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   13-FEB-2019, entry version 197.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   expressed in lymphoma cells with different susceptibility to radiation
RT   induced 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
RT   class 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:
RT   glutathione S-transferase omega 1-1 and purine nucleoside
RT   phosphorylase polymorphisms 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RP   IDENTIFICATION 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,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP   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.,
RA   Board P.G., 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
RT   glutathione 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
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a 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
RP   LYS-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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.,
RA   Buerckstuemmer T., 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
RP   BY 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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.,
RA   Ayoub D., 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
RP   COMPLEX 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=10.1097/00008571-200303000-00003;
RA   Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.;
RT   "Characterization of the human Omega class glutathione transferase
RT   genes 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
CC       reduces 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,
CC         ECO:0000269|PubMed:11511179, ECO:0000269|PubMed:17226937,
CC         ECO:0000269|PubMed:18028863, ECO:0000269|PubMed:21106529};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione
CC         disulfide + L-ascorbate; Xref=Rhea:RHEA:24424,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000269|PubMed:10783391,
CC         ECO:0000269|PubMed:11511179};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione
CC         disulfide + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC         ChEBI:CHEBI:33409, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297;
CC         EC=1.20.4.2; Evidence={ECO:0000269|PubMed:11511179};
CC   -!- ACTIVITY REGULATION: Monomethylarsonic acid reductase activity is
CC       competitively inhibited by 1-chloro 2,4-dinitrobenzene (CDNB) and
CC       by 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       P04792:HSPB1; NbExp=2; IntAct=EBI-712083, EBI-352682;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {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,
CC       pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte
CC       and heart. 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=Translation N-terminally shortened.; 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   UniGene; Hs.190028; -.
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   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   ProteinModelPortal; P78417; -.
DR   SMR; P78417; -.
DR   BioGrid; 114836; 38.
DR   IntAct; P78417; 8.
DR   STRING; 9606.ENSP00000358727; -.
DR   BindingDB; P78417; -.
DR   ChEMBL; CHEMBL3174; -.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB00163; Vitamin E.
DR   iPTMnet; P78417; -.
DR   PhosphoSitePlus; P78417; -.
DR   SwissPalm; P78417; -.
DR   BioMuta; GSTO1; -.
DR   DMDM; 6016173; -.
DR   OGP; P78417; -.
DR   UCD-2DPAGE; P78417; -.
DR   EPD; P78417; -.
DR   jPOST; P78417; -.
DR   PaxDb; P78417; -.
DR   PeptideAtlas; P78417; -.
DR   PRIDE; P78417; -.
DR   ProteomicsDB; 57621; -.
DR   TopDownProteomics; P78417-1; -. [P78417-1]
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; HPA037603; -.
DR   HPA; HPA037604; -.
DR   MIM; 605482; gene.
DR   neXtProt; NX_P78417; -.
DR   OpenTargets; ENSG00000148834; -.
DR   PharmGKB; PA133787054; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000155351; -.
DR   HOGENOM; HOG000006560; -.
DR   HOVERGEN; HBG051853; -.
DR   InParanoid; P78417; -.
DR   KO; K00799; -.
DR   OMA; EHPLKLY; -.
DR   OrthoDB; 1225872at2759; -.
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   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   ChiTaRS; GSTO1; human.
DR   EvolutionaryTrace; P78417; -.
DR   GeneWiki; GSTO1; -.
DR   GenomeRNAi; 9446; -.
DR   PRO; PR:P78417; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000148834; Expressed in 226 organ(s), highest expression level in liver.
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; TAS:Reactome.
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   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; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Oxidoreductase; Phosphoprotein;
KW   Polymorphism; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19413330}.
FT   CHAIN         2    241       Glutathione S-transferase omega-1.
FT                                /FTId=PRO_0000185884.
FT   DOMAIN       22    101       GST N-terminal.
FT   DOMAIN      106    230       GST C-terminal.
FT   REGION       85     86       Glutathione binding.
FT                                {ECO:0000269|PubMed:10783391,
FT                                ECO:0000269|PubMed:21106529}.
FT   ACT_SITE     32     32       Nucleophile.
FT                                {ECO:0000269|PubMed:10783391}.
FT   BINDING      59     59       Glutathione.
FT                                {ECO:0000269|PubMed:10783391,
FT                                ECO:0000269|PubMed:21106529}.
FT   BINDING      72     72       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000269|PubMed:10783391,
FT                                ECO:0000269|PubMed:21106529}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:19413330}.
FT   MOD_RES      57     57       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     129    129       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     143    143       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     148    148       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     152    152       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   VAR_SEQ       1     28       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_045819.
FT   VAR_SEQ     123    155       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_045820.
FT   VARIANT      32     32       C -> Y (in dbSNP:rs45529437).
FT                                /FTId=VAR_061231.
FT   VARIANT      86     86       S -> C (in dbSNP:rs11509436).
FT                                /FTId=VAR_029269.
FT   VARIANT     140    140       A -> D (in allele GSTO1*C; no effect on
FT                                protein stability; dbSNP:rs4925).
FT                                {ECO:0000269|PubMed:12618591,
FT                                ECO:0000269|PubMed:12928150,
FT                                ECO:0000269|PubMed:21106529}.
FT                                /FTId=VAR_016811.
FT   VARIANT     155    155       Missing (in allele GSTO1*B; decreased
FT                                protein stability).
FT                                {ECO:0000269|PubMed:12618591,
FT                                ECO:0000269|PubMed:12928150,
FT                                ECO:0000269|PubMed:21106529}.
FT                                /FTId=VAR_016813.
FT   VARIANT     208    208       E -> K (in dbSNP:rs11509438).
FT                                {ECO:0000269|PubMed:12928150}.
FT                                /FTId=VAR_024484.
FT   VARIANT     236    236       A -> V (in dbSNP:rs11509439).
FT                                {ECO:0000269|PubMed:12928150}.
FT                                /FTId=VAR_026583.
FT   MUTAGEN      32     32       C->A: Loss of activity.
FT                                {ECO:0000269|PubMed:17226937}.
FT   HELIX         4      6       {ECO:0000244|PDB:3VLN}.
FT   STRAND       24     28       {ECO:0000244|PDB:3VLN}.
FT   HELIX        33     45       {ECO:0000244|PDB:3VLN}.
FT   STRAND       49     54       {ECO:0000244|PDB:3VLN}.
FT   STRAND       56     58       {ECO:0000244|PDB:3LFL}.
FT   HELIX        63     66       {ECO:0000244|PDB:3VLN}.
FT   STRAND       74     76       {ECO:0000244|PDB:3VLN}.
FT   STRAND       82     85       {ECO:0000244|PDB:3VLN}.
FT   HELIX        86     96       {ECO:0000244|PDB:3VLN}.
FT   HELIX       107    120       {ECO:0000244|PDB:3VLN}.
FT   HELIX       123    131       {ECO:0000244|PDB:3VLN}.
FT   HELIX       136    160       {ECO:0000244|PDB:3VLN}.
FT   STRAND      162    164       {ECO:0000244|PDB:4IS0}.
FT   STRAND      167    169       {ECO:0000244|PDB:3VLN}.
FT   HELIX       172    184       {ECO:0000244|PDB:3VLN}.
FT   TURN        185    188       {ECO:0000244|PDB:3VLN}.
FT   HELIX       190    192       {ECO:0000244|PDB:3VLN}.
FT   STRAND      193    195       {ECO:0000244|PDB:1EEM}.
FT   HELIX       197    207       {ECO:0000244|PDB:3VLN}.
FT   HELIX       210    215       {ECO:0000244|PDB:3VLN}.
FT   HELIX       219    229       {ECO:0000244|PDB:3VLN}.
FT   TURN        230    232       {ECO:0000244|PDB:3VLN}.
FT   HELIX       236    238       {ECO:0000244|PDB:3VLN}.
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
//
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