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Q16829

- DUS7_HUMAN

UniProt

Q16829 - DUS7_HUMAN

Protein

Dual specificity protein phosphatase 7

Gene

DUSP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 4 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Regulates the activity of the MAP kinase family in response to changes in the cellular environment. PYST2-S may act as a negative regulator of PYST2-L although it is unclear whether this is by competing for transcription, translation or activation factors.1 Publication

    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 sitei331 – 3311Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. inactivation of MAPK activity Source: GOC
    2. innate immune response Source: Reactome
    3. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    5. negative regulation of MAP kinase activity Source: UniProtKB
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    8. stress-activated MAPK cascade Source: Reactome
    9. toll-like receptor 10 signaling pathway Source: Reactome
    10. toll-like receptor 2 signaling pathway Source: Reactome
    11. toll-like receptor 3 signaling pathway Source: Reactome
    12. toll-like receptor 4 signaling pathway Source: Reactome
    13. toll-like receptor 5 signaling pathway Source: Reactome
    14. toll-like receptor 9 signaling pathway Source: Reactome
    15. toll-like receptor signaling pathway Source: Reactome
    16. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    17. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    18. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_12436. ERKs are inactivated.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 7 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity protein phosphatase PYST2
    Gene namesi
    Name:DUSP7
    Synonyms:PYST2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3073. DUSP7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27530.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Dual specificity protein phosphatase 7PRO_0000094807Add
    BLAST

    Proteomic databases

    MaxQBiQ16829.
    PaxDbiQ16829.
    PRIDEiQ16829.

    PTM databases

    PhosphoSiteiQ16829.

    Expressioni

    Tissue specificityi

    Expressed at significantly higher levels in malignant hematopoietic cells than in corresponding non-malignant cells.1 Publication

    Gene expression databases

    ArrayExpressiQ16829.
    BgeeiQ16829.
    CleanExiHS_DUSP7.
    GenevestigatoriQ16829.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GHRP109122EBI-1265847,EBI-286316

    Protein-protein interaction databases

    BioGridi108182. 4 interactions.
    IntActiQ16829. 4 interactions.
    STRINGi9606.ENSP00000296483.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16829.
    SMRiQ16829. Positions 55-193, 243-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 187120RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini308 – 37669Tyrosine-protein phosphataseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 24049Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000294079.
    HOVERGENiHBG007347.
    InParanoidiQ16829.
    KOiK04459.
    OMAiLRDDGCK.
    OrthoDBiEOG793B7W.
    PhylomeDBiQ16829.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: Q16829-1) [UniParc]FASTAAdd to Basket

    Also known as: PYST2-L

    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

    MKNQLRGPPA RAHMSTSGAA AAGGTRAGSE PGAGSGSGAG TGAGAATGAG    50
    AMPCKSAEWL QEELEARGGA SLLLLDCRPH ELFESSHIET AINLAIPGLM 100
    LRRLRKGNLP IRSIIPNHAD KERFATRCKA ATVLLYDEAT AEWQPEPGAP 150
    ASVLGLLLQK LRDDGCQAYY LQGGFNKFQT EYSEHCETNV DSSSSPSSSP 200
    PTSVLGLGGL RISSDCSDGE SDRELPSSAT ESDGSPVPSS QPAFPVQILP 250
    YLYLGCAKDS TNLDVLGKYG IKYILNVTPN LPNAFEHGGE FTYKQIPISD 300
    HWSQNLSQFF PEAISFIDEA RSKKCGVLVH CLAGISRSVT VTVAYLMQKM 350
    NLSLNDAYDF VKRKKSNISP NFNFMGQLLD FERTLGLSSP CDNHASSEQL 400
    YFSTPTNHNL FPLNTLEST 419
    Length:419
    Mass (Da):44,957
    Last modified:June 28, 2011 - v4
    Checksum:i434467AC16A3F8BA
    GO
    Isoform 2 (identifier: Q16829-2) [UniParc]FASTAAdd to Basket

    Also known as: PYST2-S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-51: Missing.

    Show »
    Length:368
    Mass (Da):40,551
    Checksum:i097023C27EBC341C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti235 – 2351S → N.
    Corresponds to variant rs34821455 [ dbSNP | Ensembl ].
    VAR_051752

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5151Missing in isoform 2. 1 PublicationVSP_012822Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF508727 mRNA. Translation: AAM77606.1.
    AF508728 mRNA. No translation available.
    AC115284 Genomic DNA. No translation available.
    AL556300 mRNA. No translation available.
    BC019107 mRNA. Translation: AAH19107.2.
    BC104880 mRNA. Translation: AAI04881.1.
    BC104882 mRNA. Translation: AAI04883.1.
    X93921 mRNA. Translation: CAA63814.1.
    CCDSiCCDS33766.2. [Q16829-1]
    RefSeqiNP_001938.2. NM_001947.3. [Q16829-1]
    UniGeneiHs.591664.

    Genome annotation databases

    EnsembliENST00000495880; ENSP00000417183; ENSG00000164086. [Q16829-1]
    GeneIDi1849.
    KEGGihsa:1849.
    UCSCiuc003dct.3. human. [Q16829-1]

    Polymorphism databases

    DMDMi338817906.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF508727 mRNA. Translation: AAM77606.1 .
    AF508728 mRNA. No translation available.
    AC115284 Genomic DNA. No translation available.
    AL556300 mRNA. No translation available.
    BC019107 mRNA. Translation: AAH19107.2 .
    BC104880 mRNA. Translation: AAI04881.1 .
    BC104882 mRNA. Translation: AAI04883.1 .
    X93921 mRNA. Translation: CAA63814.1 .
    CCDSi CCDS33766.2. [Q16829-1 ]
    RefSeqi NP_001938.2. NM_001947.3. [Q16829-1 ]
    UniGenei Hs.591664.

    3D structure databases

    ProteinModelPortali Q16829.
    SMRi Q16829. Positions 55-193, 243-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108182. 4 interactions.
    IntActi Q16829. 4 interactions.
    STRINGi 9606.ENSP00000296483.

    PTM databases

    PhosphoSitei Q16829.

    Polymorphism databases

    DMDMi 338817906.

    Proteomic databases

    MaxQBi Q16829.
    PaxDbi Q16829.
    PRIDEi Q16829.

    Protocols and materials databases

    DNASUi 1849.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000495880 ; ENSP00000417183 ; ENSG00000164086 . [Q16829-1 ]
    GeneIDi 1849.
    KEGGi hsa:1849.
    UCSCi uc003dct.3. human. [Q16829-1 ]

    Organism-specific databases

    CTDi 1849.
    GeneCardsi GC03M052082.
    H-InvDB HIX0003343.
    HGNCi HGNC:3073. DUSP7.
    MIMi 602749. gene.
    neXtProti NX_Q16829.
    PharmGKBi PA27530.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000294079.
    HOVERGENi HBG007347.
    InParanoidi Q16829.
    KOi K04459.
    OMAi LRDDGCK.
    OrthoDBi EOG793B7W.
    PhylomeDBi Q16829.
    TreeFami TF105122.

    Enzyme and pathway databases

    Reactomei REACT_12436. ERKs are inactivated.

    Miscellaneous databases

    GeneWikii DUSP7.
    GenomeRNAii 1849.
    NextBioi 7575.
    PROi Q16829.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16829.
    Bgeei Q16829.
    CleanExi HS_DUSP7.
    Genevestigatori Q16829.

    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. "Characterization of the dual-specificity phosphatase PYST2 and its transcripts."
      Levy-Nissenbaum O., Sagi-Assif O., Witz I.P.
      Genes Chromosomes Cancer 39:37-47(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE, FUNCTION.
      Tissue: Monocyte.
    2. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-235 (ISOFORM 1).
    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] OF 83-419 (ISOFORM 1).
      Tissue: Brain and Lymph.
    5. "Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase."
      Groom L.A., Sneddon A.A., Alessi D.R., Dowd S., Keyse S.M.
      EMBO J. 15:3621-3632(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-419 (ISOFORM 1).
      Tissue: Testis.
    6. "Dual-specificity phosphatase Pyst2-L is constitutively highly expressed in myeloid leukemia and other malignant cells."
      Levy-Nissenbaum O., Sagi-Assif O., Kapon D., Hantisteanu S., Burg T., Raanani P., Avigdor A., Ben-Bassat I., Witz I.P.
      Oncogene 22:7649-7660(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiDUS7_HUMAN
    AccessioniPrimary (citable) accession number: Q16829
    Secondary accession number(s): Q2M3J7, Q8NFJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 125 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

    Caution

    An out-of-frame translation product, PYST2SB, has been experimentally demonstrated to be formed from the alternative promoter. The expression of the in-frame product has not yet been shown.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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