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P0C595

- DUPD1_RAT

UniProt

P0C595 - DUPD1_RAT

Protein

Dual specificity phosphatase DUPD1

Gene

Dupd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    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 sitei146 – 1461Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity phosphatase DUPD1 (EC:3.1.3.16, EC:3.1.3.48)
    Gene namesi
    Name:Dupd1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi1310229. Dupd1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Dual specificity phosphatase DUPD1PRO_0000295881Add
    BLAST

    Proteomic databases

    PRIDEiP0C595.

    PTM databases

    PhosphoSiteiP0C595.

    Expressioni

    Gene expression databases

    GenevestigatoriP0C595.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000017483.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C595.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 200148Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni145 – 1528Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG270281.
    GeneTreeiENSGT00550000074474.
    HOGENOMiHOG000233767.
    HOVERGENiHBG001524.
    InParanoidiP0C595.
    KOiK14165.
    OMAiYLMIHKD.
    OrthoDBiEOG7CZK7N.
    PhylomeDBiP0C595.
    TreeFamiTF105128.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR020405. Atypical_DUSP_famA.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    PRINTSiPR01908. ADSPHPHTASE.
    PR01909. ADSPHPHTASEA.
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0C595-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGDTKTSV KHAHPCAERL SLQQEEGEAE DYCTPGAFEL ERLFWKGSPQ    50
    YTHVNEVWPR LHVGDEATAL DRYGLQKAGF THVLNAAHGR WNVDTGPDYY 100
    RDMAIEYHGV EADDVPTFDL SIFFYSAAAF IDSALQDDHS KILVHCAMGR 150
    SRSATLVLAY LMIHKNMTLV DAIQQVAKNR CVLPNRGFLK QLRELDKQLV 200
    KQRRQAGPGA GELGL 215
    Length:215
    Mass (Da):24,073
    Last modified:July 24, 2007 - v1
    Checksum:i3B8406772551A6A5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03097387 Genomic DNA. No translation available.
    AABR03097028 Genomic DNA. No translation available.
    AW918423 mRNA. No translation available.
    AW918455 mRNA. No translation available.
    RefSeqiNP_001101838.1. NM_001108368.1.
    XP_006251709.1. XM_006251647.1.
    XP_006251710.1. XM_006251648.1.
    XP_006251711.1. XM_006251649.1.
    UniGeneiRn.162035.

    Genome annotation databases

    EnsembliENSRNOT00000017483; ENSRNOP00000017483; ENSRNOG00000013034.
    GeneIDi361003.
    KEGGirno:361003.
    UCSCiRGD:1310229. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03097387 Genomic DNA. No translation available.
    AABR03097028 Genomic DNA. No translation available.
    AW918423 mRNA. No translation available.
    AW918455 mRNA. No translation available.
    RefSeqi NP_001101838.1. NM_001108368.1.
    XP_006251709.1. XM_006251647.1.
    XP_006251710.1. XM_006251648.1.
    XP_006251711.1. XM_006251649.1.
    UniGenei Rn.162035.

    3D structure databases

    ProteinModelPortali P0C595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000017483.

    PTM databases

    PhosphoSitei P0C595.

    Proteomic databases

    PRIDEi P0C595.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000017483 ; ENSRNOP00000017483 ; ENSRNOG00000013034 .
    GeneIDi 361003.
    KEGGi rno:361003.
    UCSCi RGD:1310229. rat.

    Organism-specific databases

    CTDi 338599.
    RGDi 1310229. Dupd1.

    Phylogenomic databases

    eggNOGi NOG270281.
    GeneTreei ENSGT00550000074474.
    HOGENOMi HOG000233767.
    HOVERGENi HBG001524.
    InParanoidi P0C595.
    KOi K14165.
    OMAi YLMIHKD.
    OrthoDBi EOG7CZK7N.
    PhylomeDBi P0C595.
    TreeFami TF105128.

    Miscellaneous databases

    NextBioi 674850.
    PROi P0C595.

    Gene expression databases

    Genevestigatori P0C595.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR020405. Atypical_DUSP_famA.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    PRINTSi PR01908. ADSPHPHTASE.
    PR01909. ADSPHPHTASEA.
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "Rat genome project: generation of a rat EST (REST) catalog & rat gene index."
      Lee N.H., Glodek A., Chandra I., Mason T.M., Quackenbush J., Kerlavage A.R., Adams M.D.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-177.

    Entry informationi

    Entry nameiDUPD1_RAT
    AccessioniPrimary (citable) accession number: P0C595
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3