GSTO1_HUMAN
ID GSTO1_HUMAN Reviewed; 241 AA.
AC P78417; D3DRA3; F5H7H0; Q5TA03; Q7Z3T2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Glutathione S-transferase omega-1;
DE Short=GSTO-1;
DE EC=2.5.1.18 {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179, ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863, ECO:0000269|PubMed:21106529};
DE AltName: Full=Glutathione S-transferase omega 1-1;
DE Short=GSTO 1-1;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1 {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179};
DE AltName: Full=Monomethylarsonic acid reductase;
DE Short=MMA(V) reductase;
DE EC=1.20.4.2 {ECO:0000269|PubMed:11511179};
DE AltName: Full=S-(Phenacyl)glutathione reductase;
DE Short=SPG-R;
GN Name=GSTO1; Synonyms=GSTTLP28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Kodym R., Story M.D.;
RT "Cloning of the human homolog to a mouse protein, differentially expressed
RT in lymphoma cells with different susceptibility to radiation induced
RT apoptosis.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.0
RP ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVE SITE, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Fetus;
RX PubMed=10783391; DOI=10.1074/jbc.m001706200;
RA Board P.G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L.S.,
RA Schulte G.K., Danley D.E., Hoth L.R., Griffor M.C., Kamath A.V.,
RA Rosner M.H., Chrunyk B.A., Perregaux D.E., Gabel C.A., Geoghegan K.F.,
RA Pandit J.;
RT "Identification, characterization, and crystal structure of the Omega class
RT glutathione transferases.";
RL J. Biol. Chem. 275:24798-24806(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-140; GLU-155 DEL;
RP LYS-208 AND VAL-236.
RX PubMed=12928150; DOI=10.1289/ehp.6420;
RA Yu L., Kalla K., Guthrie E., Vidrine A., Klimecki W.T.;
RT "Genetic variation in genes associated with arsenic metabolism: glutathione
RT S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms
RT in European and indigenous Americans.";
RL Environ. Health Perspect. 111:1421-1427(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 12-21; 58-65; 133-139 AND 149-156, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=11271497;
RX DOI=10.1002/1522-2683(200011)21:17<3785::aid-elps3785>3.0.co;2-2;
RA Hubbard M.J., McHugh N.J.;
RT "Human ERp29: isolation, primary structural characterisation and two-
RT dimensional gel mapping.";
RL Electrophoresis 21:3785-3796(2000).
RN [9]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=11511179; DOI=10.1021/tx010052h;
RA Zakharyan R.A., Sampayo-Reyes A., Healy S.M., Tsaprailis G., Board P.G.,
RA Liebler D.C., Aposhian H.V.;
RT "Human monomethylarsonic acid (MMA(V)) reductase is a member of the
RT glutathione-S-transferase superfamily.";
RL Chem. Res. Toxicol. 14:1051-1057(2001).
RN [10]
RP FUNCTION, MUTAGENESIS OF CYS-32, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
RX PubMed=17226937; DOI=10.1021/tx600305y;
RA Board P.G., Anders M.W.;
RT "Glutathione transferase omega 1 catalyzes the reduction of S-
RT (phenacyl)glutathiones to acetophenones.";
RL Chem. Res. Toxicol. 20:149-154(2007).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18028863; DOI=10.1016/j.ab.2007.09.029;
RA Board P.G., Coggan M., Cappello J., Zhou H., Oakley A.J., Anders M.W.;
RT "S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione
RT transferase omega 1-1.";
RL Anal. Biochem. 374:25-30(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-143; LYS-148 AND LYS-152,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GLU-155 DEL IN COMPLEX
RP WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP CHARACTERIZATION OF VARIANTS ASP-140 AND GLU-155 DEL.
RX PubMed=21106529; DOI=10.1074/jbc.m110.197822;
RA Zhou H., Brock J., Casarotto M.G., Oakley A.J., Board P.G.;
RT "Novel folding and stability defects cause a deficiency of human
RT glutathione transferase omega 1.";
RL J. Biol. Chem. 286:4271-4279(2011).
RN [18]
RP VARIANTS ASP-140 AND GLU-155 DEL.
RX PubMed=12618591; DOI=10.1097/01.fpc.0000054062.98065.6e;
RA Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.;
RT "Characterization of the human Omega class glutathione transferase genes
RT and associated polymorphisms.";
RL Pharmacogenetics 13:131-144(2003).
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
CC dehydroascorbate reductase activities. Has S-(phenacyl)glutathione
CC reductase activity. Has also glutathione S-transferase activity.
CC Participates in the biotransformation of inorganic arsenic and reduces
CC monomethylarsonic acid (MMA) and dimethylarsonic acid.
CC {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179,
CC ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863,
CC ECO:0000269|PubMed:21106529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179,
CC ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863,
CC ECO:0000269|PubMed:21106529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC Evidence={ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC Evidence={ECO:0000269|PubMed:11511179};
CC -!- ACTIVITY REGULATION: Monomethylarsonic acid reductase activity is
CC competitively inhibited by 1-chloro 2,4-dinitrobenzene (CDNB) and by
CC deoxycholate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11511179,
CC ECO:0000269|PubMed:17226937};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10783391,
CC ECO:0000269|PubMed:21106529}.
CC -!- INTERACTION:
CC P78417; P04792: HSPB1; NbExp=2; IntAct=EBI-712083, EBI-352682;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11511179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P78417-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78417-2; Sequence=VSP_045820;
CC Name=3;
CC IsoId=P78417-3; Sequence=VSP_045819;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in liver, pancreas,
CC skeletal muscle, spleen, thymus, colon, blood leukocyte and heart.
CC Lowest expression in brain, placenta and lung.
CC {ECO:0000269|PubMed:10783391}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97673.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U90313; AAB70109.1; -; mRNA.
DR EMBL; AF212303; AAF73376.1; -; mRNA.
DR EMBL; AY817669; AAV68046.1; -; Genomic_DNA.
DR EMBL; BX537431; CAD97673.1; ALT_INIT; mRNA.
DR EMBL; AL139341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49601.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49602.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49603.1; -; Genomic_DNA.
DR EMBL; BC000127; AAH00127.1; -; mRNA.
DR CCDS; CCDS53572.1; -. [P78417-2]
DR CCDS; CCDS53573.1; -. [P78417-3]
DR CCDS; CCDS7555.1; -. [P78417-1]
DR RefSeq; NP_001177931.1; NM_001191002.1. [P78417-2]
DR RefSeq; NP_001177932.1; NM_001191003.1. [P78417-3]
DR RefSeq; NP_004823.1; NM_004832.2. [P78417-1]
DR PDB; 1EEM; X-ray; 2.00 A; A=1-241.
DR PDB; 3LFL; X-ray; 2.10 A; A/B/C=1-241.
DR PDB; 3VLN; X-ray; 1.70 A; A=1-241.
DR PDB; 4IS0; X-ray; 1.72 A; A=1-241.
DR PDB; 4YQM; X-ray; 2.38 A; A/B/C=1-241.
DR PDB; 4YQU; X-ray; 1.94 A; A/B=1-241.
DR PDB; 4YQV; X-ray; 2.06 A; A/B/C=1-241.
DR PDB; 5UEH; X-ray; 2.00 A; A=1-241.
DR PDB; 5V3Q; X-ray; 2.25 A; A=1-241.
DR PDB; 5YVN; X-ray; 1.33 A; A=1-241.
DR PDB; 5YVO; X-ray; 1.80 A; A=1-241.
DR PDB; 6MHB; X-ray; 2.75 A; A/B/C/D/E/F=1-241.
DR PDB; 6MHC; X-ray; 2.00 A; A/B=1-241.
DR PDB; 6MHD; X-ray; 2.16 A; A/B=1-241.
DR PDB; 6PNM; X-ray; 1.82 A; A=2-241.
DR PDB; 6PNN; X-ray; 2.10 A; A=2-241.
DR PDB; 6PNO; X-ray; 1.82 A; A=2-241.
DR PDBsum; 1EEM; -.
DR PDBsum; 3LFL; -.
DR PDBsum; 3VLN; -.
DR PDBsum; 4IS0; -.
DR PDBsum; 4YQM; -.
DR PDBsum; 4YQU; -.
DR PDBsum; 4YQV; -.
DR PDBsum; 5UEH; -.
DR PDBsum; 5V3Q; -.
DR PDBsum; 5YVN; -.
DR PDBsum; 5YVO; -.
DR PDBsum; 6MHB; -.
DR PDBsum; 6MHC; -.
DR PDBsum; 6MHD; -.
DR PDBsum; 6PNM; -.
DR PDBsum; 6PNN; -.
DR PDBsum; 6PNO; -.
DR AlphaFoldDB; P78417; -.
DR SMR; P78417; -.
DR BioGRID; 114836; 94.
DR IntAct; P78417; 14.
DR MINT; P78417; -.
DR STRING; 9606.ENSP00000358727; -.
DR BindingDB; P78417; -.
DR ChEMBL; CHEMBL3174; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB00163; Vitamin E.
DR GuidetoPHARMACOLOGY; 3110; -.
DR GlyConnect; 2854; 1 O-Linked glycan (1 site).
DR GlyGen; P78417; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78417; -.
DR MetOSite; P78417; -.
DR PhosphoSitePlus; P78417; -.
DR SwissPalm; P78417; -.
DR BioMuta; GSTO1; -.
DR DMDM; 6016173; -.
DR OGP; P78417; -.
DR UCD-2DPAGE; P78417; -.
DR CPTAC; CPTAC-381; -.
DR CPTAC; CPTAC-382; -.
DR EPD; P78417; -.
DR jPOST; P78417; -.
DR MassIVE; P78417; -.
DR MaxQB; P78417; -.
DR PaxDb; P78417; -.
DR PeptideAtlas; P78417; -.
DR PRIDE; P78417; -.
DR ProteomicsDB; 12755; -.
DR ProteomicsDB; 27484; -.
DR ProteomicsDB; 57621; -. [P78417-1]
DR TopDownProteomics; P78417-1; -. [P78417-1]
DR Antibodypedia; 31606; 308 antibodies from 34 providers.
DR DNASU; 9446; -.
DR Ensembl; ENST00000369710.8; ENSP00000358724.4; ENSG00000148834.13. [P78417-2]
DR Ensembl; ENST00000369713.10; ENSP00000358727.5; ENSG00000148834.13. [P78417-1]
DR Ensembl; ENST00000539281.5; ENSP00000441488.1; ENSG00000148834.13. [P78417-3]
DR GeneID; 9446; -.
DR KEGG; hsa:9446; -.
DR MANE-Select; ENST00000369713.10; ENSP00000358727.5; NM_004832.3; NP_004823.1.
DR UCSC; uc021pxr.2; human. [P78417-1]
DR CTD; 9446; -.
DR DisGeNET; 9446; -.
DR GeneCards; GSTO1; -.
DR HGNC; HGNC:13312; GSTO1.
DR HPA; ENSG00000148834; Tissue enhanced (liver).
DR MIM; 605482; gene.
DR neXtProt; NX_P78417; -.
DR OpenTargets; ENSG00000148834; -.
DR PharmGKB; PA133787054; -.
DR VEuPathDB; HostDB:ENSG00000148834; -.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000155351; -.
DR InParanoid; P78417; -.
DR OMA; ADHYSHR; -.
DR OrthoDB; 990343at2759; -.
DR PhylomeDB; P78417; -.
DR TreeFam; TF105325; -.
DR BioCyc; MetaCyc:HS07564-MON; -.
DR BRENDA; 1.20.4.2; 2681.
DR BRENDA; 1.8.5.1; 2681.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P78417; -.
DR Reactome; R-HSA-156581; Methylation.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P78417; -.
DR BioGRID-ORCS; 9446; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; GSTO1; human.
DR EvolutionaryTrace; P78417; -.
DR GeneWiki; GSTO1; -.
DR GenomeRNAi; 9446; -.
DR Pharos; P78417; Tchem.
DR PRO; PR:P78417; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P78417; protein.
DR Bgee; ENSG00000148834; Expressed in monocyte and 204 other tissues.
DR ExpressionAtlas; P78417; baseline and differential.
DR Genevisible; P78417; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0014810; P:positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR005442; GST_omega.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..241
FT /note="Glutathione S-transferase omega-1"
FT /id="PRO_0000185884"
FT DOMAIN 22..101
FT /note="GST N-terminal"
FT DOMAIN 106..230
FT /note="GST C-terminal"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:10783391"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:10783391,
FT ECO:0000269|PubMed:21106529"
FT BINDING 72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:10783391,
FT ECO:0000269|PubMed:21106529"
FT BINDING 85..86
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:10783391,
FT ECO:0000269|PubMed:21106529"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_045819"
FT VAR_SEQ 123..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045820"
FT VARIANT 32
FT /note="C -> Y (in dbSNP:rs45529437)"
FT /id="VAR_061231"
FT VARIANT 86
FT /note="S -> C (in dbSNP:rs11509436)"
FT /id="VAR_029269"
FT VARIANT 140
FT /note="A -> D (in allele GSTO1*C; no effect on protein
FT stability; dbSNP:rs4925)"
FT /evidence="ECO:0000269|PubMed:12618591,
FT ECO:0000269|PubMed:12928150, ECO:0000269|PubMed:21106529"
FT /id="VAR_016811"
FT VARIANT 155
FT /note="Missing (in allele GSTO1*B; decreased protein
FT stability)"
FT /evidence="ECO:0000269|PubMed:12618591,
FT ECO:0000269|PubMed:12928150, ECO:0000269|PubMed:21106529"
FT /id="VAR_016813"
FT VARIANT 208
FT /note="E -> K (in dbSNP:rs11509438)"
FT /evidence="ECO:0000269|PubMed:12928150"
FT /id="VAR_024484"
FT VARIANT 236
FT /note="A -> V (in dbSNP:rs11509439)"
FT /evidence="ECO:0000269|PubMed:12928150"
FT /id="VAR_026583"
FT MUTAGEN 32
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17226937"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3VLN"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5YVN"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5YVN"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3LFL"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:5YVN"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5YVN"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:5YVN"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 136..160
FT /evidence="ECO:0007829|PDB:5YVN"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4IS0"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:5YVN"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5YVN"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5YVN"
SQ SEQUENCE 241 AA; 27566 MW; 9134ABA265F5C87E CRC64;
MSGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP
EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMILELF
SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW
FERLEAMKLN ECVDHTPKLK LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG
L
