Mitogen-activated protein kinase 9

MAPK9
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3E7O, 3NPC
Identifiers
Aliases	MAPK9, JNK-55, JNK2, JNK2A, JNK2ALPHA, JNK2B, JNK2BETA, PRKM9, SAPK, SAPK1a, p54a, p54aSAPK, mitogen-activated protein kinase 9
External IDs	OMIM: 602896; MGI: 1346862; HomoloGene: 55685; GeneCards: MAPK9; OMA:MAPK9 - orthologs
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q35.3 Start 180,233,143 bp[1] End 180,292,099 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B1.2 Start 49,737,578 bp[2] End 49,777,248 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in middle temporal gyrus Brodmann area 23 cerebellar cortex cerebellar hemisphere superior frontal gyrus prefrontal cortex Pons lateral nuclear group of thalamus right hemisphere of cerebellum dorsolateral prefrontal cortex Top expressed in dorsomedial hypothalamic nucleus atrioventricular valve cerebellar cortex superior frontal gyrus parotid gland medial vestibular nucleus submandibular gland lateral hypothalamus ventral tegmental area neural layer of retina More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity MAP kinase activity kinase activity protein serine/threonine kinase activity protein binding ATP binding transcription factor binding JUN kinase activity protein serine/threonine/tyrosine kinase activity Cellular component cytosol nucleoplasm mitochondrion nucleus cytoplasm neuron projection Biological process response to cadmium ion phosphorylation rhythmic process positive regulation of apoptotic signaling pathway positive regulation of podosome assembly Fc-epsilon receptor signaling pathway protein phosphorylation positive regulation of macrophage derived foam cell differentiation positive regulation of gene expression JUN phosphorylation regulation of circadian rhythm JNK cascade response to mechanical stimulus positive regulation of apoptotic process neuron development cellular response to organic substance protein localization to tricellular tight junction cellular response to reactive oxygen species cellular response to cadmium ion peptidyl-serine phosphorylation positive regulation of protein ubiquitination positive regulation of transcription factor catabolic process regulation of gene expression intracellular signal transduction regulation of DNA-binding transcription factor activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5601 26420 Ensembl ENSG00000050748 ENSMUSG00000020366 UniProt P45984 Q9WTU6 RefSeq (mRNA) NM_001135044 NM_001308244 NM_002752 NM_139068 NM_139069 NM_139070 NM_001364607 NM_001364608 NM_001364609 NM_001364610 NM_001364611 NM_001364612 NM_001364613 NM_001163671 NM_001163672 NM_016961 NM_207692 RefSeq (protein) NP_001128516 NP_001295173 NP_002743 NP_620707 NP_620708 NP_620709 NP_001351536 NP_001351537 NP_001351538 NP_001351539 NP_001351540 NP_001351541 NP_001351542 NP_001157143 NP_001157144 NP_058657 NP_997575 Location (UCSC) Chr 5: 180.23 – 180.29 Mb Chr 11: 49.74 – 49.78 Mb PubMed search [3] [4]
Wikidata
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Mitogen-activated protein kinase 9 is an enzyme that in humans is encoded by the MAPK9 gene.[5]

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 kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation-induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.[6]

Interactions

Mitogen-activated protein kinase 9 has been shown to interact with:

• Grb2,[7][8]
• MAPK8IP1,[9][10]
• MAPK8IP2,[9]
• MAPK8IP3[11][12]
• P53,[13][14] and
• TOB1.[15]

References

1. GRCh38: Ensembl release 89: ENSG00000050748 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020366 – Ensembl, 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. Kallunki T, Su B, Tsigelny I, Sluss HK, Dérijard B, Moore G, Davis R, Karin M (Dec 1994). "JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation". Genes & Development. 8 (24): 2996–3007. doi:10.1101/gad.8.24.2996. PMID 8001819.
6. "Entrez Gene: MAPK9 mitogen-activated protein kinase 9".
7. Saleem A, Datta R, Yuan ZM, Kharbanda S, Kufe D (Dec 1995). "Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents". Cell Growth & Differentiation. 6 (12): 1651–8. PMID 9019171.
8. Kharbanda S, Saleem A, Shafman T, Emoto Y, Taneja N, Rubin E, Weichselbaum R, Woodgett J, Avruch J, Kyriakis J (Aug 1995). "Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase". The Journal of Biological Chemistry. 270 (32): 18871–4. doi:10.1074/jbc.270.32.18871. PMID 7642542.
9. Yasuda J, Whitmarsh AJ, Cavanagh J, Sharma M, Davis RJ (Oct 1999). "The JIP group of mitogen-activated protein kinase scaffold proteins". Molecular and Cellular Biology. 19 (10): 7245–54. doi:10.1128/mcb.19.10.7245. PMC 84717. PMID 10490659.
10. Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis RJ (Sep 1998). "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science. 281 (5383): 1671–4. Bibcode:1998Sci...281.1671W. doi:10.1126/science.281.5383.1671. PMID 9733513.
11. Ito M, Yoshioka K, Akechi M, Yamashita S, Takamatsu N, Sugiyama K, Hibi M, Nakabeppu Y, Shiba T, Yamamoto KI (Nov 1999). "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway". Molecular and Cellular Biology. 19 (11): 7539–48. doi:10.1128/mcb.19.11.7539. PMC 84763. PMID 10523642.
12. Kelkar N, Gupta S, Dickens M, Davis RJ (Feb 2000). "Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3". Molecular and Cellular Biology. 20 (3): 1030–43. doi:10.1128/mcb.20.3.1030-1043.2000. PMC 85220. PMID 10629060.
13. Hu MC, Qiu WR, Wang YP (Nov 1997). "JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases". Oncogene. 15 (19): 2277–87. doi:10.1038/sj.onc.1201401. PMID 9393873.
14. Lin Y, Khokhlatchev A, Figeys D, Avruch J (Dec 2002). "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis". The Journal of Biological Chemistry. 277 (50): 47991–8001. doi:10.1074/jbc.M202630200. PMID 12384512.
15. Maekawa M, Nishida E, Tanoue T (Oct 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". The Journal of Biological Chemistry. 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.

Further reading

• Lin A (2006). "The JNK Signaling Pathway (Molecular Biology Intelligence Unit)". Landes Bioscience. 1: 1–97. ISBN 978-1587061202.
• Davis RJ (2000). "Signal transduction by the JNK group of MAP kinases". Cell. 103 (2): 239–52. doi:10.1016/S0092-8674(00)00116-1. PMID 11057897. S2CID 343677.
• Liu J, Lin A (2007). "Wiring the cell signaling circuitry by the NF-kappa B and JNK1 crosstalk and its applications in human diseases". Oncogene. 26 (22): 3267–78. doi:10.1038/sj.onc.1210417. PMID 17496921. S2CID 28428831.

External links

• MAP Kinase Resource Archived 2021-04-15 at the Wayback Machine.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.