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P45984 (MK09_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

JNK cascade

Inferred from direct assay Ref.3. Source: UniProtKB

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent 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: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell morphogenesis involved in differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine production

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein targeting to mitochondrion

Inferred from electronic annotation. Source: Ensembl

regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to amine

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to stress

Traceable author statement Ref.1. Source: ProtInc

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

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

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP 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: Ensembl

transcription factor binding

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT3P407633EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Mitogen-activated protein kinase 9
PRO_0000186273

Regions

Domain26 – 321296Protein kinase
Nucleotide binding32 – 409ATP By similarity
Motif183 – 1853TXY

Sites

Active site1511Proton acceptor By similarity
Binding site551ATP By similarity

Amino acid modifications

Modified residue1831Phosphothreonine; by MAP2K7
Modified residue1851Phosphotyrosine; by MAP2K4

Natural variations

Alternative sequence216 – 23015GELVK…QGTDH → AEMVLHKVLFPGRDY in isoform Beta-1 and isoform Beta-2.
VSP_004834
Alternative sequence230 – 24213HIDQW…IEQLG → RILPRDLGPAMLS in isoform 5.
VSP_041908
Alternative sequence243 – 424182Missing in isoform 5.
VSP_041909
Alternative sequence378 – 42447DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1.
VSP_004835
Natural variant131V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.26
VAR_042260
Natural variant561K → N in a head & Neck squamous cell carcinoma sample; somatic mutation. Ref.26
VAR_042261
Natural variant2461A → T. Ref.26
Corresponds to variant rs35421153 [ dbSNP | Ensembl ].
VAR_042262
Natural variant2681G → A. Ref.7
Corresponds to variant rs35693958 [ dbSNP | Ensembl ].
VAR_025175
Natural variant3661R → I. Ref.26
Corresponds to variant rs55736180 [ dbSNP | Ensembl ].
VAR_042263

Experimental info

Sequence conflict511N → S in AAA56831. Ref.1
Sequence conflict511N → S in AAC50606. Ref.3
Sequence conflict511N → S in AAC50608. Ref.3
Sequence conflict511N → S in AAC50609. Ref.3
Sequence conflict3771S → P in AAA74740. Ref.2

Secondary structure

............................................................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-2 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 9C15DA79981290AF

FASTA42448,139
        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 

« Hide

Isoform Alpha-1 [UniParc].

Checksum: A1963C01247BDFF4
Show »

FASTA38244,051
Isoform Beta-1 [UniParc].

Checksum: 808ED1F85085CB4E
Show »

FASTA38244,223
Isoform Beta-2 [UniParc].

Checksum: A1B5FB794F373EB9
Show »

FASTA42448,311
Isoform 5 [UniParc].

Checksum: B37D5C58904AE9F1
Show »

FASTA24227,334

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.

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.
PIRA55480.
S71102.
RefSeqNP_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.
UniGeneHs.484371.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E7OX-ray2.14A/B7-362[»]
3NPCX-ray2.35A/B1-364[»]
ProteinModelPortalP45984.
SMRP45984. Positions 7-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111587. 70 interactions.
DIPDIP-270N.
DIP-281N.
IntActP45984. 36 interactions.
MINTMINT-1400230.
STRING9606.ENSP00000321410.

Chemistry

BindingDBP45984.
ChEMBLCHEMBL2096667.
GuidetoPHARMACOLOGY1497.

PTM databases

PhosphoSiteP45984.

Polymorphism databases

DMDM85700366.

2D gel databases

REPRODUCTION-2DPAGEP45984.

Proteomic databases

PaxDbP45984.
PRIDEP45984.

Protocols and materials databases

DNASU5601.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343111; ENSP00000345524; ENSG00000050748. [P45984-3]
ENST00000393360; ENSP00000377028; ENSG00000050748. [P45984-2]
ENST00000425491; ENSP00000397422; ENSG00000050748. [P45984-5]
ENST00000452135; ENSP00000394560; ENSG00000050748. [P45984-1]
ENST00000455781; ENSP00000389338; ENSG00000050748. [P45984-4]
GeneID5601.
KEGGhsa:5601.
UCSCuc003mls.4. human. [P45984-1]
uc003mlt.4. human. [P45984-2]
uc003mlv.4. human. [P45984-3]
uc010jlc.3. human. [P45984-4]
uc011dgx.2. human. [P45984-5]

Organism-specific databases

CTD5601.
GeneCardsGC05M179595.
HGNCHGNC:6886. MAPK9.
HPACAB008910.
HPA055483.
MIM602896. gene.
neXtProtNX_P45984.
PharmGKBPA30630.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
KOK04440.
OMAWEERNKN.
OrthoDBEOG7PCJGV.
PhylomeDBP45984.
TreeFamTF105100.

Enzyme and pathway databases

BRENDA2.7.11.24. 2681.
ReactomeREACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP45984.

Gene expression databases

ArrayExpressP45984.
BgeeP45984.
CleanExHS_MAPK9.
GenevestigatorP45984.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01772. JNKMAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPK9. human.
EvolutionaryTraceP45984.
GeneWikiMitogen-activated_protein_kinase_9.
GenomeRNAi5601.
NextBio21752.
PROP45984.
SOURCESearch...

Entry information

Entry nameMK09_HUMAN
AccessionPrimary (citable) accession number: P45984
Secondary accession number(s): A8K0S3 expand/collapse secondary AC list , 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: April 16, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM