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P51452

- DUS3_HUMAN

UniProt

P51452 - DUS3_HUMAN

Protein

Dual specificity protein phosphatase 3

Gene

DUSP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2.2 Publications

    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 sitei124 – 1241Phosphocysteine intermediate

    GO - Molecular functioni

    1. MAP kinase phosphatase activity Source: UniProtKB
    2. protein tyrosine/serine/threonine phosphatase activity Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. inactivation of MAPK activity Source: UniProtKB
    2. innate immune response Source: Reactome
    3. in utero embryonic development Source: Ensembl
    4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    6. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    7. negative regulation of JNK cascade Source: UniProtKB
    8. negative regulation of MAPK cascade Source: UniProtKB
    9. negative regulation of T cell activation Source: UniProtKB
    10. negative regulation of T cell receptor signaling pathway Source: UniProtKB
    11. neurotrophin TRK receptor signaling pathway Source: Reactome
    12. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    13. positive regulation of mitotic cell cycle Source: UniProtKB
    14. stress-activated MAPK cascade Source: Reactome
    15. toll-like receptor 10 signaling pathway Source: Reactome
    16. toll-like receptor 2 signaling pathway Source: Reactome
    17. toll-like receptor 3 signaling pathway Source: Reactome
    18. toll-like receptor 4 signaling pathway Source: Reactome
    19. toll-like receptor 5 signaling pathway Source: Reactome
    20. toll-like receptor 9 signaling pathway Source: Reactome
    21. toll-like receptor signaling pathway Source: Reactome
    22. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    23. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    24. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_12436. ERKs are inactivated.
    SignaLinkiP51452.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 3 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity protein phosphatase VHR
    Vaccinia H1-related phosphatase
    Short name:
    VHR
    Gene namesi
    Name:DUSP3
    Synonyms:VHR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3069. DUSP3.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. immunological synapse Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27526.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185Dual specificity protein phosphatase 3PRO_0000094795Add
    BLAST

    Proteomic databases

    MaxQBiP51452.
    PaxDbiP51452.
    PRIDEiP51452.

    2D gel databases

    UCD-2DPAGEP51452.

    PTM databases

    PhosphoSiteiP51452.

    Expressioni

    Gene expression databases

    ArrayExpressiP51452.
    BgeeiP51452.
    CleanExiHS_DUSP3.
    GenevestigatoriP51452.

    Organism-specific databases

    HPAiCAB025265.

    Interactioni

    Subunit structurei

    Interacts with VRK3, which seems to activate it's phosphatase activity.By similarity

    Protein-protein interaction databases

    BioGridi108178. 9 interactions.
    IntActiP51452. 5 interactions.
    MINTiMINT-5001069.
    STRINGi9606.ENSP00000226004.

    Structurei

    Secondary structure

    1
    185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 169
    Beta strandi19 – 213
    Beta strandi27 – 348
    Beta strandi37 – 404
    Helixi42 – 454
    Helixi48 – 547
    Beta strandi58 – 614
    Beta strandi64 – 674
    Helixi76 – 783
    Turni79 – 824
    Beta strandi84 – 874
    Helixi98 – 1014
    Helixi102 – 11413
    Turni115 – 1173
    Beta strandi120 – 1234
    Beta strandi125 – 1295
    Helixi130 – 14314
    Helixi147 – 15711
    Helixi164 – 17916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J4XX-ray2.75A2-185[»]
    1VHRX-ray2.10A/B2-185[»]
    3F81X-ray1.90A/B3-185[»]
    ProteinModelPortaliP51452.
    SMRiP51452. Positions 7-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51452.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 16971Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000233767.
    HOVERGENiHBG001524.
    InParanoidiP51452.
    KOiK17614.
    OMAiPCNEVIP.
    OrthoDBiEOG7CZK7N.
    PhylomeDBiP51452.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51452-1) [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

    MSGSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVTPRIYVG NASVAQDIPK    50
    LQKLGITHVL NAAEGRSFMH VNTNANFYKD SGITYLGIKA NDTQEFNLSA 100
    YFERAADFID QALAQKNGRV LVHCREGYSR SPTLVIAYLM MRQKMDVKSA 150
    LSIVRQNREI GPNDGFLAQL CQLNDRLAKE GKLKP 185
    Length:185
    Mass (Da):20,478
    Last modified:October 1, 1996 - v1
    Checksum:iC1045DD9B226FD94
    GO
    Isoform 2 (identifier: P51452-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: MSGSFELSVQDLNDLLSDGSGCYSLPSQPCNEVTPRIYVGNA → M

    Note: No experimental confirmation available.

    Show »
    Length:144
    Mass (Da):16,163
    Checksum:i21CA189AF19D20B3
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242MSGSF…YVGNA → M in isoform 2. 1 PublicationVSP_056284Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05147 mRNA. Translation: AAA35777.1.
    BT019522 mRNA. Translation: AAV38329.1.
    CH471178 Genomic DNA. Translation: EAW51667.1.
    CH471178 Genomic DNA. Translation: EAW51668.1.
    BC002682 mRNA. Translation: AAH02682.1.
    BC035701 mRNA. Translation: AAH35701.1.
    AC003098 Genomic DNA. No translation available.
    AC055813 Genomic DNA. No translation available.
    CCDSiCCDS11469.1.
    PIRiA47196.
    RefSeqiNP_004081.1. NM_004090.3.
    UniGeneiHs.181046.

    Genome annotation databases

    EnsembliENST00000226004; ENSP00000226004; ENSG00000108861.
    ENST00000397937; ENSP00000443014; ENSG00000108861.
    GeneIDi1845.
    KEGGihsa:1845.
    UCSCiuc002ied.4. human.

    Polymorphism databases

    DMDMi1718191.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05147 mRNA. Translation: AAA35777.1 .
    BT019522 mRNA. Translation: AAV38329.1 .
    CH471178 Genomic DNA. Translation: EAW51667.1 .
    CH471178 Genomic DNA. Translation: EAW51668.1 .
    BC002682 mRNA. Translation: AAH02682.1 .
    BC035701 mRNA. Translation: AAH35701.1 .
    AC003098 Genomic DNA. No translation available.
    AC055813 Genomic DNA. No translation available.
    CCDSi CCDS11469.1.
    PIRi A47196.
    RefSeqi NP_004081.1. NM_004090.3.
    UniGenei Hs.181046.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J4X X-ray 2.75 A 2-185 [» ]
    1VHR X-ray 2.10 A/B 2-185 [» ]
    3F81 X-ray 1.90 A/B 3-185 [» ]
    ProteinModelPortali P51452.
    SMRi P51452. Positions 7-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108178. 9 interactions.
    IntActi P51452. 5 interactions.
    MINTi MINT-5001069.
    STRINGi 9606.ENSP00000226004.

    Chemistry

    BindingDBi P51452.
    ChEMBLi CHEMBL2635.

    PTM databases

    PhosphoSitei P51452.

    Polymorphism databases

    DMDMi 1718191.

    2D gel databases

    UCD-2DPAGE P51452.

    Proteomic databases

    MaxQBi P51452.
    PaxDbi P51452.
    PRIDEi P51452.

    Protocols and materials databases

    DNASUi 1845.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000226004 ; ENSP00000226004 ; ENSG00000108861 .
    ENST00000397937 ; ENSP00000443014 ; ENSG00000108861 .
    GeneIDi 1845.
    KEGGi hsa:1845.
    UCSCi uc002ied.4. human.

    Organism-specific databases

    CTDi 1845.
    GeneCardsi GC17M041856.
    H-InvDB HIX0013868.
    HGNCi HGNC:3069. DUSP3.
    HPAi CAB025265.
    MIMi 600183. gene.
    neXtProti NX_P51452.
    PharmGKBi PA27526.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000233767.
    HOVERGENi HBG001524.
    InParanoidi P51452.
    KOi K17614.
    OMAi PCNEVIP.
    OrthoDBi EOG7CZK7N.
    PhylomeDBi P51452.
    TreeFami TF105128.

    Enzyme and pathway databases

    Reactomei REACT_12436. ERKs are inactivated.
    SignaLinki P51452.

    Miscellaneous databases

    ChiTaRSi DUSP3. human.
    EvolutionaryTracei P51452.
    GeneWikii DUSP3.
    GenomeRNAii 1845.
    NextBioi 7555.
    PROi P51452.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51452.
    Bgeei P51452.
    CleanExi HS_DUSP3.
    Genevestigatori P51452.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Duodenum and Uterus.
    6. "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway."
      Todd J.L., Tanner K.G., Denu J.M.
      J. Biol. Chem. 274:13271-13280(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Crystal structure of the dual specificity protein phosphatase VHR."
      Yuvaniyama J., Denu J.M., Dixon J.E., Saper M.A.
      Science 272:1328-1331(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    9. "Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase."
      Schumacher M.A., Todd J.L., Rice A.E., Tanner K.G., Denu J.M.
      Biochemistry 41:3009-3017(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 2-185, FUNCTION.
    10. "Multidentate small-molecule inhibitors of vaccinia H1-related (VHR) phosphatase decrease proliferation of cervix cancer cells."
      Wu S., Vossius S., Rahmouni S., Miletic A.V., Vang T., Vazquez-Rodriguez J., Cerignoli F., Arimura Y., Williams S., Hayes T., Moutschen M., Vasile S., Pellecchia M., Mustelin T., Tautz L.
      J. Med. Chem. 52:6716-6723(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-185.

    Entry informationi

    Entry nameiDUS3_HUMAN
    AccessioniPrimary (citable) accession number: P51452
    Secondary accession number(s): D3DX45, Q5U0J1, Q8IYJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 138 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 17
      Human chromosome 17: 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