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Information on EC 2.7.11.24 - mitogen-activated protein kinase and Organism(s) Rattus norvegicus and UniProt Accession P49187

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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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Rattus norvegicus
UNIPROT: P49187
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
mapk, p38, erk1/2, p38 mapk, mitogen-activated protein kinase, map kinase, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, p38mapk, p38 map kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mitogen-activated protein kinase 9
-
c-Jun N-terminal kinase
-
-
c-Jun N-terminal kinase 3
-
-
cp38a
-
-
-
-
cp38b
-
-
-
-
CSAID binding protein
-
-
-
-
CSBP
-
-
-
-
Cytokine suppressive anti-inflammatory drug binding protein
-
-
-
-
ERK1-MAP kinase
-
ERK1/2 mitogen-activated protein kinase
-
-
ERK5
-
-
-
-
extracellular signal-regulated kinase
-
-
extracellular signal-regulated kinase 1
-
extracellular signal-regulated kinase 1/2
-
-
extracellular signal-regulated kinase 2
extracellular-regulated kinase
-
-
glycogen synthase kinase-3
-
-
JUN N-terminal kinase 1/2
-
-
MAP ERK 1/2 kinase
-
-
MAP kinase
MAP kinase MXI2
-
-
-
-
MAP kinase p38 beta
-
-
-
-
MAP kinase p38 delta
-
-
-
-
MAP kinase p38 gamma
-
-
-
-
MAP kinase p38a
-
-
-
-
MAP kinase p38alpha
-
-
-
-
MAP kinase p38b
-
-
-
-
mitogen-activated ERK kinase
-
-
mitogen-activated kinase
-
-
mitogen-activated protein kinase
mitogen-activated protein kinase 13
-
mitogen-activated protein kinase 3
-
mitogen-activated protein kinase 6
-
mitogen-activated protein kinase 8
-
mitogen-activated protein kinase 9
-
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
-
-
-
-
p38 MAP kinase
-
-
p38 mitogen-activated protein kinase
p38-delta mitogen-activated protein kinase
-
p38-MAPK
-
-
p38alpha MAP kinase
-
p38alpha mitogen-activated protein kinase
-
p38b
-
-
-
-
SAPK2A
-
-
-
-
stress-activated protein kinase
-
-
stress-activated protein kinase 2a
-
-
-
-
additional information
-
the enzyme belongs to the MAPK superfamily of enzymes
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
proline-directed kinase
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
show the reaction diagram
ATP + Elk1
ADP + phosphorylated Elk1
show the reaction diagram
ATP + Ets-1
ADP + phosphorylated Ets-1
show the reaction diagram
-
-
-
-
?
ATP + JunD
ADP + phosphorylated JunD
show the reaction diagram
-
-
-
-
?
ATP + MEK
ADP + phosphorylated MEK
show the reaction diagram
-
-
binding to ERK requires docking domain and the kinase interaction motif
-
?
ATP + p38
ADP + phosphorylated p38
show the reaction diagram
-
-
-
-
?
ATP + phospholipase C-gamma1
ADP + phosphorylated phospholipase C-gamma1
show the reaction diagram
ATP + protein
ADP + phosphoprotein
show the reaction diagram
ATP + RSK
ADP + phosphorylated RSK
show the reaction diagram
-
-
binding to ERK requires docking domain
-
?
ATP + sodium channel Na(v)1.6
ADP + phosphorylated sodium channel Na(v)1.6
show the reaction diagram
-
-
-
-
?
ATP + sodium channel Na(v)1.7
ADP + phosphorylated sodium channel Na(v)1.7
show the reaction diagram
-
-
-
-
?
ATP + sodium channel Na(v)1.8
ADP + phosphorylated sodium channel Na(v)1.8
show the reaction diagram
-
-
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
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 + c-Jun
ADP + phosphorylated c-Jun
show the reaction diagram
ATP + Elk1
ADP + phosphorylated Elk1
show the reaction diagram
ATP + phospholipase C-gamma1
ADP + phosphorylated phospholipase C-gamma1
show the reaction diagram
the reaction is performed by activated phosphorylated ERK2, phosphorylation inhibits phospholipase C-gamma1
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
show the reaction diagram
-
phosphorylation of tyrosine hydroxylase at Ser8 and Ser31 by ERK1 and ERK2 is involved in regulation of catecholamine biosynthesis
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-diamino-2,3-dicyano-1,4-bis(o-aminophenylmercapto)butadiene
-
U0126
2-(2'-amino-3'-methoxyphenyl)oxanaphthalen-4-one
-
PD98059
2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one
-
PD98059
6-[1-(2-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(2-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(3-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(3-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(4-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(4-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazole
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[5-amino-1-ethyl-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1-methyl-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-(1-methylethyl)-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1S)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
hypericin
-
hypericin-mediated inhibition of glutamate release appears to involve the suppression of mitogen-activated protein kinase pathway
MKP1/2
-
may dampen ERK activity during the G1/S transition, is involved in reducing strength and duration of ERK signaling
-
MKP3
-
selective for ERK1 and 2
-
N-(1-methylethyl)-6-(1-phenyl-1H-pyrazol-5-yl)-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-(4-phenyl-1,3-oxazol-5-yl)-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-(4-phenyl-1H-imidazol-5-yl)-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-[1-(2-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-[1-(3-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-[1-(4-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
-
N-ethyl-6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
-
PD169316
-
i.e. 4-(4-fluorophenyl)-2-(4-nitrophenyl)-5-(4-pyridyl)-1H-imidazole, a specific p38 MAPK inhibitor, reduces 5-hydroxytryptamine uptake in cells, inhibits SERT phosphorylation
PD98059
phospholipase C-gamma1 D-domain
-
SB202190
-
inhibition of p38 MAPK and modulation of ERK, enhanced strain-induced ERK1/2 activation at 20 min and its restriction after 24 h
SB203580
SP600125
U0126
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADAMTS4
-
EC 3.4.24.82
-
amitriptyline
-
up-regulates ERK1/2 phosphorylation and activity 8fold at 0.01 mM, the addition of nor-binaltorphimine (100 nM) reduces the amitriptyline stimulatory effect by 70%
beta-phorbol-13-acetate
-
stimulates SERT phosphorylation
D-amphetamine
-
stimulates SERT phosphorylation
Epidermal growth factor
-
induces potent transient activation of the ERK pathway
glial cell line-derived neurotrophic factor
-
GDNF
-
Insulin
-
causes weak activation
-
nerve growth factor
-
alters outcome of ERK signaling
-
neurotrophic growth factor
-
NGF
-
Ras
-
essential for ERK activation, the three isoforms N-Ras, K-Ras and H-Ras have an important role in spatial and temporal ERK signaling
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000175
6-[1-(2-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.00002
6-[1-(2-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000072
6-[1-(3-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000033
6-[1-(3-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.001
6-[1-(4-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
above, inhibition of p38alpha MAP kinase
0.000048
6-[1-(4-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000016
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000047
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazole
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000064
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.00001
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000065
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000033
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000027
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000016
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000017
6-[5-amino-1-ethyl-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000011
6-[5-amino-3-(2-fluorophenyl)-1-methyl-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000037
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-(1-methylethyl)-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000032
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000055
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1S)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000021
N-(1-methylethyl)-6-(1-phenyl-1H-pyrazol-5-yl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000021
N-(1-methylethyl)-6-(4-phenyl-1,3-oxazol-5-yl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000033
N-(1-methylethyl)-6-(4-phenyl-1H-imidazol-5-yl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000146
N-(1-methylethyl)-6-[1-(2-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000033
N-(1-methylethyl)-6-[1-(3-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.001
N-(1-methylethyl)-6-[1-(4-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
above, inhibition of p38alpha MAP kinase
0.000012
N-ethyl-6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.3
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
insulin-treated rat 1 HIRc B cells
Manually annotated by BRENDA team
p38-delta is expressed predominantly in the developing gut and the septum transversum in the mouse embryo at 9.5 days, its expression begins to be expanded to many specific tissues in the 12.5-day embryo. At 15.5 days, p38-delta is expressed virtually in most developing epithelia in embryos
Manually annotated by BRENDA team
-
prostate endothelial cells
Manually annotated by BRENDA team
-
dorsal root ganglion
Manually annotated by BRENDA team
-
diethylnitrosamine-induced liver tumor
Manually annotated by BRENDA team
-
the MAPK family enzymes have regulatory function in the myocardium
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
ERK3 is targeted to the Golgi or endoplasmic reticulum as an intermediate compartment during translocation from cytoplasm to nucleus, ERK3 possesses a C-terminally targeting motif for the Golgi apparatus
Manually annotated by BRENDA team
additional information
subcellular localization of wild-type and mutant enzymes, overview, ERK3 translocates from cytoplasm to the nucleus in a temporally regulated exit from a membraneous organelle, nuclear translocation is cell cycle-dependent, mechanism
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
structure-based assignment of Ile, Leu, and Val methyl groups in the active and inactive forms of extracellular signal-regulated kinase 2, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MK10_RAT
464
0
52532
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
x * 100000, about, recombinant ERK3, SDS-PAGE
40000
-
determined by SDS-PAGE and Western-blot analysis
42000
-
x * 44000, ERK1, SDS-PAGE, x * 42000, ERK2, SDS-PAGE
43000
x * 43000, SDS-PAGE
44000
-
x * 44000, ERK1, SDS-PAGE, x * 42000, ERK2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
enzyme is activated through phosphorylation of Tyr and Thr residues
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of ERK2, PDB ID 1ERK
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D546V
site-directed mutagenesis, the mutant enzyme is exclusively localized in the nucleus and especially in the Golgi apparatus, not in the cytoplasm, in contrast to the wild-type enzyme
I101A
site-directed mutagenesis
I124A
site-directed mutagenesis
I238A
site-directed mutagenesis
K717S
site-directed mutagenesis, the mutant enzyme is exclusively localized in the nucleus and Golgi apparatus, not in the cytoplasm, in contrast to the wild-type enzyme
L102A/Q103A
site-directed mutagenesis
L105A
site-directed mutagenesis
L110A
site-directed mutagenesis
L113A
site-directed mutagenesis
L154A
site-directed mutagenesis
L155A
site-directed mutagenesis
L161A
site-directed mutagenesis
L198A
site-directed mutagenesis
L235A
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of synaptosomes
-
recombinant 0P-ERK2 wild-type and mutants from Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS7 cells
expression of GFP-tagged wild-type and mutant ERK3 in human Hela and T98G cells, and in rat 2 cells, fluorescent immunoaffinity subcellular localization study
expression of p38 MAPK in HEK293 cells
-
recombinant expression of wild-type and mutant 0P-ERK2 proteins in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase in the phosphorylated ERK/ERK is observed in the prostate of hyperinsulinemic rats, high fat diet-feeding induced hyperinsulinemic condition leads to up-regulation of MEK/ERK signaling
-
neither the content of extracellular signal-regulated kinase 1/2 nor that of p38 MAPK were modified by undernutrition
-
the amount of Jun N-terminal kinase undergoes a slight but significant decrease by undernutrition, the degree of p38-MAPK phosphorylation (Thr180 and Tyr182) is decreased 4fold by food-restriction
-
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
Boulton, T.G.; Gregory, J.S.; Cobb, M.H.
Purification and properties of extracellular signal-regulated kinase 1, an insulin-stimulated microtubule-associated protein 2 kinase
Biochemistry
30
278-286
1991
Rattus norvegicus (P21708)
Manually annotated by BRENDA team
Hu, M.C.; Wang, Y.P.; Mikhail, A.; Qiu, W.R.; Tan, T.H.
Murine p38-delta mitogen-activated protein kinase, a developmentally regulated protein kinase that is activated by stress and proinflammatory cytokines
J. Biol. Chem.
274
7095-7102
1999
Homo sapiens (O15264), Homo sapiens, Rattus norvegicus (Q9WTY9)
Manually annotated by BRENDA team
Yung, Y.; Yao, Z.; Hanoch, T.; Seger, R.
ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK
J. Biol. Chem.
275
15799-15808
2000
Rattus norvegicus (P21708)
Manually annotated by BRENDA team
Marquardt, B.; Stabel, S.
Sequence of a rat cDNA encoding the ERK1-MAP kinase
Gene
120
297-299
1992
Rattus norvegicus (P21708)
Manually annotated by BRENDA team
Seger, R.; Ahn, N.G.; Boulton, T.G.; Yancopoulos, G.D.; Panayotatos, N.; Radziejewska, E.; Ericsson, L.; Bratlien, R.L.; Cobb, M.H.; Krebs, E.G.
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation
Proc. Natl. Acad. Sci. USA
88
6142-6146
1991
Rattus norvegicus (P21708)
Manually annotated by BRENDA team
De Miguel, C.; Kligman, D.; Patel, J.; Detera-Wadleigh, S.D.
Molecular analysis of microtubule-associated protein-2 kinase cDNA from mouse and rat brain
DNA Cell Biol.
10
505-514
1991
Rattus norvegicus (P21708)
Manually annotated by BRENDA team
Boulton, T.G.; Yancopoulos, G.D.; Gregory, J.S.; Slaughter, C.; Moomaw, C.; Hsu, J.; Cobb, M.H.
An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control
Science
249
64-67
1990
Rattus norvegicus (P21708)
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
Rattus norvegicus (P27704), Mus musculus (P63085)
Manually annotated by BRENDA team
Clerk, A.; Fuller, S.J.; Michael, A.; Sugden, P.H.
Stimulation of "stress-regulated" mitogen-activated protein kinases (stress-activated protein kinases/c-Jun N-terminal kinases and p38-mitogen-activated protein kinases) in perfused rat hearts by oxidative and other stresses
J. Biol. Chem.
273
7228-7234
1998
Rattus norvegicus (P49185)
Manually annotated by BRENDA team
Kyriakis, J.M.; Banerjee, P.; Nikolakaki, E.; Dai, T.; Rubie, E.A.; Ahmad, M.F.; Avruch, J.; Woodgett, J.R.
The stress-activated protein kinase subfamily of c-Jun kinases
Nature
369
156-160
1994
Rattus norvegicus (P49185), Rattus norvegicus (P49186), Rattus norvegicus (P49187)
Manually annotated by BRENDA team
Royo, M.; Daubner, S.C.; Fitzpatrick, P.F.
Specificity of the MAP kinase ERK2 for phosphorylation of tyrosine hydroxylase
Arch. Biochem. Biophys.
423
247-252
2004
Rattus norvegicus
Manually annotated by BRENDA team
Lee, J.Y.; Yu, B.P.; Chung, H.Y.
Activation mechanisms of endothelial NF-kappaB, IKK, and MAP kinase by tert-butyl hydroperoxide
Free Radic. Res.
39
399-409
2005
Rattus norvegicus
Manually annotated by BRENDA team
Buckley, C.T.; Sekiya, F.; Kim, Y.J.; Rhee, S.G.; Caldwell, K.K.
Identification of phospholipase C-gamma1 as a mitogen-activated protein kinase substrate
J. Biol. Chem.
279
41807-41814
2004
Rattus norvegicus, Rattus norvegicus (P63086)
Manually annotated by BRENDA team
Samuvel, D.J.; Jayanthi, L.D.; Bhat, N.R.; Ramamoorthy, S.
A role for p38 mitogen-activated protein kinase in the regulation of the serotonin transporter: evidence for distinct cellular mechanisms involved in transporter surface expression
J. Neurosci.
25
29-41
2005
Rattus norvegicus
Manually annotated by BRENDA team
Bind, E.; Kleyner, Y.; Skowronska-Krawczyk, D.; Bien, E.; Dynlacht, B.D.; Sanchez, I.
A novel mechanism for mitogen-activated protein kinase localization
Mol. Biol. Cell
15
4457-4466
2004
Rattus norvegicus (P27704)
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, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Lewthwaite, J.C.; Bastow, E.R.; Lamb, K.J.; Blenis, J.; Wheeler-Jones, C.P.; Pitsillides, A.A.
A specific mechanomodulatory role for p38 MAPK in embryonic joint articular surface cell MEK-ERK pathway regulation
J. Biol. Chem.
281
11011-11018
2006
Gallus gallus, Rattus norvegicus
Manually annotated by BRENDA team
Murphy, L.O.; Blenis, J.
MAPK signal specificity: the right place at the right time
Trends Biochem. Sci.
31
268-275
2006
Rattus norvegicus, Xenopus sp.
Manually annotated by BRENDA team
Liu, C.; Lin, J.; Pitt, S.; Zhang, R.F.; Sack, J.S.; Kiefer, S.E.; Kish, K.; Doweyko, A.M.; Zhang, H.; Marathe, P.H.; Trzaskos, J.; Mckinnon, M.; Dodd, J.H.; Barrish, J.C.; Schieven, G.L.; Leftheris, K.
Benzothiazole based inhibitors of p38alpha MAP kinase
Bioorg. Med. Chem. Lett.
18
1874-1879
2008
Rattus norvegicus (P70618)
Manually annotated by BRENDA team
Chen, L.; Liu, L.; Huang, S.
Cadmium activates the mitogen-activated protein kinase (MAPK) pathway via induction of reactive oxygen species and inhibition of protein phosphatases 2A and 5
Free Radic. Biol. Med.
45
1035-1044
2008
Homo sapiens, Homo sapiens (P27361), Homo sapiens (P28482), Rattus norvegicus, Rattus norvegicus (P21708), Rattus norvegicus (P63086)
Manually annotated by BRENDA team
Hamel, M.G.; Ajmo, J.M.; Leonardo, C.C.; Zuo, F.; Sandy, J.D.; Gottschall, P.E.
Multimodal signaling by the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) promotes neurite extension
Exp. Neurol.
210
428-440
2008
Rattus norvegicus
Manually annotated by BRENDA team
Chen, B.; Ma, Y.; Meng, R.; Xiong, Z.; Zhang, C.; Chen, G.; Zhang, A.; Dong, Y.
MG132, a proteasome inhibitor, attenuates pressure-overload-induced cardiac hypertrophy in rats by modulation of mitogen-activated protein kinase signals
Acta Biochim. Biophys. Sin. (Shanghai)
42
253-258
2010
Rattus norvegicus
Manually annotated by BRENDA team
Li, F.; Ruan, H.; Fan, C.; Zeng, B.; Wang, C.; Wang, X.
Efficient inhibition of the formation of joint adhesions by ERK2 small interfering RNAs
Biochem. Biophys. Res. Commun.
391
795-799
2010
Rattus norvegicus
Manually annotated by BRENDA team
Fahrenholz, M.; Real, R.; Kueken, A.; Saxena, A.; Orzechowski, H.D.
Single low-dose administration of pharmacological inhibitor of mitogen-activated ERK kinase to the adventitia of the injured rat carotid artery suppresses neointima formation and inhibits nuclear ERK signaling
Eur. J. Pharmacol.
617
90-96
2009
Rattus norvegicus
Manually annotated by BRENDA team
Chang, Y.; Wang, S.J.
Hypericin, the active component of St. Johns wort, inhibits glutamate release in the rat cerebrocortical synaptosomes via a mitogen-activated protein kinase-dependent pathway
Eur. J. Pharmacol.
634
53-61
2010
Rattus norvegicus
Manually annotated by BRENDA team
Hanajiri, K.; Mitsui, H.; Maruyama, T.; Hashimoto, N.; Sata, M.; Omata, M.
Echographic detection of diethylnitrosamine-induced liver tumors in rats and the effect of the intratumoral injection of an inhibitor of c-Jun N-terminal kinase
J. Gastroenterol. Hepatol.
24
866-871
2009
Rattus norvegicus
Manually annotated by BRENDA team
Lizarraga-Mollinedo, E.; Fernandez-Millan, E.; de Miguel-Santos, L.; Martinez-Honduvilla, C.J.; Alvarez, C.; Escriva, F.
Early undernutrition increases glycogen content and reduces the activated forms of GSK3, AMPK, p38 MAPK, and JNK in the cerebral cortex of suckling rats
J. Neurochem.
112
123-133
2010
Rattus norvegicus
Manually annotated by BRENDA team
Stamboulian, S.; Choi, J.S.; Ahn, H.S.; Chang, Y.W.; Tyrrell, L.; Black, J.A.; Waxman, S.G.; Dib-Hajj, S.D.
ERK1/2 mitogen-activated protein kinase phosphorylates sodium channel Na(v)1.7 and alters its gating properties
J. Neurosci.
30
1637-1647
2010
Rattus norvegicus
Manually annotated by BRENDA team
Onali, P.; Dedoni, S.; Olianas, M.C.
Direct agonist activity of tricyclic antidepressants at distinct opioid receptor subtypes
J. Pharmacol. Exp. Ther.
332
255-265
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Vikram, A.; Jena, G.B.; Ramarao, P.
Increased cell proliferation and contractility of prostate in insulin resistant rats: linking hyperinsulinemia with benign prostate hyperplasia
Prostate
70
79-89
2010
Rattus norvegicus
Manually annotated by BRENDA team
Blaha, L.; Babica, P.; Hilscherova, K.; Upham, B.L.
Inhibition of gap-junctional intercellular communication and activation of mitogen-activated protein kinases by cyanobacterial extracts--indications of novel tumor-promoting cyanotoxins?
Toxicon
55
126-134
2010
Rattus norvegicus
Manually annotated by BRENDA team
Xiao, Y.; Warner, L.R.; Latham, M.P.; Ahn, N.G.; Pardi, A.
Structure-based assignment of Ile, Leu, and Val methyl groups in the active and inactive forms of the mitogen-activated protein kinase extracellular signal-regulated kinase 2
Biochemistry
54
4307-4319
2015
Rattus norvegicus (P63086)
Manually annotated by BRENDA team