.; Lin, C.W.; Wu, M.S.; Chen, Y.C.
Cobalt protoporphyrin inhibition of lipopolysaccharide or lipoteichoic acid-induced nitric oxide production via blocking c-Jun N-terminal kinase activation and nitric oxide enzyme activity
Chem. Biol. Interact.
180
202-210
2009
Mus musculus
Manually annotated by BRENDA team
Yao, K.; Cho, Y.Y.; Bode, A.M.; Vummenthala, A.; Park, J.G.; Liu, K.; Pang, Y.P.; Dong, Z.
A selective small-molecule inhibitor of c-Jun N-terminal kinase 1
FEBS Lett.
583
2208-2212
2009
Homo sapiens (P45983), Mus musculus
Manually annotated by BRENDA team
Peifer, C.; Abadleh, M.; Bischof, J.; Hauser, D.; Schattel, V.; Hirner, H.; Knippschild, U.; Laufer, S.
3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of p38alpha mitogen activated protein kinase and casein kinase 1delta
J. Med. Chem.
52
7618-7630
2009
Mus musculus (P47811)
Manually annotated by BRENDA team
Koch, P.; Jahns, H.; Schattel, V.; Goettert, M.; Laufer, S.
Pyridinylquinoxalines and pyridinylpyridopyrazines as lead compounds for novel p38 alpha mitogen-activated protein kinase inhibitors
J. Med. Chem.
53
1128-1137
2010
Mus musculus
Manually annotated by BRENDA team
Koeberle, A.; Pergola, C.; Shindou, H.; Koeberle, S.C.; Shimizu, T.; Laufer, S.A.; Werz, O.
Role of p38 mitogen-activated protein kinase in linking stearoyl-CoA desaturase-1 activity with endoplasmic reticulum homeostasis
FASEB J.
29
2439-2449
2015
Mus musculus
Manually annotated by BRENDA team
Bardwell, A.J.; Bardwell, L.
Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions
J. Biol. Chem.
290
26661-26674
2015
Homo sapiens (P45983), Homo sapiens (P45984), Homo sapiens (Q15759), Mus musculus (P63085)
Manually annotated by BRENDA team
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