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Information on EC 2.7.11.24 - mitogen-activated protein kinase and Organism(s) Xenopus laevis and UniProt Accession Q8QHK8

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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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Xenopus laevis
UNIPROT: Q8QHK8
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The taxonomic range for the selected organisms is: Xenopus laevis
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 8
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cp38a
-
-
-
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cp38b
-
-
-
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CSAID binding protein
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-
-
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CSBP
-
-
-
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Cytokine suppressive anti-inflammatory drug binding protein
-
-
-
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ERK5
-
-
-
-
MAP kinase
MAP kinase MXI2
-
-
-
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MAP kinase p38 beta
-
-
-
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MAP kinase p38 delta
-
-
-
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MAP kinase p38 gamma
-
-
-
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MAP kinase p38a
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-
-
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MAP kinase p38alpha
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-
-
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MAP kinase p38b
-
-
-
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MAPK-activated protein kinase-2
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MAPKAP kinase-2
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mitogen-activated protein kinase
mitogen-activated protein kinase 2
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Mitogen-activated protein kinase p38 beta
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-
-
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Mitogen-activated protein kinase p38 delta
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-
-
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Mitogen-activated protein kinase p38 gamma
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-
-
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Mitogen-activated protein kinase p38a
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-
-
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Mitogen-activated protein kinase p38alpha
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-
-
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Mitogen-activated protein kinase p38b
-
-
-
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p38b
-
-
-
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SAPK2A
-
-
-
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stress-activated protein kinase 2a
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
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 + Mps1
ADP + phosphorylated Mps1
show the reaction diagram
-
Mps1 phosphorylation by MAPK at S844, spindle checkpoint requires phosphorylation at S844, may create a phosphoepitope that allows Mps1 to interact with kinetochores
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-
?
ATP + Smad1
ADP + phosphorylated Smad1
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 + Smad1
ADP + phosphorylated Smad1
show the reaction diagram
-
the MAP kinase antagonizes Smad1 in signaling during development of axis and neural specification, Smad1 is involved in dorsal-ventral patterning in embryos
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
U0126
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MAPK inhibitor, treatment of metaphase egg extracts reduces Mps1 phosphorylation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
enzyme is activated in vitro by the p42 and p44 isoforms of MAPK, p42/p44MAPK
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MK08_XENLA
426
0
47928
Swiss-Prot
other Location (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
tyrosine phosphorylated during oocyte maturation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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effects of overexpression of substrate Smad1 mutant S187A/S195A/S205A/S213A compared to overexpression of Smad1 wild-type, ventralizing of embryos, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type MAP kinase and mutants in embryos by microinjection
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
increased phosphorylation at M phase is dependent on MAPK, controls several major steps in the spindle checkpoint
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Posada, J.; Cooper, J.A.
Requirements for phosphorylation of MAP kinase during meiosis in Xenopus oocytes
Science
255
212-215
1992
Xenopus laevis (P26696), Xenopus laevis
Manually annotated by BRENDA team
Posada, J.; Sanghera, J.; Pelech, S.; Aebersold, R.; Cooper, J.A.
Tyrosine phosphorylation and activation of homologous protein kinases during oocyte maturation and mitogenic activation of fibroblasts
Mol. Cell. Biol.
11
2517-2528
1991
Xenopus laevis (P26696)
Manually annotated by BRENDA team
Gotoh, Y.; Moriyama, K.; Matsuda, S.; Okumura, E.; Kishimoto, T.; Kawasaki, H.; Suzuki, K.; Yahara, I.; Sakai, H.; Nishida, E.
Xenopus M phase MAP kinase: isolation of its cDNA and activation by MPF
EMBO J.
10
2661-2668
1991
Xenopus laevis (P26696)
Manually annotated by BRENDA team
Rouse, J.; Cohen, P.; Trigon, S.; Morange, M.; Alonso-Llamazares, A.; Zamanillo, D.; Hunt, T.; Nebreda, A.R.
A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
Cell
78
1027-1037
1994
Xenopus laevis (P47812)
Manually annotated by BRENDA team
Yamanaka, H.; Moriguchi, T.; Masuyama, N.; Kusakabe, M.; Hanafusa, H.; Takada, R.; Takada, S.; Nishida, E.
JNK functions in the non-canonical Wnt pathway to regulate convergent extension movements in vertebrates
EMBO Rep.
3
69-75
2002
Xenopus laevis (Q8QHK8)
Manually annotated by BRENDA team
Sater, A.K.; El-Hodiri, H.M.; Goswami, M.; Alexander, T.B.; Al-Sheikh, O.; Etkin, L.D.; Akif Uzman, J.
Evidence for antagonism of BMP-4 signals by MAP kinase during Xenopus axis determination and neural specification
Differentiation
71
434-444
2003
Xenopus laevis
Manually annotated by BRENDA team
Zhao, Y.; Chen, R.H.
Mps1 phosphorylation by MAP kinase is required for kinetochore localization of spindle-checkpoint proteins
Curr. Biol.
16
1764-1769
2006
Xenopus laevis
Manually annotated by BRENDA team