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Q16644

- MAPK3_HUMAN

UniProt

Q16644 - MAPK3_HUMAN

Protein

MAP kinase-activated protein kinase 3

Gene

MAPKAPK3

Organism
Homo sapiens (Human)
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 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    Activated following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited by ligand 5B (2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one) and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive inhibitors.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731ATPPROSITE-ProRule annotation
    Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi50 – 589ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of MAPK activity Source: Reactome
    2. innate immune response Source: Reactome
    3. macropinocytosis Source: UniProtKB
    4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. peptidyl-serine phosphorylation Source: BHF-UCL
    8. Ras protein signal transduction Source: Reactome
    9. response to cytokine Source: UniProtKB
    10. response to lipopolysaccharide Source: UniProtKB
    11. response to stress Source: ProtInc
    12. signal transduction Source: ProtInc
    13. stress-activated MAPK cascade Source: Reactome
    14. toll-like receptor 10 signaling pathway Source: Reactome
    15. toll-like receptor 2 signaling pathway Source: Reactome
    16. toll-like receptor 3 signaling pathway Source: Reactome
    17. toll-like receptor 4 signaling pathway Source: Reactome
    18. toll-like receptor 5 signaling pathway Source: Reactome
    19. toll-like receptor 9 signaling pathway Source: Reactome
    20. toll-like receptor signaling pathway Source: UniProtKB
    21. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    22. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    23. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_12065. p38MAPK events.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    SignaLinkiQ16644.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MAP kinase-activated protein kinase 3 (EC:2.7.11.1)
    Short name:
    MAPK-activated protein kinase 3
    Short name:
    MAPKAP kinase 3
    Short name:
    MAPKAP-K3
    Short name:
    MAPKAPK-3
    Short name:
    MK-3
    Alternative name(s):
    Chromosome 3p kinase
    Short name:
    3pK
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6888. MAPKAPK3.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Predominantly located in the nucleus, when activated it translocates to the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nuclear membrane Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731K → M: Higher affinity toward PCH2. 1 Publication

    Organism-specific databases

    PharmGKBiPA30632.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 382382MAP kinase-activated protein kinase 3PRO_0000086293Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei201 – 2011Phosphothreonine; by MAPK14By similarity
    Modified residuei251 – 2511Phosphoserine; by MAPK14By similarity
    Modified residuei307 – 3071Phosphoserine; by autocatalysisBy similarity
    Modified residuei313 – 3131Phosphothreonine; by MAPK14By similarity

    Post-translational modificationi

    Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1. Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-201, Ser-251 and Thr-313 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ16644.
    PaxDbiQ16644.
    PeptideAtlasiQ16644.
    PRIDEiQ16644.

    PTM databases

    PhosphoSiteiQ16644.

    Expressioni

    Tissue specificityi

    Widely expressed, with a higher expression level observed in heart and skeletal muscle. No expression in brain.2 Publications

    Gene expression databases

    ArrayExpressiQ16644.
    BgeeiQ16644.
    CleanExiHS_MAPKAPK3.
    GenevestigatoriQ16644.

    Organism-specific databases

    HPAiHPA049533.

    Interactioni

    Subunit structurei

    Heterodimer with p38-alpha/MAPK14. The heterodimer with p38-alpha/MAPK14 forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface By similarity. Interacts with TCF3 and with polycomb proteins, such as PCH2 and BMI1/PCGF4.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279585EBI-1384657,EBI-6377335From a different organism.
    HSPB1P047923EBI-1384657,EBI-352682
    MAPK14Q165393EBI-1384657,EBI-73946

    Protein-protein interaction databases

    BioGridi113617. 19 interactions.
    IntActiQ16644. 12 interactions.
    MINTiMINT-3032958.
    STRINGi9606.ENSP00000350639.

    Structurei

    Secondary structure

    1
    382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi39 – 413
    Beta strandi43 – 5311
    Beta strandi56 – 638
    Turni64 – 663
    Beta strandi69 – 7810
    Helixi79 – 9113
    Beta strandi100 – 1089
    Beta strandi111 – 1199
    Helixi126 – 1316
    Helixi140 – 15920
    Helixi169 – 1713
    Beta strandi172 – 1754
    Beta strandi183 – 1853
    Helixi218 – 23720
    Turni267 – 2693
    Beta strandi271 – 2733
    Helixi275 – 28410
    Helixi289 – 2913
    Helixi295 – 3006
    Helixi302 – 3054
    Helixi307 – 3093
    Helixi317 – 3237
    Helixi325 – 3273
    Helixi328 – 34316
    Beta strandi344 – 3463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FHRX-ray1.90A33-349[»]
    3FXWX-ray2.00A33-349[»]
    3R1NX-ray2.09A33-349[»]
    3SHEX-ray2.25A33-349[»]
    ProteinModelPortaliQ16644.
    SMRiQ16644. Positions 33-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16644.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 304261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni307 – 34337Autoinhibitory helixBy similarityAdd
    BLAST
    Regioni345 – 36925p38 MAPK-binding siteBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi335 – 34410Nuclear export signal (NES)By similarity
    Motifi350 – 3534Bipartite nuclear localization signal 1By similarity
    Motifi364 – 3685Bipartite nuclear localization signal 2By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233031.
    HOVERGENiHBG106948.
    InParanoidiQ16644.
    KOiK04444.
    OMAiIRMGQYG.
    OrthoDBiEOG786H3M.
    PhylomeDBiQ16644.
    TreeFamiTF312891.

    Family and domain databases

    Gene3Di4.10.1170.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR027442. MAPKAPK_C.
    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.

    Q16644-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL    50
    GLGVNGKVLE CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI 100
    LDVYENMHHG KRCLLIIMEC MEGGELFSRI QERGDQAFTE REAAEIMRDI 150
    GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD AVLKLTDFGF AKETTQNALQ 200
    TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP PFYSNTGQAI 250
    SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN 300
    HPWINQSMVV PQTPLHTARV LQEDKDHWDE VKEEMTSALA TMRVDYDQVK 350
    IKDLKTSNNR LLNKRRKKQA GSSSASQGCN NQ 382
    Length:382
    Mass (Da):42,987
    Last modified:November 1, 1996 - v1
    Checksum:i405F958B7F54E6F3
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_040755
    Natural varianti105 – 1051E → A in an ovarian endometrioid sample; somatic mutation. 1 Publication
    VAR_040756
    Natural varianti276 – 2761D → Y.1 Publication
    Corresponds to variant rs56107897 [ dbSNP | Ensembl ].
    VAR_040757

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43784 mRNA. Translation: AAC50428.1.
    U09578 mRNA. Translation: AAD09136.1.
    AB451303 mRNA. Translation: BAG70117.1.
    CH471055 Genomic DNA. Translation: EAW65131.1.
    BC001662 mRNA. Translation: AAH01662.1.
    BC007591 mRNA. Translation: AAH07591.1.
    BC010407 mRNA. Translation: AAH10407.1.
    CCDSiCCDS2832.1.
    PIRiJC6094.
    RefSeqiNP_001230854.1. NM_001243925.1.
    NP_001230855.1. NM_001243926.1.
    NP_004626.1. NM_004635.4.
    UniGeneiHs.234521.
    Hs.735013.

    Genome annotation databases

    EnsembliENST00000357955; ENSP00000350639; ENSG00000114738.
    ENST00000446044; ENSP00000396467; ENSG00000114738.
    GeneIDi7867.
    KEGGihsa:7867.
    UCSCiuc003day.2. human.

    Polymorphism databases

    DMDMi74762148.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43784 mRNA. Translation: AAC50428.1 .
    U09578 mRNA. Translation: AAD09136.1 .
    AB451303 mRNA. Translation: BAG70117.1 .
    CH471055 Genomic DNA. Translation: EAW65131.1 .
    BC001662 mRNA. Translation: AAH01662.1 .
    BC007591 mRNA. Translation: AAH07591.1 .
    BC010407 mRNA. Translation: AAH10407.1 .
    CCDSi CCDS2832.1.
    PIRi JC6094.
    RefSeqi NP_001230854.1. NM_001243925.1.
    NP_001230855.1. NM_001243926.1.
    NP_004626.1. NM_004635.4.
    UniGenei Hs.234521.
    Hs.735013.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FHR X-ray 1.90 A 33-349 [» ]
    3FXW X-ray 2.00 A 33-349 [» ]
    3R1N X-ray 2.09 A 33-349 [» ]
    3SHE X-ray 2.25 A 33-349 [» ]
    ProteinModelPortali Q16644.
    SMRi Q16644. Positions 33-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113617. 19 interactions.
    IntActi Q16644. 12 interactions.
    MINTi MINT-3032958.
    STRINGi 9606.ENSP00000350639.

    Chemistry

    BindingDBi Q16644.
    ChEMBLi CHEMBL4670.
    GuidetoPHARMACOLOGYi 2095.

    PTM databases

    PhosphoSitei Q16644.

    Polymorphism databases

    DMDMi 74762148.

    Proteomic databases

    MaxQBi Q16644.
    PaxDbi Q16644.
    PeptideAtlasi Q16644.
    PRIDEi Q16644.

    Protocols and materials databases

    DNASUi 7867.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357955 ; ENSP00000350639 ; ENSG00000114738 .
    ENST00000446044 ; ENSP00000396467 ; ENSG00000114738 .
    GeneIDi 7867.
    KEGGi hsa:7867.
    UCSCi uc003day.2. human.

    Organism-specific databases

    CTDi 7867.
    GeneCardsi GC03P050648.
    HGNCi HGNC:6888. MAPKAPK3.
    HPAi HPA049533.
    MIMi 602130. gene.
    neXtProti NX_Q16644.
    PharmGKBi PA30632.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233031.
    HOVERGENi HBG106948.
    InParanoidi Q16644.
    KOi K04444.
    OMAi IRMGQYG.
    OrthoDBi EOG786H3M.
    PhylomeDBi Q16644.
    TreeFami TF312891.

    Enzyme and pathway databases

    Reactomei REACT_12065. p38MAPK events.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    SignaLinki Q16644.

    Miscellaneous databases

    ChiTaRSi MAPKAPK3. human.
    EvolutionaryTracei Q16644.
    GeneWikii MAPKAPK3.
    GenomeRNAii 7867.
    NextBioi 30313.
    PROi Q16644.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16644.
    Bgeei Q16644.
    CleanExi HS_MAPKAPK3.
    Genevestigatori Q16644.

    Family and domain databases

    Gene3Di 4.10.1170.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR027442. MAPKAPK_C.
    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. "Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase."
      McLaughlin M.M., Kumar S., McDonnell P.C., Van Horn S., Lee J.C., Livi G.P., Young P.R.
      J. Biol. Chem. 271:8488-8492(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    2. "3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region."
      Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G.
      , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.
      Mol. Cell. Biol. 16:868-876(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION BY MAPK1/ERK2 AND MAPK3/ERK1.
      Tissue: Heart.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Colon and Skin.
    6. "A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress."
      Clifton A.D., Young P.R., Cohen P.
      FEBS Lett. 392:209-214(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF HSPB1.
    7. "Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation."
      Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.
      J. Biol. Chem. 274:18947-18956(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1.
    8. "Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity."
      Neufeld B., Grosse-Wilde A., Hoffmeyer A., Jordan B.W., Chen P., Dinev D., Ludwig S., Rapp U.R.
      J. Biol. Chem. 275:20239-20242(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TCF3.
    9. "Mitogen-activated 3p kinase is active in the nucleus."
      Zakowski V., Keramas G., Kilian K., Rapp U.R., Ludwig S.
      Exp. Cell Res. 299:101-109(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1."
      Voncken J.W., Niessen H., Neufeld B., Rennefahrt U., Dahlmans V., Kubben N., Holzer B., Ludwig S., Rapp U.R.
      J. Biol. Chem. 280:5178-5187(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-73, INTERACTION WITH PHC2 AND BMI1.
    11. "Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex."
      Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N., Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L., Ghosh S., Cohen P.
      Biochem. J. 409:711-722(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TAB3.
    12. "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].
    13. "MAPKAP kinases MK2 and MK3 in inflammation: complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin."
      Ronkina N., Menon M.B., Schwermann J., Tiedje C., Hitti E., Kotlyarov A., Gaestel M.
      Biochem. Pharmacol. 80:1915-1920(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: REVIEW.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand."
      Cheng R., Felicetti B., Palan S., Toogood-Johnson I., Scheich C., Barker J., Whittaker M., Hesterkamp T.
      Protein Sci. 19:168-173(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR P4O.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR 5B.
    19. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-28; ALA-105 AND TYR-276.

    Entry informationi

    Entry nameiMAPK3_HUMAN
    AccessioniPrimary (citable) accession number: Q16644
    Secondary accession number(s): B5BU67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 127 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 3
      Human chromosome 3: 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