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Q9H4Y5

- GSTO2_HUMAN

UniProt

Q9H4Y5 - GSTO2_HUMAN

Protein

Glutathione S-transferase omega-2

Gene

GSTO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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).1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei32 – 321Nucleophile
    Binding sitei59 – 591Glutathione1 Publication
    Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    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. glutathione derivative biosynthetic process Source: Reactome
    3. L-ascorbic acid metabolic process Source: UniProtKB
    4. oxidation-reduction process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. vitamin metabolic process Source: Reactome
    7. water-soluble vitamin metabolic process Source: Reactome
    8. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 2681.
    ReactomeiREACT_11202. Vitamin C (ascorbate) metabolism.
    REACT_6926. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23064. GSTO2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341Y → A: Abolishes DHAR activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA133787053.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 243243Glutathione S-transferase omega-2PRO_0000185888Add
    BLAST

    Proteomic databases

    PaxDbiQ9H4Y5.
    PRIDEiQ9H4Y5.

    PTM databases

    PhosphoSiteiQ9H4Y5.

    Expressioni

    Tissue specificityi

    Expressed in a range of tissues, including the liver, kidney, skeletal muscle and prostate. Strongest expression in the testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9H4Y5.
    BgeeiQ9H4Y5.
    CleanExiHS_GSTO2.
    GenevestigatoriQ9H4Y5.

    Organism-specific databases

    HPAiHPA048141.

    Interactioni

    Protein-protein interaction databases

    BioGridi125638. 1 interaction.
    STRINGi9606.ENSP00000345023.

    Structurei

    Secondary structure

    1
    243
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 285
    Helixi33 – 4412
    Beta strandi49 – 546
    Beta strandi56 – 583
    Helixi61 – 655
    Beta strandi74 – 763
    Beta strandi82 – 854
    Helixi86 – 9611
    Helixi107 – 11913
    Turni120 – 1223
    Helixi123 – 13614
    Helixi141 – 16121
    Beta strandi168 – 1703
    Helixi173 – 18311
    Helixi185 – 1884
    Helixi191 – 1944
    Helixi198 – 20811
    Helixi211 – 2166
    Helixi220 – 23112
    Helixi235 – 2384

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q18X-ray1.70A/B1-239[»]
    3Q19X-ray1.90A/B1-239[»]
    3QAGX-ray2.00A1-239[»]
    ProteinModelPortaliQ9H4Y5.
    SMRiQ9H4Y5. Positions 4-239.
    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 binding

    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.
    HOGENOMiHOG000006560.
    HOVERGENiHBG051853.
    InParanoidiQ9H4Y5.
    KOiK00799.
    OMAiFCNLEEI.
    OrthoDBiEOG71CFNG.
    PhylomeDBiQ9H4Y5.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H4Y5-1) [UniParc]FASTAAdd to Basket

    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

    MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE    50
    VVNINLRNKP EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR 100
    KLFPYDPYER ARQKMLLELF CKVPHLTKEC LVALRCGREC TNLKAALRQE 150
    FSNLEEILEY QNTTFFGGTC ISMIDYLLWP WFERLDVYGI LDCVSHTPAL 200
    RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF GLC 243
    Length:243
    Mass (Da):28,254
    Last modified:March 1, 2001 - v1
    Checksum:i45A959432BCF490A
    GO
    Isoform 2 (identifier: Q9H4Y5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         123-156: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:209
    Mass (Da):24,399
    Checksum:i4FEFB66449685934
    GO
    Isoform 3 (identifier: Q9H4Y5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-28: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:215
    Mass (Da):25,387
    Checksum:iA04CD756F6EB962F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151A → V in AAP47743. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti130 – 1301C → Y.
    Corresponds to variant rs45582439 [ dbSNP | Ensembl ].
    VAR_049492
    Natural varianti142 – 1421N → D.1 Publication
    Corresponds to variant rs156697 [ dbSNP | Ensembl ].
    VAR_016812

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 3. 1 PublicationVSP_045267Add
    BLAST
    Alternative sequencei123 – 15634Missing in isoform 2. 1 PublicationVSP_042567Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY350731 mRNA. Translation: AAR02452.1.
    AY209189 mRNA. Translation: AAP47743.1.
    AK291886 mRNA. Translation: BAF84575.1.
    AK296266 mRNA. Translation: BAG58978.1.
    AL139341 Genomic DNA. No translation available.
    AL162742 Genomic DNA. Translation: CAC16040.1.
    AL162742 Genomic DNA. Translation: CAI12107.1.
    CH471066 Genomic DNA. Translation: EAW49600.1.
    BC046194 mRNA. No translation available.
    BC056918 mRNA. Translation: AAH56918.1.
    AY191318 mRNA. Translation: AAO23573.1.
    CCDSiCCDS53574.1. [Q9H4Y5-2]
    CCDS53575.1. [Q9H4Y5-3]
    CCDS7556.1. [Q9H4Y5-1]
    RefSeqiNP_001177942.1. NM_001191013.1. [Q9H4Y5-2]
    NP_001177943.1. NM_001191014.1. [Q9H4Y5-3]
    NP_001177944.1. NM_001191015.1.
    NP_899062.1. NM_183239.1. [Q9H4Y5-1]
    XP_006717686.1. XM_006717623.1. [Q9H4Y5-1]
    UniGeneiHs.107384.
    Hs.203634.

    Genome annotation databases

    EnsembliENST00000338595; ENSP00000345023; ENSG00000065621. [Q9H4Y5-1]
    ENST00000369707; ENSP00000358721; ENSG00000065621. [Q9H4Y5-3]
    ENST00000450629; ENSP00000390986; ENSG00000065621. [Q9H4Y5-2]
    GeneIDi119391.
    KEGGihsa:119391.
    UCSCiuc001kyb.3. human. [Q9H4Y5-1]
    uc010qqx.2. human. [Q9H4Y5-2]

    Polymorphism databases

    DMDMi34922124.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY350731 mRNA. Translation: AAR02452.1 .
    AY209189 mRNA. Translation: AAP47743.1 .
    AK291886 mRNA. Translation: BAF84575.1 .
    AK296266 mRNA. Translation: BAG58978.1 .
    AL139341 Genomic DNA. No translation available.
    AL162742 Genomic DNA. Translation: CAC16040.1 .
    AL162742 Genomic DNA. Translation: CAI12107.1 .
    CH471066 Genomic DNA. Translation: EAW49600.1 .
    BC046194 mRNA. No translation available.
    BC056918 mRNA. Translation: AAH56918.1 .
    AY191318 mRNA. Translation: AAO23573.1 .
    CCDSi CCDS53574.1. [Q9H4Y5-2 ]
    CCDS53575.1. [Q9H4Y5-3 ]
    CCDS7556.1. [Q9H4Y5-1 ]
    RefSeqi NP_001177942.1. NM_001191013.1. [Q9H4Y5-2 ]
    NP_001177943.1. NM_001191014.1. [Q9H4Y5-3 ]
    NP_001177944.1. NM_001191015.1.
    NP_899062.1. NM_183239.1. [Q9H4Y5-1 ]
    XP_006717686.1. XM_006717623.1. [Q9H4Y5-1 ]
    UniGenei Hs.107384.
    Hs.203634.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3Q18 X-ray 1.70 A/B 1-239 [» ]
    3Q19 X-ray 1.90 A/B 1-239 [» ]
    3QAG X-ray 2.00 A 1-239 [» ]
    ProteinModelPortali Q9H4Y5.
    SMRi Q9H4Y5. Positions 4-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125638. 1 interaction.
    STRINGi 9606.ENSP00000345023.

    Chemistry

    ChEMBLi CHEMBL2161.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei Q9H4Y5.

    Polymorphism databases

    DMDMi 34922124.

    Proteomic databases

    PaxDbi Q9H4Y5.
    PRIDEi Q9H4Y5.

    Protocols and materials databases

    DNASUi 119391.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338595 ; ENSP00000345023 ; ENSG00000065621 . [Q9H4Y5-1 ]
    ENST00000369707 ; ENSP00000358721 ; ENSG00000065621 . [Q9H4Y5-3 ]
    ENST00000450629 ; ENSP00000390986 ; ENSG00000065621 . [Q9H4Y5-2 ]
    GeneIDi 119391.
    KEGGi hsa:119391.
    UCSCi uc001kyb.3. human. [Q9H4Y5-1 ]
    uc010qqx.2. human. [Q9H4Y5-2 ]

    Organism-specific databases

    CTDi 119391.
    GeneCardsi GC10P106018.
    HGNCi HGNC:23064. GSTO2.
    HPAi HPA048141.
    MIMi 612314. gene.
    neXtProti NX_Q9H4Y5.
    PharmGKBi PA133787053.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000006560.
    HOVERGENi HBG051853.
    InParanoidi Q9H4Y5.
    KOi K00799.
    OMAi FCNLEEI.
    OrthoDBi EOG71CFNG.
    PhylomeDBi Q9H4Y5.
    TreeFami TF105325.

    Enzyme and pathway databases

    BRENDAi 2.5.1.18. 2681.
    Reactomei REACT_11202. Vitamin C (ascorbate) metabolism.
    REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    GeneWikii GSTO2.
    GenomeRNAii 119391.
    NextBioi 80409.
    PROi Q9H4Y5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H4Y5.
    Bgeei Q9H4Y5.
    CleanExi HS_GSTO2.
    Genevestigatori Q9H4Y5.

    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. "Cloning and characterization of human GSTO-2 gene."
      Wang L., Xie Y., Mao Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Xu J., Xie Y., Mao Y.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Skeletal muscle and Thalamus.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 3).
      Tissue: Brain and Pancreatic carcinoma.
    7. "Characterization of the human Omega class glutathione transferase genes and associated polymorphisms."
      Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.
      Pharmacogenetics 13:131-144(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-243 (ISOFORM 1), VARIANT ASP-142, TISSUE SPECIFICITY.
      Tissue: Testis.
    8. "Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimer's and Parkinson's diseases."
      Schmuck E.M., Board P.G., Whitbread A.K., Tetlow N., Cavanaugh J.A., Blackburn A.C., Masoumi A.
      Pharmacogenet. Genomics 15:493-501(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
    9. "Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases."
      Zhou H., Brock J., Liu D., Board P.G., Oakley A.J.
      J. Mol. Biol. 420:190-203(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-239 ALONE AND IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-34.

    Entry informationi

    Entry nameiGSTO2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H4Y5
    Secondary accession number(s): A8K771
    , B4DJW6, E7ESD6, Q49TW5, Q5GM70, Q5JU15, Q86WP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 117 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 10
      Human chromosome 10: 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