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Q99956

- DUS9_HUMAN

UniProt

Q99956 - DUS9_HUMAN

Protein

Dual specificity protein phosphatase 9

Gene

DUSP9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Inactivates MAP kinases. Has a specificity for the ERK family.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei290 – 2901Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. inactivation of MAPK activity Source: ProtInc
    2. JNK cascade Source: ProtInc
    3. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BRENDAi3.1.3.48. 2681.
    SignaLinkiQ99956.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 9 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Mitogen-activated protein kinase phosphatase 4
    Short name:
    MAP kinase phosphatase 4
    Short name:
    MKP-4
    Gene namesi
    Name:DUSP9
    Synonyms:MKP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3076. DUSP9.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27533.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384Dual specificity protein phosphatase 9PRO_0000094812Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei351 – 3511Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99956.
    PaxDbiQ99956.
    PRIDEiQ99956.

    PTM databases

    PhosphoSiteiQ99956.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99956.
    BgeeiQ99956.
    CleanExiHS_DUSP9.
    GenevestigatoriQ99956.

    Organism-specific databases

    HPAiHPA003336.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK14Q165393EBI-3906678,EBI-73946
    Mapk14P478112EBI-3906678,EBI-298727From a different organism.

    Protein-protein interaction databases

    BioGridi108185. 7 interactions.
    IntActiQ99956. 9 interactions.
    STRINGi9606.ENSP00000345853.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi205 – 2084
    Beta strandi211 – 2144
    Helixi218 – 2203
    Helixi222 – 2276
    Beta strandi230 – 2356
    Beta strandi237 – 2393
    Turni243 – 2464
    Beta strandi251 – 2544
    Helixi259 – 2646
    Helixi265 – 28117
    Beta strandi285 – 2895
    Beta strandi291 – 2955
    Helixi296 – 30914
    Helixi313 – 32311
    Helixi331 – 34414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HXPX-ray1.83A201-345[»]
    3LJ8X-ray2.70A202-347[»]
    ProteinModelPortaliQ99956.
    SMRiQ99956. Positions 3-144, 202-347.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99956.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 139122RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini203 – 384182Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000294079.
    HOVERGENiHBG007347.
    InParanoidiQ99956.
    KOiK04459.
    OMAiEPDRDSM.
    PhylomeDBiQ99956.
    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.
    [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.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99956-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGLGRSCLW LRRELSPPRP RLLLLDCRSR ELYESARIGG ALSVALPALL    50
    LRRLRRGSLS VRALLPGPPL QPPPPAPVLL YDQGGGRRRR GEAEAEAEEW 100
    EAESVLGTLL QKLREEGYLA YYLQGGFSRF QAECPHLCET SLAGRAGSSM 150
    APVPGPVPVV GLGSLCLGSD CSDAESEADR DSMSCGLDSE GATPPPVGLR 200
    ASFPVQILPN LYLGSARDSA NLESLAKLGI RYILNVTPNL PNFFEKNGDF 250
    HYKQIPISDH WSQNLSRFFP EAIEFIDEAL SQNCGVLVHC LAGVSRSVTV 300
    TVAYLMQKLH LSLNDAYDLV KRKKSNISPN FNFMGQLLDF ERSLRLEERH 350
    SQEQGSGGQA SAASNPPSFF TTPTSDGAFE LAPT 384
    Length:384
    Mass (Da):41,868
    Last modified:May 1, 1997 - v1
    Checksum:iF8598CA95AB379B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08302 mRNA. Translation: CAA69610.1.
    U52111 Genomic DNA. No translation available.
    CH471172 Genomic DNA. Translation: EAW72847.1.
    CH471172 Genomic DNA. Translation: EAW72848.1.
    CH471172 Genomic DNA. Translation: EAW72849.1.
    CCDSiCCDS14724.1.
    RefSeqiNP_001386.1. NM_001395.3.
    XP_005274712.1. XM_005274655.2.
    UniGeneiHs.144879.
    Hs.744909.

    Genome annotation databases

    EnsembliENST00000342782; ENSP00000345853; ENSG00000130829.
    ENST00000370167; ENSP00000359186; ENSG00000130829.
    GeneIDi1852.
    KEGGihsa:1852.
    UCSCiuc004fhx.4. human.

    Polymorphism databases

    DMDMi3913541.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08302 mRNA. Translation: CAA69610.1 .
    U52111 Genomic DNA. No translation available.
    CH471172 Genomic DNA. Translation: EAW72847.1 .
    CH471172 Genomic DNA. Translation: EAW72848.1 .
    CH471172 Genomic DNA. Translation: EAW72849.1 .
    CCDSi CCDS14724.1.
    RefSeqi NP_001386.1. NM_001395.3.
    XP_005274712.1. XM_005274655.2.
    UniGenei Hs.144879.
    Hs.744909.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HXP X-ray 1.83 A 201-345 [» ]
    3LJ8 X-ray 2.70 A 202-347 [» ]
    ProteinModelPortali Q99956.
    SMRi Q99956. Positions 3-144, 202-347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108185. 7 interactions.
    IntActi Q99956. 9 interactions.
    STRINGi 9606.ENSP00000345853.

    PTM databases

    PhosphoSitei Q99956.

    Polymorphism databases

    DMDMi 3913541.

    Proteomic databases

    MaxQBi Q99956.
    PaxDbi Q99956.
    PRIDEi Q99956.

    Protocols and materials databases

    DNASUi 1852.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342782 ; ENSP00000345853 ; ENSG00000130829 .
    ENST00000370167 ; ENSP00000359186 ; ENSG00000130829 .
    GeneIDi 1852.
    KEGGi hsa:1852.
    UCSCi uc004fhx.4. human.

    Organism-specific databases

    CTDi 1852.
    GeneCardsi GC0XP152907.
    HGNCi HGNC:3076. DUSP9.
    HPAi HPA003336.
    MIMi 300134. gene.
    neXtProti NX_Q99956.
    PharmGKBi PA27533.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000294079.
    HOVERGENi HBG007347.
    InParanoidi Q99956.
    KOi K04459.
    OMAi EPDRDSM.
    PhylomeDBi Q99956.
    TreeFami TF105122.

    Enzyme and pathway databases

    BRENDAi 3.1.3.48. 2681.
    SignaLinki Q99956.

    Miscellaneous databases

    EvolutionaryTracei Q99956.
    GenomeRNAii 1852.
    NextBioi 7585.
    PROi Q99956.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99956.
    Bgeei Q99956.
    CleanExi HS_DUSP9.
    Genevestigatori Q99956.

    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.
    [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.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4."
      Muda M., Boschert U., Smith A., Antonsonn B., Gillieron C., Chabert C., Camps M., Martinou I., Ashworth A., Arkinstall S.
      J. Biol. Chem. 272:5141-5151(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 201-345.

    Entry informationi

    Entry nameiDUS9_HUMAN
    AccessioniPrimary (citable) accession number: Q99956
    Secondary accession number(s): D3DWU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 129 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 X
      Human chromosome X: 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