MAPK10

MAPK10
Available structures PDB Ortholog 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
Aliases	MAPK10, JNK3, JNK3A, PRKM10, SAPK1b, p493F12, p54bSAPK, mitogen-activated protein kinase 10
External IDs	MGI: 1346863 HomoloGene: 56439 GeneCards: MAPK10
Genetically Related Diseases
peripheral artery disease[1]
Targeted by Drug
pyrazolanthrone[2]
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • MAP kinase activity • kinase activity • protein serine/threonine kinase activity • protein binding • JUN kinase activity • ATP binding • MAP kinase kinase activity Cellular component • cytoplasm • cytosol • membrane • nucleoplasm • mitochondrion • nucleus • plasma membrane • intracellular Biological process • phosphorylation • response to light stimulus • rhythmic process • Fc-epsilon receptor signaling pathway • protein phosphorylation • JNK cascade • regulation of sequence-specific DNA binding transcription factor activity • regulation of circadian rhythm • signal transduction • JUN phosphorylation • activation of MAPK activity • MAPK cascade Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
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_001081567 NM_009158 NM_001310683 NM_001310685 NM_001310686 NM_001318102 NM_001318131
RefSeq (protein)	NP_002744.1 NP_620446.1 NP_620448.1 NP_001304996.1 NP_001304997.1 NP_001304998.1 NP_001304997.1	NP_001297615.1
Location (UCSC)	Chr 4: 86.02 – 86.59 Mb	Chr 5: 102.91 – 103.21 Mb
PubMed search	[3]	[4]
Wikidata

View/Edit Human

View/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.^[5][6][7]

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.^[7]

Interactions

MAPK10 has been shown to interact with MAPK8IP3.^[8][9][10]

References

1. "Diseases that are genetically associated with MAPK10 view/edit references on wikidata".
2. "Drugs that physically interact with Mitogen-activated protein kinase 10 view/edit references on wikidata".
3. "Human PubMed Reference:".
4. "Mouse PubMed Reference:".
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. 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. PMID 12189133.

Further reading

• Freedman BD, Liu QH, Del Corno M, Collman RG (2003). "HIV-1 gp120 chemokine receptor-mediated signaling in human macrophages". Immunol. Res. 27 (2-3): 261–76. doi:10.1385/IR:27:2-3:261. PMID 12857973.
• Lee C, Liu QH, Tomkowicz B, Yi Y, Freedman BD, Collman RG (2003). "Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways". J. Leukoc. Biol. 74 (5): 676–82. doi:10.1189/jlb.0503206. PMID 12960231.
• Pulverer BJ, Kyriakis JM, Avruch J, Nikolakaki E, Woodgett JR (1991). "Phosphorylation of c-jun mediated by MAP kinases". Nature. 353 (6345): 670–4. doi:10.1038/353670a0. PMID 1922387.
• Mohit AA, Martin JH, Miller CA (1995). "p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system". Neuron. 14 (1): 67–78. doi:10.1016/0896-6273(95)90241-4. PMID 7826642.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Jabado N, Pallier A, Jauliac S, Fischer A, Hivroz C (1997). "gp160 of HIV or anti-CD4 monoclonal antibody ligation of CD4 induces inhibition of JNK and ERK-2 activities in human peripheral CD4+ T lymphocytes". Eur. J. Immunol. 27 (2): 397–404. doi:10.1002/eji.1830270209. PMID 9045910.
• Yang DD, Kuan CY, Whitmarsh AJ, Rincón M, Zheng TS, Davis RJ, Rakic P, Flavell RA (1997). "Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene". Nature. 389 (6653): 865–70. doi:10.1038/39899. PMID 9349820.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hu MC, Qiu WR, Wang YP (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.
• Lannuzel A, Barnier JV, Hery C, Huynh VT, Guibert B, Gray F, Vincent JD, Tardieu M (1997). "Human immunodeficiency virus type 1 and its coat protein gp120 induce apoptosis and activate JNK and ERK mitogen-activated protein kinases in human neurons". Ann. Neurol. 42 (6): 847–56. doi:10.1002/ana.410420605. PMID 9403476.
• Xie X, Gu Y, Fox T, Coll JT, Fleming MA, Markland W, Caron PR, Wilson KP, Su MS (1998). "Crystal structure of JNK3: a kinase implicated in neuronal apoptosis". Structure. 6 (8): 983–91. doi:10.1016/S0969-2126(98)00100-2. PMID 9739089.
• "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 1998. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Koyano S, Ito M, Takamatsu N, Shiba T, Yamamoto K, Yoshioka K (1999). "A novel Jun N-terminal kinase (JNK)-binding protein that enhances the activation of JNK by MEK kinase 1 and TGF-beta-activated kinase 1". FEBS Lett. 457 (3): 385–8. doi:10.1016/S0014-5793(99)01084-4. PMID 10471813.
• Ito M, Yoshioka K, Akechi M, Yamashita S, Takamatsu N, Sugiyama K, Hibi M, Nakabeppu Y, Shiba T, Yamamoto KI (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.
• Kelkar N, Gupta S, Dickens M, Davis RJ (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.
• Lisnock J, Griffin P, Calaycay J, Frantz B, Parsons J, O'Keefe SJ, LoGrasso P (2000). "Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3 alpha 1". Biochemistry. 39 (11): 3141–8. doi:10.1021/bi992410. PMID 10715136.
• McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ (2000). "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science. 290 (5496): 1574–7. doi:10.1126/science.290.5496.1574. PMID 11090355.
• Pouysségur J (2000). "Signal transduction. An arresting start for MAPK". Science. 290 (5496): 1515–8. doi:10.1126/science.290.5496.1515. PMID 11185509.
• Habelhah H, Shah K, Huang L, Ostareck-Lederer A, Burlingame AL, Shokat KM, Hentze MW, Ronai Z (2001). "ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation". Nat. Cell Biol. 3 (3): 325–30. doi:10.1038/35060131. PMID 11231586.

External links

• MAP Kinase Resource .