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Q8K2Q2

- GSTO2_MOUSE

UniProt

Q8K2Q2 - GSTO2_MOUSE

Protein

Glutathione S-transferase omega-2

Gene

Gsto2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) By similarity.By similarity

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.
    2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
    Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei32 – 321NucleophileBy similarity
    Binding sitei59 – 591GlutathioneBy similarity
    Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. glutathione dehydrogenase (ascorbate) activity Source: UniProtKB
    2. glutathione transferase activity Source: UniProtKB-EC
    3. methylarsonate reductase activity Source: UniProtKB-EC
    4. oxidoreductase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to arsenic-containing substance Source: UniProtKB
    2. L-ascorbic acid metabolic process Source: UniProtKB
    3. oxidation-reduction process Source: UniProtKB
    4. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_215258. Vitamin C (ascorbate) metabolism.
    REACT_215316. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase omega-2 (EC:2.5.1.18)
    Short name:
    GSTO-2
    Alternative name(s):
    Glutathione S-transferase omega 2-2
    Short name:
    GSTO 2-2
    Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
    Monomethylarsonic acid reductase (EC:1.20.4.2)
    Short name:
    MMA(V) reductase
    Gene namesi
    Name:Gsto2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1915464. Gsto2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Glutathione S-transferase omega-2PRO_0000239141Add
    BLAST

    Proteomic databases

    PaxDbiQ8K2Q2.
    PRIDEiQ8K2Q2.

    PTM databases

    PhosphoSiteiQ8K2Q2.

    Expressioni

    Gene expression databases

    BgeeiQ8K2Q2.
    CleanExiMM_GSTO2.
    GenevestigatoriQ8K2Q2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K2Q2.
    SMRiQ8K2Q2. Positions 7-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10180GST N-terminalAdd
    BLAST
    Domaini106 – 231126GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 862Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. Omega family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    GeneTreeiENSGT00390000005479.
    HOGENOMiHOG000006560.
    HOVERGENiHBG051853.
    InParanoidiQ8K2Q2.
    KOiK00799.
    OMAiFCNLEEI.
    OrthoDBiEOG71CFNG.
    PhylomeDBiQ8K2Q2.
    TreeFamiTF105325.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR005442. GST_omega.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF13417. GST_N_3. 1 hit.
    [Graphical view]
    PRINTSiPR01625. GSTRNSFRASEO.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8K2Q2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGDLSRCLG KGSCPPGPVP EGVIRIYSMR FCPYSHRARL VLKAKGIRHE    50
    VININLKSKP DWYYTKHPFG QIPVLENSQC QLVYESVIAC EYLDDVYPGR 100
    KLFPYDPYER ARQKMLLELF CKVPPLSKEC LIALRCGRDC TDLKVALRQE 150
    LCNMEEILEY QNTTFFGGDC ISMIDYLVWP WFERLDVYGL ADCVNHTPML 200
    RLWIASMKQD PAVCALHTDK SVFLGFLNLY FQNNPCAFDF GLCNPIIR 248
    Length:248
    Mass (Da):28,599
    Last modified:October 1, 2002 - v1
    Checksum:iADB9FCFCA9F0FE48
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK077086 mRNA. Translation: BAC36604.1.
    BC030371 mRNA. Translation: AAH30371.1.
    CCDSiCCDS29894.1.
    RefSeqiNP_080895.2. NM_026619.2.
    NP_084327.1. NM_030051.1.
    UniGeneiMm.63791.

    Genome annotation databases

    EnsembliENSMUST00000056159; ENSMUSP00000052592; ENSMUSG00000025069.
    ENSMUST00000120645; ENSMUSP00000113409; ENSMUSG00000025069.
    GeneIDi68214.
    KEGGimmu:68214.
    UCSCiuc008hvs.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK077086 mRNA. Translation: BAC36604.1 .
    BC030371 mRNA. Translation: AAH30371.1 .
    CCDSi CCDS29894.1.
    RefSeqi NP_080895.2. NM_026619.2.
    NP_084327.1. NM_030051.1.
    UniGenei Mm.63791.

    3D structure databases

    ProteinModelPortali Q8K2Q2.
    SMRi Q8K2Q2. Positions 7-239.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8K2Q2.

    Proteomic databases

    PaxDbi Q8K2Q2.
    PRIDEi Q8K2Q2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056159 ; ENSMUSP00000052592 ; ENSMUSG00000025069 .
    ENSMUST00000120645 ; ENSMUSP00000113409 ; ENSMUSG00000025069 .
    GeneIDi 68214.
    KEGGi mmu:68214.
    UCSCi uc008hvs.1. mouse.

    Organism-specific databases

    CTDi 119391.
    MGIi MGI:1915464. Gsto2.

    Phylogenomic databases

    eggNOGi COG0625.
    GeneTreei ENSGT00390000005479.
    HOGENOMi HOG000006560.
    HOVERGENi HBG051853.
    InParanoidi Q8K2Q2.
    KOi K00799.
    OMAi FCNLEEI.
    OrthoDBi EOG71CFNG.
    PhylomeDBi Q8K2Q2.
    TreeFami TF105325.

    Enzyme and pathway databases

    Reactomei REACT_215258. Vitamin C (ascorbate) metabolism.
    REACT_215316. Glutathione conjugation.

    Miscellaneous databases

    NextBioi 326722.
    PROi Q8K2Q2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8K2Q2.
    CleanExi MM_GSTO2.
    Genevestigatori Q8K2Q2.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR005442. GST_omega.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    PRINTSi PR01625. GSTRNSFRASEO.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Testis.
    2. "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].
      Strain: FVB/N-3.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiGSTO2_MOUSE
    AccessioniPrimary (citable) accession number: Q8K2Q2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 90 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