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Q9UNI6

- DUS12_HUMAN

UniProt

Q9UNI6 - DUS12_HUMAN

Protein

Dual specificity protein phosphatase 12

Gene

DUSP12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei115 – 1151Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    2. protein tyrosine phosphatase activity Source: ProtInc
    3. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. peptidyl-tyrosine dephosphorylation Source: GOC
    3. positive regulation of glucokinase activity Source: RefGenome
    4. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 12 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity tyrosine phosphatase YVH1
    Gene namesi
    Name:DUSP12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3067. DUSP12.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27522.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Dual specificity protein phosphatase 12PRO_0000094818Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UNI6.
    PaxDbiQ9UNI6.
    PeptideAtlasiQ9UNI6.
    PRIDEiQ9UNI6.

    PTM databases

    PhosphoSiteiQ9UNI6.

    Expressioni

    Tissue specificityi

    Ubiquitous, highest expression in spleen, testis, ovary, and peripheral blood leukocytes and lower expression in liver and lung.

    Gene expression databases

    BgeeiQ9UNI6.
    CleanExiHS_DUSP12.
    GenevestigatoriQ9UNI6.

    Organism-specific databases

    HPAiHPA008840.

    Interactioni

    Protein-protein interaction databases

    BioGridi116424. 7 interactions.
    IntActiQ9UNI6. 7 interactions.
    MINTiMINT-1415234.
    STRINGi9606.ENSP00000356920.

    Structurei

    Secondary structure

    1
    340
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 314
    Beta strandi34 – 374
    Helixi39 – 435
    Helixi45 – 517
    Beta strandi53 – 6210
    Beta strandi76 – 816
    Helixi91 – 933
    Helixi94 – 10613
    Beta strandi110 – 1145
    Beta strandi116 – 1205
    Helixi121 – 13414
    Helixi138 – 14811
    Helixi156 – 16712
    Helixi177 – 18610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JNBX-ray3.00A27-193[»]
    4KI9X-ray2.00A27-189[»]
    ProteinModelPortaliQ9UNI6.
    SMRiQ9UNI6. Positions 27-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini88 – 16073Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000243638.
    HOVERGENiHBG051421.
    InParanoidiQ9UNI6.
    KOiK14819.
    OMAiKITHILT.
    OrthoDBiEOG7Z95MG.
    PhylomeDBiQ9UNI6.
    TreeFamiTF105123.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR016278. DUSP12.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR007087. Znf_C2H2.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000941. DUSP12. 1 hit.
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UNI6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEAPGPSDG CELSNPSASR VSCAGQMLEV QPGLYFGGAA AVAEPDHLRE    50
    AGITAVLTVD SEEPSFKAGP GVEDLWRLFV PALDKPETDL LSHLDRCVAF 100
    IGQARAEGRA VLVHCHAGVS RSVAIITAFL MKTDQLPFEK AYEKLQILKP 150
    EAKMNEGFEW QLKLYQAMGY EVDTSSAIYK QYRLQKVTEK YPELQNLPQE 200
    LFAVDPTTVS QGLKDEVLYK CRKCRRSLFR SSSILDHREG SGPIAFAHKR 250
    MTPSSMLTTG RQAQCTSYFI EPVQWMESAL LGVMDGQLLC PKCSAKLGSF 300
    NWYGEQCSCG RWITPAFQIH KNRVDEMKIL PVLGSQTGKI 340
    Length:340
    Mass (Da):37,687
    Last modified:May 1, 2000 - v1
    Checksum:i56B52192B42C73EB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511A → E.
    Corresponds to variant rs35106830 [ dbSNP | Ensembl ].
    VAR_033899

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119226 mRNA. Translation: AAD51134.1.
    BT006633 mRNA. Translation: AAP35279.1.
    AL359541 Genomic DNA. Translation: CAH74153.1.
    BC006286 mRNA. Translation: AAH06286.1.
    CCDSiCCDS1234.1.
    RefSeqiNP_009171.1. NM_007240.1.
    UniGeneiHs.416216.

    Genome annotation databases

    EnsembliENST00000367943; ENSP00000356920; ENSG00000081721.
    GeneIDi11266.
    KEGGihsa:11266.
    UCSCiuc001gbo.3. human.

    Polymorphism databases

    DMDMi9973073.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119226 mRNA. Translation: AAD51134.1 .
    BT006633 mRNA. Translation: AAP35279.1 .
    AL359541 Genomic DNA. Translation: CAH74153.1 .
    BC006286 mRNA. Translation: AAH06286.1 .
    CCDSi CCDS1234.1.
    RefSeqi NP_009171.1. NM_007240.1.
    UniGenei Hs.416216.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JNB X-ray 3.00 A 27-193 [» ]
    4KI9 X-ray 2.00 A 27-189 [» ]
    ProteinModelPortali Q9UNI6.
    SMRi Q9UNI6. Positions 27-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116424. 7 interactions.
    IntActi Q9UNI6. 7 interactions.
    MINTi MINT-1415234.
    STRINGi 9606.ENSP00000356920.

    PTM databases

    PhosphoSitei Q9UNI6.

    Polymorphism databases

    DMDMi 9973073.

    Proteomic databases

    MaxQBi Q9UNI6.
    PaxDbi Q9UNI6.
    PeptideAtlasi Q9UNI6.
    PRIDEi Q9UNI6.

    Protocols and materials databases

    DNASUi 11266.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367943 ; ENSP00000356920 ; ENSG00000081721 .
    GeneIDi 11266.
    KEGGi hsa:11266.
    UCSCi uc001gbo.3. human.

    Organism-specific databases

    CTDi 11266.
    GeneCardsi GC01P161719.
    HGNCi HGNC:3067. DUSP12.
    HPAi HPA008840.
    MIMi 604835. gene.
    neXtProti NX_Q9UNI6.
    PharmGKBi PA27522.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000243638.
    HOVERGENi HBG051421.
    InParanoidi Q9UNI6.
    KOi K14819.
    OMAi KITHILT.
    OrthoDBi EOG7Z95MG.
    PhylomeDBi Q9UNI6.
    TreeFami TF105123.

    Miscellaneous databases

    GeneWikii DUSP12.
    GenomeRNAii 11266.
    NextBioi 42871.
    PROi Q9UNI6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UNI6.
    CleanExi HS_DUSP12.
    Genevestigatori Q9UNI6.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR016278. DUSP12.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR007087. Znf_C2H2.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000941. DUSP12. 1 hit.
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the human YVH1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function."
      Muda M., Manning E.R., Orth K., Dixon J.E.
      J. Biol. Chem. 274:23991-23995(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Placenta.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDUS12_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNI6
    Secondary accession number(s): Q5VXA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 131 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 1
      Human chromosome 1: 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