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Q16690

- DUS5_HUMAN

UniProt

Q16690 - DUS5_HUMAN

Protein

Dual specificity protein phosphatase 5

Gene

DUSP5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Displays phosphatase activity toward several substrates. The highest relative activity is toward ERK1.

    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 sitei263 – 2631Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
    2. protein binding Source: IntAct
    3. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    4. protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. endoderm formation Source: RefGenome
    2. peptidyl-tyrosine dephosphorylation Source: GOC
    3. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SignaLinkiQ16690.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 5 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity protein phosphatase hVH3
    Gene namesi
    Name:DUSP5
    Synonyms:VH3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3071. DUSP5.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27528.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384Dual specificity protein phosphatase 5PRO_0000094802Add
    BLAST

    Proteomic databases

    MaxQBiQ16690.
    PaxDbiQ16690.
    PRIDEiQ16690.

    PTM databases

    PhosphoSiteiQ16690.

    Expressioni

    Gene expression databases

    BgeeiQ16690.
    CleanExiHS_DUSP5.
    GenevestigatoriQ16690.

    Organism-specific databases

    HPAiHPA055143.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK1P284824EBI-7487376,EBI-959949

    Protein-protein interaction databases

    BioGridi108180. 3 interactions.
    IntActiQ16690. 1 interaction.
    MINTiMINT-8277166.
    STRINGi9606.ENSP00000358596.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi180 – 1834
    Beta strandi186 – 1905
    Helixi191 – 1944
    Helixi197 – 2037
    Beta strandi207 – 2104
    Beta strandi223 – 2275
    Helixi239 – 2413
    Helixi242 – 25413
    Beta strandi259 – 26810
    Helixi269 – 28214
    Helixi286 – 29611
    Helixi304 – 31714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G6ZX-ray2.70A/B/C178-384[»]
    ProteinModelPortaliQ16690.
    SMRiQ16690. Positions 22-140, 178-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16690.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 141123RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini180 – 384205Tyrosine-protein phosphataseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi53 – 7422Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi79 – 824Poly-Gly

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOVERGENiHBG007347.
    InParanoidiQ16690.
    KOiK04459.
    OMAiSPVHQLK.
    OrthoDBiEOG75MVWD.
    PhylomeDBiQ16690.
    TreeFamiTF105122.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR000340. 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]
    PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
    PRINTSiPR01764. 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]

    Sequencei

    Sequence statusi: Complete.

    Q16690-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV    50
    VLRRARGGAV SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR 100
    EESAARVVLT SLLACLPAGP RVYFLKGGYE TFYSEYPECC VDVKPISQEK 150
    IESERALISQ CGKPVVNVSY RPAYDQGGPV EILPFLYLGS AYHASKCEFL 200
    ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS HFQEAIDFID 250
    CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV 300
    SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ 350
    GAYCTFPASV LAPVPTHSTV SELSRSPVAT ATSC 384
    Length:384
    Mass (Da):42,047
    Last modified:November 25, 2008 - v2
    Checksum:i2E4B2938F886CB4E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 113RQL → GHV in AAA64693. (PubMed:7961985)Curated
    Sequence conflicti71 – 711A → R in AAA64693. (PubMed:7961985)Curated
    Sequence conflicti105 – 1062AR → F in AAA64693. (PubMed:7961985)Curated
    Sequence conflicti220 – 2201A → M in AAA64693. (PubMed:7961985)Curated
    Sequence conflicti220 – 2201A → M in AAB06261. (PubMed:7836374)Curated
    Sequence conflicti220 – 2201A → M in AAH62545. (PubMed:15489334)Curated
    Sequence conflicti382 – 3821T → Q in AAA64693. (PubMed:7961985)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti154 – 1541E → D.
    Corresponds to variant rs2282238 [ dbSNP | Ensembl ].
    VAR_020298
    Natural varianti220 – 2201A → T.
    Corresponds to variant rs1889566 [ dbSNP | Ensembl ].
    VAR_059777
    Natural varianti220 – 2201A → V.
    Corresponds to variant rs1889565 [ dbSNP | Ensembl ].
    VAR_059778
    Natural varianti322 – 3221P → L.
    Corresponds to variant rs35101549 [ dbSNP | Ensembl ].
    VAR_047368

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15932 mRNA. Translation: AAA64693.2.
    U16996 mRNA. Translation: AAB06261.1.
    AL355512 Genomic DNA. Translation: CAI15120.1.
    BC062545 mRNA. Translation: AAH62545.1.
    CCDSiCCDS7566.1.
    PIRiI38890.
    RefSeqiNP_004410.3. NM_004419.3.
    UniGeneiHs.2128.

    Genome annotation databases

    EnsembliENST00000369583; ENSP00000358596; ENSG00000138166.
    GeneIDi1847.
    KEGGihsa:1847.
    UCSCiuc001kzd.3. human.

    Polymorphism databases

    DMDMi215273975.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15932 mRNA. Translation: AAA64693.2 .
    U16996 mRNA. Translation: AAB06261.1 .
    AL355512 Genomic DNA. Translation: CAI15120.1 .
    BC062545 mRNA. Translation: AAH62545.1 .
    CCDSi CCDS7566.1.
    PIRi I38890.
    RefSeqi NP_004410.3. NM_004419.3.
    UniGenei Hs.2128.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G6Z X-ray 2.70 A/B/C 178-384 [» ]
    ProteinModelPortali Q16690.
    SMRi Q16690. Positions 22-140, 178-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108180. 3 interactions.
    IntActi Q16690. 1 interaction.
    MINTi MINT-8277166.
    STRINGi 9606.ENSP00000358596.

    Chemistry

    ChEMBLi CHEMBL1250380.

    PTM databases

    PhosphoSitei Q16690.

    Polymorphism databases

    DMDMi 215273975.

    Proteomic databases

    MaxQBi Q16690.
    PaxDbi Q16690.
    PRIDEi Q16690.

    Protocols and materials databases

    DNASUi 1847.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369583 ; ENSP00000358596 ; ENSG00000138166 .
    GeneIDi 1847.
    KEGGi hsa:1847.
    UCSCi uc001kzd.3. human.

    Organism-specific databases

    CTDi 1847.
    GeneCardsi GC10P112247.
    H-InvDB HIX0001673.
    HGNCi HGNC:3071. DUSP5.
    HPAi HPA055143.
    MIMi 603069. gene.
    neXtProti NX_Q16690.
    PharmGKBi PA27528.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOVERGENi HBG007347.
    InParanoidi Q16690.
    KOi K04459.
    OMAi SPVHQLK.
    OrthoDBi EOG75MVWD.
    PhylomeDBi Q16690.
    TreeFami TF105122.

    Enzyme and pathway databases

    SignaLinki Q16690.

    Miscellaneous databases

    ChiTaRSi DUSP5. human.
    EvolutionaryTracei Q16690.
    GeneWikii DUSP5.
    GenomeRNAii 1847.
    NextBioi 7565.
    PROi Q16690.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16690.
    CleanExi HS_DUSP5.
    Genevestigatori Q16690.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi 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 ]
    PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
    PRINTSi 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. "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
      Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
      J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary gland.
    2. Bottaro D.P.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines."
      Kwak S.P., Dixon J.E.
      J. Biol. Chem. 270:1156-1160(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      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: Lymph.
    6. "Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase."
      Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J.
      Proteins 66:253-258(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 178-384, ACTIVE SITE.

    Entry informationi

    Entry nameiDUS5_HUMAN
    AccessioniPrimary (citable) accession number: Q16690
    Secondary accession number(s): Q12997, Q5T603
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 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 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3