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Q9WVS8

- MK07_MOUSE

UniProt

Q9WVS8 - MK07_MOUSE

Protein

Mitogen-activated protein kinase 7

Gene

Mapk7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression By similarity. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF) By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei84 – 841ATPPROSITE-ProRule annotation
    Active sitei182 – 1821Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 699ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: UniProtKB
    5. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. cellular response to hydrogen peroxide Source: Ensembl
    4. cellular response to transforming growth factor beta stimulus Source: Ensembl
    5. negative regulation of apoptotic process Source: MGI
    6. negative regulation of endothelial cell apoptotic process Source: Ensembl
    7. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    8. negative regulation of heterotypic cell-cell adhesion Source: Ensembl
    9. negative regulation of NFAT protein import into nucleus Source: MGI
    10. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
    11. negative regulation of response to cytokine stimulus Source: Ensembl
    12. peptidyl-serine phosphorylation Source: MGI
    13. positive regulation of protein metabolic process Source: Ensembl
    14. positive regulation of transcription from RNA polymerase II promoter in response to stress Source: Ensembl
    15. protein phosphorylation Source: UniProtKB
    16. regulation of angiogenesis Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Differentiation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_210064. ERKs are inactivated.
    REACT_215063. ERK/MAPK targets.
    REACT_216232. Signalling to ERK5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 7 (EC:2.7.11.24)
    Short name:
    MAP kinase 7
    Short name:
    MAPK 7
    Alternative name(s):
    Big MAP kinase 1
    Short name:
    BMK-1
    Extracellular signal-regulated kinase 5
    Short name:
    ERK-5
    Gene namesi
    Name:Mapk7
    Synonyms:Bmk1, Erk5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1346347. Mapk7.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. NucleusPML body By similarity
    Note: Translocates to the nucleus upon activation.By similarity
    Isoform 1 : Cytoplasm By similarity. Nucleus By similarity
    Note: Isoform 1 is detected in cytoplasm and nucleus.By similarity
    Isoform 2 : Nucleus By similarity
    Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation By similarity.By similarity
    Isoform 3 : Nucleus By similarity
    Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. nucleus Source: MGI
    4. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 806805Mitogen-activated protein kinase 7PRO_0000186261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei710 – 7101PhosphoserineBy similarity
    Modified residuei723 – 7231PhosphothreonineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ9WVS8.

    PTM databases

    PhosphoSiteiQ9WVS8.

    Expressioni

    Tissue specificityi

    Detected in testis, brain, kidney, lung and heart. Detected in total embryo (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9WVS8.
    CleanExiMM_MAPK7.
    GenevestigatoriQ9WVS8.

    Interactioni

    Subunit structurei

    Interacts with MAP2K5 By similarity. Forms oligomers. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D By similarity. Interacts with SGK1 By similarity. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204806. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WVS8.
    SMRiQ9WVS8. Positions 11-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 347293Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 7776Required for cytoplasmic targetingAdd
    BLAST
    Regioni78 – 13962Required for binding to MAP2K5Add
    BLAST
    Regioni140 – 406267Necessary for oligomerizationAdd
    BLAST
    Regioni407 – 806400May not be required for kinase activity; required to stimulate MEF2C activityAdd
    BLAST
    Regioni505 – 53935Nuclear localization signalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi219 – 2213TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi434 – 46532Pro-richAdd
    BLAST
    Compositional biasi521 – 5244Poly-Arg
    Compositional biasi578 – 700123Pro-richAdd
    BLAST

    Domaini

    The second proline-rich region may interact with actin targeting the kinase to a specific location in the cell.
    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.
    GeneTreeiENSGT00550000074298.
    HOVERGENiHBG108137.
    InParanoidiQ9WVS8.
    KOiK04464.
    OMAiIIETIGT.
    PhylomeDBiQ9WVS8.
    TreeFamiTF105099.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9WVS8-1) [UniParc]FASTAAdd to Basket

    Also known as: Big MAP kinase 1a, mERK5a

    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

    MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD    50
    VGDEYEIIET IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL 100
    RELKILKHFK HDNIIAIKDI LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS 150
    SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH RDLKPSNLLV NENCELKIGD 200
    FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT QAIDLWSVGC 250
    IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 300
    LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY 350
    HDPDDEPDCA PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR 400
    FQPSLQPVAS EPVCPDVEMP SPWAPSGDCA MESPPPALPP CSDPAPDTVD 450
    LTLQPAPPAS ELAPPKREGA ISDNTKAALK AALLKSLRSR LRDGPSAPLE 500
    APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER KERGAGTLGG 550
    PSTDPLAGLV LSDNDRSLLE RWTRMARPPA PAPAPAPAPA PAPSSAQPTS 600
    TPTGPVSQST GPLQPAGSIP GPASQPVCPP PGPVPQPAGP IPAPLQTAPS 650
    TSLLASQSLV PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV 700
    NLVTQQLSKS QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA 750
    DGPQDGQADS ASLSASLLAD WLEGHGMNPA DIESLQREIQ MDSPMLLSDL 800
    PDLQEP 806
    Length:806
    Mass (Da):87,733
    Last modified:November 1, 1999 - v1
    Checksum:iE7CC41C4BBDE0633
    GO
    Isoform 2 (identifier: Q9WVS8-2) [UniParc]FASTAAdd to Basket

    Also known as: Big MAP kinase 1b, mERK5b

    The sequence of this isoform differs from the canonical sequence as follows:
         2-77: AEPLKEEDGE...VVSSARRRLT → MCGLLSRG

    Note: May not have a kinase activity. May not stimulate MEF2C activity. May function as dominant negative inhibitor of the ERK5 signaling pathway.

    Show »
    Length:738
    Mass (Da):80,511
    Checksum:i7909E06820499AF5
    GO
    Isoform 3 (identifier: Q9WVS8-3) [UniParc]FASTAAdd to Basket

    Also known as: Big MAP kinase 1c, mERK5c

    The sequence of this isoform differs from the canonical sequence as follows:
         2-139: Missing.

    Note: May not have a kinase activity. May not stimulate MEF2C activity. May function as dominant negative inhibitor of the ERK5 signaling pathway.

    Show »
    Length:668
    Mass (Da):72,594
    Checksum:i8B0E505EA2545FFA
    GO
    Isoform 4 (identifier: Q9WVS8-4) [UniParc]FASTAAdd to Basket

    Also known as: Big MAP kinase 1d, mERK5-T

    The sequence of this isoform differs from the canonical sequence as follows:
         493-806: DGPSAPLEAP...LSDLPDLQEP → GGVWAQQLSG

    Note: Unable to translocate from the cytoplasm to the nucleus.

    Show »
    Length:502
    Mass (Da):55,914
    Checksum:i905BD56BC58913D8
    GO
    Isoform 5 (identifier: Q9WVS8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         757-806: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:756
    Mass (Da):82,314
    Checksum:iC0CCFA5D2F8C84F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911N → D in BAE28357. (PubMed:16141072)Curated
    Sequence conflicti308 – 3081P → H in BAE28357. (PubMed:16141072)Curated
    Sequence conflicti331 – 3311E → K in AAI00399. (PubMed:15489334)Curated
    Sequence conflicti409 – 4091A → V in AAD39394. (PubMed:11139578)Curated
    Sequence conflicti409 – 4091A → V in AAD39395. (PubMed:11139578)Curated
    Sequence conflicti409 – 4091A → V in AAD39396. (PubMed:11139578)Curated
    Sequence conflicti424 – 4241A → R in AAD39394. (PubMed:11139578)Curated
    Sequence conflicti424 – 4241A → R in AAD39395. (PubMed:11139578)Curated
    Sequence conflicti424 – 4241A → R in AAD39396. (PubMed:11139578)Curated
    Sequence conflicti578 – 5781P → PPAPA in BAE28357. (PubMed:16141072)Curated
    Sequence conflicti578 – 5781P → PPAPA in BAE33103. (PubMed:16141072)Curated
    Sequence conflicti588 – 5881A → R in AAD39394. (PubMed:11139578)Curated
    Sequence conflicti588 – 5881A → R in AAD39395. (PubMed:11139578)Curated
    Sequence conflicti588 – 5881A → R in AAD39396. (PubMed:11139578)Curated
    Sequence conflicti592 – 5921A → Q in AAD39394. (PubMed:11139578)Curated
    Sequence conflicti592 – 5921A → Q in AAD39395. (PubMed:11139578)Curated
    Sequence conflicti592 – 5921A → Q in AAD39396. (PubMed:11139578)Curated
    Sequence conflicti618 – 6181S → C in AAD39394. (PubMed:11139578)Curated
    Sequence conflicti618 – 6181S → C in AAD39395. (PubMed:11139578)Curated
    Sequence conflicti618 – 6181S → C in AAD39396. (PubMed:11139578)Curated
    Sequence conflicti642 – 6421P → A in AAD39394. (PubMed:11139578)Curated
    Sequence conflicti642 – 6421P → A in AAD39395. (PubMed:11139578)Curated
    Sequence conflicti642 – 6421P → A in AAD39396. (PubMed:11139578)Curated
    Sequence conflicti803 – 8031L → V in BAE28357. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 139138Missing in isoform 3. 1 PublicationVSP_035201Add
    BLAST
    Alternative sequencei2 – 7776AEPLK…RRRLT → MCGLLSRG in isoform 2. 2 PublicationsVSP_035202Add
    BLAST
    Alternative sequencei493 – 806314DGPSA…DLQEP → GGVWAQQLSG in isoform 4. 1 PublicationVSP_035203Add
    BLAST
    Alternative sequencei757 – 80650Missing in isoform 5. 1 PublicationVSP_035204Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB019373 mRNA. Translation: BAA82039.1.
    AF126159 mRNA. Translation: AAD39394.1.
    AF126160 mRNA. Translation: AAD39395.1.
    AF126161 mRNA. Translation: AAD39396.1.
    AK148119 mRNA. Translation: BAE28357.1.
    AK155187 mRNA. Translation: BAE33103.1.
    AY534740 mRNA. Translation: AAS38576.1.
    BC100398 mRNA. Translation: AAI00399.1.
    AL604029 Genomic DNA. Translation: CAI24182.1.
    AL604029 Genomic DNA. Translation: CAI24184.1.
    AL604029 Genomic DNA. Translation: CAI24185.1.
    CCDSiCCDS24814.1. [Q9WVS8-1]
    RefSeqiNP_001277962.1. NM_001291033.1.
    NP_001277963.1. NM_001291034.1. [Q9WVS8-1]
    NP_001277964.1. NM_001291035.1.
    NP_001277965.1. NM_001291036.1.
    NP_001277966.1. NM_001291037.1.
    NP_035971.1. NM_011841.2. [Q9WVS8-1]
    XP_006533340.1. XM_006533277.1. [Q9WVS8-1]
    XP_006533341.1. XM_006533278.1. [Q9WVS8-5]
    UniGeneiMm.38172.

    Genome annotation databases

    EnsembliENSMUST00000079080; ENSMUSP00000078087; ENSMUSG00000001034. [Q9WVS8-1]
    GeneIDi23939.
    KEGGimmu:23939.
    UCSCiuc007jho.1. mouse. [Q9WVS8-2]
    uc007jhp.1. mouse. [Q9WVS8-1]
    uc007jht.1. mouse. [Q9WVS8-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB019373 mRNA. Translation: BAA82039.1 .
    AF126159 mRNA. Translation: AAD39394.1 .
    AF126160 mRNA. Translation: AAD39395.1 .
    AF126161 mRNA. Translation: AAD39396.1 .
    AK148119 mRNA. Translation: BAE28357.1 .
    AK155187 mRNA. Translation: BAE33103.1 .
    AY534740 mRNA. Translation: AAS38576.1 .
    BC100398 mRNA. Translation: AAI00399.1 .
    AL604029 Genomic DNA. Translation: CAI24182.1 .
    AL604029 Genomic DNA. Translation: CAI24184.1 .
    AL604029 Genomic DNA. Translation: CAI24185.1 .
    CCDSi CCDS24814.1. [Q9WVS8-1 ]
    RefSeqi NP_001277962.1. NM_001291033.1.
    NP_001277963.1. NM_001291034.1. [Q9WVS8-1 ]
    NP_001277964.1. NM_001291035.1.
    NP_001277965.1. NM_001291036.1.
    NP_001277966.1. NM_001291037.1.
    NP_035971.1. NM_011841.2. [Q9WVS8-1 ]
    XP_006533340.1. XM_006533277.1. [Q9WVS8-1 ]
    XP_006533341.1. XM_006533278.1. [Q9WVS8-5 ]
    UniGenei Mm.38172.

    3D structure databases

    ProteinModelPortali Q9WVS8.
    SMRi Q9WVS8. Positions 11-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204806. 3 interactions.

    PTM databases

    PhosphoSitei Q9WVS8.

    Proteomic databases

    PRIDEi Q9WVS8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079080 ; ENSMUSP00000078087 ; ENSMUSG00000001034 . [Q9WVS8-1 ]
    GeneIDi 23939.
    KEGGi mmu:23939.
    UCSCi uc007jho.1. mouse. [Q9WVS8-2 ]
    uc007jhp.1. mouse. [Q9WVS8-1 ]
    uc007jht.1. mouse. [Q9WVS8-4 ]

    Organism-specific databases

    CTDi 5598.
    MGIi MGI:1346347. Mapk7.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074298.
    HOVERGENi HBG108137.
    InParanoidi Q9WVS8.
    KOi K04464.
    OMAi IIETIGT.
    PhylomeDBi Q9WVS8.
    TreeFami TF105099.

    Enzyme and pathway databases

    Reactomei REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_210064. ERKs are inactivated.
    REACT_215063. ERK/MAPK targets.
    REACT_216232. Signalling to ERK5.

    Miscellaneous databases

    NextBioi 303745.
    PROi Q9WVS8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9WVS8.
    CleanExi MM_MAPK7.
    Genevestigatori Q9WVS8.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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 PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus."
      Kamakura S., Moriguchi T., Nishida E.
      J. Biol. Chem. 274:26563-26571(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains."
      Yan C., Luo H., Lee J.-D., Abe J.-I., Berk B.C.
      J. Biol. Chem. 276:10870-10878(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: C57BL/6.
    3. "Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice variant."
      McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R.
      Gene 345:183-190(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION.
      Strain: C57BL/6.
      Tissue: Bone marrow.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: NOD.
    5. "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 5).
      Strain: C57BL/6J.
      Tissue: Kidney.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. "Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells."
      Dinev D., Jordan B.W.M., Neufeld B., Lee J.-D., Lindemann D., Rapp U.R., Ludwig S.
      EMBO Rep. 2:829-834(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival."
      Dong F., Gutkind J.S., Larner A.C.
      J. Biol. Chem. 276:10811-10816(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure."
      Hayashi M., Kim S.W., Imanaka-Yoshida K., Yoshida T., Abel E.D., Eliceiri B., Yang Y., Ulevitch R.J., Lee J.D.
      J. Clin. Invest. 113:1138-1148(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMK07_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVS8
    Secondary accession number(s): Q3U2N7
    , Q3UG52, Q497T0, Q5NCN6, Q5NCN7, Q5NCN9, Q6QLU8, Q9R1D9, Q9WVF3, Q9WVF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3