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P63085

- MK01_MOUSE

UniProt

P63085 - MK01_MOUSE

Protein

Mitogen-activated protein kinase 1

Gene

Mapk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation By similarity.By similarity
    Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-183 and Tyr-185 in response to external stimuli like insulin or NGF. Both phosphorylations are required for activity. This phosphorylation causes dramatic conformational changes, which enable full activation and interaction of MAPK1/ERK2 with its substrates. Phosphorylation on Ser-27 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521ATPPROSITE-ProRule annotation
    Binding sitei52 – 521InhibitorBy similarity
    Binding sitei106 – 1061Inhibitor; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei112 – 1121InhibitorBy similarity
    Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation
    Binding sitei152 – 1521InhibitorBy similarity
    Binding sitei164 – 1641InhibitorBy similarity
    Binding sitei165 – 1651InhibitorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinase activity Source: MGI
    3. MAP kinase activity Source: MGI
    4. phosphotyrosine binding Source: MGI
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: MGI
    7. protein serine/threonine kinase activity Source: UniProtKB
    8. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. B cell receptor signaling pathway Source: MGI
    3. caveolin-mediated endocytosis Source: UniProtKB
    4. cell cycle Source: UniProtKB-KW
    5. cellular response to DNA damage stimulus Source: MGI
    6. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: MGI
    7. cytosine metabolic process Source: MGI
    8. ERBB signaling pathway Source: Ensembl
    9. ERK1 and ERK2 cascade Source: Ensembl
    10. labyrinthine layer blood vessel development Source: MGI
    11. lipopolysaccharide-mediated signaling pathway Source: MGI
    12. mammary gland epithelial cell proliferation Source: MGI
    13. MAPK cascade Source: MGI
    14. MAPK import into nucleus Source: Ensembl
    15. negative regulation of cell differentiation Source: MGI
    16. organ morphogenesis Source: MGI
    17. peptidyl-serine phosphorylation Source: UniProtKB
    18. peptidyl-threonine phosphorylation Source: UniProtKB
    19. positive regulation of cell migration Source: Ensembl
    20. positive regulation of cell proliferation Source: Ensembl
    21. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
    22. positive regulation of transcription, DNA-templated Source: Ensembl
    23. positive regulation of translation Source: Ensembl
    24. protein phosphorylation Source: MGI
    25. regulation of cytoskeleton organization Source: UniProtKB
    26. regulation of early endosome to late endosome transport Source: UniProtKB
    27. regulation of Golgi inheritance Source: UniProtKB
    28. regulation of protein stability Source: UniProtKB
    29. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    30. regulation of stress-activated MAPK cascade Source: UniProtKB
    31. response to epidermal growth factor Source: UniProtKB
    32. response to estrogen Source: Ensembl
    33. response to exogenous dsRNA Source: MGI
    34. response to lipopolysaccharide Source: MGI
    35. response to toxic substance Source: Ensembl
    36. sensory perception of pain Source: Ensembl
    37. T cell receptor signaling pathway Source: MGI
    38. transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188530. FCERI mediated MAPK activation.
    REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_188970. Oxidative Stress Induced Senescence.
    REACT_188971. Oncogene Induced Senescence.
    REACT_198245. RSK activation.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_198614. Growth hormone receptor signaling.
    REACT_198647. Advanced glycosylation endproduct receptor signaling.
    REACT_204811. Activation of the AP-1 family of transcription factors.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_210064. ERKs are inactivated.
    REACT_215063. ERK/MAPK targets.
    REACT_215461. Signal transduction by L1.
    REACT_217633. phospho-PLA2 pathway.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_222185. Regulation of HSF1-mediated heat shock response.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 1 (EC:2.7.11.24)
    Short name:
    MAP kinase 1
    Short name:
    MAPK 1
    Alternative name(s):
    ERT1
    Extracellular signal-regulated kinase 2
    Short name:
    ERK-2
    MAP kinase isoform p42
    Short name:
    p42-MAPK
    Mitogen-activated protein kinase 2
    Short name:
    MAP kinase 2
    Short name:
    MAPK 2
    Gene namesi
    Name:Mapk1
    Synonyms:Erk2, Mapk, Prkm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1346858. Mapk1.

    Subcellular locationi

    Cytoplasmcytoskeletonspindle By similarity. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasm
    Note: Associated with the spindle during prometaphase and metaphase By similarity. PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention. Phosphorylation at Ser-244 and Ser-246 as well as autophosphorylation at Thr-188 promote nuclear localization By similarity.By similarity

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. cytoplasm Source: MGI
    3. cytoskeleton Source: UniProtKB
    4. cytosol Source: UniProtKB
    5. dendrite cytoplasm Source: Ensembl
    6. early endosome Source: UniProtKB
    7. focal adhesion Source: UniProtKB
    8. Golgi apparatus Source: UniProtKB
    9. late endosome Source: UniProtKB
    10. microtubule organizing center Source: UniProtKB-SubCell
    11. mitochondrion Source: UniProtKB
    12. mitotic spindle Source: UniProtKB
    13. nucleoplasm Source: Reactome
    14. nucleus Source: UniProtKB
    15. perikaryon Source: Ensembl
    16. protein complex Source: Ensembl
    17. pseudopodium Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 358357Mitogen-activated protein kinase 1PRO_0000186248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei27 – 271Phosphoserine; by SGK1By similarity
    Modified residuei183 – 1831Phosphothreonine; by MAP2K1 and MAP2K25 Publications
    Modified residuei185 – 1851Phosphotyrosine; by MAP2K1 and MAP2K25 Publications
    Modified residuei188 – 1881Phosphothreonine; by autocatalysisBy similarity
    Modified residuei244 – 2441PhosphoserineBy similarity
    Modified residuei246 – 2461PhosphoserineBy similarity
    Modified residuei282 – 2821PhosphoserineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme. Ligand-activated ALK induces tyrosine phosphorylation By similarity. Dephosphorylated by PTPRJ at Tyr-185 By similarity. Phosphorylated upon FLT3 and KIT signaling By similarity.By similarity
    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP63085.
    PaxDbiP63085.
    PRIDEiP63085.

    PTM databases

    PhosphoSiteiP63085.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiP63085.
    BgeeiP63085.
    CleanExiMM_MAPK1.
    GenevestigatoriP63085.

    Interactioni

    Subunit structurei

    Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (via phosphorylated form) with TPR (via C-terminal region and phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases following EGF stimulation By similarity. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation By similarity. Interacts with DCC By similarity. Interacts with MORG1, PEA15 and MKNK2. MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation. The phosphorylated form interacts with PML By similarity. Interacts with STYX By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dlg4Q621083EBI-397697,EBI-300895
    Dusp6Q9DBB12EBI-397697,EBI-7812384
    GSK3BP498412EBI-397697,EBI-373586From a different organism.
    Hivep1Q031724EBI-397697,EBI-646850
    Mknk2Q8CDB023EBI-397697,EBI-646209
    Nupl1Q8R332-13EBI-397697,EBI-646962
    PtprrQ621325EBI-397697,EBI-6954051
    Rps6ka4Q9Z2B93EBI-397697,EBI-412887

    Protein-protein interaction databases

    BioGridi204966. 33 interactions.
    DIPiDIP-661N.
    IntActiP63085. 21 interactions.
    MINTiMINT-125264.

    Structurei

    3D structure databases

    ProteinModelPortaliP63085.
    SMRiP63085. Positions 10-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 311289Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni103 – 1064Inhibitor-bindingBy similarity
    Regioni151 – 1522Inhibitor-bindingBy similarity

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 76Poly-Ala

    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.
    GeneTreeiENSGT00550000074298.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiP63085.
    KOiK04371.
    OMAiVCSAYDR.
    OrthoDBiEOG7M3J0K.
    PhylomeDBiP63085.
    TreeFamiTF105097.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008349. MAPK_ERK1/2.
    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]
    PRINTSiPR01770. ERK1ERK2MAPK.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P63085-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA    50
    IKKISPFEHQ TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY 100
    IVQDLMETDL YKLLKTQHLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP 150
    SNLLLNTTCD LKICDFGLAR VADPDHDHTG FLTEYVATRW YRAPEIMLNS 200
    KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG ILGSPSQEDL 250
    NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI 300
    EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA 350
    RFQPGYRS 358
    Length:358
    Mass (Da):41,276
    Last modified:January 23, 2007 - v3
    Checksum:i3BBCF22471EDBA0B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58712 mRNA. Translation: CAA41548.1.
    AK035386 mRNA. Translation: BAC29053.1.
    AK048127 mRNA. Translation: BAC33251.1.
    AK087925 mRNA. Translation: BAC40044.1.
    AK132241 mRNA. Translation: BAE21053.1.
    BC058258 mRNA. Translation: AAH58258.1.
    D10939 mRNA. Translation: BAA01733.1.
    CCDSiCCDS27992.1.
    PIRiS16444.
    RefSeqiNP_001033752.1. NM_001038663.1.
    NP_036079.1. NM_011949.3.
    XP_006522210.1. XM_006522147.1.
    UniGeneiMm.196581.

    Genome annotation databases

    EnsembliENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358.
    ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358.
    ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
    GeneIDi26413.
    KEGGimmu:26413.
    UCSCiuc007yjq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58712 mRNA. Translation: CAA41548.1 .
    AK035386 mRNA. Translation: BAC29053.1 .
    AK048127 mRNA. Translation: BAC33251.1 .
    AK087925 mRNA. Translation: BAC40044.1 .
    AK132241 mRNA. Translation: BAE21053.1 .
    BC058258 mRNA. Translation: AAH58258.1 .
    D10939 mRNA. Translation: BAA01733.1 .
    CCDSi CCDS27992.1.
    PIRi S16444.
    RefSeqi NP_001033752.1. NM_001038663.1.
    NP_036079.1. NM_011949.3.
    XP_006522210.1. XM_006522147.1.
    UniGenei Mm.196581.

    3D structure databases

    ProteinModelPortali P63085.
    SMRi P63085. Positions 10-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204966. 33 interactions.
    DIPi DIP-661N.
    IntActi P63085. 21 interactions.
    MINTi MINT-125264.

    Chemistry

    BindingDBi P63085.
    ChEMBLi CHEMBL2111454.

    PTM databases

    PhosphoSitei P63085.

    Proteomic databases

    MaxQBi P63085.
    PaxDbi P63085.
    PRIDEi P63085.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023462 ; ENSMUSP00000023462 ; ENSMUSG00000063358 .
    ENSMUST00000069107 ; ENSMUSP00000065983 ; ENSMUSG00000063358 .
    ENSMUST00000115731 ; ENSMUSP00000111396 ; ENSMUSG00000063358 .
    GeneIDi 26413.
    KEGGi mmu:26413.
    UCSCi uc007yjq.1. mouse.

    Organism-specific databases

    CTDi 5594.
    MGIi MGI:1346858. Mapk1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074298.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi P63085.
    KOi K04371.
    OMAi VCSAYDR.
    OrthoDBi EOG7M3J0K.
    PhylomeDBi P63085.
    TreeFami TF105097.

    Enzyme and pathway databases

    Reactomei REACT_188530. FCERI mediated MAPK activation.
    REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_188970. Oxidative Stress Induced Senescence.
    REACT_188971. Oncogene Induced Senescence.
    REACT_198245. RSK activation.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_198614. Growth hormone receptor signaling.
    REACT_198647. Advanced glycosylation endproduct receptor signaling.
    REACT_204811. Activation of the AP-1 family of transcription factors.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_210064. ERKs are inactivated.
    REACT_215063. ERK/MAPK targets.
    REACT_215461. Signal transduction by L1.
    REACT_217633. phospho-PLA2 pathway.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_222185. Regulation of HSF1-mediated heat shock response.

    Miscellaneous databases

    ChiTaRSi MAPK1. mouse.
    NextBioi 304409.
    PROi P63085.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63085.
    Bgeei P63085.
    CleanExi MM_MAPK1.
    Genevestigatori P63085.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008349. MAPK_ERK1/2.
    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 ]
    PRINTSi PR01770. ERK1ERK2MAPK.
    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. "Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation."
      Her J.-H., Wu J.-S., Rall T.B., Sturgill T.W., Weber M.J.
      Nucleic Acids Res. 19:3743-3743(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss.
      Tissue: Fibroblast.
    2. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Brain, Head, Thymus and Urinary bladder.
    3. "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: Eye.
    4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 54-65; 76-89; 137-162; 171-189; 193-201 AND 260-268, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "Novel CDC2-related protein kinases produced in murine hematopoietic stem cells."
      Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.
      Gene 124:305-306(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-190.
      Strain: CBA.
      Tissue: Bone marrow.
    6. "Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase)."
      Payne D.M., Rossomando A.J., Martino P., Erickson A.K., Her J.-H., Shabanowitz J., Hunt D.F., Weber M.J., Sturgill T.W.
      EMBO J. 10:885-892(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-183 AND TYR-185, PARTIAL PROTEIN SEQUENCE.
    7. "Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells."
      Zhang S., Mantel C., Broxmeyer H.E.
      J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
    8. "Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways."
      Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C., Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J., Kanakura Y., Berdel W.E., Serve H.
      Blood 96:3907-3914(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
    9. "Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells."
      Ku H., Meier K.E.
      J. Biol. Chem. 275:11333-11340(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PXN.
    10. Cited for: INTERACTION WITH PEA15, SUBCELLULAR LOCATION, FUNCTION OF THE MAPK ERK CASCADE.
    11. "Molecular interpretation of ERK signal duration by immediate early gene products."
      Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.
      Nat. Cell Biol. 4:556-564(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FOS, SUBCELLULAR LOCATION.
    12. "Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists."
      Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E., Bissonette E.A., Weber M.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MORG1.
    13. "bHLH-zip transcription factor Spz1 mediates mitogen-activated protein kinase cell proliferation, transformation, and tumorigenesis."
      Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H.
      Cancer Res. 65:4041-4050(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION OF SPZ1.
    14. "Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties."
      Parra J.L., Buxade M., Proud C.G.
      J. Biol. Chem. 280:37623-37633(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MKNK2.
    15. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    18. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    19. Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
    20. "The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions."
      Yoon S., Seger R.
      Growth Factors 24:21-44(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    21. "The ERK signaling cascade--views from different subcellular compartments."
      Yao Z., Seger R.
      BioFactors 35:407-416(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, REVIEW ON SUBCELLULAR LOCATION.
    22. "The ERK cascade: distinct functions within various subcellular organelles."
      Wortzel I., Seger R.
      Genes Cancer 2:195-209(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
    23. Cited for: ISGYLATION.

    Entry informationi

    Entry nameiMK01_MOUSE
    AccessioniPrimary (citable) accession number: P63085
    Secondary accession number(s): P27703, Q3V1U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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