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P36507

- MP2K2_HUMAN

UniProt

P36507 - MP2K2_HUMAN

Protein

Dual specificity mitogen-activated protein kinase kinase 2

Gene

MAP2K2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei10 – 112Cleavage; by anthrax lethal factor
    Binding sitei101 – 1011ATPPROSITE-ProRule annotation
    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: UniProtKB
    3. PDZ domain binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
    6. protein serine/threonine kinase activator activity Source: UniProtKB
    7. protein serine/threonine kinase activity Source: Reactome
    8. protein tyrosine kinase activity Source: UniProtKB-KW
    9. scaffold protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: UniProtKB
    2. activation of MAPKK activity Source: Reactome
    3. axon guidance Source: Reactome
    4. epidermal growth factor receptor signaling pathway Source: Reactome
    5. ERK1 and ERK2 cascade Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. fibroblast growth factor receptor signaling pathway Source: Reactome
    8. innate immune response Source: Reactome
    9. insulin receptor signaling pathway Source: Reactome
    10. MAPK cascade Source: Reactome
    11. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    12. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    13. neurotrophin TRK receptor signaling pathway Source: Reactome
    14. peptidyl-serine autophosphorylation Source: UniProtKB
    15. positive regulation of cell motility Source: Ensembl
    16. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
    17. Ras protein signal transduction Source: Reactome
    18. regulation of early endosome to late endosome transport Source: UniProtKB
    19. regulation of Golgi inheritance Source: UniProtKB
    20. regulation of stress-activated MAPK cascade Source: UniProtKB
    21. small GTPase mediated signal transduction Source: Reactome
    22. stress-activated MAPK cascade Source: Reactome
    23. toll-like receptor 10 signaling pathway Source: Reactome
    24. toll-like receptor 2 signaling pathway Source: Reactome
    25. toll-like receptor 3 signaling pathway Source: Reactome
    26. toll-like receptor 4 signaling pathway Source: Reactome
    27. toll-like receptor 5 signaling pathway Source: Reactome
    28. toll-like receptor 9 signaling pathway Source: Reactome
    29. toll-like receptor signaling pathway Source: Reactome
    30. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    31. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    32. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    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. 2681.
    ReactomeiREACT_1183. ERK2 activation.
    REACT_22272. Signal transduction by L1.
    REACT_614. RAF phosphorylates MEK.
    REACT_9470. Signaling by FGFR.
    REACT_962. MEK activation.
    SignaLinkiP36507.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6842. MAP2K2.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Cardiofaciocutaneous syndrome 4 (CFC4) [MIM:615280]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571F → C in CFC4. 1 Publication
    VAR_035095
    Natural varianti57 – 571F → V in CFC4. 1 Publication
    VAR_069781
    Natural varianti128 – 1281P → Q in CFC4; results in increased kinase activity. 1 Publication
    VAR_069782
    Natural varianti134 – 1341Y → H in CFC4. 1 Publication
    VAR_069783

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation, Ectodermal dysplasia, Mental retardation

    Organism-specific databases

    MIMi615280. phenotype.
    Orphaneti1340. Cardiofaciocutaneous syndrome.
    PharmGKBiPA30587.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 400400Dual specificity mitogen-activated protein kinase kinase 2PRO_0000086372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei222 – 2221O-acetylserine; by Yersinia yopJ; alternate1 Publication
    Modified residuei222 – 2221Phosphoserine; by RAF; alternate1 Publication
    Modified residuei226 – 2261O-acetylserine; by Yersinia yopJ; alternate1 Publication
    Modified residuei226 – 2261Phosphoserine; alternate1 Publication
    Modified residuei293 – 2931Phosphoserine1 Publication
    Modified residuei295 – 2951Phosphoserine2 Publications
    Modified residuei394 – 3941Phosphothreonine4 Publications
    Modified residuei396 – 3961Phosphothreonine2 Publications

    Post-translational modificationi

    MAPKK is itself dependent on Ser/Thr phosphorylation for activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1). Phosphorylated by MAP2K1/MEK1 By similarity.By similarity
    Acetylation of Ser-222 and Ser-226 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP36507.
    PaxDbiP36507.
    PeptideAtlasiP36507.
    PRIDEiP36507.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00003783.

    PTM databases

    PhosphoSiteiP36507.

    Miscellaneous databases

    PMAP-CutDBP36507.

    Expressioni

    Gene expression databases

    ArrayExpressiP36507.
    BgeeiP36507.
    CleanExiHS_MAP2K2.
    GenevestigatoriP36507.

    Organism-specific databases

    HPAiCAB003835.
    HPA051993.

    Interactioni

    Subunit structurei

    Interacts with MORG1 By similarity. Interacts with SGK1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARAFP103984EBI-1056930,EBI-365961
    DLG1Q1295910EBI-1056930,EBI-357481

    Protein-protein interaction databases

    BioGridi111591. 22 interactions.
    DIPiDIP-29119N.
    IntActiP36507. 14 interactions.
    MINTiMINT-99667.
    STRINGi9606.ENSP00000262948.

    Structurei

    Secondary structure

    1
    400
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi69 – 713
    Beta strandi72 – 809
    Beta strandi85 – 917
    Turni92 – 943
    Beta strandi97 – 1037
    Helixi110 – 11910
    Helixi120 – 1223
    Beta strandi133 – 14816
    Helixi155 – 1617
    Beta strandi162 – 1643
    Helixi167 – 18620
    Helixi197 – 1993
    Beta strandi200 – 2023
    Beta strandi208 – 2103
    Helixi217 – 2226
    Helixi236 – 2394
    Helixi246 – 26217
    Helixi272 – 2798
    Helixi318 – 32710
    Turni335 – 3373
    Helixi340 – 34910
    Turni354 – 3563
    Helixi360 – 3645
    Helixi367 – 3748
    Helixi379 – 3868

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S9IX-ray3.20A/B55-400[»]
    4H3QX-ray2.20B4-16[»]
    ProteinModelPortaliP36507.
    SMRiP36507. Positions 60-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36507.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 369298Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi266 – 31550Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234206.
    HOVERGENiHBG108518.
    InParanoidiP36507.
    KOiK04369.
    OMAiLSAITEY.
    OrthoDBiEOG7HF1KZ.
    PhylomeDBiP36507.
    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.

    P36507-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELELDEQQ    50
    KKRLEAFLTQ KAKVGELKDD DFERISELGA GNGGVVTKVQ HRPSGLIMAR 100
    KLIHLEIKPA IRNQIIRELQ VLHECNSPYI VGFYGAFYSD GEISICMEHM 150
    DGGSLDQVLK EAKRIPEEIL GKVSIAVLRG LAYLREKHQI MHRDVKPSNI 200
    LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMAPERLQ GTHYSVQSDI 250
    WSMGLSLVEL AVGRYPIPPP DAKELEAIFG RPVVDGEEGE PHSISPRPRP 300
    PGRPVSGHGM DSRPAMAIFE LLDYIVNEPP PKLPNGVFTP DFQEFVNKCL 350
    IKNPAERADL KMLTNHTFIK RSEVEEVDFA GWLCKTLRLN QPGTPTRTAV 400
    Length:400
    Mass (Da):44,424
    Last modified:June 1, 1994 - v1
    Checksum:i3401D522515C30A5
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571F → C in CFC4. 1 Publication
    VAR_035095
    Natural varianti57 – 571F → V in CFC4. 1 Publication
    VAR_069781
    Natural varianti128 – 1281P → Q in CFC4; results in increased kinase activity. 1 Publication
    VAR_069782
    Natural varianti134 – 1341Y → H in CFC4. 1 Publication
    VAR_069783

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11285 mRNA. No translation available.
    BC000471 mRNA. Translation: AAH00471.1.
    BC018645 mRNA. Translation: AAH18645.1.
    CCDSiCCDS12120.1.
    PIRiA46723.
    RefSeqiNP_109587.1. NM_030662.3.
    UniGeneiHs.465627.

    Genome annotation databases

    EnsembliENST00000262948; ENSP00000262948; ENSG00000126934.
    GeneIDi5605.
    KEGGihsa:5605.
    UCSCiuc002lzj.3. human.

    Polymorphism databases

    DMDMi547915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11285 mRNA. No translation available.
    BC000471 mRNA. Translation: AAH00471.1 .
    BC018645 mRNA. Translation: AAH18645.1 .
    CCDSi CCDS12120.1.
    PIRi A46723.
    RefSeqi NP_109587.1. NM_030662.3.
    UniGenei Hs.465627.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S9I X-ray 3.20 A/B 55-400 [» ]
    4H3Q X-ray 2.20 B 4-16 [» ]
    ProteinModelPortali P36507.
    SMRi P36507. Positions 60-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111591. 22 interactions.
    DIPi DIP-29119N.
    IntActi P36507. 14 interactions.
    MINTi MINT-99667.
    STRINGi 9606.ENSP00000262948.

    Chemistry

    BindingDBi P36507.
    ChEMBLi CHEMBL2964.
    GuidetoPHARMACOLOGYi 2063.

    PTM databases

    PhosphoSitei P36507.

    Polymorphism databases

    DMDMi 547915.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00003783.

    Proteomic databases

    MaxQBi P36507.
    PaxDbi P36507.
    PeptideAtlasi P36507.
    PRIDEi P36507.

    Protocols and materials databases

    DNASUi 5605.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262948 ; ENSP00000262948 ; ENSG00000126934 .
    GeneIDi 5605.
    KEGGi hsa:5605.
    UCSCi uc002lzj.3. human.

    Organism-specific databases

    CTDi 5605.
    GeneCardsi GC19M004090.
    GeneReviewsi MAP2K2.
    H-InvDB HIX0033655.
    HGNCi HGNC:6842. MAP2K2.
    HPAi CAB003835.
    HPA051993.
    MIMi 601263. gene.
    615280. phenotype.
    neXtProti NX_P36507.
    Orphaneti 1340. Cardiofaciocutaneous syndrome.
    PharmGKBi PA30587.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234206.
    HOVERGENi HBG108518.
    InParanoidi P36507.
    KOi K04369.
    OMAi LSAITEY.
    OrthoDBi EOG7HF1KZ.
    PhylomeDBi P36507.
    TreeFami TF105137.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 2681.
    Reactomei REACT_1183. ERK2 activation.
    REACT_22272. Signal transduction by L1.
    REACT_614. RAF phosphorylates MEK.
    REACT_9470. Signaling by FGFR.
    REACT_962. MEK activation.
    SignaLinki P36507.

    Miscellaneous databases

    ChiTaRSi MAP2K2. human.
    EvolutionaryTracei P36507.
    GeneWikii MAP2K2.
    GenomeRNAii 5605.
    NextBioi 21780.
    PMAP-CutDB P36507.
    PROi P36507.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36507.
    Bgeei P36507.
    CleanExi HS_MAP2K2.
    Genevestigatori P36507.

    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. "Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2."
      Zheng C.-F., Guan K.-L.
      J. Biol. Chem. 268:11435-11439(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Muscle and Skin.
    3. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 40-51; 53-61; 64-100; 102-112; 164-172; 194-205; 265-297; 362-371 AND 389-397, PHOSPHORYLATION AT THR-394, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    4. "Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling."
      Mittal R., Peak-Chew S.Y., McMahon H.T.
      Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 210-231, INACTIVATION BY YERSINIA YOPJ, PHOSPHORYLATION AT SER-222 AND SER-226, ACETYLATION AT SER-222 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY.
    5. Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
    6. "Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
      Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
      Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration."
      Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J., Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M., Hur G.M.
      J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGK1.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome."
      Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A., Cruz M.S., McCormick F., Rauen K.A.
      Science 311:1287-1290(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CFC4 CYS-57.
    19. Cited for: VARIANTS CFC4 VAL-57 AND HIS-134.
    20. "Molecular and functional analysis of a novel MEK2 mutation in cardio-facio-cutaneous syndrome: transmission through four generations."
      Rauen K.A., Tidyman W.E., Estep A.L., Sampath S., Peltier H.M., Bale S.J., Lacassie Y.
      Am. J. Med. Genet. A 152:807-814(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CFC4 GLN-128, CHARACTERIZATION OF VARIANT CFC4 GLN-128.

    Entry informationi

    Entry nameiMP2K2_HUMAN
    AccessioniPrimary (citable) accession number: P36507
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 169 of the entry and version 1 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3