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MAPK10

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Protein-coding gene in the species Homo sapiens
MAPK10
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1JNK, 1PMN, 1PMU, 1PMV, 2B1P, 2EXC, 2O0U, 2O2U, 2OK1, 2P33, 2R9S, 2WAJ, 2ZDT, 2ZDU, 3CGF, 3CGO, 3DA6, 3FI2, 3FI3, 3FV8, 3G90, 3G9L, 3G9N, 3KVX, 3OXI, 3OY1, 3PTG, 3RTP, 3TTI, 3TTJ, 3V6R, 3V6S, 4H36, 4H39, 4H3B, 4KKG, 4KKH, 4U79, 4W4V, 4W4W, 4W4X, 4W4Y, 4WHZ, 4Y46, 4Y5H, 4Z9L, 4X21

Identifiers
AliasesMAPK10, JNK3, JNK3A, PRKM10, SAPK1b, p493F12, p54bSAPK, mitogen-activated protein kinase 10
External IDsOMIM: 602897; MGI: 1346863; HomoloGene: 56439; GeneCards: MAPK10; OMA:MAPK10 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)
Chromosome 4 (human)Genomic location for MAPK10Genomic location for MAPK10
Band4q21.3Start85,990,007 bp
End86,594,625 bp
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)
Chromosome 5 (mouse)Genomic location for MAPK10Genomic location for MAPK10
Band5|5 E5Start103,055,814 bp
End103,359,200 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • prefrontal cortex

  • right frontal lobe

  • Brodmann area 9

  • primary visual cortex

  • middle temporal gyrus

  • Brodmann area 23

  • cingulate gyrus

  • anterior cingulate cortex

  • endothelial cell

  • frontal pole
Top expressed in
  • substantia nigra

  • motor neuron

  • medial vestibular nucleus

  • anterior amygdaloid area

  • subiculum

  • medial geniculate nucleus

  • prefrontal cortex

  • medial dorsal nucleus

  • primary motor cortex

  • mammillary body
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5602

26414

Ensembl

ENSG00000109339

ENSMUSG00000046709

UniProt

P53779
Q499Y8

Q61831

RefSeq (mRNA)
NM_002753
NM_138980
NM_138981
NM_138982
NM_001318067

NM_001318068
NM_001318069
NM_001351624
NM_001351625
NM_001363657

NM_001081567
NM_009158
NM_001310683
NM_001310685
NM_001310686

NM_001318102
NM_001318131

RefSeq (protein)
NP_001304996
NP_001304997
NP_001304998
NP_002744
NP_620446

NP_620448
NP_001338553
NP_001338554
NP_001350586
NP_001304997.1

NP_001075036
NP_001297612
NP_001297614
NP_001297615
NP_001305031

NP_001305060
NP_033184
NP_001394501
NP_001394502
NP_001394503
NP_001394504
NP_001394505
NP_001394506
NP_001394507
NP_001394508
NP_001394509
NP_001394513
NP_001394515
NP_001394517
NP_001394518
NP_001394521
NP_001394524
NP_001394528
NP_001394529
NP_001394530

Location (UCSC)Chr 4: 85.99 – 86.59 MbChr 5: 103.06 – 103.36 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Mitogen-activated protein kinase 10 also known as c-Jun N-terminal kinase 3 (JNK3) is an enzyme that in humans is encoded by the MAPK10 gene.

Function

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This protein is a neuronal-specific form of c-Jun N-terminal kinases (JNKs). Through its phosphorylation and nuclear localization, this kinase plays regulatory roles in the signaling pathways during neuronal apoptosis. Beta-arrestin 2, a receptor-regulated MAP kinase scaffold protein, is found to interact with, and stimulate the phosphorylation of this kinase by MAP kinase kinase 4 (MKK4). Cyclin-dependent kinase 5 can phosphorylate, and inhibit the activity of this kinase, which may be important in preventing neuronal apoptosis. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

Interactions

MAPK10 has been shown to interact with MAPK8IP3.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000109339Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000046709Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Gupta S, Barrett T, Whitmarsh AJ, Cavanagh J, Sluss HK, Dérijard B, Davis RJ (July 1996). "Selective interaction of JNK protein kinase isoforms with transcription factors". EMBO J. 15 (11): 2760–70. doi:10.1002/j.1460-2075.1996.tb00636.x. PMC 450211. PMID 8654373.
  6. Yoshida S, Harada H, Nagai H, Fukino K, Teramoto A, Emi M (November 2002). "Head-to-head juxtaposition of Fas-associated phosphatase-1 (FAP-1) and c-Jun NH2-terminal kinase 3 (JNK3) genes: genomic structure and seven polymorphisms of the FAP-1 gene". J. Hum. Genet. 47 (11): 614–9. doi:10.1007/s100380200094. PMID 12436199.
  7. ^ "Entrez Gene: MAPK10 mitogen-activated protein kinase 10".
  8. Ito M, Yoshioka K, Akechi M, Yamashita S, Takamatsu N, Sugiyama K, Hibi M, Nakabeppu Y, Shiba T, Yamamoto KI (November 1999). "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 (11): 7539–48. doi:10.1128/mcb.19.11.7539. PMC 84763. PMID 10523642.
  9. Kelkar N, Gupta S, Dickens M, Davis RJ (February 2000). "Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3". Mol. Cell. Biol. 20 (3): 1030–43. doi:10.1128/MCB.20.3.1030-1043.2000. PMC 85220. PMID 10629060.
  10. Matsuura H, Nishitoh H, Takeda K, Matsuzawa A, Amagasa T, Ito M, Yoshioka K, Ichijo H (October 2002). "Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade". J. Biol. Chem. 277 (43): 40703–9. doi:10.1074/jbc.M202004200. hdl:2297/2692. PMID 12189133.

Further reading

External links

PDB gallery
  • 1jnk: THE C-JUN N-TERMINAL KINASE (JNK3S) COMPLEXED WITH MGAMP-PNP 1jnk: THE C-JUN N-TERMINAL KINASE (JNK3S) COMPLEXED WITH MGAMP-PNP
  • 1pmn: Crystal structure of JNK3 in complex with an imidazole-pyrimidine inhibitor 1pmn: Crystal structure of JNK3 in complex with an imidazole-pyrimidine inhibitor
  • 1pmq: The structure of JNK3 in complex with an imidazole-pyrimidine inhibitor 1pmq: The structure of JNK3 in complex with an imidazole-pyrimidine inhibitor
  • 1pmu: The crystal structure of JNK3 in complex with a phenantroline inhibitor 1pmu: The crystal structure of JNK3 in complex with a phenantroline inhibitor
  • 1pmv: The structure of JNK3 in complex with a dihydroanthrapyrazole inhibitor 1pmv: The structure of JNK3 in complex with a dihydroanthrapyrazole inhibitor
  • 1ukh: Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 1ukh: Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125
  • 1uki: Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 1uki: Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125
  • 2b1p: inhibitor complex of JNK3 2b1p: inhibitor complex of JNK3
  • 2exc: Inhibitor complex of JNK3 2exc: Inhibitor complex of JNK3
  • 2g01: Pyrazoloquinolones as Novel, Selective JNK1 inhibitors 2g01: Pyrazoloquinolones as Novel, Selective JNK1 inhibitors
  • 2gmx: Selective Aminopyridine-Based C-Jun N-terminal Kinase inhibitors with cellular activity 2gmx: Selective Aminopyridine-Based C-Jun N-terminal Kinase inhibitors with cellular activity
  • 2h96: Discovery of Potent, Highly Selective, and Orally Bioavailable Pyridine Carboxamide C-jun NH2-terminal Kinase Inhibitors 2h96: Discovery of Potent, Highly Selective, and Orally Bioavailable Pyridine Carboxamide C-jun NH2-terminal Kinase Inhibitors
  • 2no3: Novel 4-anilinopyrimidines as potent JNK1 Inhibitors 2no3: Novel 4-anilinopyrimidines as potent JNK1 Inhibitors
  • 2o0u: Crystal structure of human JNK3 complexed with N-{3-cyano-6--4,5,6,7-tetrahydrothienopyridin-2-yl}-1-naphthalenecarboxamide 2o0u: Crystal structure of human JNK3 complexed with N-{3-cyano-6--4,5,6,7-tetrahydrothienopyridin-2-yl}-1-naphthalenecarboxamide
  • 2o2u: Crystal structure of human JNK3 complexed with N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide 2o2u: Crystal structure of human JNK3 complexed with N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide
  • 2ok1: Crystal structure of JNK3 bound to N-benzyl-4-(4-(3-chlorophenyl)-1H-pyrazol-3-yl)-1H-pyrrole-2-carboxamide 2ok1: Crystal structure of JNK3 bound to N-benzyl-4-(4-(3-chlorophenyl)-1H-pyrazol-3-yl)-1H-pyrrole-2-carboxamide
Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)
Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)
Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
Dual-specificity kinases (EC 2.7.12)
MAP2K
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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