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Q63932

- MP2K2_MOUSE

UniProt

Q63932 - MP2K2_MOUSE

Protein

Dual specificity mitogen-activated protein kinase kinase 2

Gene

Map2k2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Inhibited by serine/threonine phosphatase 2A.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei10 – 112Cleavage; by anthrax lethal factorBy similarity
    Binding sitei101 – 1011ATP
    Active sitei194 – 1941Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi78 – 869ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase activity Source: Ensembl
    3. protein binding Source: IntAct
    4. protein complex scaffold Source: BHF-UCL
    5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
    6. protein serine/threonine kinase activator activity Source: Ensembl
    7. protein serine/threonine kinase activity Source: UniProtKB-KW
    8. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of MAPK activity Source: UniProtKB
    2. peptidyl-serine autophosphorylation Source: Ensembl
    3. positive regulation of cell motility Source: BHF-UCL
    4. regulation of early endosome to late endosome transport Source: UniProtKB
    5. regulation of Golgi inheritance Source: UniProtKB
    6. regulation of stress-activated MAPK cascade Source: UniProtKB

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.12.2. 3474.
    ReactomeiREACT_215461. Signal transduction by L1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity mitogen-activated protein kinase kinase 2 (EC:2.7.12.2)
    Short name:
    MAP kinase kinase 2
    Short name:
    MAPKK 2
    Alternative name(s):
    ERK activator kinase 2
    MAPK/ERK kinase 2
    Short name:
    MEK 2
    Gene namesi
    Name:Map2k2
    Synonyms:Mek2, Mkk2, Prkmk2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1346867. Map2k2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. cell cortex Source: Ensembl
    3. cytoplasm Source: MGI
    4. cytoplasmic side of plasma membrane Source: Ensembl
    5. cytosol Source: UniProtKB
    6. early endosome Source: UniProtKB
    7. endoplasmic reticulum Source: Ensembl
    8. focal adhesion Source: UniProtKB
    9. Golgi apparatus Source: UniProtKB
    10. late endosome Source: UniProtKB
    11. microtubule Source: Ensembl
    12. mitochondrion Source: UniProtKB
    13. nucleus Source: UniProtKB
    14. perinuclear region of cytoplasm Source: Ensembl
    15. peroxisomal membrane Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011K → M: Inactivation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Dual specificity mitogen-activated protein kinase kinase 2PRO_0000086373Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei222 – 2221Phosphoserine; by RAFBy similarity
    Modified residuei226 – 2261Phosphoserine; by RAFBy similarity
    Modified residuei293 – 2931PhosphoserineBy similarity
    Modified residuei295 – 2951PhosphoserineBy similarity
    Modified residuei395 – 3951PhosphothreonineBy similarity
    Modified residuei397 – 3971PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF or MEKK1) regulates positively the kinase activity. Phosphorylated by MAP2K1/MEK1. Low levels of autophosphorylation have been observed.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ63932.
    PaxDbiQ63932.
    PRIDEiQ63932.

    PTM databases

    PhosphoSiteiQ63932.

    Expressioni

    Tissue specificityi

    Expressed in adult intestine, kidney, liver, lung, pancreas, spleen, thymus, and at high levels in the neonatal brain. Lower expression is found in adult brain and heart.

    Gene expression databases

    ArrayExpressiQ63932.
    BgeeiQ63932.
    CleanExiMM_MAP2K2.
    GenevestigatoriQ63932.

    Interactioni

    Subunit structurei

    Interacts with MORG1. Interacts with SGK1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rgs12Q8CGE93EBI-397724,EBI-7340552

    Protein-protein interaction databases

    BioGridi204950. 5 interactions.
    DIPiDIP-454N.
    IntActiQ63932. 7 interactions.
    MINTiMINT-1518275.
    STRINGi10090.ENSMUSP00000121111.

    Structurei

    3D structure databases

    ProteinModelPortaliQ63932.
    SMRiQ63932. Positions 60-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 370299Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi266 – 31651Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00690000101918.
    HOGENOMiHOG000234206.
    HOVERGENiHBG108518.
    InParanoidiQ9D7B0.
    KOiK04369.
    OMAiRLKQPST.
    OrthoDBiEOG7HF1KZ.
    TreeFamiTF105137.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    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.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q63932-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELDLDEQQ    50
    RKRLEAFLTQ KAKVGELKDD DFERISELGA GNGGVVTKAR HRPSGLIMAR 100
    KLIHLEIKPA VRNQIIRELQ VLHECNSPYI VGFYGAFYSD GEISICMEHM 150
    DGGSLDQVLK EAKRIPEDIL GKVSIAVLRG LAYLREKHQI MHRDVKPSNI 200
    LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMSPERLQ GTHYSVQSDI 250
    WSMGLSLVEL AIGRYPIPPP DAKELEASFG RPVVDGADGE PHSVSPRPRP 300
    PGRPISVGHG MDSRPAMAIF ELLDYIVNEP PPKLPSGVFS SDFQEFVNKC 350
    LIKNPAERAD LKLLMNHAFI KRSEGEEVDF AGWLCRTLRL KQPSTPTRTA 400
    V 401
    Length:401
    Mass (Da):44,402
    Last modified:July 27, 2011 - v2
    Checksum:iF00CD807E86F5B26
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961L → F in AAC60678. (PubMed:8297798)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68267 mRNA. Translation: AAC60678.1.
    AK009392 mRNA. Translation: BAB26261.1.
    AK080574 mRNA. Translation: BAC37945.1.
    CH466553 Genomic DNA. Translation: EDL31456.1.
    CCDSiCCDS24044.1.
    RefSeqiNP_075627.2. NM_023138.4.
    UniGeneiMm.275436.

    Genome annotation databases

    EnsembliENSMUST00000143517; ENSMUSP00000121111; ENSMUSG00000035027.
    GeneIDi26396.
    KEGGimmu:26396.
    UCSCiuc007gfx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68267 mRNA. Translation: AAC60678.1 .
    AK009392 mRNA. Translation: BAB26261.1 .
    AK080574 mRNA. Translation: BAC37945.1 .
    CH466553 Genomic DNA. Translation: EDL31456.1 .
    CCDSi CCDS24044.1.
    RefSeqi NP_075627.2. NM_023138.4.
    UniGenei Mm.275436.

    3D structure databases

    ProteinModelPortali Q63932.
    SMRi Q63932. Positions 60-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204950. 5 interactions.
    DIPi DIP-454N.
    IntActi Q63932. 7 interactions.
    MINTi MINT-1518275.
    STRINGi 10090.ENSMUSP00000121111.

    PTM databases

    PhosphoSitei Q63932.

    Proteomic databases

    MaxQBi Q63932.
    PaxDbi Q63932.
    PRIDEi Q63932.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000143517 ; ENSMUSP00000121111 ; ENSMUSG00000035027 .
    GeneIDi 26396.
    KEGGi mmu:26396.
    UCSCi uc007gfx.2. mouse.

    Organism-specific databases

    CTDi 5605.
    MGIi MGI:1346867. Map2k2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00690000101918.
    HOGENOMi HOG000234206.
    HOVERGENi HBG108518.
    InParanoidi Q9D7B0.
    KOi K04369.
    OMAi RLKQPST.
    OrthoDBi EOG7HF1KZ.
    TreeFami TF105137.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 3474.
    Reactomei REACT_215461. Signal transduction by L1.

    Miscellaneous databases

    ChiTaRSi MAP2K2. mouse.
    NextBioi 304343.
    PROi Q63932.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q63932.
    Bgeei Q63932.
    CleanExi MM_MAP2K2.
    Genevestigatori Q63932.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    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 PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues."
      Brott B.K., Alessandrini A., Largaespada D.A., Copeland N.G., Jenkins N.A., Crews C.M., Erikson R.L.
      Cell Growth Differ. 4:921-929(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
      Strain: BALB/c.
      Tissue: Neonatal brain.
    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.
      Tissue: Cerebellum and Tongue.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product."
      Crews C.M., Erikson R.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:8205-8209(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 118-140 AND 210-238.
      Tissue: T-cell.
    5. "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.
    6. Cited for: INTERACTION WITH MAP2K1/MEK1, PHOSPHORYLATION BY MAP2K1/MEK1, FUNCTION IN ERK SIGNALING.

    Entry informationi

    Entry nameiMP2K2_MOUSE
    AccessioniPrimary (citable) accession number: Q63932
    Secondary accession number(s): Q9D7B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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