ID   GSTA2_HUMAN             Reviewed;         222 AA.
AC   P09210; Q12759; Q16491; Q9NTY6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 4.
DT   04-NOV-2026, entry version 236.
DE   RecName: Full=Glutathione S-transferase A2;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:10395737, ECO:0000269|PubMed:15077012};
DE   AltName: Full=GST HA subunit 2;
DE   AltName: Full=GST class-alpha member 2;
DE   AltName: Full=GST-gamma;
DE   AltName: Full=GSTA2-2 {ECO:0000303|PubMed:20083122};
DE   AltName: Full=GTH2 {ECO:0000303|PubMed:3036131};
DE   AltName: Full=Lipid-hydroperoxide glutathione peroxidase A2 {ECO:0000305|PubMed:10395737};
DE            EC=1.11.1.12 {ECO:0000269|PubMed:10395737};
GN   Name=GSTA2 {ECO:0000312|HGNC:HGNC:4627}; Synonyms=GST2;
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], VARIANT THR-112, AND TISSUE SPECIFICITY.
RX   PubMed=3036131; DOI=10.1016/0006-291x(87)91345-3;
RA   Rhoads D.M., Zarlengo R.P., Tu C.-P.D.;
RT   "The basic glutathione S-transferases from human livers are products of
RT   separate genes.";
RL   Biochem. Biophys. Res. Commun. 145:474-481(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-210.
RC   TISSUE=Liver;
RX   PubMed=1329668; DOI=10.1016/0003-9861(92)90475-c;
RA   Rohrdanz E., Nguyen T., Pickett C.B.;
RT   "Isolation and characterization of the human glutathione S-transferase A2
RT   subunit gene.";
RL   Arch. Biochem. Biophys. 298:747-752(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-210.
RC   TISSUE=Blood;
RX   PubMed=1497629; DOI=10.1042/bj2850925;
RA   Klone A., Hussnatter R., Sies H.;
RT   "Cloning, sequencing and characterization of the human alpha glutathione S-
RT   transferase gene corresponding to the cDNA clone pGTH2.";
RL   Biochem. J. 285:925-928(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-112.
RC   TISSUE=Lung;
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   [6]
RP   PROTEIN SEQUENCE OF 2-170; 188-195 AND 209-222.
RX   PubMed=8431482; DOI=10.1016/0167-4838(93)90234-i;
RA   Ahmad H., Singhal S.S., Saxena M., Awasthi Y.C.;
RT   "Characterization of two novel subunits of the alpha-class glutathione S-
RT   transferases of human liver.";
RL   Biochim. Biophys. Acta 1161:333-336(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 63-155 AND 208-222.
RX   PubMed=2604726; DOI=10.1042/bj2640437;
RA   Hayes J.D., Kerr L.A., Cronshaw A.D.;
RT   "Evidence that glutathione S-transferases B1B1 and B2B2 are the products of
RT   separate genes and that their expression in human liver is subject to
RT   inter-individual variation. Molecular relationships between the B1 and B2
RT   subunits and other alpha class glutathione S-transferases.";
RL   Biochem. J. 264:437-445(1989).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10395737; DOI=10.1006/abbi.1999.1277;
RA   Zhao T., Singhal S.S., Piper J.T., Cheng J., Pandya U., Clark-Wronski J.,
RA   Awasthi S., Awasthi Y.C.;
RT   "The role of human glutathione S-transferases hGSTA1-1 and hGSTA2-2 in
RT   protection against oxidative stress.";
RL   Arch. Biochem. Biophys. 367:216-224(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=12067250; DOI=10.1021/tx025519i;
RA   Dreij K., Sundberg K., Johansson A.S., Nordling E., Seidel A., Persson B.,
RA   Mannervik B., Jernstroem B.;
RT   "Catalytic activities of human alpha class glutathione transferases toward
RT   carcinogenic dibenzo[a,l]pyrene diol epoxides.";
RL   Chem. Res. Toxicol. 15:825-831(2002).
RN   [10]
RP   FUNCTION.
RX   PubMed=28478157; DOI=10.1016/j.toxlet.2017.05.003;
RA   Zhang Y., den Braver-Sewradj S.P., Vos J.C., Vermeulen N.P.E.,
RA   Commandeur J.N.M.;
RT   "Human glutathione S-transferases- and NAD(P)H:quinone oxidoreductase 1-
RT   catalyzed inactivation of reactive quinoneimines of amodiaquine and N-
RT   desethylamodiaquine: Possible implications for susceptibility to
RT   amodiaquine-induced liver toxicity.";
RL   Toxicol. Lett. 275:83-91(2017).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY, AND SUBUNIT.
RX   PubMed=7892174; DOI=10.1002/prot.340200306;
RA   Zeng K., Rose J.P., Chen H.C., Strickland C.L., Tu C.P., Wang B.C.;
RT   "A surface mutant (G82R) of a human alpha-glutathione S-transferase shows
RT   decreased thermal stability and a new mode of molecular association in the
RT   crystal.";
RL   Proteins 20:259-263(1994).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH GLUTATHIONE AND
RP   DELTA5-ANDROSTENE-3-17-DIONE, AND SUBUNIT.
RX   PubMed=20083122; DOI=10.1016/j.jmb.2010.01.023;
RA   Tars K., Olin B., Mannervik B.;
RT   "Structural basis for featuring of steroid isomerase activity in alpha
RT   class glutathione transferases.";
RL   J. Mol. Biol. 397:332-340(2010).
RN   [13]
RP   VARIANTS THR-112 AND ALA-210.
RX   PubMed=11668220; DOI=10.1097/00008571-200110000-00007;
RA   Tetlow N., Liu D., Board P.;
RT   "Polymorphism of human alpha class glutathione transferases.";
RL   Pharmacogenetics 11:609-617(2001).
RN   [14]
RP   VARIANT SER-110, CHARACTERIZATION OF VARIANT SER-110, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15077012; DOI=10.1097/00008571-200402000-00005;
RA   Tetlow N., Board P.G.;
RT   "Functional polymorphism of human glutathione transferase A2.";
RL   Pharmacogenetics 14:111-116(2004).
RN   [15]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-112, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- FUNCTION: Glutathione S-transferase involved in the clearance of a
CC       variety of electrophilic toxic compounds by glutathione conjugation,
CC       including harmful products generated during oxidative stress and
CC       xenobiotics such as environmental toxins, drugs, and carcinogens
CC       including derivatives of polycyclic aromatic hydrocarbons
CC       (PubMed:10395737, PubMed:12067250, PubMed:15077012, PubMed:28478157).
CC       Catalyzes the nucleophilic attack of the sulfur atom of glutathione on
CC       the electrophilic groups of a wide range of substrates
CC       (PubMed:10395737, PubMed:12067250, PubMed:15077012, PubMed:28478157).
CC       Involved in the protection from oxidative stress through its
CC       glutathione-dependent peroxidase activity toward lipid hydroperoxides,
CC       including linoleic acid hydroperoxides, dilinoleoyl phosphatidylcholine
CC       hydroperoxide, and dilinoleoyl phosphatidylethanolamine hydroperoxide
CC       (PubMed:10395737). Can also catalyze glutathione conjugation with 4-
CC       hydroxynonenal (4-HNE), a toxic product of lipid peroxidation
CC       (PubMed:10395737). Is involved in the protection from toxic effects of
CC       bis (2-ethylhexyl) phthalate (DEHP) on male fertility through the
CC       activation of the PI3K-AKT signaling pathway (By similarity). In vitro,
CC       it catalyzes the reduction of cumene hydroperoxide (PubMed:10395737,
CC       PubMed:15077012). {ECO:0000250|UniProtKB:P10648,
CC       ECO:0000269|PubMed:10395737, ECO:0000269|PubMed:12067250,
CC       ECO:0000269|PubMed:15077012, ECO:0000269|PubMed:28478157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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:15077012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000305|PubMed:15077012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a
CC         hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O;
CC         Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019;
CC         EC=1.11.1.12; Evidence={ECO:0000269|PubMed:10395737};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC         S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:10395737, ECO:0000269|PubMed:15077012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51221;
CC         Evidence={ECO:0000305|PubMed:10395737, ECO:0000305|PubMed:15077012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-hydroxynon-2-enal + glutathione = 3-(glutathion-S-yl)-4-
CC         hydroxynonanal; Xref=Rhea:RHEA:85343, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58968, ChEBI:CHEBI:234318;
CC         Evidence={ECO:0000269|PubMed:10395737};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:85344;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC         glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:10395737};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione =
CC         (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide +
CC         H2O; Xref=Rhea:RHEA:76687, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297, ChEBI:CHEBI:60955, ChEBI:CHEBI:77852;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76688;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
CC         (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
CC         H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC         Evidence={ECO:0000305|PubMed:10395737};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:69651, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:78673,
CC         ChEBI:CHEBI:131607; Evidence={ECO:0000269|PubMed:10395737,
CC         ECO:0000269|PubMed:15077012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652;
CC         Evidence={ECO:0000305|PubMed:10395737, ECO:0000305|PubMed:15077012};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=650 uM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:15077012};
CC         KM=630 uM for 1-chloro-2,4-dinitrobenzene (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:10395737};
CC         KM=190 uM for glutathione {ECO:0000269|PubMed:15077012};
CC         KM=80 uM for (E)-4-hydroxynon-2-enal (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:10395737};
CC         KM=60 uM for cumene hydroperoxide (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:10395737};
CC         KM=47 uM for dilinoleoyl phosphatidylcholine hydroperoxide (at 37
CC         degrees Celsius) {ECO:0000269|PubMed:10395737};
CC         KM=40 uM for dilinoleoyl phosphatidylethanolamine hydroperoxide (at
CC         30 degrees Celsius) {ECO:0000269|PubMed:10395737};
CC         KM=36 uM for 9-hydroperoxy-(10E,12Z)-octadecadienoate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:10395737};
CC         KM=36 uM for 13-hydroperoxy-(9Z,11E)-octadecadienoate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:10395737};
CC         KM=6.6 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (at
CC         37 degrees Celsius) {ECO:0000269|PubMed:10395737};
CC   -!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
CC       {ECO:0000269|PubMed:20083122, ECO:0000269|PubMed:7892174}.
CC   -!- INTERACTION:
CC       P09210; O15217: GSTA4; NbExp=13; IntAct=EBI-10196201, EBI-752440;
CC       P09210; Q7RTV2: GSTA5; NbExp=5; IntAct=EBI-10196201, EBI-13328621;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:3036131}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   EMBL; M16594; AAA52616.1; -; mRNA.
DR   EMBL; S45640; AAB23672.1; -; Genomic_DNA.
DR   EMBL; S45627; AAB23672.1; JOINED; Genomic_DNA.
DR   EMBL; S45629; AAB23672.1; JOINED; Genomic_DNA.
DR   EMBL; S45636; AAB23672.1; JOINED; Genomic_DNA.
DR   EMBL; S45637; AAB23672.1; JOINED; Genomic_DNA.
DR   EMBL; S45639; AAB23672.1; JOINED; Genomic_DNA.
DR   EMBL; X65727; CAA46642.1; -; Genomic_DNA.
DR   EMBL; X65728; CAA46642.1; JOINED; Genomic_DNA.
DR   EMBL; X65729; CAA46642.1; JOINED; Genomic_DNA.
DR   EMBL; X65730; CAA46642.1; JOINED; Genomic_DNA.
DR   EMBL; X65731; CAA46642.1; JOINED; Genomic_DNA.
DR   EMBL; X65732; CAA46642.1; JOINED; Genomic_DNA.
DR   EMBL; AL109918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002895; AAH02895.1; -; mRNA.
DR   CCDS; CCDS4944.1; -.
DR   PIR; S24330; S24330.
DR   PIR; S29658; S29658.
DR   RefSeq; NP_000837.3; NM_000846.5.
DR   RefSeq; XP_047274640.1; XM_047418684.1.
DR   RefSeq; XP_054211232.1; XM_054355257.1.
DR   PDB; 1AGS; X-ray; 2.50 A; A/B=2-222.
DR   PDB; 2VCT; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-222.
DR   PDB; 2WJU; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-222.
DR   PDB; 4ACS; X-ray; 2.10 A; A/B/C/D=1-222.
DR   AlphaFoldDB; P09210; -.
DR   SMR; P09210; -.
DR   BioGRID; 109194; 11.
DR   FunCoup; P09210; 162.
DR   IntAct; P09210; 9.
DR   NDEx; IQUERY-CP-GSTA2; 12 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000420168; -.
DR   BindingDB; P09210; -.
DR   ChEMBL; CHEMBL2241; -.
DR   DrugBank; DB14001; alpha-Tocopherol succinate.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB00993; Azathioprine.
DR   DrugBank; DB01008; Busulfan.
DR   DrugBank; DB00291; Chlorambucil.
DR   DrugBank; DB00608; Chloroquine.
DR   DrugBank; DB00636; Clofibrate.
DR   DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR   DrugBank; DB03619; Deoxycholic acid.
DR   DrugBank; DB00903; Etacrynic acid.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB03310; Glutathione disulfide.
DR   DrugBank; DB00163; Vitamin E.
DR   GlyGen; P09210; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P09210; -.
DR   PhosphoSitePlus; P09210; -.
DR   BioMuta; GSTA2; -.
DR   DMDM; 126302551; -.
DR   REPRODUCTION-2DPAGE; IPI00745233; -.
DR   jPOST; P09210; -.
DR   MassIVE; P09210; -.
DR   PaxDb; 9606-ENSP00000420168; -.
DR   PeptideAtlas; P09210; -.
DR   ProteomicsDB; 52206; -.
DR   Antibodypedia; 30929; 244 antibodies from 30 providers.
DR   DNASU; 2939; -.
DR   Ensembl; ENST00000493422.3; ENSP00000420168.1; ENSG00000244067.4.
DR   Ensembl; ENST00000873254.1; ENSP00000543313.1; ENSG00000244067.4.
DR   Ensembl; ENST00000873256.1; ENSP00000543315.1; ENSG00000244067.4.
DR   Ensembl; ENST00000873257.1; ENSP00000543316.1; ENSG00000244067.4.
DR   Ensembl; ENST00000873260.1; ENSP00000543319.1; ENSG00000244067.4.
DR   Ensembl; ENST00000873261.1; ENSP00000543320.1; ENSG00000244067.4.
DR   Ensembl; ENST00000873262.1; ENSP00000543321.1; ENSG00000244067.4.
DR   GeneID; 2939; -.
DR   KEGG; hsa:2939; -.
DR   MANE-Select; ENST00000493422.3; ENSP00000420168.1; NM_000846.5; NP_000837.3.
DR   UCSC; uc003pay.4; human.
DR   AGR; HGNC:4627; -.
DR   ClinPGx; PA29017; -.
DR   CTD; 2939; -.
DR   DisGeNET; 2939; -.
DR   GeneCards; GSTA2; -.
DR   HGNC; HGNC:4627; GSTA2.
DR   HPA; ENSG00000244067; Group enriched (kidney, liver).
DR   MIM; 138360; gene.
DR   OpenTargets; ENSG00000244067; -.
DR   VEuPathDB; HostDB:ENSG00000244067; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000164034; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   InParanoid; P09210; -.
DR   OMA; AEIIRWM; -.
DR   OrthoDB; 414243at2759; -.
DR   PAN-GO; P09210; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P09210; -.
DR   BioCyc; MetaCyc:HS01846-MONOMER; -.
DR   BRENDA; 2.5.1.18; 2681.
DR   PathwayCommons; P09210; -.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR   Reactome; R-HSA-9748787; Azathioprine ADME.
DR   SABIO-RK; P09210; -.
DR   SignaLink; P09210; -.
DR   BioGRID-ORCS; 2939; 19 hits in 1038 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   ChiTaRS; GSTA2; human.
DR   EvolutionaryTrace; P09210; -.
DR   GeneWiki; GSTA2; -.
DR   GenomeRNAi; 2939; -.
DR   Pharos; P09210; Tbio.
DR   PRO; PR:P09210; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P09210; protein.
DR   Bgee; ENSG00000244067; Expressed in body of pancreas and 69 other cell types or tissues.
DR   ExpressionAtlas; P09210; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd03208; GST_C_Alpha; 1.
DR   CDD; cd03077; GST_N_Alpha; 1.
DR   FunFam; 1.20.1050.10:FF:000005; Glutathione S-transferase A1; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR050213; GST_superfamily.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF262; GLUTATHIONE S-TRANSFERASE A2; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Oxidoreductase; Peroxidase; Proteomics identification; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30115,
FT                   ECO:0000269|PubMed:8431482"
FT   CHAIN           2..222
FT                   /note="Glutathione S-transferase A2"
FT                   /id="PRO_0000185784"
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..207
FT                   /note="GST C-terminal"
FT   REGION          199..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:20083122"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:20083122"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:20083122"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:20083122"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   MOD_RES         4
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   VARIANT         110
FT                   /note="P -> S (2-fold decreased glutathione transferase
FT                   activity with 1-chloro-2,4-dinitrobenzene as substrate;
FT                   4-fold decreased glutathione peroxidase activity with
FT                   cumene hydroperoxide as substrate; dbSNP:rs2234951)"
FT                   /evidence="ECO:0000269|PubMed:15077012"
FT                   /id="VAR_014495"
FT   VARIANT         112
FT                   /note="S -> T (in dbSNP:rs2180314)"
FT                   /evidence="ECO:0000269|PubMed:11668220,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:3036131,
FT                   ECO:0007744|PubMed:24275569"
FT                   /id="VAR_012205"
FT   VARIANT         149
FT                   /note="V -> A (in dbSNP:rs2266631)"
FT                   /id="VAR_014496"
FT   VARIANT         210
FT                   /note="E -> A (in dbSNP:rs6577)"
FT                   /evidence="ECO:0000269|PubMed:11668220,
FT                   ECO:0000269|PubMed:1329668, ECO:0000269|PubMed:1497629"
FT                   /id="VAR_012206"
FT   CONFLICT        10..12
FT                   /note="SNI -> FNA (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="I -> T (in Ref. 3; CAA46642)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19
FT                   /note="I -> T (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="K -> R (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="T -> I (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:4ACS"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           17..25
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           86..108
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           117..127
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           128..132
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           133..143
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           155..170
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   TURN            172..177
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           179..190
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           192..197
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           204..208
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:2VCT"
FT   HELIX           217..221
FT                   /evidence="ECO:0007829|PDB:2VCT"
SQ   SEQUENCE   222 AA;  25664 MW;  2823565A693A30AC CRC64;
     MAEKPKLHYS NIRGRMESIR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI
     DGMKLVQTRA ILNYIASKYN LYGKDIKEKA LIDMYIEGIA DLGEMILLLP FSQPEEQDAK
     LALIQEKTKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL
     LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEESRKIF RF
//