GenomeNet

Database: UniProt/SWISS-PROT
Entry: GSTO1_HUMAN
LinkDB: GSTO1_HUMAN
Original site: 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   12-AUG-2020, entry version 208.
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};
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   SMR; P78417; -.
DR   BioGRID; 114836; 69.
DR   IntAct; P78417; 10.
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   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   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; 272 antibodies.
DR   Ensembl; ENST00000369710; ENSP00000358724; ENSG00000148834. [P78417-2]
DR   Ensembl; ENST00000369713; ENSP00000358727; ENSG00000148834. [P78417-1]
DR   Ensembl; ENST00000539281; ENSP00000441488; ENSG00000148834. [P78417-3]
DR   GeneID; 9446; -.
DR   KEGG; hsa:9446; -.
DR   UCSC; uc021pxr.2; human. [P78417-1]
DR   CTD; 9446; -.
DR   DisGeNET; 9446; -.
DR   EuPathDB; HostDB:ENSG00000148834.12; -.
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   eggNOG; KOG0406; Eukaryota.
DR   GeneTree; ENSGT00940000155351; -.
DR   InParanoid; P78417; -.
DR   KO; K00799; -.
DR   OMA; EHPLKLY; -.
DR   OrthoDB; 990343at2759; -.
DR   PhylomeDB; P78417; -.
DR   TreeFam; TF105325; -.
DR   BioCyc; MetaCyc:HS07564-MONOMER; -.
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   BioGRID-ORCS; 9446; 7 hits in 872 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 liver and 237 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; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
DR   GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; TAS:Reactome.
DR   GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
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   Gene3D; 3.40.30.10; -; 1.
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; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
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; Polymorphism;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|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   REGION          85..86
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000269|PubMed:10783391,
FT                   ECO:0000269|PubMed:21106529"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:10783391"
FT   BINDING         59
FT                   /note="Glutathione"
FT                   /evidence="ECO:0000269|PubMed:10783391,
FT                   ECO:0000269|PubMed:21106529"
FT   BINDING         72
FT                   /note="Glutathione; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:10783391,
FT                   ECO:0000269|PubMed:21106529"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:19413330"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         143
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:3VLN"
FT   STRAND          24..28
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           33..44
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   STRAND          49..54
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   STRAND          56..58
FT                   /evidence="ECO:0000244|PDB:3LFL"
FT   HELIX           61..65
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   STRAND          74..76
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   STRAND          82..85
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           86..96
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           107..120
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           123..129
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   TURN            130..132
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           136..160
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:4IS0"
FT   STRAND          167..169
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           172..182
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           184..187
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           190..193
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           197..207
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           210..215
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           219..229
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   TURN            230..232
FT                   /evidence="ECO:0000244|PDB:5YVN"
FT   HELIX           236..238
FT                   /evidence="ECO:0000244|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
//
DBGET integrated database retrieval system