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Q13164

- MK07_HUMAN

UniProt

Q13164 - MK07_HUMAN

Protein

Mitogen-activated protein kinase 7

Gene

MAPK7

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 (02 Sep 2008)
      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. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation By similarity. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF).By similarity2 Publications

    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: ProtInc
    3. mitogen-activated protein kinase binding Source: BHF-UCL
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cAMP-mediated signaling Source: BHF-UCL
    2. cell cycle Source: UniProtKB-KW
    3. cell differentiation Source: UniProtKB-KW
    4. cellular response to growth factor stimulus Source: BHF-UCL
    5. cellular response to hydrogen peroxide Source: BHF-UCL
    6. cellular response to laminar fluid shear stress Source: BHF-UCL
    7. cellular response to transforming growth factor beta stimulus Source: UniProtKB
    8. innate immune response Source: Reactome
    9. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    11. negative regulation of cAMP catabolic process Source: BHF-UCL
    12. negative regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
    13. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
    14. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    15. negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
    16. negative regulation of inflammatory response Source: BHF-UCL
    17. negative regulation of NFAT protein import into nucleus Source: Ensembl
    18. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
    19. negative regulation of response to cytokine stimulus Source: BHF-UCL
    20. neurotrophin TRK receptor signaling pathway Source: Reactome
    21. peptidyl-serine phosphorylation Source: Ensembl
    22. positive regulation of protein metabolic process Source: BHF-UCL
    23. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    24. positive regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL
    25. regulation of angiogenesis Source: Ensembl
    26. signal transduction Source: ProtInc
    27. stress-activated MAPK cascade Source: Reactome
    28. toll-like receptor 10 signaling pathway Source: Reactome
    29. toll-like receptor 2 signaling pathway Source: Reactome
    30. toll-like receptor 3 signaling pathway Source: Reactome
    31. toll-like receptor 4 signaling pathway Source: Reactome
    32. toll-like receptor 5 signaling pathway Source: Reactome
    33. toll-like receptor 9 signaling pathway Source: Reactome
    34. toll-like receptor signaling pathway Source: Reactome
    35. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    36. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    37. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    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

    BRENDAi2.7.11.24. 2681.
    ReactomeiREACT_12020. Signalling to ERK5.
    REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    SignaLinkiQ13164.

    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, PRKM7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6880. MAPK7.

    Subcellular locationi

    Cytoplasm. Nucleus. NucleusPML body
    Note: Translocates to the nucleus upon activation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: BHF-UCL
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi219 – 2213TEY → AEF: Loss activation by MAP2K5. 1 Publication

    Organism-specific databases

    PharmGKBiPA30625.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 816815Mitogen-activated protein kinase 7PRO_0000186260Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei720 – 7201Phosphoserine2 Publications
    Modified residuei733 – 7331Phosphothreonine2 Publications

    Post-translational modificationi

    Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme By similarity. Autophosphorylated in vitro on threonine and tyrosine residues when the C-terminal part of the kinase, which could have a regulatory role, is absent.By similarity2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13164.
    PaxDbiQ13164.
    PRIDEiQ13164.

    PTM databases

    PhosphoSiteiQ13164.

    Expressioni

    Tissue specificityi

    Expressed in many adult tissues. Abundant in heart, placenta, lung, kidney and skeletal muscle. Not detectable in liver.1 Publication

    Gene expression databases

    ArrayExpressiQ13164.
    BgeeiQ13164.
    CleanExiHS_MAPK7.
    GenevestigatoriQ13164.

    Organism-specific databases

    HPAiCAB018561.
    HPA031031.

    Interactioni

    Subunit structurei

    Interacts with MAP2K5. Forms oligomers By similarity. 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. Preferentially interacts with PML isoform PML-4 but shows interaction also with its other isoforms: isoform PML-1, isoform PML-2, isoform PML-3 and isoform PML-6.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAP2K5Q131632EBI-1213983,EBI-307294
    PMLP295906EBI-1213983,EBI-295890

    Protein-protein interaction databases

    BioGridi111584. 55 interactions.
    IntActiQ13164. 28 interactions.
    STRINGi9606.ENSP00000311005.

    Structurei

    Secondary structure

    1
    816
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni45 – 484
    Turni52 – 543
    Beta strandi55 – 584
    Beta strandi68 – 747
    Turni75 – 773
    Beta strandi80 – 867
    Turni87 – 904
    Helixi93 – 10816
    Beta strandi117 – 1204
    Turni127 – 1293
    Beta strandi133 – 1386
    Beta strandi141 – 1433
    Helixi144 – 1485
    Beta strandi149 – 1524
    Helixi156 – 17520
    Helixi185 – 1873
    Beta strandi188 – 1903
    Beta strandi196 – 1983
    Helixi216 – 2183
    Beta strandi226 – 2283
    Helixi230 – 2345
    Helixi242 – 25716
    Helixi267 – 27812
    Helixi283 – 2864
    Beta strandi288 – 2903
    Turni292 – 2943
    Helixi295 – 2984
    Beta strandi299 – 3013
    Helixi309 – 3124
    Beta strandi314 – 3163
    Helixi318 – 32710
    Helixi332 – 3343
    Helixi338 – 3414
    Helixi345 – 3473
    Turni348 – 3503
    Helixi353 – 3553
    Helixi366 – 3694
    Beta strandi370 – 3723
    Helixi374 – 38310
    Helixi386 – 3905
    Beta strandi396 – 3983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q8YX-ray2.00B215-223[»]
    4B99X-ray2.80A1-397[»]
    4IC7X-ray2.60A/D1-431[»]
    4IC8X-ray2.80A/B1-431[»]
    ProteinModelPortaliQ13164.
    SMRiQ13164. Positions 46-400.
    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 targetingBy similarityAdd
    BLAST
    Regioni78 – 13962Required for binding to MAP2K5By similarityAdd
    BLAST
    Regioni140 – 406267Necessary for oligomerizationBy similarityAdd
    BLAST
    Regioni407 – 806400May not be required for kinase activity; required to stimulate MEF2C activityBy similarityAdd
    BLAST
    Regioni505 – 53935Nuclear localization signalBy similarityAdd
    BLAST

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi338 – 3414Poly-Ala
    Compositional biasi403 – 694292Pro-richAdd
    BLAST
    Compositional biasi513 – 54331Arg-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.
    HOVERGENiHBG108137.
    InParanoidiQ13164.
    KOiK04464.
    OMAiIIETIGT.
    OrthoDBiEOG70PBX2.
    PhylomeDBiQ13164.
    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 (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: Q13164-1) [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

    MAEPLKEEDG EDGSAEPPGP VKAEPAHTAA SVAAKNLALL KARSFDVTFD    50
    VGDEYEIIET IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL 100
    RELKILKHFK HDNIIAIKDI LRPTVPYGEF KSVYVVLDLM 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 EPGCPDVEMP SPWAPSGDCA MESPPPAPPP CPGPAPDTID 450
    LTLQPPPPVS EPAPPKKDGA ISDNTKAALK AALLKSLRSR LRDGPSAPLE 500
    APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER KERGAGASGG 550
    PSTDPLAGLV LSDNDRSLLE RWTRMARPAA PALTSVPAPA PAPTPTPTPV 600
    QPTSPPPGPV AQPTGPQPQS AGSTSGPVPQ PACPPPGPAP HPTGPPGPIP 650
    VPAPPQIATS TSLLAAQSLV PPPGLPGSST PGVLPYFPPG LPPPDAGGAP 700
    QSSMSESPDV NLVTQQLSKS QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF 750
    LNQSFDMGVA DGPQDGQADS ASLSASLLAD WLEGHGMNPA DIESLQREIQ 800
    MDSPMLLADL PDLQDP 816
    Length:816
    Mass (Da):88,386
    Last modified:September 2, 2008 - v2
    Checksum:i27729FE31658CE3B
    GO
    Isoform 2 (identifier: Q13164-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-139: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:677
    Mass (Da):73,218
    Checksum:iEC01D3784EB8AAB0
    GO
    Isoform 3 (identifier: Q13164-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS

    Show »
    Length:533
    Mass (Da):59,328
    Checksum:i6E654D7CA1287E32
    GO
    Isoform 4 (identifier: Q13164-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: MAEPLKEEDG...TVPYGEFKSV → MLFFHTMPSA...HASLLPSPSS
         493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS

    Note: No experimental confirmation available.

    Show »
    Length:451
    Mass (Da):50,152
    Checksum:iE0FAC412C3DE60F9
    GO

    Sequence cautioni

    The sequence AAA81381.1 differs from that shown. Reason: Frameshift at positions 19 and 32.
    The sequence BAD92848.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti610 – 6101V → L in AAA81381. (PubMed:7646528)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti535 – 5351R → H.1 Publication
    VAR_046225
    Natural varianti550 – 5501G → A.1 Publication
    Corresponds to variant rs56388327 [ dbSNP | Ensembl ].
    VAR_042257

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 139139Missing in isoform 2. 1 PublicationVSP_035198Add
    BLAST
    Alternative sequencei1 – 133133MAEPL…EFKSV → MLFFHTMPSAPMGSQGKAVT CLESEGCGEDGACPWSVIRP THASLLPSPSS in isoform 4. 1 PublicationVSP_035199Add
    BLAST
    Alternative sequencei493 – 816324DGPSA…DLQDP → GALWAGRVGRGETWTWTRLQ AFTFSPAQLPRKWPQRTPGG S in isoform 3 and isoform 4. 2 PublicationsVSP_035200Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29725 mRNA. Translation: AAA82931.1.
    U29726 mRNA. Translation: AAA82932.1.
    U29727 Genomic DNA. Translation: AAA82933.1.
    U25278 mRNA. Translation: AAA81381.1. Frameshift.
    AY534741 mRNA. Translation: AAS38577.1.
    AB209611 mRNA. Translation: BAD92848.1. Different initiation.
    CH471212 Genomic DNA. Translation: EAW50883.1.
    CH471212 Genomic DNA. Translation: EAW50886.1.
    BC007404 mRNA. Translation: AAH07404.1.
    BC007992 mRNA. Translation: AAH07992.1.
    BC009963 mRNA. Translation: AAH09963.1.
    BC030134 mRNA. Translation: AAH30134.1.
    CCDSiCCDS11206.1. [Q13164-1]
    CCDS11207.1. [Q13164-2]
    PIRiB56708.
    RefSeqiNP_002740.2. NM_002749.3. [Q13164-1]
    NP_620601.1. NM_139032.2. [Q13164-2]
    NP_620602.2. NM_139033.2. [Q13164-1]
    NP_620603.2. NM_139034.2. [Q13164-1]
    XP_005256776.1. XM_005256719.1. [Q13164-2]
    XP_006721623.1. XM_006721560.1. [Q13164-1]
    UniGeneiHs.150136.

    Genome annotation databases

    EnsembliENST00000299612; ENSP00000299612; ENSG00000166484. [Q13164-2]
    ENST00000308406; ENSP00000311005; ENSG00000166484. [Q13164-1]
    ENST00000395602; ENSP00000378966; ENSG00000166484. [Q13164-1]
    ENST00000395604; ENSP00000378968; ENSG00000166484. [Q13164-1]
    GeneIDi5598.
    KEGGihsa:5598.
    UCSCiuc002gvn.3. human. [Q13164-1]

    Polymorphism databases

    DMDMi205371766.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29725 mRNA. Translation: AAA82931.1 .
    U29726 mRNA. Translation: AAA82932.1 .
    U29727 Genomic DNA. Translation: AAA82933.1 .
    U25278 mRNA. Translation: AAA81381.1 . Frameshift.
    AY534741 mRNA. Translation: AAS38577.1 .
    AB209611 mRNA. Translation: BAD92848.1 . Different initiation.
    CH471212 Genomic DNA. Translation: EAW50883.1 .
    CH471212 Genomic DNA. Translation: EAW50886.1 .
    BC007404 mRNA. Translation: AAH07404.1 .
    BC007992 mRNA. Translation: AAH07992.1 .
    BC009963 mRNA. Translation: AAH09963.1 .
    BC030134 mRNA. Translation: AAH30134.1 .
    CCDSi CCDS11206.1. [Q13164-1 ]
    CCDS11207.1. [Q13164-2 ]
    PIRi B56708.
    RefSeqi NP_002740.2. NM_002749.3. [Q13164-1 ]
    NP_620601.1. NM_139032.2. [Q13164-2 ]
    NP_620602.2. NM_139033.2. [Q13164-1 ]
    NP_620603.2. NM_139034.2. [Q13164-1 ]
    XP_005256776.1. XM_005256719.1. [Q13164-2 ]
    XP_006721623.1. XM_006721560.1. [Q13164-1 ]
    UniGenei Hs.150136.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q8Y X-ray 2.00 B 215-223 [» ]
    4B99 X-ray 2.80 A 1-397 [» ]
    4IC7 X-ray 2.60 A/D 1-431 [» ]
    4IC8 X-ray 2.80 A/B 1-431 [» ]
    ProteinModelPortali Q13164.
    SMRi Q13164. Positions 46-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111584. 55 interactions.
    IntActi Q13164. 28 interactions.
    STRINGi 9606.ENSP00000311005.

    Chemistry

    BindingDBi Q13164.
    ChEMBLi CHEMBL5332.
    GuidetoPHARMACOLOGYi 2093.

    PTM databases

    PhosphoSitei Q13164.

    Polymorphism databases

    DMDMi 205371766.

    Proteomic databases

    MaxQBi Q13164.
    PaxDbi Q13164.
    PRIDEi Q13164.

    Protocols and materials databases

    DNASUi 5598.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299612 ; ENSP00000299612 ; ENSG00000166484 . [Q13164-2 ]
    ENST00000308406 ; ENSP00000311005 ; ENSG00000166484 . [Q13164-1 ]
    ENST00000395602 ; ENSP00000378966 ; ENSG00000166484 . [Q13164-1 ]
    ENST00000395604 ; ENSP00000378968 ; ENSG00000166484 . [Q13164-1 ]
    GeneIDi 5598.
    KEGGi hsa:5598.
    UCSCi uc002gvn.3. human. [Q13164-1 ]

    Organism-specific databases

    CTDi 5598.
    GeneCardsi GC17P019281.
    HGNCi HGNC:6880. MAPK7.
    HPAi CAB018561.
    HPA031031.
    MIMi 602521. gene.
    neXtProti NX_Q13164.
    PharmGKBi PA30625.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108137.
    InParanoidi Q13164.
    KOi K04464.
    OMAi IIETIGT.
    OrthoDBi EOG70PBX2.
    PhylomeDBi Q13164.
    TreeFami TF105099.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    Reactomei REACT_12020. Signalling to ERK5.
    REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    SignaLinki Q13164.

    Miscellaneous databases

    GeneWikii MAPK7.
    GenomeRNAii 5598.
    NextBioi 21728.
    PROi Q13164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13164.
    Bgeei Q13164.
    CleanExi HS_MAPK7.
    Genevestigatori Q13164.

    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. "Primary structure of BMK1: a new mammalian map kinase."
      Lee J.-D., Ulevitch R.J., Han J.
      Biochem. Biophys. Res. Commun. 213:715-724(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Placenta.
    2. "Components of a new human protein kinase signal transduction pathway."
      Zhou G., Bao Z.Q., Dixon J.E.
      J. Biol. Chem. 270:12665-12669(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAP2K5, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    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 3).
      Tissue: Placenta.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Spleen.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Muscle and Pancreas.
    7. Bienvenut W.V., Fleming J., Leug H.Y.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-35; 75-98; 119-131; 198-205; 296-343; 377-392; 468-485; 489-505; 544-571; 720-735 AND 798-816, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    8. "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C."
      Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D.
      EMBO J. 16:7054-7066(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 219-THR--TYR-221.
    9. "Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor."
      Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J., Lee J.-D.
      Nature 395:713-716(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    10. "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase."
      Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y., Lee J.D.
      J. Biol. Chem. 276:8631-8634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SGK1.
    11. "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.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction."
      Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III, Lee J.D.
      Oncogene 32:3156-3164(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PML.
    15. "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] HIS-535 AND ALA-550.

    Entry informationi

    Entry nameiMK07_HUMAN
    AccessioniPrimary (citable) accession number: Q13164
    Secondary accession number(s): Q16634
    , Q59F50, Q6QLU7, Q7L4P4, Q969G1, Q96G51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 2, 2008
    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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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