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P45984

- MK09_HUMAN

UniProt

P45984 - MK09_HUMAN

Protein

Mitogen-activated protein kinase 9

Gene

MAPK9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    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.
    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.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551ATPPROSITE-ProRule annotation
    Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 409ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: Ensembl
    3. JUN kinase activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to growth factor stimulus Source: Ensembl
    2. cellular response to interleukin-1 Source: Ensembl
    3. cellular response to lipopolysaccharide Source: Ensembl
    4. cellular response to tumor necrosis factor Source: Ensembl
    5. cellular response to UV Source: Ensembl
    6. central nervous system development Source: Ensembl
    7. Fc-epsilon receptor signaling pathway Source: Reactome
    8. innate immune response Source: Reactome
    9. JNK cascade Source: UniProtKB
    10. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    11. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    12. neuron projection development Source: Ensembl
    13. positive regulation of apoptotic process Source: Ensembl
    14. positive regulation of apoptotic signaling pathway Source: Ensembl
    15. positive regulation of cell morphogenesis involved in differentiation Source: Ensembl
    16. positive regulation of chemokine production Source: Ensembl
    17. positive regulation of gene expression Source: BHF-UCL
    18. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    19. positive regulation of nitric oxide biosynthetic process Source: Ensembl
    20. positive regulation of nitric-oxide synthase biosynthetic process Source: Ensembl
    21. positive regulation of prostaglandin biosynthetic process Source: Ensembl
    22. positive regulation of prostaglandin secretion Source: Ensembl
    23. positive regulation of protein phosphorylation Source: Ensembl
    24. positive regulation of transcription, DNA-templated Source: Ensembl
    25. protein targeting to mitochondrion Source: Ensembl
    26. regulation of JNK cascade Source: Ensembl
    27. regulation of protein ubiquitination Source: Ensembl
    28. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    29. release of cytochrome c from mitochondria Source: Ensembl
    30. response to amine Source: Ensembl
    31. response to cadmium ion Source: Ensembl
    32. response to drug Source: Ensembl
    33. response to mechanical stimulus Source: Ensembl
    34. response to stress Source: ProtInc
    35. response to toxic substance Source: Ensembl
    36. stress-activated MAPK cascade Source: Reactome
    37. toll-like receptor 10 signaling pathway Source: Reactome
    38. toll-like receptor 2 signaling pathway Source: Reactome
    39. toll-like receptor 3 signaling pathway Source: Reactome
    40. toll-like receptor 4 signaling pathway Source: Reactome
    41. toll-like receptor 5 signaling pathway Source: Reactome
    42. toll-like receptor 9 signaling pathway Source: Reactome
    43. toll-like receptor signaling pathway Source: Reactome
    44. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    45. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    46. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 2681.
    ReactomeiREACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    SignaLinkiP45984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 9 (EC:2.7.11.24)
    Short name:
    MAP kinase 9
    Short name:
    MAPK 9
    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 namesi
    Name:MAPK9
    Synonyms:JNK2, PRKM9, SAPK1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6886. MAPK9.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30630.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Mitogen-activated protein kinase 9PRO_0000186273Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphothreonine; by MAP2K71 Publication
    Modified residuei185 – 1851Phosphotyrosine; by MAP2K41 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Autophosphorylated in vitro.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP45984.
    PaxDbiP45984.
    PRIDEiP45984.

    2D gel databases

    REPRODUCTION-2DPAGEP45984.

    PTM databases

    PhosphoSiteiP45984.

    Expressioni

    Gene expression databases

    ArrayExpressiP45984.
    BgeeiP45984.
    CleanExiHS_MAPK9.
    GenevestigatoriP45984.

    Organism-specific databases

    HPAiCAB008910.
    HPA055483.

    Interactioni

    Subunit structurei

    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.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAT3P407633EBI-713586,EBI-518675

    Protein-protein interaction databases

    BioGridi111587. 71 interactions.
    DIPiDIP-270N.
    DIP-281N.
    IntActiP45984. 39 interactions.
    MINTiMINT-1400230.
    STRINGi9606.ENSP00000321410.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 156
    Beta strandi18 – 236
    Beta strandi26 – 338
    Beta strandi38 – 458
    Turni46 – 494
    Beta strandi50 – 589
    Helixi64 – 7916
    Beta strandi88 – 925
    Turni98 – 1003
    Beta strandi105 – 1095
    Beta strandi112 – 1143
    Helixi115 – 1184
    Helixi125 – 14420
    Helixi154 – 1563
    Beta strandi157 – 1593
    Beta strandi165 – 1673
    Turni176 – 1783
    Beta strandi180 – 1834
    Helixi189 – 1913
    Helixi194 – 1974
    Helixi206 – 22015
    Helixi232 – 24110
    Helixi246 – 2505
    Helixi254 – 2618
    Helixi271 – 2744
    Helixi277 – 2793
    Helixi286 – 30116
    Turni306 – 3083
    Helixi312 – 3165
    Helixi319 – 3224
    Helixi327 – 3304
    Turni341 – 3433
    Helixi349 – 36012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E7OX-ray2.14A/B7-362[»]
    3NPCX-ray2.35A/B1-364[»]
    ProteinModelPortaliP45984.
    SMRiP45984. Positions 7-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45984.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 321296Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi183 – 1853TXY

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    KOiK04440.
    OMAiSSMSTEH.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiP45984.
    TreeFamiTF105100.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01772. JNKMAPKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform Alpha-2 (identifier: P45984-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI    50
    NVAVKKLSRP FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE 100
    FQDVYLVMEL MDANLCQVIH MELDHERMSY LLYQMLCGIK HLHSAGIIHR 150
    DLKPSNIVVK SDCTLKILDF GLARTACTNF MMTPYVVTRY YRAPEVILGM 200
    GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ LGTPSAEFMK 250
    KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 300
    MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE 350
    EWKELIYKEV MDWEERSKNG VVKDQPSDAA VSSNATPSQS SSINDISSMS 400
    TEQTLASDTD SSLDASTGPL EGCR 424
    Length:424
    Mass (Da):48,139
    Last modified:January 24, 2006 - v2
    Checksum:i9C15DA79981290AF
    GO
    Isoform Alpha-1 (identifier: P45984-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:382
    Mass (Da):44,051
    Checksum:iA1963C01247BDFF4
    GO
    Isoform Beta-1 (identifier: P45984-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:382
    Mass (Da):44,223
    Checksum:i808ED1F85085CB4E
    GO
    Isoform Beta-2 (identifier: P45984-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:424
    Mass (Da):48,311
    Checksum:iA1B5FB794F373EB9
    GO
    Isoform 5 (identifier: P45984-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:242
    Mass (Da):27,334
    Checksum:iB37D5C58904AE9F1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511N → S in AAA56831. (PubMed:7969172)Curated
    Sequence conflicti51 – 511N → S in AAC50606. (PubMed:8654373)Curated
    Sequence conflicti51 – 511N → S in AAC50608. (PubMed:8654373)Curated
    Sequence conflicti51 – 511N → S in AAC50609. (PubMed:8654373)Curated
    Sequence conflicti377 – 3771S → P in AAA74740. (PubMed:8001819)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042260
    Natural varianti56 – 561K → N in a head & Neck squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042261
    Natural varianti246 – 2461A → T.1 Publication
    Corresponds to variant rs35421153 [ dbSNP | Ensembl ].
    VAR_042262
    Natural varianti268 – 2681G → A.1 Publication
    Corresponds to variant rs35693958 [ dbSNP | Ensembl ].
    VAR_025175
    Natural varianti366 – 3661R → I.1 Publication
    Corresponds to variant rs55736180 [ dbSNP | Ensembl ].
    VAR_042263

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei216 – 23015GELVK…QGTDH → AEMVLHKVLFPGRDY in isoform Beta-1 and isoform Beta-2. 1 PublicationVSP_004834Add
    BLAST
    Alternative sequencei230 – 24213HIDQW…IEQLG → RILPRDLGPAMLS in isoform 5. 1 PublicationVSP_041908Add
    BLAST
    Alternative sequencei243 – 424182Missing in isoform 5. 1 PublicationVSP_041909Add
    BLAST
    Alternative sequencei378 – 42447DAAVS…LEGCR → AQMQQ in isoform Alpha-1 and isoform Beta-1. CuratedVSP_004835Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS43409.1. [P45984-2]
    CCDS43410.1. [P45984-3]
    CCDS4453.1. [P45984-1]
    CCDS4454.1. [P45984-4]
    CCDS47356.1. [P45984-5]
    PIRiA55480.
    S71102.
    RefSeqiNP_001128516.1. NM_001135044.1. [P45984-5]
    NP_002743.3. NM_002752.4. [P45984-1]
    NP_620707.1. NM_139068.2. [P45984-2]
    NP_620708.1. NM_139069.2. [P45984-3]
    NP_620709.1. NM_139070.2. [P45984-4]
    XP_006714954.1. XM_006714891.1. [P45984-1]
    UniGeneiHs.484371.

    Genome annotation databases

    EnsembliENST00000343111; ENSP00000345524; ENSG00000050748. [P45984-3]
    ENST00000393360; ENSP00000377028; ENSG00000050748. [P45984-2]
    ENST00000425491; ENSP00000397422; ENSG00000050748. [P45984-5]
    ENST00000452135; ENSP00000394560; ENSG00000050748. [P45984-1]
    ENST00000455781; ENSP00000389338; ENSG00000050748. [P45984-4]
    GeneIDi5601.
    KEGGihsa:5601.
    UCSCiuc003mls.4. human. [P45984-1]
    uc003mlt.4. human. [P45984-2]
    uc003mlv.4. human. [P45984-3]
    uc010jlc.3. human. [P45984-4]
    uc011dgx.2. human. [P45984-5]

    Polymorphism databases

    DMDMi85700366.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS43409.1. [P45984-2 ]
    CCDS43410.1. [P45984-3 ]
    CCDS4453.1. [P45984-1 ]
    CCDS4454.1. [P45984-4 ]
    CCDS47356.1. [P45984-5 ]
    PIRi A55480.
    S71102.
    RefSeqi NP_001128516.1. NM_001135044.1. [P45984-5 ]
    NP_002743.3. NM_002752.4. [P45984-1 ]
    NP_620707.1. NM_139068.2. [P45984-2 ]
    NP_620708.1. NM_139069.2. [P45984-3 ]
    NP_620709.1. NM_139070.2. [P45984-4 ]
    XP_006714954.1. XM_006714891.1. [P45984-1 ]
    UniGenei Hs.484371.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P45984.
    SMRi P45984. Positions 7-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111587. 71 interactions.
    DIPi DIP-270N.
    DIP-281N.
    IntActi P45984. 39 interactions.
    MINTi MINT-1400230.
    STRINGi 9606.ENSP00000321410.

    Chemistry

    BindingDBi P45984.
    ChEMBLi CHEMBL4179.
    GuidetoPHARMACOLOGYi 1497.

    PTM databases

    PhosphoSitei P45984.

    Polymorphism databases

    DMDMi 85700366.

    2D gel databases

    REPRODUCTION-2DPAGE P45984.

    Proteomic databases

    MaxQBi P45984.
    PaxDbi P45984.
    PRIDEi P45984.

    Protocols and materials databases

    DNASUi 5601.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343111 ; ENSP00000345524 ; ENSG00000050748 . [P45984-3 ]
    ENST00000393360 ; ENSP00000377028 ; ENSG00000050748 . [P45984-2 ]
    ENST00000425491 ; ENSP00000397422 ; ENSG00000050748 . [P45984-5 ]
    ENST00000452135 ; ENSP00000394560 ; ENSG00000050748 . [P45984-1 ]
    ENST00000455781 ; ENSP00000389338 ; ENSG00000050748 . [P45984-4 ]
    GeneIDi 5601.
    KEGGi hsa:5601.
    UCSCi uc003mls.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

    CTDi 5601.
    GeneCardsi GC05M179595.
    HGNCi HGNC:6886. MAPK9.
    HPAi CAB008910.
    HPA055483.
    MIMi 602896. gene.
    neXtProti NX_P45984.
    PharmGKBi PA30630.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    KOi K04440.
    OMAi SSMSTEH.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi P45984.
    TreeFami TF105100.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    Reactomei REACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    SignaLinki P45984.

    Miscellaneous databases

    ChiTaRSi MAPK9. human.
    EvolutionaryTracei P45984.
    GeneWikii Mitogen-activated_protein_kinase_9.
    GenomeRNAii 5601.
    NextBioi 21752.
    PROi P45984.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45984.
    Bgeei P45984.
    CleanExi HS_MAPK9.
    Genevestigatori P45984.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01772. JNKMAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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: PHOSPHORYLATION AT THR-183 AND TYR-185, 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. 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. 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.

    Entry informationi

    Entry nameiMK09_HUMAN
    AccessioniPrimary (citable) accession number: P45984
    Secondary accession number(s): A8K0S3
    , B5BU66, B5M0B4, D3DWQ8, D3DWQ9, Q15708, Q15710, Q15711, Q8N5C5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3