Mitogen-activated protein kinase 9

Mitogen-activated protein kinase 9 is an enzyme that in humans is encoded by the MAPK9 gene.[5]

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
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-B1.3 Start 49,846,751 bp[2] End 49,886,421 bp[2]
RNA expression pattern 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 • GO:0001948 protein binding • ATP binding • transcription factor binding • JUN kinase activity • protein serine/threonine/tyrosine kinase activity Cellular component • cytosol • nucleoplasm • mitochondrion • cell 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 • GO:0007243 intracellular signal transduction • regulation of sequence-specific 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: 49.85 – 49.89 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.
• 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.

External links

• MAP Kinase Resource .

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