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Q9H1R2

- DUS15_HUMAN

UniProt

Q9H1R2 - DUS15_HUMAN

Protein

Dual specificity protein phosphatase 15

Gene

DUSP15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 4 (30 Apr 2003)
      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 sitei85 – 851Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of JNK cascade Source: RefGenome
    2. protein dephosphorylation Source: RefGenome
    3. regulation of cell proliferation Source: RefGenome
    4. transforming growth factor beta receptor signaling pathway Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SABIO-RKQ9H1R2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 15 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    VH1-related member Y
    Vaccinia virus VH1-related dual-specific protein phosphatase Y
    Gene namesi
    Name:DUSP15
    Synonyms:C20orf57, VHY
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16190. C20orf57.
    HGNC:16236. DUSP15.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851C → S: Loss of phosphatase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA27524.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Dual specificity protein phosphatase 15PRO_0000094824Add
    BLAST

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    PaxDbiQ9H1R2.
    PRIDEiQ9H1R2.

    PTM databases

    PhosphoSiteiQ9H1R2.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9H1R2.
    BgeeiQ9H1R2.
    CleanExiHS_C20orf57.
    HS_DUSP15.
    GenevestigatoriQ9H1R2.

    Organism-specific databases

    HPAiHPA031114.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-1752795,EBI-389883
    PLCG1P191742EBI-1752795,EBI-79387

    Protein-protein interaction databases

    BioGridi126164. 2 interactions.
    IntActiQ9H1R2. 9 interactions.
    MINTiMINT-7241177.

    Structurei

    Secondary structure

    1
    295
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 124
    Helixi16 – 183
    Helixi20 – 256
    Beta strandi30 – 345
    Beta strandi46 – 505
    Helixi60 – 634
    Helixi64 – 7613
    Beta strandi81 – 855
    Beta strandi88 – 903
    Helixi91 – 10414
    Helixi108 – 11710
    Helixi126 – 13712
    Helixi139 – 1457

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YZ4X-ray2.40A/B5-145[»]
    ProteinModelPortaliQ9H1R2.
    SMRiQ9H1R2. Positions 5-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H1R2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 13271Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000007880.
    HOVERGENiHBG054344.
    InParanoidiQ9H1R2.
    KOiK14165.
    OMAiCRQGSAT.
    OrthoDBiEOG7966HM.
    PhylomeDBiQ9H1R2.
    TreeFamiTF105126.

    Family and domain databases

    Gene3Di2.60.200.10. 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.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR017855. SMAD_dom-like.
    IPR008984. SMAD_FHA_domain.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    PRINTSiPR01908. ADSPHPHTASE.
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H1R2-1) [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

    MTEGVLPGLY LGNFIDAKDL DQLGRNKITH IISIHESPQP LLQDITYLRI    50
    PVADTPEVPI KKHFKECINF IHCCRLNGGN CLVHCFAGIS RSTTIVTAYV 100
    MTVTGLGWRD VLEAIKATRP IANPNPGFRQ QLEEFGWASS QKGARHRTSK 150
    TSGAQCPPMT SATCLLAARV ALLSAALVRE ATGRTAQRCR LSPRAAAERL 200
    LGPPPHVAAG WSPDPKYQIC LCFGEEDPGP TQHPKEQLIM ADVQVQLRPG 250
    SSSCTLSAST ERPDGSSTPG NPDGITHLQC SCLHPKRAAS SSCTR 295
    Length:295
    Mass (Da):31,882
    Last modified:April 30, 2003 - v4
    Checksum:i28F8A687ECB5C219
    GO
    Isoform 2 (identifier: Q9H1R2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
         233-295: Missing.

    Note: Derived from EST data.

    Show »
    Length:232
    Mass (Da):25,851
    Checksum:i806EB3DFA4167D76
    GO
    Isoform 3 (identifier: Q9H1R2-3) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MTEG → MGNGMTK
         143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
         233-295: Missing.

    Note: Initiator Met-1 is removed. Myristoylated on Gly-2.

    Show »
    Length:235
    Mass (Da):26,152
    Checksum:iA3AF26789894FECB
    GO
    Isoform 4 (identifier: Q9H1R2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.
         143-232: GARHRTSKTS...FGEEDPGPTQ → LRRQLEERFG...PRCLSRKGGK
         233-295: Missing.

    Show »
    Length:132
    Mass (Da):14,721
    Checksum:iF1690DF488891012
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 4. 1 PublicationVSP_043107Add
    BLAST
    Alternative sequencei1 – 44MTEG → MGNGMTK in isoform 3. 1 PublicationVSP_019228
    Alternative sequencei143 – 23290GARHR…PGPTQ → LRRQLEERFGESPFRDEEEL RALLPLCKRCRQGSATSASS AGPHSAASEGTVQRLVPRTP REAHRPLPLLARVKQTFSCL PRCLSRKGGK in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_007292Add
    BLAST
    Alternative sequencei233 – 29563Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_007293Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK091960 mRNA. Translation: BAG52450.1.
    AK097430 mRNA. Translation: BAC05048.1.
    AL160175 Genomic DNA. Translation: CAI12819.1.
    AL160175 Genomic DNA. Translation: CAI12821.1.
    AL160175 Genomic DNA. Translation: CAI12822.1.
    CH471077 Genomic DNA. Translation: EAW76410.1.
    BC056911 mRNA. Translation: AAH56911.1.
    BM554314 mRNA. No translation available.
    CCDSiCCDS13193.1. [Q9H1R2-3]
    CCDS42862.1. [Q9H1R2-4]
    RefSeqiNP_001012662.1. NM_001012644.1. [Q9H1R2-4]
    NP_542178.2. NM_080611.3. [Q9H1R2-3]
    NP_817130.1. NM_177991.1. [Q9H1R2-4]
    UniGeneiHs.434108.
    Hs.585017.

    Genome annotation databases

    EnsembliENST00000278979; ENSP00000278979; ENSG00000149599. [Q9H1R2-1]
    ENST00000339738; ENSP00000341658; ENSG00000149599. [Q9H1R2-3]
    ENST00000375966; ENSP00000365133; ENSG00000149599. [Q9H1R2-2]
    ENST00000398083; ENSP00000381157; ENSG00000149599. [Q9H1R2-4]
    ENST00000398084; ENSP00000381158; ENSG00000149599. [Q9H1R2-4]
    ENST00000486996; ENSP00000419818; ENSG00000149599. [Q9H1R2-4]
    GeneIDi128853.
    KEGGihsa:128853.
    UCSCiuc002wwu.1. human. [Q9H1R2-1]
    uc002wwv.1. human. [Q9H1R2-4]
    uc002wwx.1. human. [Q9H1R2-3]

    Polymorphism databases

    DMDMi30316387.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK091960 mRNA. Translation: BAG52450.1 .
    AK097430 mRNA. Translation: BAC05048.1 .
    AL160175 Genomic DNA. Translation: CAI12819.1 .
    AL160175 Genomic DNA. Translation: CAI12821.1 .
    AL160175 Genomic DNA. Translation: CAI12822.1 .
    CH471077 Genomic DNA. Translation: EAW76410.1 .
    BC056911 mRNA. Translation: AAH56911.1 .
    BM554314 mRNA. No translation available.
    CCDSi CCDS13193.1. [Q9H1R2-3 ]
    CCDS42862.1. [Q9H1R2-4 ]
    RefSeqi NP_001012662.1. NM_001012644.1. [Q9H1R2-4 ]
    NP_542178.2. NM_080611.3. [Q9H1R2-3 ]
    NP_817130.1. NM_177991.1. [Q9H1R2-4 ]
    UniGenei Hs.434108.
    Hs.585017.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YZ4 X-ray 2.40 A/B 5-145 [» ]
    ProteinModelPortali Q9H1R2.
    SMRi Q9H1R2. Positions 5-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126164. 2 interactions.
    IntActi Q9H1R2. 9 interactions.
    MINTi MINT-7241177.

    Chemistry

    ChEMBLi CHEMBL2396507.

    PTM databases

    PhosphoSitei Q9H1R2.

    Polymorphism databases

    DMDMi 30316387.

    Proteomic databases

    PaxDbi Q9H1R2.
    PRIDEi Q9H1R2.

    Protocols and materials databases

    DNASUi 128853.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278979 ; ENSP00000278979 ; ENSG00000149599 . [Q9H1R2-1 ]
    ENST00000339738 ; ENSP00000341658 ; ENSG00000149599 . [Q9H1R2-3 ]
    ENST00000375966 ; ENSP00000365133 ; ENSG00000149599 . [Q9H1R2-2 ]
    ENST00000398083 ; ENSP00000381157 ; ENSG00000149599 . [Q9H1R2-4 ]
    ENST00000398084 ; ENSP00000381158 ; ENSG00000149599 . [Q9H1R2-4 ]
    ENST00000486996 ; ENSP00000419818 ; ENSG00000149599 . [Q9H1R2-4 ]
    GeneIDi 128853.
    KEGGi hsa:128853.
    UCSCi uc002wwu.1. human. [Q9H1R2-1 ]
    uc002wwv.1. human. [Q9H1R2-4 ]
    uc002wwx.1. human. [Q9H1R2-3 ]

    Organism-specific databases

    CTDi 128853.
    GeneCardsi GC20M030443.
    GC20U990068.
    H-InvDB HIX0015716.
    HGNCi HGNC:16190. C20orf57.
    HGNC:16236. DUSP15.
    HPAi HPA031114.
    neXtProti NX_Q9H1R2.
    PharmGKBi PA27524.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000007880.
    HOVERGENi HBG054344.
    InParanoidi Q9H1R2.
    KOi K14165.
    OMAi CRQGSAT.
    OrthoDBi EOG7966HM.
    PhylomeDBi Q9H1R2.
    TreeFami TF105126.

    Enzyme and pathway databases

    SABIO-RK Q9H1R2.

    Miscellaneous databases

    EvolutionaryTracei Q9H1R2.
    GeneWikii DUSP15.
    GenomeRNAii 128853.
    NextBioi 82475.
    PROi Q9H1R2.

    Gene expression databases

    ArrayExpressi Q9H1R2.
    Bgeei Q9H1R2.
    CleanExi HS_C20orf57.
    HS_DUSP15.
    Genevestigatori Q9H1R2.

    Family and domain databases

    Gene3Di 2.60.200.10. 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.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR017855. SMAD_dom-like.
    IPR008984. SMAD_FHA_domain.
    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.
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    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. "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] (ISOFORMS 1 AND 4).
      Tissue: Testis.
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2 AND 3).
      Tissue: Brain and PNS.
    5. "VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX."
      Alonso A., Narisawa S., Bogetz J., Tautz L., Hadzic R., Huynh H., Williams S., Gjoerloff-Wingren A., Bremer M.C.D., Holsinger L.J., Millan J.L., Mustelin T.
      J. Biol. Chem. 279:32586-32591(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-85, MYRISTOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase."
      Yoon T.-S., Jeong D.G., Kim J.H., Cho Y.H., Son J.H., Lee J.W., Ryu S.E., Kim S.J.
      Proteins 61:694-697(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-157 (ISOFORM 3).

    Entry informationi

    Entry nameiDUS15_HUMAN
    AccessioniPrimary (citable) accession number: Q9H1R2
    Secondary accession number(s): A6NH79
    , A8MVC8, Q5QP62, Q5QP63, Q5QP65, Q6PGN7, Q8N826, Q9BX24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 131 of the entry and version 4 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 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3