Mitogen-activated protein kinase 9

Rendering based on PDB 3E7O.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3E7O, 3NPC

Identifiers

Symbols

MAPK9 ; JNK-55; JNK2; JNK2A; JNK2ALPHA; JNK2B; JNK2BETA; PRKM9; SAPK; SAPK1a; p54a; p54aSAPK

External IDs

OMIM: 602896 MGI: 1346862 HomoloGene: 55685 IUPHAR: 1497 ChEMBL: 4179 GeneCards: MAPK9 Gene

EC number

2.7.11.24

Gene ontology
Molecular function	• JUN kinase activity • protein binding • ATP binding • transcription factor binding • cysteine-type endopeptidase activator activity involved in apoptotic process • mitogen-activated protein kinase kinase kinase binding
Cellular component	• nucleoplasm • mitochondrion • cytosol
Biological process	• release of cytochrome c from mitochondria • positive regulation of protein phosphorylation • toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • protein targeting to mitochondrion • activation of cysteine-type endopeptidase activity involved in apoptotic process • response to stress • JNK cascade • JUN phosphorylation • central nervous system development • response to mechanical stimulus • response to toxic substance • positive regulation of gene expression • positive regulation of macrophage derived foam cell differentiation • positive regulation of cell morphogenesis involved in differentiation • response to amine • neuron projection development • positive regulation of prostaglandin biosynthetic process • regulation of protein ubiquitination • positive regulation of prostaglandin secretion • positive regulation of chemokine production • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • toll-like receptor 5 signaling pathway • toll-like receptor 9 signaling pathway • toll-like receptor 10 signaling pathway • cellular response to UV • TRIF-dependent toll-like receptor signaling pathway • Fc-epsilon receptor signaling pathway • toll-like receptor TLR1:TLR2 signaling pathway • toll-like receptor TLR6:TLR2 signaling pathway • response to drug • positive regulation of apoptotic process • innate immune response • positive regulation of nitric oxide biosynthetic process • positive regulation of transcription, DNA-templated • regulation of JNK cascade • response to cadmium ion • regulation of sequence-specific DNA binding transcription factor activity • stress-activated MAPK cascade • positive regulation of nitric-oxide synthase biosynthetic process • cellular response to lipopolysaccharide • cellular response to interleukin-1 • cellular response to tumor necrosis factor • cellular response to growth factor stimulus • positive regulation of apoptotic signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
179.66 – 179.72 Mb

Chr 11:
49.85 – 49.89 Mb

PubMed search

Mitogen-activated protein kinase 9 is an enzyme that in humans is encoded by the MAPK9 gene.^[1]

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.^[2]

Interactions

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

References

↑ Kallunki T, Su B, Tsigelny I, Sluss HK, Derijard B, Moore G, Davis R, Karin M (January 1995). "JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation". Genes Dev 8 (24): 2996–3007. doi:10.1101/gad.8.24.2996. PMID 8001819.
↑ "Entrez Gene: MAPK9 mitogen-activated protein kinase 9".
↑ Saleem A, Datta R, Yuan ZM, Kharbanda S, Kufe D (December 1995). "Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents". Cell Growth Differ. 6 (12): 1651–8. PMID 9019171.
↑ Kharbanda S, Saleem A, Shafman T, Emoto Y, Taneja N, Rubin E, Weichselbaum R, Woodgett J, Avruch J, Kyriakis J (August 1995). "Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase". J. Biol. Chem. 270 (32): 18871–4. doi:10.1074/jbc.270.32.18871. PMID 7642542.
↑ 5.0 5.1 Yasuda J, Whitmarsh AJ, Cavanagh J, Sharma M, Davis RJ (October 1999). "The JIP group of mitogen-activated protein kinase scaffold proteins". Mol. Cell. Biol. 19 (10): 7245–54. PMC 84717. PMID 10490659.
↑ Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis RJ (September 1998). "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science 281 (5383): 1671–4. doi:10.1126/science.281.5383.1671. PMID 9733513.
↑ 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. PMC 84763. PMID 10523642.
↑ 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.
↑ Hu MC, Qiu WR, Wang YP (November 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.
↑ Lin Y, Khokhlatchev A, Figeys D, Avruch J (December 2002). "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis". J. Biol. Chem. 277 (50): 47991–8001. doi:10.1074/jbc.M202630200. PMID 12384512.
↑ Maekawa M, Nishida E, Tanoue T (October 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". J. Biol. Chem. 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.

External links

MAP Kinase Resource .

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.
Freedman BD, Liu QH, Del Corno M, Collman RG (2004). "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 et al. (2004). "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.
Denys H; Desmet R; Stragier M et al. (1978). "Cystitis emphysematosa". Acta urologica Belgica 45 (4): 327–31. PMID 602896.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Livingstone C, Patel G, Jones N (1995). "ATF-2 contains a phosphorylation-dependent transcriptional activation domain". EMBO J. 14 (8): 1785–97. PMC 398272. PMID 7737129.
Sluss HK, Barrett T, Dérijard B, Davis RJ (1994). "Signal transduction by tumor necrosis factor mediated by JNK protein kinases". Mol. Cell. Biol. 14 (12): 8376–84. PMC 359376. PMID 7969172.
Gille H, Strahl T, Shaw PE (1996). "Activation of ternary complex factor Elk-1 by stress-activated protein kinases". Curr. Biol. 5 (10): 1191–200. doi:10.1016/S0960-9822(95)00235-1. PMID 8548291.
Chu Y; Solski PA; Khosravi-Far R et al. (1996). "The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation". J. Biol. Chem. 271 (11): 6497–501. doi:10.1074/jbc.271.11.6497. PMID 8626452.
Bocco JL; Bahr A; Goetz J et al. (1996). "In vivo association of ATFa with JNK/SAP kinase activities". Oncogene 12 (9): 1971–80. PMID 8649858.
Gupta S; Barrett T; Whitmarsh AJ et al. (1996). "Selective interaction of JNK protein kinase isoforms with transcription factors". EMBO J. 15 (11): 2760–70. PMC 450211. PMID 8654373.
Kallunki T, Deng T, Hibi M, Karin M (1997). "c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions". Cell 87 (5): 929–39. doi:10.1016/S0092-8674(00)81999-6. PMID 8945519.
Jabado N; Pallier A; Jauliac S et al. (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.
Janknecht R, Hunter T (1997). "Convergence of MAP kinase pathways on the ternary complex factor Sap-1a". EMBO J. 16 (7): 1620–7. doi:10.1093/emboj/16.7.1620. PMC 1169766. PMID 9130707.
Fukunaga R, Hunter T (1997). "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates". EMBO J. 16 (8): 1921–33. doi:10.1093/emboj/16.8.1921. PMC 1169795. PMID 9155018.
Chow CW; Rincón M; Cavanagh J et al. (1997). "Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway". Science 278 (5343): 1638–41. doi:10.1126/science.278.5343.1638. PMID 9374467.
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 et al. (1998). "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.
Fuchs SY; Xie B; Adler V et al. (1998). "c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors". J. Biol. Chem. 272 (51): 32163–8. doi:10.1074/jbc.272.51.32163. PMID 9405416.

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

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)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

(3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDC2L5 CRKRS PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(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)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Biochemistry overview
Enzymes overview
By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
  - 2.7.10
  - 11-12
- 8
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
  - 22
  - 23
  - 24
- 5
- 6
- 7
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

Mitogen-activated protein kinase 9

Interactions

References

External links

Further reading