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Q9D0T2

- DUS12_MOUSE

UniProt

Q9D0T2 - DUS12_MOUSE

Protein

Dual specificity protein phosphatase 12

Gene

Dusp12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei114 – 1141Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
    3. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. positive regulation of glucokinase activity Source: Ensembl

    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 phosphatase T-DSP4
    Dual specificity phosphatase VH1
    Gene namesi
    Name:Dusp12
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1890614. Dusp12.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Dual specificity protein phosphatase 12PRO_0000094819Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9D0T2.
    PRIDEiQ9D0T2.

    PTM databases

    PhosphoSiteiQ9D0T2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D0T2.
    BgeeiQ9D0T2.
    CleanExiMM_DUSP12.
    GenevestigatoriQ9D0T2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D0T2.
    SMRiQ9D0T2. Positions 28-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini87 – 16175Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00740000115610.
    HOGENOMiHOG000243638.
    HOVERGENiHBG051421.
    InParanoidiQ9D0T2.
    KOiK14819.
    OMAiKITHILT.
    PhylomeDBiQ9D0T2.
    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.
    [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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9D0T2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEAQGSNHG CERQAPTASP ASSAGHAVEV RPGLYLGGAA AVAEPGHLRE    50
    AGITAVLTVD SEPAFPAGAG FEGLRSLFVP ALDKPETDLL SHLDRCVAFI 100
    GQARSEGRAV LVHCHAGVSR SVAVVMAFIM KTDQLTFEKA YDILRTVKPE 150
    AKVNEGFEWQ LKLYEAMGYE VDTSSAFYKQ YRLQKVTEKC PKLWNLPQEL 200
    FAVDPTTISQ GLKDDILYKC RKCRRSLFRH SSILGHSEGS GPIAFAHKRT 250
    APSSVLTTGS QAQCTSYFIE PVQWMESTLL GVMDGQLLCP KCSAKLGSFN 300
    WYGEQCSCGR WITPAFQIHK NRVDEMKMLP VLGSQTKKL 339
    Length:339
    Mass (Da):37,159
    Last modified:June 1, 2001 - v1
    Checksum:iB6A254D319BEC98F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71S → T in AAG44739. (PubMed:11130991)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF280810 mRNA. Translation: AAK69508.1.
    AF268196 mRNA. Translation: AAG44739.1.
    AK004488 mRNA. Translation: BAB23328.1.
    CCDSiCCDS15474.1.
    RefSeqiNP_075662.2. NM_023173.2.
    UniGeneiMm.34365.

    Genome annotation databases

    EnsembliENSMUST00000027970; ENSMUSP00000027970; ENSMUSG00000026659.
    GeneIDi80915.
    KEGGimmu:80915.
    UCSCiuc007dml.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF280810 mRNA. Translation: AAK69508.1 .
    AF268196 mRNA. Translation: AAG44739.1 .
    AK004488 mRNA. Translation: BAB23328.1 .
    CCDSi CCDS15474.1.
    RefSeqi NP_075662.2. NM_023173.2.
    UniGenei Mm.34365.

    3D structure databases

    ProteinModelPortali Q9D0T2.
    SMRi Q9D0T2. Positions 28-185.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9D0T2.

    Proteomic databases

    PaxDbi Q9D0T2.
    PRIDEi Q9D0T2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027970 ; ENSMUSP00000027970 ; ENSMUSG00000026659 .
    GeneIDi 80915.
    KEGGi mmu:80915.
    UCSCi uc007dml.1. mouse.

    Organism-specific databases

    CTDi 11266.
    MGIi MGI:1890614. Dusp12.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00740000115610.
    HOGENOMi HOG000243638.
    HOVERGENi HBG051421.
    InParanoidi Q9D0T2.
    KOi K14819.
    OMAi KITHILT.
    PhylomeDBi Q9D0T2.
    TreeFami TF105123.

    Miscellaneous databases

    NextBioi 350298.
    PROi Q9D0T2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D0T2.
    Bgeei Q9D0T2.
    CleanExi MM_DUSP12.
    Genevestigatori Q9D0T2.

    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.
    [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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of putative dual specificity phosphatase T-DSP4."
      Aoyama K., Matsuda T., Aoki N.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "mVH1, a dual-specificity phosphatase whose expression is cell cycle regulated."
      Zhang X.M., Dormady S.P., Chaung W., Basch R.S.
      Mamm. Genome 11:1154-1156(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.

    Entry informationi

    Entry nameiDUS12_MOUSE
    AccessioniPrimary (citable) accession number: Q9D0T2
    Secondary accession number(s): Q9EQD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3