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P78417

- GSTO1_HUMAN

UniProt

P78417 - GSTO1_HUMAN

Protein

Glutathione S-transferase omega-1

Gene

GSTO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.5 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Monomethylarsonic acid reductase activity is competitively inhibited by 1-chloro 2,4-dinitrobenzene (CDNB) and by deoxycholate.

    pH dependencei

    Optimum pH is 8.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei32 – 321Nucleophile1 Publication
    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
    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. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    5. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    6. positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
    7. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    8. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    9. small molecule metabolic process Source: Reactome
    10. xenobiotic catabolic process Source: UniProtKB
    11. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07564-MONOMER.
    ReactomeiREACT_11202. Vitamin C (ascorbate) metabolism.
    REACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase omega-1 (EC:2.5.1.18)
    Short name:
    GSTO-1
    Alternative name(s):
    Glutathione S-transferase omega 1-1
    Short name:
    GSTO 1-1
    Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
    Monomethylarsonic acid reductase (EC:1.20.4.2)
    Short name:
    MMA(V) reductase
    S-(Phenacyl)glutathione reductase
    Short name:
    SPG-R
    Gene namesi
    Name:GSTO1
    Synonyms:GSTTLP28
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:13312. GSTO1.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321C → A: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA133787054.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 241240Glutathione S-transferase omega-1PRO_0000185884Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei57 – 571N6-acetyllysine1 Publication
    Modified residuei143 – 1431N6-acetyllysine1 Publication
    Modified residuei148 – 1481N6-acetyllysine1 Publication
    Modified residuei152 – 1521N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP78417.
    PaxDbiP78417.
    PeptideAtlasiP78417.
    PRIDEiP78417.

    2D gel databases

    OGPiP78417.
    UCD-2DPAGEP78417.

    PTM databases

    PhosphoSiteiP78417.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest expression in liver, pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte and heart. Lowest expression in brain, placenta and lung.1 Publication

    Gene expression databases

    ArrayExpressiP78417.
    BgeeiP78417.
    CleanExiHS_GSTO1.
    GenevestigatoriP78417.

    Organism-specific databases

    HPAiHPA037603.
    HPA037604.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi114836. 11 interactions.
    IntActiP78417. 7 interactions.
    MINTiMINT-1384709.
    STRINGi9606.ENSP00000358727.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Beta strandi24 – 285
    Helixi33 – 4513
    Beta strandi49 – 546
    Beta strandi56 – 583
    Helixi63 – 664
    Beta strandi74 – 763
    Beta strandi82 – 854
    Helixi86 – 9611
    Helixi107 – 12014
    Helixi123 – 1319
    Helixi136 – 16025
    Beta strandi162 – 1643
    Beta strandi167 – 1693
    Helixi172 – 18413
    Turni185 – 1884
    Helixi190 – 1923
    Beta strandi193 – 1953
    Helixi197 – 20711
    Helixi210 – 2156
    Helixi219 – 22911
    Turni230 – 2323
    Helixi236 – 2383

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EEMX-ray2.00A1-241[»]
    3LFLX-ray2.10A/B/C1-241[»]
    3VLNX-ray1.70A1-241[»]
    4IS0X-ray1.72A1-241[»]
    ProteinModelPortaliP78417.
    SMRiP78417. Positions 3-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78417.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10180GST N-terminalAdd
    BLAST
    Domaini106 – 230125GST 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.
    InParanoidiP78417.
    KOiK00799.
    OMAiHKAYLDS.
    OrthoDBiEOG71CFNG.
    PhylomeDBiP78417.
    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.
    IPR004046. GST_C.
    IPR005442. GST_omega.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78417-1) [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

    MSGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE    50
    VININLKNKP EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK 100
    KLLPDDPYEK ACQKMILELF SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF 150
    TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW FERLEAMKLN ECVDHTPKLK 200
    LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG L 241
    Length:241
    Mass (Da):27,566
    Last modified:January 1, 1998 - v2
    Checksum:i9134ABA265F5C87E
    GO
    Isoform 2 (identifier: P78417-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         123-155: Missing.

    Show »
    Length:208
    Mass (Da):23,709
    Checksum:iF00CDE200E2A1738
    GO
    Isoform 3 (identifier: P78417-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:213
    Mass (Da):24,796
    Checksum:iC3F8EBA348399628
    GO

    Sequence cautioni

    The sequence CAD97673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321C → Y.
    Corresponds to variant rs45529437 [ dbSNP | Ensembl ].
    VAR_061231
    Natural varianti86 – 861S → C.
    Corresponds to variant rs11509436 [ dbSNP | Ensembl ].
    VAR_029269
    Natural varianti140 – 1401A → D in allele GSTO1*C; no effect on protein stability. 2 Publications
    Corresponds to variant rs4925 [ dbSNP | Ensembl ].
    VAR_016811
    Natural varianti155 – 1551Missing in allele GSTO1*B; decreased protein stability. 2 Publications
    VAR_016813
    Natural varianti208 – 2081E → K.1 Publication
    Corresponds to variant rs11509438 [ dbSNP | Ensembl ].
    VAR_024484
    Natural varianti236 – 2361A → V.1 Publication
    Corresponds to variant rs11509439 [ dbSNP | Ensembl ].
    VAR_026583

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 3. CuratedVSP_045819Add
    BLAST
    Alternative sequencei123 – 15533Missing in isoform 2. CuratedVSP_045820Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90313 mRNA. Translation: AAB70109.1.
    AF212303 mRNA. Translation: AAF73376.1.
    AY817669 Genomic DNA. Translation: AAV68046.1.
    BX537431 mRNA. Translation: CAD97673.1. Different initiation.
    AL139341 Genomic DNA. Translation: CAI17224.1.
    CH471066 Genomic DNA. Translation: EAW49601.1.
    CH471066 Genomic DNA. Translation: EAW49602.1.
    CH471066 Genomic DNA. Translation: EAW49603.1.
    BC000127 mRNA. Translation: AAH00127.1.
    CCDSiCCDS53572.1. [P78417-2]
    CCDS53573.1. [P78417-3]
    CCDS7555.1. [P78417-1]
    RefSeqiNP_001177931.1. NM_001191002.1. [P78417-2]
    NP_001177932.1. NM_001191003.1. [P78417-3]
    NP_004823.1. NM_004832.2. [P78417-1]
    UniGeneiHs.190028.

    Genome annotation databases

    EnsembliENST00000369710; ENSP00000358724; ENSG00000148834. [P78417-2]
    ENST00000369713; ENSP00000358727; ENSG00000148834. [P78417-1]
    ENST00000539281; ENSP00000441488; ENSG00000148834. [P78417-3]
    GeneIDi9446.
    KEGGihsa:9446.
    UCSCiuc001kya.3. human. [P78417-1]

    Polymorphism databases

    DMDMi6016173.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90313 mRNA. Translation: AAB70109.1 .
    AF212303 mRNA. Translation: AAF73376.1 .
    AY817669 Genomic DNA. Translation: AAV68046.1 .
    BX537431 mRNA. Translation: CAD97673.1 . Different initiation.
    AL139341 Genomic DNA. Translation: CAI17224.1 .
    CH471066 Genomic DNA. Translation: EAW49601.1 .
    CH471066 Genomic DNA. Translation: EAW49602.1 .
    CH471066 Genomic DNA. Translation: EAW49603.1 .
    BC000127 mRNA. Translation: AAH00127.1 .
    CCDSi CCDS53572.1. [P78417-2 ]
    CCDS53573.1. [P78417-3 ]
    CCDS7555.1. [P78417-1 ]
    RefSeqi NP_001177931.1. NM_001191002.1. [P78417-2 ]
    NP_001177932.1. NM_001191003.1. [P78417-3 ]
    NP_004823.1. NM_004832.2. [P78417-1 ]
    UniGenei Hs.190028.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EEM X-ray 2.00 A 1-241 [» ]
    3LFL X-ray 2.10 A/B/C 1-241 [» ]
    3VLN X-ray 1.70 A 1-241 [» ]
    4IS0 X-ray 1.72 A 1-241 [» ]
    ProteinModelPortali P78417.
    SMRi P78417. Positions 3-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114836. 11 interactions.
    IntActi P78417. 7 interactions.
    MINTi MINT-1384709.
    STRINGi 9606.ENSP00000358727.

    Chemistry

    BindingDBi P78417.
    ChEMBLi CHEMBL3174.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P78417.

    Polymorphism databases

    DMDMi 6016173.

    2D gel databases

    OGPi P78417.
    UCD-2DPAGE P78417.

    Proteomic databases

    MaxQBi P78417.
    PaxDbi P78417.
    PeptideAtlasi P78417.
    PRIDEi P78417.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369710 ; ENSP00000358724 ; ENSG00000148834 . [P78417-2 ]
    ENST00000369713 ; ENSP00000358727 ; ENSG00000148834 . [P78417-1 ]
    ENST00000539281 ; ENSP00000441488 ; ENSG00000148834 . [P78417-3 ]
    GeneIDi 9446.
    KEGGi hsa:9446.
    UCSCi uc001kya.3. human. [P78417-1 ]

    Organism-specific databases

    CTDi 9446.
    GeneCardsi GC10P106004.
    HGNCi HGNC:13312. GSTO1.
    HPAi HPA037603.
    HPA037604.
    MIMi 605482. gene.
    neXtProti NX_P78417.
    PharmGKBi PA133787054.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000006560.
    HOVERGENi HBG051853.
    InParanoidi P78417.
    KOi K00799.
    OMAi HKAYLDS.
    OrthoDBi EOG71CFNG.
    PhylomeDBi P78417.
    TreeFami TF105325.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07564-MONOMER.
    Reactomei REACT_11202. Vitamin C (ascorbate) metabolism.
    REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    ChiTaRSi GSTO1. human.
    EvolutionaryTracei P78417.
    GeneWikii GSTO1.
    GenomeRNAii 9446.
    NextBioi 35384.
    PROi P78417.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78417.
    Bgeei P78417.
    CleanExi HS_GSTO1.
    Genevestigatori P78417.

    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.
    IPR004046. GST_C.
    IPR005442. GST_omega.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    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 of the human homolog to a mouse protein, differentially expressed in lymphoma cells with different susceptibility to radiation induced apoptosis."
      Kodym R., Story M.D.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Fetus.
    3. "Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans."
      Yu L., Kalla K., Guthrie E., Vidrine A., Klimecki W.T.
      Environ. Health Perspect. 111:1421-1427(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-140; GLU-155 DEL; LYS-208 AND VAL-236.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Eye.
    8. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
      Hubbard M.J., McHugh N.J.
      Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 12-21; 58-65; 133-139 AND 149-156, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    9. "Human monomethylarsonic acid (MMA(V)) reductase is a member of the glutathione-S-transferase superfamily."
      Zakharyan R.A., Sampayo-Reyes A., Healy S.M., Tsaprailis G., Board P.G., Liebler D.C., Aposhian H.V.
      Chem. Res. Toxicol. 14:1051-1057(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    10. "Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones."
      Board P.G., Anders M.W.
      Chem. Res. Toxicol. 20:149-154(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-32, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
    11. "S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1."
      Board P.G., Coggan M., Cappello J., Zhou H., Oakley A.J., Anders M.W.
      Anal. Biochem. 374:25-30(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    12. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-143; LYS-148 AND LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1."
      Zhou H., Brock J., Casarotto M.G., Oakley A.J., Board P.G.
      J. Biol. Chem. 286:4271-4279(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GLU-155 DEL, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, CHARACTERIZATION OF VARIANTS ASP-140 AND GLU-155 DEL.
    16. "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: VARIANTS ASP-140 AND GLU-155 DEL.

    Entry informationi

    Entry nameiGSTO1_HUMAN
    AccessioniPrimary (citable) accession number: P78417
    Secondary accession number(s): D3DRA3
    , F5H7H0, Q5TA03, Q7Z3T2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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, Direct protein sequencing, 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