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O14733

- MP2K7_HUMAN

UniProt

O14733 - MP2K7_HUMAN

Protein

Dual specificity mitogen-activated protein kinase kinase 7

Gene

MAP2K7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by phosphorylation by specific MAP kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3, MAP3K11/MLK3 and MAP3K12/DLK.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei44 – 452Cleavage; by anthrax lethal factor
    Sitei76 – 772Cleavage; by anthrax lethal factor
    Binding sitei149 – 1491ATPPROSITE-ProRule annotation
    Active sitei243 – 2431Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi126 – 1349ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. JUN kinase kinase activity Source: Ensembl
    3. magnesium ion binding Source: UniProtKB
    4. MAP kinase kinase activity Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase binding Source: UniProtKB
    7. protein phosphatase binding Source: BHF-UCL
    8. protein serine/threonine kinase activity Source: UniProtKB-KW
    9. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of JUN kinase activity Source: BHF-UCL
    2. apoptotic process Source: UniProtKB-KW
    3. cellular response to sorbitol Source: Ensembl
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. innate immune response Source: Reactome
    6. JNK cascade Source: Reactome
    7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    9. positive regulation of neuron apoptotic process Source: Ensembl
    10. response to stress Source: UniProtKB
    11. signal transduction Source: ProtInc
    12. stress-activated MAPK cascade Source: UniProtKB
    13. toll-like receptor 10 signaling pathway Source: Reactome
    14. toll-like receptor 2 signaling pathway Source: Reactome
    15. toll-like receptor 3 signaling pathway Source: Reactome
    16. toll-like receptor 4 signaling pathway Source: Reactome
    17. toll-like receptor 5 signaling pathway Source: Reactome
    18. toll-like receptor 9 signaling pathway Source: Reactome
    19. toll-like receptor signaling pathway Source: Reactome
    20. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    21. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    22. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Apoptosis, Stress response

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.12.2. 2681.
    ReactomeiREACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    SignaLinkiO14733.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity mitogen-activated protein kinase kinase 7 (EC:2.7.12.2)
    Short name:
    MAP kinase kinase 7
    Short name:
    MAPKK 7
    Alternative name(s):
    JNK-activating kinase 2
    MAPK/ERK kinase 7
    Short name:
    MEK 7
    Stress-activated protein kinase kinase 4
    Short name:
    SAPK kinase 4
    Short name:
    SAPKK-4
    Short name:
    SAPKK4
    c-Jun N-terminal kinase kinase 2
    Short name:
    JNK kinase 2
    Short name:
    JNKK 2
    Gene namesi
    Name:MAP2K7
    Synonyms:JNKK2, MEK7, MKK7, PRKMK7, SKK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6847. MAP2K7.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA284.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 419418Dual specificity mitogen-activated protein kinase kinase 7PRO_0000086388Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei271 – 2711Phosphoserine; by MAP3KBy similarity
    Modified residuei275 – 2751Phosphothreonine; by MAP3KBy similarity

    Post-translational modificationi

    Activated by phosphorylation on Ser-271 and Thr-275 by MAP kinase kinase kinases (MAP3Ks).By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14733.
    PaxDbiO14733.
    PRIDEiO14733.

    PTM databases

    PhosphoSiteiO14733.

    Miscellaneous databases

    PMAP-CutDBO14733.

    Expressioni

    Tissue specificityi

    Ubiquitous; with highest level of expression in skeletal muscle. Isoform 3 is found at low levels in placenta, fetal liver, and skeletal muscle.3 Publications

    Gene expression databases

    ArrayExpressiO14733.
    BgeeiO14733.
    CleanExiHS_MAP2K7.
    GenevestigatoriO14733.

    Organism-specific databases

    HPAiCAB004262.
    HPA001633.

    Interactioni

    Subunit structurei

    Interacts with isoform 1 of VRK2. Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 By similarity. Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1 and MAP3K1/MEKK1 By similarity. Interacts with MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold proteins. Interacts with RASSF7, the interaction promotes phosphorylation.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFLARO15519-12EBI-492605,EBI-4567563
    LRRK2Q5S0073EBI-492605,EBI-5323863
    MAP3K7O433183EBI-492605,EBI-358684
    MAPK8P459833EBI-492627,EBI-286483
    MAPK8IP1Q9UQF25EBI-492605,EBI-78404

    Protein-protein interaction databases

    BioGridi111595. 34 interactions.
    IntActiO14733. 18 interactions.
    MINTiMINT-1378223.
    STRINGi9606.ENSP00000381066.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi105 – 11410
    Helixi117 – 1193
    Beta strandi120 – 1256
    Beta strandi134 – 1396
    Turni140 – 1423
    Beta strandi145 – 1528
    Helixi157 – 17216
    Turni173 – 1753
    Beta strandi182 – 1876
    Beta strandi189 – 1968
    Beta strandi200 – 2023
    Helixi203 – 2108
    Helixi216 – 23722
    Helixi246 – 2483
    Beta strandi249 – 2513
    Beta strandi257 – 2593
    Helixi286 – 2894
    Helixi302 – 31716
    Turni321 – 3244
    Helixi328 – 33710
    Beta strandi345 – 3473
    Helixi351 – 36010
    Turni365 – 3673
    Helixi371 – 3744
    Helixi378 – 3858
    Helixi390 – 39910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DYLX-ray2.45A101-405[»]
    ProteinModelPortaliO14733.
    SMRiO14733. Positions 53-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14733.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini120 – 380261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 5721D domainBy similarityAdd
    BLAST
    Regioni377 – 40024DVD domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2 – 3029Sequence AnalysisAdd
    BLAST

    Domaini

    The DVD domain (residues 377-400) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation.1 Publication
    The D domain (residues 37-57) contains a conserved docking site and is required for the binding to MAPK substrates.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108518.
    KOiK04431.
    OrthoDBiEOG7J9VPW.
    PhylomeDBiO14733.
    TreeFamiTF350701.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14733-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND    50
    GGSRSPSSES SPQHPTPPAR PRHMLGLPST LFTPRSMESI EIDQKLQEIM 100
    KQTGYLTIGG QRYQAEINDL ENLGEMGSGT CGQVWKMRFR KTGHVIAVKQ 150
    MRRSGNKEEN KRILMDLDVV LKSHDCPYIV QCFGTFITNT DVFIAMELMG 200
    TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI HRDVKPSNIL 250
    LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD 300
    IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS 350
    GDFQSFVKDC LTKDHRKRPK YNKLLEHSFI KRYETLEVDV ASWFKDVMAK 400
    TESPRTSGVL SQPHLPFFR 419
    Length:419
    Mass (Da):47,485
    Last modified:May 30, 2000 - v2
    Checksum:iF1B22E050F54299A
    GO
    Isoform 2 (identifier: O14733-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         111-111: Q → QVPPSLWRGEGGGPARLDPSWERQWGAGGGGRAPGTLQPSLSSQ

    Note: May be due to intron retention.

    Show »
    Length:462
    Mass (Da):51,881
    Checksum:iDF3496066961B0C7
    GO
    Isoform 3 (identifier: O14733-3) [UniParc]FASTAAdd to Basket

    Also known as: gamma1

    The sequence of this isoform differs from the canonical sequence as follows:
         42-42: T → IIVITLSPAPAPSQRAA

    Show »
    Length:435
    Mass (Da):49,071
    Checksum:i8812A87DB28F2C22
    GO
    Isoform 4 (identifier: O14733-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         312-312: L → LPCPSPSQ

    Note: No experimental confirmation available.

    Show »
    Length:426
    Mass (Da):48,182
    Checksum:i7934E29217D8A137
    GO

    Sequence cautioni

    The sequence AAB97813.1 differs from that shown. Reason: Frameshift at positions 402 and 410.
    The sequence AAB97813.1 differs from that shown. Reason: Erroneous termination at position 420. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941Q → H in AAB97813. (PubMed:9312068)Curated
    Sequence conflicti106 – 1061L → P in ABE03013. (PubMed:16442502)Curated
    Sequence conflicti133 – 1331Q → P in AAB97813. (PubMed:9312068)Curated
    Sequence conflicti142 – 1421T → N in AAB88048. (PubMed:9372971)Curated
    Sequence conflicti407 – 4071S → N in AAB97813. (PubMed:9312068)Curated
    Sequence conflicti415 – 4151L → LG in AAB97813. (PubMed:9312068)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181N → S.1 Publication
    Corresponds to variant rs56316660 [ dbSNP | Ensembl ].
    VAR_040825
    Natural varianti138 – 1381R → C.1 Publication
    Corresponds to variant rs56106612 [ dbSNP | Ensembl ].
    VAR_040826
    Natural varianti162 – 1621R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040827
    Natural varianti162 – 1621R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040828
    Natural varianti195 – 1951A → T.1 Publication
    Corresponds to variant rs55800262 [ dbSNP | Ensembl ].
    VAR_040829
    Natural varianti259 – 2591L → F.1 Publication
    Corresponds to variant rs1053566 [ dbSNP | Ensembl ].
    VAR_029890

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei42 – 421T → IIVITLSPAPAPSQRAA in isoform 3. 1 PublicationVSP_022309
    Alternative sequencei111 – 1111Q → QVPPSLWRGEGGGPARLDPS WERQWGAGGGGRAPGTLQPS LSSQ in isoform 2. 1 PublicationVSP_004883
    Alternative sequencei312 – 3121L → LPCPSPSQ in isoform 4. 1 PublicationVSP_022310

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF014401 mRNA. Translation: AAB88048.1.
    AF006689 mRNA. Translation: AAB97813.1. Sequence problems.
    AF013588 mRNA. Translation: AAC16272.1.
    AF013589 mRNA. Translation: AAC16273.1.
    DQ445915 mRNA. Translation: ABE03013.1.
    AF022805 mRNA. Translation: AAC26142.1.
    AK313899 mRNA. Translation: BAG36622.1.
    CH471139 Genomic DNA. Translation: EAW68964.1.
    CH471139 Genomic DNA. Translation: EAW68968.1.
    BC038295 mRNA. Translation: AAH38295.1.
    AF003199 mRNA. Translation: AAB63374.1.
    CCDSiCCDS42491.1. [O14733-1]
    RefSeqiNP_660186.1. NM_145185.2. [O14733-1]
    XP_005272546.1. XM_005272489.1. [O14733-3]
    XP_005272547.1. XM_005272490.1. [O14733-4]
    UniGeneiHs.531754.

    Genome annotation databases

    EnsembliENST00000397979; ENSP00000381066; ENSG00000076984. [O14733-1]
    ENST00000397981; ENSP00000381068; ENSG00000076984. [O14733-4]
    ENST00000397983; ENSP00000381070; ENSG00000076984. [O14733-3]
    GeneIDi5609.
    KEGGihsa:5609.
    UCSCiuc002mit.3. human. [O14733-1]
    uc002miv.2. human. [O14733-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF014401 mRNA. Translation: AAB88048.1 .
    AF006689 mRNA. Translation: AAB97813.1 . Sequence problems.
    AF013588 mRNA. Translation: AAC16272.1 .
    AF013589 mRNA. Translation: AAC16273.1 .
    DQ445915 mRNA. Translation: ABE03013.1 .
    AF022805 mRNA. Translation: AAC26142.1 .
    AK313899 mRNA. Translation: BAG36622.1 .
    CH471139 Genomic DNA. Translation: EAW68964.1 .
    CH471139 Genomic DNA. Translation: EAW68968.1 .
    BC038295 mRNA. Translation: AAH38295.1 .
    AF003199 mRNA. Translation: AAB63374.1 .
    CCDSi CCDS42491.1. [O14733-1 ]
    RefSeqi NP_660186.1. NM_145185.2. [O14733-1 ]
    XP_005272546.1. XM_005272489.1. [O14733-3 ]
    XP_005272547.1. XM_005272490.1. [O14733-4 ]
    UniGenei Hs.531754.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DYL X-ray 2.45 A 101-405 [» ]
    ProteinModelPortali O14733.
    SMRi O14733. Positions 53-402.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111595. 34 interactions.
    IntActi O14733. 18 interactions.
    MINTi MINT-1378223.
    STRINGi 9606.ENSP00000381066.

    Chemistry

    BindingDBi O14733.
    ChEMBLi CHEMBL3530.
    DrugBanki DB00773. Etoposide.
    GuidetoPHARMACOLOGYi 2068.

    PTM databases

    PhosphoSitei O14733.

    Proteomic databases

    MaxQBi O14733.
    PaxDbi O14733.
    PRIDEi O14733.

    Protocols and materials databases

    DNASUi 5609.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397979 ; ENSP00000381066 ; ENSG00000076984 . [O14733-1 ]
    ENST00000397981 ; ENSP00000381068 ; ENSG00000076984 . [O14733-4 ]
    ENST00000397983 ; ENSP00000381070 ; ENSG00000076984 . [O14733-3 ]
    GeneIDi 5609.
    KEGGi hsa:5609.
    UCSCi uc002mit.3. human. [O14733-1 ]
    uc002miv.2. human. [O14733-4 ]

    Organism-specific databases

    CTDi 5609.
    GeneCardsi GC19P007968.
    HGNCi HGNC:6847. MAP2K7.
    HPAi CAB004262.
    HPA001633.
    MIMi 603014. gene.
    neXtProti NX_O14733.
    PharmGKBi PA284.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108518.
    KOi K04431.
    OrthoDBi EOG7J9VPW.
    PhylomeDBi O14733.
    TreeFami TF350701.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 2681.
    Reactomei REACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    SignaLinki O14733.

    Miscellaneous databases

    EvolutionaryTracei O14733.
    GeneWikii MAP2K7.
    GenomeRNAii 5609.
    NextBioi 21802.
    PMAP-CutDB O14733.
    PROi O14733.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14733.
    Bgeei O14733.
    CleanExi HS_MAP2K7.
    Genevestigatori O14733.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    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 ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of human JNKK2, a novel jun NH2-terminal kinase-specific kinase."
      Wu Z., Wu J., Jacinto E., Karin M.
      Mol. Cell. Biol. 17:7407-7416(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Heart and Skeletal muscle.
    2. "Identification of c-Jun NH2-terminal protein kinase (JNK)-activating kinase 2 as an activator of JNK but not p38."
      Lu X., Nemoto S., Lin A.
      J. Biol. Chem. 272:24751-24754(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION.
    3. "Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli."
      Foltz I.N., Gerl R.E., Wieler J.S., Luckach M., Salmon R.A., Schrader J.W.
      J. Biol. Chem. 273:9344-9351(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANT PHE-259.
      Tissue: Fetal kidney.
    4. "Cloning and expression of human mitogen-activated protein kinase kinase 7gamma1."
      Michael L., Swantek J., Robinson M.J.
      Biochem. Biophys. Res. Commun. 341:679-683(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ENZYME REGULATION, TISSUE SPECIFICITY.
    5. "Molecular cloning of human JNKK2 reveals a novel kinase module for c-Jun N-terminal kinase activation."
      Yang J., New L., Yong J., Han J., Su B.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF MAPK8/JNK1 AND MAPK9/JNK2.
    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 1).
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 4).
      Tissue: Testis.
    9. "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase."
      Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.
      Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-260 (ISOFORMS 1/4).
    10. "The JIP group of mitogen-activated protein kinase scaffold proteins."
      Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.
      Mol. Cell. Biol. 19:7245-7254(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK8IP1/JIP1 AND MAPK8IP2/JIP2.
    11. "Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
      Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
      Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
    12. "Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade."
      Matsuura H., Nishitoh H., Takeda K., Matsuzawa A., Amagasa T., Ito M., Yoshioka K., Ichijo H.
      J. Biol. Chem. 277:40703-40709(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK8IP3/JIP3.
    13. "Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases."
      Takekawa M., Tatebayashi K., Saito H.
      Mol. Cell 18:295-306(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    14. "Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
      Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
      PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VRK2.
    15. "Differential regulation and properties of MAPKs."
      Raman M., Chen W., Cobb M.H.
      Oncogene 26:3100-3112(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ENZYME REGULATION.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. "Diverse physiological functions of MKK4 and MKK7 during early embryogenesis."
      Asaoka Y., Nishina H.
      J. Biochem. 148:393-401(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    18. "RASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting the activity of phosphorylated-MKK7."
      Takahashi S., Ebihara A., Kajiho H., Kontani K., Nishina H., Katada T.
      Cell Death Differ. 18:645-655(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASSF7.
    19. "The bottleneck of JNK signaling: molecular and functional characteristics of MKK4 and MKK7."
      Haeusgen W., Herdegen T., Waetzig V.
      Eur. J. Cell Biol. 90:536-544(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON REGULATION, REVIEW ON FUNCTION.
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Crystal structure of human mitogen-activated protein kinase kinase 7 activated mutant (s287d, t291d)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 101-405.
    22. "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] SER-118; CYS-138; CYS-162; HIS-162 AND THR-195.

    Entry informationi

    Entry nameiMP2K7_HUMAN
    AccessioniPrimary (citable) accession number: O14733
    Secondary accession number(s): B2R9S5
    , D6W659, O14648, O14816, O60452, O60453, Q1PG43, Q8IY10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 145 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 19
      Human chromosome 19: 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