P45984 (MK09_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 9
Short name=MAP kinase 9
Short name=MAPK 9
EC=2.7.11.24

Alternative name(s):
JNK-55
Stress-activated protein kinase 1a
Short name=SAPK1a
Stress-activated protein kinase JNK2
c-Jun N-terminal kinase 2

Gene names

Name:	MAPK9
Synonyms:	JNK2, PRKM9, SAPK1A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Ref.12 Ref.15 Ref.18 Ref.21 Ref.22 Ref.23 MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it. Ref.12 Ref.15 Ref.18 Ref.21 Ref.22 Ref.23
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium. Ref.13
Enzyme regulation	Activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7 phosphorylates Tyr-183 preferentially. Inhibited by dual specificity phosphatases, such as DUSP1.
Subunit structure	Interacts with MECOM and DCLK2 By similarity. Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway. Interacts with NFATC4. Interacts with ATF7; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN. Interacts with BCL10. Interacts with CTNNB1 and GSK3B. Ref.12 Ref.14 Ref.16 Ref.17 Ref.21
Subcellular location	Cytoplasm. Nucleus Ref.21.
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome cellular response to UV Inferred from electronic annotation. Source: Compara cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to interleukin-1 Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara central nervous system development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of apoptotic signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cell morphogenesis involved in differentiation Inferred from electronic annotation. Source: Compara positive regulation of chemokine production Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from mutant phenotype PubMed 18262097. Source: BHF-UCL positive regulation of macrophage derived foam cell differentiation Inferred from mutant phenotype PubMed 18262097. Source: BHF-UCL positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of prostaglandin biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of prostaglandin secretion Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara protein targeting to mitochondrion Inferred from electronic annotation. Source: Compara regulation of JNK cascade Inferred from electronic annotation. Source: Compara regulation of protein ubiquitination Inferred from electronic annotation. Source: Compara regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara response to amine stimulus Inferred from electronic annotation. Source: Compara response to cadmium ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from electronic annotation. Source: Compara toll-like receptor 10 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 5 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 9 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR1:TLR2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR6:TLR2 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome cytosolic part Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW JUN kinase activity Inferred from direct assay Ref.3. Source: UniProtKB cysteine-type endopeptidase activator activity involved in apoptotic process Inferred from electronic annotation. Source: Compara transcription factor binding Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAT3	P40763	3	EBI-713586,EBI-518675

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha-2 (identifier: P45984-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Alpha-1 (identifier: P45984-2)

The sequence of this isoform differs from the canonical sequence as follows:
     378-424: DAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR → AQMQQ

Isoform Beta-1 (identifier: P45984-3)

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: GELVKGCVIFQGTDH → AEMVLHKVLFPGRDY
     378-424: DAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR → AQMQQ

Isoform Beta-2 (identifier: P45984-4)

The sequence of this isoform differs from the canonical sequence as follows:
     216-230: GELVKGCVIFQGTDH → AEMVLHKVLFPGRDY

Isoform 5 (identifier: P45984-5)

The sequence of this isoform differs from the canonical sequence as follows:
     230-242: HIDQWNKVIEQLG → RILPRDLGPAMLS
     243-424: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

Mitogen-activated protein kinase 9

PRO_0000186273

Regions

Domain

26 – 321

296

Protein kinase

Nucleotide binding

32 – 40

9

ATP By similarity

Motif

183 – 185

3

TXY

Sites

Active site

151

1

Proton acceptor By similarity

Binding site

55

1

ATP By similarity

Amino acid modifications

Modified residue

183

1

Phosphothreonine; by MAP2K7

Modified residue

185

1

Phosphotyrosine; by MAP2K4

Natural variations

Alternative sequence

216 – 230

15

GELVK…QGTDH → AEMVLHKVLFPGRDY in isoform Beta-1 and isoform Beta-2.

VSP_004834

Alternative sequence

230 – 242

13

HIDQW…IEQLG → RILPRDLGPAMLS in isoform 5.

VSP_041908

Alternative sequence

243 – 424

182

Missing in isoform 5.

VSP_041909

Alternative sequence

378 – 424

47

DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1.

VSP_004835

Natural variant

13

1

V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.26

VAR_042260

Natural variant

56

1

K → N in a head & Neck squamous cell carcinoma sample; somatic mutation. Ref.26

VAR_042261

Natural variant

246

1

A → T. Ref.26
Corresponds to variant rs35421153 [ dbSNP | Ensembl ].

VAR_042262

Natural variant

268

1

G → A. Ref.7
Corresponds to variant rs35693958 [ dbSNP | Ensembl ].

VAR_025175

Natural variant

366

1

R → I. Ref.26
Corresponds to variant rs55736180 [ dbSNP | Ensembl ].

VAR_042263

Experimental info

Sequence conflict

51

1

N → S in AAA56831. Ref.1

Sequence conflict

51

1

N → S in AAC50606. Ref.3

Sequence conflict

51

1

N → S in AAC50608. Ref.3

Sequence conflict

51

1

N → S in AAC50609. Ref.3

Sequence conflict

377

1

S → P in AAA74740. Ref.2

Secondary structure

1

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424

Helix Strand Turn

Details...

Beta strand

10 – 15

6

Beta strand

18 – 23

6

Beta strand

26 – 33

8

Beta strand

38 – 45

8

Turn

46 – 49

4

Beta strand

50 – 58

9

Helix

64 – 79

16

Beta strand

88 – 92

5

Turn

98 – 100

3

Beta strand

105 – 109

5

Beta strand

112 – 114

3

Helix

115 – 118

4

Helix

125 – 144

20

Helix

154 – 156

3

Beta strand

157 – 159

3

Beta strand

165 – 167

3

Turn

176 – 178

3

Beta strand

180 – 183

4

Helix

189 – 191

3

Helix

194 – 197

4

Helix

206 – 220

15

Helix

232 – 241

10

Helix

246 – 250

5

Helix

254 – 261

8

Helix

271 – 274

4

Helix

277 – 279

3

Helix

286 – 301

16

Turn

306 – 308

3

Helix

312 – 316

5

Helix

319 – 322

4

Helix

327 – 330

4

Turn

341 – 343

3

Helix

349 – 360

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-2 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 9C15DA79981290AF	FASTA	424	48,139
	10 20 30 40 50 60 MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 70 80 90 100 110 120 FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 130 140 150 160 170 180 MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 190 200 210 220 230 240 MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ 250 260 270 280 290 300 LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 310 320 330 340 350 360 MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV 370 380 390 400 410 420 MDWEERSKNG VVKDQPSDAA VSSNATPSQS SSINDISSMS TEQTLASDTD SSLDASTGPL EGCR
	Isoform Alpha-1 [UniParc]. Checksum: A1963C01247BDFF4	FASTA	382	44,051
	10 20 30 40 50 60 MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 70 80 90 100 110 120 FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 130 140 150 160 170 180 MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 190 200 210 220 230 240 MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ 250 260 270 280 290 300 LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 310 320 330 340 350 360 MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV 370 380 MDWEERSKNG VVKDQPSAQM QQ
	Isoform Beta-1 [UniParc]. Checksum: 808ED1F85085CB4E	FASTA	382	44,223
	10 20 30 40 50 60 MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 70 80 90 100 110 120 FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 130 140 150 160 170 180 MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 190 200 210 220 230 240 MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ 250 260 270 280 290 300 LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 310 320 330 340 350 360 MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV 370 380 MDWEERSKNG VVKDQPSAQM QQ
	Isoform Beta-2 [UniParc]. Checksum: A1B5FB794F373EB9	FASTA	424	48,311
	10 20 30 40 50 60 MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 70 80 90 100 110 120 FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 130 140 150 160 170 180 MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 190 200 210 220 230 240 MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ 250 260 270 280 290 300 LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 310 320 330 340 350 360 MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV 370 380 390 400 410 420 MDWEERSKNG VVKDQPSDAA VSSNATPSQS SSINDISSMS TEQTLASDTD SSLDASTGPL EGCR
	Isoform 5 [UniParc]. Checksum: B37D5C58904AE9F1	FASTA	242	27,334
	10 20 30 40 50 60 MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 70 80 90 100 110 120 FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 130 140 150 160 170 180 MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 190 200 210 220 230 240 MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMGELVK GCVIFQGTDR ILPRDLGPAM LS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Signal transduction by tumor necrosis factor mediated by JNK protein kinases." Sluss H.K., Barrett T., Derijard B., Davis R.J. Mol. Cell. Biol. 14:8376-8384(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation." Kallunki T., Su B., Tsigelny I., Sluss H.K., Derijard B., Moore G., Davis R., Karin M. Genes Dev. 8:2996-3007(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Selective interaction of JNK protein kinase isoforms with transcription factors." Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K., Derijard B., Davis R.J. EMBO J. 15:2760-2770(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Brain.
[4]	"Molecular cloning and characterization of novel human JNK2 (MAPK9) transcript variants that show different stimulation activities on AP-1." Wang P., Xiong Y., Ma C., Shi T., Ma D. BMB Rep. 43:738-743(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2). Tissue: Amygdala.
[7]	NIEHS SNPs program Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-268.
[8]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
[9]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[12]	"Role of the ATFa/JNK2 complex in Jun activation." De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F., Kedinger C., Chatton B. Oncogene 18:3491-3500(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATF7, FUNCTION.
[13]	"Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7." Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M., Cohen P. Biochem. J. 352:145-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION BY MAP2K4 AND MAP2K7, COFACTOR.
[14]	"Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein." Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A. Biochem. J. 389:73-82(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPAG9.
[15]	"The nucleolus as a stress sensor: JNK2 inactivates the transcription factor TIF-IA and down-regulates rRNA synthesis." Mayer C., Bierhoff H., Grummt I. Genes Dev. 19:933-941(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RRN3.
[16]	"Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation." Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y., Bode A.M., Dong Z. Cancer Res. 67:8725-8735(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFATC4.
[17]	"The CARMA1-Bcl10 signaling complex selectively regulates JNK2 kinase in the T cell receptor-signaling pathway." Blonska M., Pappu B.P., Matsumoto R., Li H., Su B., Wang D., Lin X. Immunity 26:55-66(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCL10.
[18]	"Cooperation between JNK1 and JNK2 in activation of p53 apoptotic pathway." Oleinik N.V., Krupenko N.I., Krupenko S.A. Oncogene 26:7222-7230(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP53.
[19]	"CARMA1-mediated NF-kappaB and JNK activation in lymphocytes." Blonska M., Lin X. Immunol. Rev. 228:199-211(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[20]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"GSK3beta is involved in JNK2-mediated beta-catenin inhibition." Hu D., Bi X., Fang W., Han A., Yang W. PLoS ONE 4:E6640-E6640(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
[22]	"c-Jun NH2-terminal kinase-2 mediates osmotic stress-induced tight junction disruption in the intestinal epithelium." Samak G., Suzuki T., Bhargava A., Rao R.K. Am. J. Physiol. 299:G572-G584(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"JNK phosphorylates Yes-associated protein (YAP) to regulate apoptosis." Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A., Basu S. Cell Death Dis. 1:E29-E29(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF YAP1.
[24]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity." Shaw D., Wang S.M., Villasenor A.G., Tsing S., Walter D., Browner M.F., Barnett J., Kuglstatter A. J. Mol. Biol. 383:885-893(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 7-362.
[26]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-13; ASN-56; THR-246 AND ILE-366.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L31951 mRNA. Translation: AAA56831.1.
U09759 mRNA. Translation: AAA74740.1.
U34821 mRNA. Translation: AAC50606.1.
U35002 mRNA. Translation: AAC50608.1.
U35003 mRNA. Translation: AAC50609.1.
EU927388 mRNA. Translation: ACH57450.1.
CR536580 mRNA. Translation: CAG38817.1.
AK289638 mRNA. Translation: BAF82327.1.
DQ066599 Genomic DNA. Translation: AAY46156.1.
AB451302 mRNA. Translation: BAG70116.1.
AB451355 mRNA. Translation: BAG70169.1.
AC008610 Genomic DNA. No translation available.
AC104115 Genomic DNA. No translation available.
CH471165 Genomic DNA. Translation: EAW53759.1.
CH471165 Genomic DNA. Translation: EAW53757.1.
CH471165 Genomic DNA. Translation: EAW53758.1.
CH471165 Genomic DNA. Translation: EAW53762.1.
BC032539 mRNA. Translation: AAH32539.1.

IPI

IPI00024673.
IPI00220382.
IPI00220383.
IPI00303550.

PIR

A55480.
S71102.

RefSeq

NP_001128516.1. NM_001135044.1.
NP_002743.3. NM_002752.4.
NP_620707.1. NM_139068.2.
NP_620708.1. NM_139069.2.
NP_620709.1. NM_139070.2.

UniGene

Hs.484371.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E7O	X-ray	2.14	A/B	7-362	[»]
3NPC	X-ray	2.35	A/B	1-364	[»]

ProteinModelPortal

P45984.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-270N.
DIP-281N.

IntAct

P45984. 23 interactions.

MINT

MINT-1400230.

STRING

9606.ENSP00000321410.

PTM databases

PhosphoSite

P45984.

Polymorphism databases

DMDM

85700366.

2D gel databases

REPRODUCTION-2DPAGE

P45984.

Proteomic databases

PaxDb

P45984.

PRIDE

P45984.

Protocols and materials databases

DNASU

5601.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343111; ENSP00000345524; ENSG00000050748.
ENST00000393360; ENSP00000377028; ENSG00000050748.
ENST00000425491; ENSP00000397422; ENSG00000050748.
ENST00000452135; ENSP00000394560; ENSG00000050748.
ENST00000455781; ENSP00000389338; ENSG00000050748.

GeneID

5601.

KEGG

hsa:5601.

UCSC

uc003mls.4. human.
uc003mlt.4. human.
uc003mlv.4. human.
uc010jlc.3. human.
uc011dgx.2. human.

Organism-specific databases

CTD

5601.

GeneCards

GC05M179595.

HGNC

HGNC:6886. MAPK9.

HPA

CAB008910.

MIM

602896. gene.

neXtProt

NX_P45984.

PharmGKB

PA30630.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

KO

K04440.

OMA

DWEERNK.

OrthoDB

EOG48SGT3.

PhylomeDB

P45984.

Enzyme and pathway databases

BRENDA

2.7.11.24. 2681.

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
foxopathway. FoxO family signaling.
glypican_3pathway. Glypican 3 network.
il12_stat4pathway. IL12 signaling mediated by STAT4.
il2_1pathway. IL2-mediated signaling events.
p75ntrpathway. p75(NTR)-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Reactome

REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

SignaLink

P45984.

Gene expression databases

ArrayExpress

P45984.

Bgee

P45984.

CleanEx

HS_MAPK9.

Genevestigator

P45984.

GermOnline

ENSG00000050748. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01772. JNKMAPKINASE.

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P45984.

ChEMBL

CHEMBL4179.

ChiTaRS

MAPK9. human.

EvolutionaryTrace

P45984.

GenomeRNAi

5601.

NextBio

21752.

SOURCE

Search...

Entry information

Entry name

MK09_HUMAN

Accession

Primary (citable) accession number: P45984
Secondary accession number(s): A8K0S3 , B5BU66, B5M0B4, D3DWQ8, D3DWQ9, Q15708, Q15710, Q15711, Q8N5C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 24, 2006
Last modified:	May 29, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.