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Q16659

- MK06_HUMAN

UniProt

Q16659 - MK06_HUMAN

Protein

Mitogen-activated protein kinase 6

Gene

MAPK6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6. May promote entry in the cell cycle By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by phosphorylation at Ser-189.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491ATPPROSITE-ProRule annotation
    Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: ProtInc

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. protein phosphorylation Source: UniProtKB
    3. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 2681.
    SignaLinkiQ16659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 6 (EC:2.7.11.24)
    Short name:
    MAP kinase 6
    Short name:
    MAPK 6
    Alternative name(s):
    Extracellular signal-regulated kinase 3
    Short name:
    ERK-3
    MAP kinase isoform p97
    Short name:
    p97-MAPK
    Gene namesi
    Name:MAPK6
    Synonyms:ERK3, PRKM6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6879. MAPK6.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Translocates to the cytoplasm following interaction with MAPKAPK5.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30624.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 721721Mitogen-activated protein kinase 6PRO_0000186257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei189 – 1891Phosphoserine; by PAK1, PAK2 and PAK33 Publications

    Post-translational modificationi

    Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in catalytic activation. Phosphorylated by MAPKAPK5 at other sites.3 Publications
    Ubiquitination at Met-1 leads to degradation by the proteasome pathway.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16659.
    PaxDbiQ16659.
    PRIDEiQ16659.

    PTM databases

    PhosphoSiteiQ16659.

    Expressioni

    Tissue specificityi

    Highest expression in the skeletal muscle, followed by the brain. Also found in heart, placenta, lung, liver, pancreas, kidney and skin fibroblasts.

    Gene expression databases

    BgeeiQ16659.
    CleanExiHS_MAPK6.
    GenevestigatoriQ16659.

    Organism-specific databases

    HPAiCAB005184.
    HPA030262.
    HPA047825.

    Interactioni

    Subunit structurei

    Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE motif) MAPKAPK5 By similarity. Interacts with UBE3A; this interaction may be indirect and mediated by HERC2, possibly via HERC2 interaction with NEURL4.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPKAPK5Q8IW413EBI-1384105,EBI-1201460
    vifP125042EBI-1384105,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi111583. 175 interactions.
    IntActiQ16659. 173 interactions.
    MINTiMINT-8247530.
    STRINGi9606.ENSP00000261845.

    Structurei

    Secondary structure

    1
    721
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 163
    Turni17 – 193
    Beta strandi20 – 256
    Beta strandi34 – 396
    Turni40 – 423
    Beta strandi45 – 528
    Helixi56 – 7015
    Beta strandi80 – 845
    Beta strandi102 – 1098
    Beta strandi112 – 1143
    Helixi115 – 1195
    Helixi126 – 14520
    Helixi155 – 1573
    Beta strandi158 – 1614
    Turni162 – 1654
    Beta strandi166 – 1694
    Helixi190 – 1923
    Helixi200 – 2045
    Helixi211 – 22717
    Helixi237 – 24711
    Helixi253 – 2608
    Helixi265 – 2706
    Helixi278 – 2814
    Helixi287 – 2948
    Helixi301 – 3033
    Helixi307 – 3115
    Helixi314 – 3174

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I6LX-ray2.25A/B9-327[»]
    ProteinModelPortaliQ16659.
    SMRiQ16659. Positions 13-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16659.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 316297Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi189 – 1913SEG motif
    Motifi332 – 3376FRIEDE motif

    Domaini

    In contrast to classical MAPKs, the TXY motif within the activation loop is replaced by the SEG motif, whose phosphorylation activates the MAP kinases.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233020.
    HOVERGENiHBG104376.
    InParanoidiQ16659.
    KOiK06855.
    OMAiEHDWPIH.
    OrthoDBiEOG780RKS.
    PhylomeDBiQ16659.
    TreeFamiTF105098.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR008350. MAPK_ERK3/4.
    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]
    PRINTSiPR01771. ERK3ERK4MAPK.
    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.

    Q16659-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK    50
    IVLTDPQSVK HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE 100
    LNSVYIVQEY METDLANVLE QGPLLEEHAR LFMYQLLRGL KYIHSANVLH 150
    RDLKPANLFI NTEDLVLKIG DFGLARIMDP HYSHKGHLSE GLVTKWYRSP 200
    RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ MQLILESIPV 250
    VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS 300
    PMDRLTAEEA LSHPYMSIYS FPMDEPISSH PFHIEDEVDD ILLMDETHSH 350
    IYNWERYHDC QFSEHDWPVH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK 400
    YLDGDREKYL EDPAFDTNYS TEPCWQYSDH HENKYCDLEC SHTCNYKTRS 450
    SSYLDNLVWR ESEVNHYYEP KLIIDLSNWK EQSKEKSDKK GKSKCERNGL 500
    VKAQIALEEA SQQLAGKERE KNQGFDFDSF IAGTIQLSSQ HEPTDVVDKL 550
    NDLNSSVSQL ELKSLISKSV SQEKQEKGMA NLAQLEALYQ SSWDSQFVSG 600
    GEDCFFINQF CEVRKDEQVE KENTYTSYLD KFFSRKEDTE MLETEPVEDG 650
    KLGERGHEEG FLNNSGEFLF NKQLESIGIP QFHSPVGSPL KSIQATLTPS 700
    AMKSSPQIPH QTYSSILKHL N 721
    Length:721
    Mass (Da):82,681
    Last modified:November 1, 1996 - v1
    Checksum:iDAA3AAA9B98BB31F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291K → R in BAG36392. (PubMed:14702039)Curated
    Sequence conflicti527 – 5271F → L in BAG70115. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti290 – 2901L → V.2 Publications
    Corresponds to variant rs35697691 [ dbSNP | Ensembl ].
    VAR_042256

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80692 mRNA. Translation: CAA56709.1.
    L77964 mRNA. Translation: AAA98769.1.
    AF420474 mRNA. Translation: AAL17605.1.
    AK313633 mRNA. Translation: BAG36392.1.
    CR749401 mRNA. Translation: CAH18246.1.
    AB451301 mRNA. Translation: BAG70115.1.
    BC035492 mRNA. Translation: AAH35492.1.
    CCDSiCCDS10147.1.
    PIRiA56352.
    RefSeqiNP_002739.1. NM_002748.3.
    XP_005254593.1. XM_005254536.2.
    XP_005254594.1. XM_005254537.1.
    XP_005254595.1. XM_005254538.1.
    XP_005254596.1. XM_005254539.2.
    UniGeneiHs.411847.

    Genome annotation databases

    EnsembliENST00000261845; ENSP00000261845; ENSG00000069956.
    GeneIDi5597.
    KEGGihsa:5597.
    UCSCiuc002abp.3. human.

    Polymorphism databases

    DMDMi2499596.

    Keywords - Coding sequence diversityi

    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
    X80692 mRNA. Translation: CAA56709.1 .
    L77964 mRNA. Translation: AAA98769.1 .
    AF420474 mRNA. Translation: AAL17605.1 .
    AK313633 mRNA. Translation: BAG36392.1 .
    CR749401 mRNA. Translation: CAH18246.1 .
    AB451301 mRNA. Translation: BAG70115.1 .
    BC035492 mRNA. Translation: AAH35492.1 .
    CCDSi CCDS10147.1.
    PIRi A56352.
    RefSeqi NP_002739.1. NM_002748.3.
    XP_005254593.1. XM_005254536.2.
    XP_005254594.1. XM_005254537.1.
    XP_005254595.1. XM_005254538.1.
    XP_005254596.1. XM_005254539.2.
    UniGenei Hs.411847.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I6L X-ray 2.25 A/B 9-327 [» ]
    ProteinModelPortali Q16659.
    SMRi Q16659. Positions 13-358.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111583. 175 interactions.
    IntActi Q16659. 173 interactions.
    MINTi MINT-8247530.
    STRINGi 9606.ENSP00000261845.

    Chemistry

    BindingDBi Q16659.
    ChEMBLi CHEMBL5121.
    GuidetoPHARMACOLOGYi 2092.

    PTM databases

    PhosphoSitei Q16659.

    Polymorphism databases

    DMDMi 2499596.

    Proteomic databases

    MaxQBi Q16659.
    PaxDbi Q16659.
    PRIDEi Q16659.

    Protocols and materials databases

    DNASUi 5597.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261845 ; ENSP00000261845 ; ENSG00000069956 .
    GeneIDi 5597.
    KEGGi hsa:5597.
    UCSCi uc002abp.3. human.

    Organism-specific databases

    CTDi 5597.
    GeneCardsi GC15P052311.
    HGNCi HGNC:6879. MAPK6.
    HPAi CAB005184.
    HPA030262.
    HPA047825.
    MIMi 602904. gene.
    neXtProti NX_Q16659.
    PharmGKBi PA30624.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233020.
    HOVERGENi HBG104376.
    InParanoidi Q16659.
    KOi K06855.
    OMAi EHDWPIH.
    OrthoDBi EOG780RKS.
    PhylomeDBi Q16659.
    TreeFami TF105098.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    SignaLinki Q16659.

    Miscellaneous databases

    EvolutionaryTracei Q16659.
    GeneWikii MAPK6.
    GenomeRNAii 5597.
    NextBioi 21724.
    PROi Q16659.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16659.
    CleanExi HS_MAPK6.
    Genevestigatori Q16659.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR008350. MAPK_ERK3/4.
    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 PR01771. ERK3ERK4MAPK.
    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 p97MAPK, a novel human homolog of rat ERK-3."
      Zhu A.X., Zhao Y., Moller D.E., Flier J.S.
      Mol. Cell. Biol. 14:8202-8211(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal skeletal muscle.
    2. "Primary structure, expression and chromosomal locus of a human homolog of rat ERK3."
      Meloche S., Beatty B.G., Pellerin J.
      Oncogene 13:1575-1579(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Smooth muscle.
    3. "ERK-3 cDNA clone isolated from human oral cancer."
      Saranath D., Mahale A., Rai R., Dedhia P.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Oral cancer.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Trachea.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Esophageal carcinoma.
    6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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], VARIANT VAL-290.
      Tissue: Placenta.
    8. "N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome."
      Coulombe P., Rodier G., Bonneil E., Thibault P., Meloche S.
      Mol. Cell. Biol. 24:6140-6150(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT MET-1.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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.
    12. "Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein kinase 5 signaling pathway."
      Deleris P., Trost M., Topisirovic I., Tanguay P.L., Borden K.L., Thibault P., Meloche S.
      J. Biol. Chem. 286:6470-6478(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-189.
    13. "Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
      Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
      Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE3A AND NEURL4.
    14. "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: VARIANT [LARGE SCALE ANALYSIS] VAL-290.

    Entry informationi

    Entry nameiMK06_HUMAN
    AccessioniPrimary (citable) accession number: Q16659
    Secondary accession number(s): B2R945
    , B5BU65, Q68DH4, Q8IYN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 140 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, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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

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