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 24-JAN-2024, entry version 226. DE RecName: Full=Glutathione S-transferase A2; DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P10648}; 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; DE AltName: Full=GTH2; GN Name=GSTA2; 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 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), 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 [9] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) 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 [10] 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 [11] 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: Catalyzes the conjugation of glutathione to a large variety CC of electrophilic compounds. {ECO:0000250|UniProtKB:P10648}. 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:0000250|UniProtKB:P10648}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; CC Evidence={ECO:0000250|UniProtKB:P10648}; 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=11; IntAct=EBI-10196201, EBI-752440; CC P09210; Q7RTV2: GSTA5; NbExp=4; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_000846.4. DR RefSeq; XP_011512834.1; XM_011514532.2. 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=1-221. DR PDBsum; 1AGS; -. DR PDBsum; 2VCT; -. DR PDBsum; 2WJU; -. DR PDBsum; 4ACS; -. DR AlphaFoldDB; P09210; -. DR SMR; P09210; -. DR BioGRID; 109194; 10. DR IntAct; P09210; 5. 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 MaxQB; P09210; -. DR PaxDb; 9606-ENSP00000420168; -. DR PeptideAtlas; P09210; -. DR ProteomicsDB; 52206; -. DR Antibodypedia; 30929; 255 antibodies from 28 providers. DR DNASU; 2939; -. DR Ensembl; ENST00000493422.3; ENSP00000420168.1; ENSG00000244067.3. 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 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 neXtProt; NX_P09210; -. DR OpenTargets; ENSG00000244067; -. DR PharmGKB; PA29017; -. DR VEuPathDB; HostDB:ENSG00000244067; -. DR eggNOG; KOG1695; Eukaryota. DR GeneTree; ENSGT00940000164034; -. DR HOGENOM; CLU_039475_4_0_1; -. DR InParanoid; P09210; -. DR OMA; EMIMQLP; -. DR OrthoDB; 3412208at2759; -. DR PhylomeDB; P09210; -. DR TreeFam; TF105321; -. 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 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 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; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF107; 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; 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 Reference proteome; 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 207..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 (in dbSNP:rs2234951)" 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..130 FT /evidence="ECO:0007829|PDB:2VCT" FT HELIX 132..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 210..220 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 //