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Q9Y6W6

- DUS10_HUMAN

UniProt

Q9Y6W6 - DUS10_HUMAN

Protein

Dual specificity protein phosphatase 10

Gene

DUSP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei408 – 4081Phosphocysteine intermediate2 Publications

    GO - Molecular functioni

    1. MAP kinase phosphatase activity Source: UniProtKB
    2. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
    3. phosphatase activity Source: UniProtKB
    4. phosphoprotein phosphatase activity Source: ProtInc
    5. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    6. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. inactivation of MAPK activity Source: UniProtKB
    2. JNK cascade Source: ProtInc
    3. negative regulation of JNK cascade Source: RefGenome
    4. negative regulation of JUN kinase activity Source: RefGenome
    5. negative regulation of respiratory burst involved in inflammatory response Source: Ensembl
    6. protein dephosphorylation Source: UniProtKB
    7. regulation of adaptive immune response Source: Ensembl
    8. response to lipopolysaccharide Source: Ensembl
    9. response to stress Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BRENDAi3.1.3.48. 2681.
    SignaLinkiQ9Y6W6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 10 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Mitogen-activated protein kinase phosphatase 5
    Short name:
    MAP kinase phosphatase 5
    Short name:
    MKP-5
    Gene namesi
    Name:DUSP10
    Synonyms:MKP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3065. DUSP10.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. Golgi apparatus Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1812FM → DD: Reduced enzyme activity with MAPK14. 1 Publication
    Mutagenesisi203 – 2042RR → AA: Strongly reduced affinity for MAPK14. Almost abolishes enzyme activity with MAPK14. 1 Publication

    Organism-specific databases

    PharmGKBiPA27520.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Dual specificity protein phosphatase 10PRO_0000094813Add
    BLAST

    Proteomic databases

    PaxDbiQ9Y6W6.
    PRIDEiQ9Y6W6.

    PTM databases

    PhosphoSiteiQ9Y6W6.

    Expressioni

    Tissue specificityi

    Detected in brain.1 Publication

    Gene expression databases

    BgeeiQ9Y6W6.
    CleanExiHS_DUSP10.
    GenevestigatoriQ9Y6W6.

    Organism-specific databases

    HPAiHPA016758.

    Interactioni

    Subunit structurei

    Monomer. Interacts with MAPK14.3 Publications

    Protein-protein interaction databases

    BioGridi116389. 11 interactions.
    IntActiQ9Y6W6. 10 interactions.
    MINTiMINT-8208613.
    STRINGi9606.ENSP00000355866.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi152 – 1609
    Beta strandi173 – 1764
    Helixi180 – 1856
    Beta strandi186 – 1883
    Helixi199 – 2068
    Helixi212 – 2176
    Helixi224 – 2307
    Beta strandi233 – 2364
    Helixi243 – 2453
    Beta strandi248 – 2503
    Helixi251 – 26111
    Beta strandi267 – 2693
    Helixi272 – 2765
    Turni277 – 2793
    Helixi281 – 2833
    Beta strandi284 – 2863
    Beta strandi323 – 3264
    Beta strandi329 – 3324
    Helixi336 – 3383
    Helixi340 – 3456
    Beta strandi348 – 3536
    Beta strandi356 – 3583
    Helixi363 – 3653
    Beta strandi368 – 3725
    Beta strandi378 – 3803
    Helixi384 – 3863
    Helixi387 – 39913
    Beta strandi403 – 4075
    Beta strandi409 – 4135
    Helixi414 – 42613
    Helixi431 – 44111
    Helixi449 – 46315
    Helixi478 – 4825

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZZWX-ray1.60A/B320-467[»]
    2OUCX-ray2.20A/B148-287[»]
    2OUDX-ray2.80A315-482[»]
    3TG1X-ray2.71B139-288[»]
    ProteinModelPortaliQ9Y6W6.
    SMRiQ9Y6W6. Positions 148-287, 315-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6W6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 285118RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini384 – 45370Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 21517Interaction with MAP kinasesAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000069871.
    HOVERGENiHBG102158.
    InParanoidiQ9Y6W6.
    KOiK04459.
    OMAiTCPANQM.
    OrthoDBiEOG75QR5B.
    PhylomeDBiQ9Y6W6.
    TreeFamiTF105122.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR008343. MKP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR001763. Rhodanese-like_dom.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    PF00581. Rhodanese. 1 hit.
    [Graphical view]
    PRINTSiPR01908. ADSPHPHTASE.
    PR01764. MAPKPHPHTASE.
    SMARTiSM00195. DSPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    SSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6W6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV    50
    VSLKAANLTY MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG 100
    TTTTAIGTST TCPANQMVNN NENTGSLSPS SGVGSPVSGT PKQLASIKII 150
    YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF MEYNKSHIQG AVHINCADKI 200
    SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT NEPSRVMPSQ 250
    PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA 300
    SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY 350
    VINVTTHLPL YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC 400
    GKGLLIHCQA GVSRSATIVI AYLMKHTRMT MTDAYKFVKG KRPIISPNLN 450
    FMGQLLEFEE DLNNGVTPRI LTPKLMGVET VV 482
    Length:482
    Mass (Da):52,642
    Last modified:November 1, 1999 - v1
    Checksum:iA8CB74ABF9498CD4
    GO
    Isoform 2 (identifier: Q9Y6W6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-342: Missing.

    Show »
    Length:140
    Mass (Da):16,110
    Checksum:iCE151F365D042516
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 342342Missing in isoform 2. 2 PublicationsVSP_036549Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026436 mRNA. Translation: BAA81668.1.
    AF179212 mRNA. Translation: AAD51857.1.
    AK022513 mRNA. Translation: BAB14070.1.
    AL590966 Genomic DNA. Translation: CAH71120.1.
    CH471100 Genomic DNA. Translation: EAW93283.1.
    CH471100 Genomic DNA. Translation: EAW93285.1.
    CH471100 Genomic DNA. Translation: EAW93286.1.
    CH471100 Genomic DNA. Translation: EAW93287.1.
    BC020608 mRNA. Translation: AAH20608.1.
    BC031405 mRNA. Translation: AAH31405.1.
    BC063826 mRNA. Translation: AAH63826.1.
    CCDSiCCDS1528.1. [Q9Y6W6-1]
    RefSeqiNP_009138.1. NM_007207.5. [Q9Y6W6-1]
    UniGeneiHs.497822.
    Hs.732301.

    Genome annotation databases

    EnsembliENST00000323825; ENSP00000322015; ENSG00000143507. [Q9Y6W6-2]
    ENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
    ENST00000544095; ENSP00000441302; ENSG00000143507. [Q9Y6W6-2]
    GeneIDi11221.
    KEGGihsa:11221.
    UCSCiuc001hmx.2. human. [Q9Y6W6-2]
    uc001hmy.2. human. [Q9Y6W6-1]

    Polymorphism databases

    DMDMi20138090.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026436 mRNA. Translation: BAA81668.1 .
    AF179212 mRNA. Translation: AAD51857.1 .
    AK022513 mRNA. Translation: BAB14070.1 .
    AL590966 Genomic DNA. Translation: CAH71120.1 .
    CH471100 Genomic DNA. Translation: EAW93283.1 .
    CH471100 Genomic DNA. Translation: EAW93285.1 .
    CH471100 Genomic DNA. Translation: EAW93286.1 .
    CH471100 Genomic DNA. Translation: EAW93287.1 .
    BC020608 mRNA. Translation: AAH20608.1 .
    BC031405 mRNA. Translation: AAH31405.1 .
    BC063826 mRNA. Translation: AAH63826.1 .
    CCDSi CCDS1528.1. [Q9Y6W6-1 ]
    RefSeqi NP_009138.1. NM_007207.5. [Q9Y6W6-1 ]
    UniGenei Hs.497822.
    Hs.732301.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZZW X-ray 1.60 A/B 320-467 [» ]
    2OUC X-ray 2.20 A/B 148-287 [» ]
    2OUD X-ray 2.80 A 315-482 [» ]
    3TG1 X-ray 2.71 B 139-288 [» ]
    ProteinModelPortali Q9Y6W6.
    SMRi Q9Y6W6. Positions 148-287, 315-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116389. 11 interactions.
    IntActi Q9Y6W6. 10 interactions.
    MINTi MINT-8208613.
    STRINGi 9606.ENSP00000355866.

    Chemistry

    ChEMBLi CHEMBL2396511.

    PTM databases

    PhosphoSitei Q9Y6W6.

    Polymorphism databases

    DMDMi 20138090.

    Proteomic databases

    PaxDbi Q9Y6W6.
    PRIDEi Q9Y6W6.

    Protocols and materials databases

    DNASUi 11221.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323825 ; ENSP00000322015 ; ENSG00000143507 . [Q9Y6W6-2 ]
    ENST00000366899 ; ENSP00000355866 ; ENSG00000143507 . [Q9Y6W6-1 ]
    ENST00000544095 ; ENSP00000441302 ; ENSG00000143507 . [Q9Y6W6-2 ]
    GeneIDi 11221.
    KEGGi hsa:11221.
    UCSCi uc001hmx.2. human. [Q9Y6W6-2 ]
    uc001hmy.2. human. [Q9Y6W6-1 ]

    Organism-specific databases

    CTDi 11221.
    GeneCardsi GC01M221874.
    HGNCi HGNC:3065. DUSP10.
    HPAi HPA016758.
    MIMi 608867. gene.
    neXtProti NX_Q9Y6W6.
    PharmGKBi PA27520.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000069871.
    HOVERGENi HBG102158.
    InParanoidi Q9Y6W6.
    KOi K04459.
    OMAi TCPANQM.
    OrthoDBi EOG75QR5B.
    PhylomeDBi Q9Y6W6.
    TreeFami TF105122.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.
    SignaLinki Q9Y6W6.

    Miscellaneous databases

    EvolutionaryTracei Q9Y6W6.
    GeneWikii DUSP10.
    GenomeRNAii 11221.
    NextBioi 42707.
    PROi Q9Y6W6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y6W6.
    CleanExi HS_DUSP10.
    Genevestigatori Q9Y6W6.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR008343. MKP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR001763. Rhodanese-like_dom.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    PF00581. Rhodanese. 1 hit.
    [Graphical view ]
    PRINTSi PR01908. ADSPHPHTASE.
    PR01764. MAPKPHPHTASE.
    SMARTi SM00195. DSPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5."
      Tanoue T., Moriguchi T., Nishida E.
      J. Biol. Chem. 274:19949-19956(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases."
      Theodosiou A., Smith A., Gillieron C., Arkinstall S., Ashworth A.
      Oncogene 18:6981-6988(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 2).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain, Lung, PNS and Testis.
    7. "Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase."
      Jeong D.G., Yoon T.S., Kim J.H., Shim M.Y., Jung S.K., Son J.H., Ryu S.E., Kim S.J.
      J. Mol. Biol. 360:946-955(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 320-467, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, ACTIVE SITE.
    8. "Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5."
      Tao X., Tong L.
      Protein Sci. 16:880-886(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 148-287, SUBUNIT, ACTIVE SITE.
    9. "A distinct interaction mode revealed by the crystal structure of the kinase p38alpha with the MAPK binding domain of the phosphatase MKP5."
      Zhang Y.Y., Wu J.W., Wang Z.X.
      Sci. Signal. 4:RA88-RA88(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 139-288 IN COMPLEX WITH MAPK14, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAPK14, MUTAGENESIS OF 180-PHE-MET-181 AND 203-ARG-ARG-204.

    Entry informationi

    Entry nameiDUS10_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6W6
    Secondary accession number(s): D3DTB4, Q6GSI4, Q9H9Z5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 133 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3