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Q9H596

- DUS21_HUMAN

UniProt

Q9H596 - DUS21_HUMAN

Protein

Dual specificity protein phosphatase 21

Gene

DUSP21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine.

    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 sitei106 – 1061Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. peptidyl-tyrosine dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 21 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Low molecular weight dual specificity phosphatase 21
    Short name:
    LMW-DSP21
    Gene namesi
    Name:DUSP21
    Synonyms:LMWDSP21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:20476. DUSP21.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. integral component of mitochondrial inner membrane Source: Ensembl
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134967875.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190Dual specificity protein phosphatase 21PRO_0000094834Add
    BLAST

    Proteomic databases

    PaxDbiQ9H596.
    PRIDEiQ9H596.

    Expressioni

    Tissue specificityi

    Expressed in testis.1 Publication

    Gene expression databases

    BgeeiQ9H596.
    CleanExiHS_DUSP21.
    GenevestigatoriQ9H596.

    Interactioni

    Protein-protein interaction databases

    BioGridi121980. 2 interactions.
    IntActiQ9H596. 1 interaction.
    MINTiMINT-3068077.
    STRINGi9606.ENSP00000343244.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H596.
    SMRiQ9H596. Positions 22-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 161141Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 12886Sufficient for mitochondrial localizationBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000233766.
    HOVERGENiHBG051422.
    InParanoidiQ9H596.
    KOiK14165.
    OMAiFWEQLIN.
    OrthoDBiEOG7PK90H.
    PhylomeDBiQ9H596.
    TreeFamiTF316009.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR020420. Atypical_DUSP_famB.
    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.
    PR01910. ADSPHPHTASEB.
    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.

    Q9H596-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTASASSFSS SQGVQQPSIY SFSQITRSLF LSNGVAANDK LLLSSNRITA    50
    IVNASVEVVN VFFEGIQYIK VPVTDARDSR LYDFFDPIAD LIHTIDMRQG 100
    RTLLHCMAGV SRSASLCLAY LMKYHSMSLL DAHTWTKSRR PIIRPNNGFW 150
    EQLINYEFKL FNNNTVRMIN SPVGNIPDIY EKDLRMMISM 190
    Length:190
    Mass (Da):21,529
    Last modified:March 1, 2001 - v1
    Checksum:i3E52BA31A4944EE3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901M → I in CAG33440. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035644
    Natural varianti186 – 1861M → T.2 Publications
    Corresponds to variant rs1045031 [ dbSNP | Ensembl ].
    VAR_019423

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF533018 mRNA. Translation: AAN59788.1.
    AY156515 mRNA. Translation: AAO17295.1.
    CR457159 mRNA. Translation: CAG33440.1.
    AL133545 Genomic DNA. Translation: CAC10195.1.
    BC119755 mRNA. Translation: AAI19756.1.
    BC119756 mRNA. Translation: AAI19757.1.
    CCDSiCCDS14264.1.
    RefSeqiNP_071359.3. NM_022076.3.
    UniGeneiHs.534478.

    Genome annotation databases

    EnsembliENST00000339042; ENSP00000343244; ENSG00000189037.
    GeneIDi63904.
    KEGGihsa:63904.
    UCSCiuc004dgd.3. human.

    Polymorphism databases

    DMDMi50400652.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF533018 mRNA. Translation: AAN59788.1 .
    AY156515 mRNA. Translation: AAO17295.1 .
    CR457159 mRNA. Translation: CAG33440.1 .
    AL133545 Genomic DNA. Translation: CAC10195.1 .
    BC119755 mRNA. Translation: AAI19756.1 .
    BC119756 mRNA. Translation: AAI19757.1 .
    CCDSi CCDS14264.1.
    RefSeqi NP_071359.3. NM_022076.3.
    UniGenei Hs.534478.

    3D structure databases

    ProteinModelPortali Q9H596.
    SMRi Q9H596. Positions 22-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121980. 2 interactions.
    IntActi Q9H596. 1 interaction.
    MINTi MINT-3068077.
    STRINGi 9606.ENSP00000343244.

    Polymorphism databases

    DMDMi 50400652.

    Proteomic databases

    PaxDbi Q9H596.
    PRIDEi Q9H596.

    Protocols and materials databases

    DNASUi 63904.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339042 ; ENSP00000343244 ; ENSG00000189037 .
    GeneIDi 63904.
    KEGGi hsa:63904.
    UCSCi uc004dgd.3. human.

    Organism-specific databases

    CTDi 63904.
    GeneCardsi GC0XP044703.
    HGNCi HGNC:20476. DUSP21.
    MIMi 300678. gene.
    neXtProti NX_Q9H596.
    PharmGKBi PA134967875.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000233766.
    HOVERGENi HBG051422.
    InParanoidi Q9H596.
    KOi K14165.
    OMAi FWEQLIN.
    OrthoDBi EOG7PK90H.
    PhylomeDBi Q9H596.
    TreeFami TF316009.

    Miscellaneous databases

    GenomeRNAii 63904.
    NextBioi 65608.
    PROi Q9H596.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H596.
    CleanExi HS_DUSP21.
    Genevestigatori Q9H596.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR020420. Atypical_DUSP_famB.
    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.
    PR01910. ADSPHPHTASEB.
    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. "Identification and characterization of two novel low-molecular-weight dual specificity phosphatases."
      Hood K.L., Tobin J.F., Yoon C.
      Biochem. Biophys. Res. Commun. 298:545-551(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Cloning and characterization of a new DUSP homolog gene."
      Mao Y., Xie Y., Dai J.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-186.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-186.
    4. "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].
    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].
    6. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-167.

    Entry informationi

    Entry nameiDUS21_HUMAN
    AccessioniPrimary (citable) accession number: Q9H596
    Secondary accession number(s): Q0VDA6, Q6IAJ6, Q6YDQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 107 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3