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Glutathione S-transferase A2 (EC 2.5.1.18) (GST HA subunit 2) (GST class-alpha member 2) (GST-gamma) (GSTA2-2) (GTH2)

 GSTA2_HUMAN             Reviewed;         222 AA.
P09210; Q12759; Q16491; Q9NTY6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 4.
27-SEP-2017, entry version 189.
RecName: Full=Glutathione S-transferase A2;
EC=2.5.1.18;
AltName: Full=GST HA subunit 2;
AltName: Full=GST class-alpha member 2;
AltName: Full=GST-gamma;
AltName: Full=GSTA2-2;
AltName: Full=GTH2;
Name=GSTA2; Synonyms=GST2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-112.
PubMed=3036131; DOI=10.1016/0006-291X(87)91345-3;
Rhoads D.M., Zarlengo R.P., Tu C.-P.D.;
"The basic glutathione S-transferases from human livers are products
of separate genes.";
Biochem. Biophys. Res. Commun. 145:474-481(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-210.
TISSUE=Liver;
PubMed=1329668; DOI=10.1016/0003-9861(92)90475-C;
Rohrdanz E., Nguyen T., Pickett C.B.;
"Isolation and characterization of the human glutathione S-transferase
A2 subunit gene.";
Arch. Biochem. Biophys. 298:747-752(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-210.
TISSUE=Blood;
PubMed=1497629; DOI=10.1042/bj2850925;
Klone A., Hussnatter R., Sies H.;
"Cloning, sequencing and characterization of the human alpha
glutathione S-transferase gene corresponding to the cDNA clone
pGTH2.";
Biochem. J. 285:925-928(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-112.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-170; 188-195 AND 209-222.
PubMed=8431482; DOI=10.1016/0167-4838(93)90234-I;
Ahmad H., Singhal S.S., Saxena M., Awasthi Y.C.;
"Characterization of two novel subunits of the alpha-class glutathione
S-transferases of human liver.";
Biochim. Biophys. Acta 1161:333-336(1993).
[7]
PROTEIN SEQUENCE OF 63-155 AND 208-222.
PubMed=2604726; DOI=10.1042/bj2640437;
Hayes J.D., Kerr L.A., Cronshaw A.D.;
"Evidence that glutathione S-transferases B1B1 and B2B2 are the
products of separate genes and that their expression in human liver is
subject to inter-individual variation. Molecular relationships between
the B1 and B2 subunits and other alpha class glutathione S-
transferases.";
Biochem. J. 264:437-445(1989).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
PubMed=7892174; DOI=10.1002/prot.340200306;
Zeng K., Rose J.P., Chen H.C., Strickland C.L., Tu C.P., Wang B.C.;
"A surface mutant (G82R) of a human alpha-glutathione S-transferase
shows decreased thermal stability and a new mode of molecular
association in the crystal.";
Proteins 20:259-263(1994).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
DELTA5-ANDROSTENE-3-17-DIONE, AND SUBUNIT.
PubMed=20083122; DOI=10.1016/j.jmb.2010.01.023;
Tars K., Olin B., Mannervik B.;
"Structural basis for featuring of steroid isomerase activity in alpha
class glutathione transferases.";
J. Mol. Biol. 397:332-340(2010).
[10]
VARIANTS THR-112 AND ALA-210.
PubMed=11668220; DOI=10.1097/00008571-200110000-00007;
Tetlow N., Liu D., Board P.;
"Polymorphism of human alpha class glutathione transferases.";
Pharmacogenetics 11:609-617(2001).
[11]
VARIANT [LARGE SCALE ANALYSIS] THR-112, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
{ECO:0000269|PubMed:20083122, ECO:0000269|PubMed:7892174}.
-!- INTERACTION:
O15217:GSTA4; NbExp=8; IntAct=EBI-10196201, EBI-752440;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Liver.
-!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
{ECO:0000305}.
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EMBL; M16594; AAA52616.1; -; mRNA.
EMBL; S45640; AAB23672.1; -; Genomic_DNA.
EMBL; S45627; AAB23672.1; JOINED; Genomic_DNA.
EMBL; S45629; AAB23672.1; JOINED; Genomic_DNA.
EMBL; S45636; AAB23672.1; JOINED; Genomic_DNA.
EMBL; S45637; AAB23672.1; JOINED; Genomic_DNA.
EMBL; S45639; AAB23672.1; JOINED; Genomic_DNA.
EMBL; X65727; CAA46642.1; -; Genomic_DNA.
EMBL; X65728; CAA46642.1; JOINED; Genomic_DNA.
EMBL; X65729; CAA46642.1; JOINED; Genomic_DNA.
EMBL; X65730; CAA46642.1; JOINED; Genomic_DNA.
EMBL; X65731; CAA46642.1; JOINED; Genomic_DNA.
EMBL; X65732; CAA46642.1; JOINED; Genomic_DNA.
EMBL; AL109918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002895; AAH02895.1; -; mRNA.
CCDS; CCDS4944.1; -.
PIR; S24330; S24330.
PIR; S29658; S29658.
RefSeq; NP_000837.3; NM_000846.4.
RefSeq; XP_011512834.1; XM_011514532.2.
UniGene; Hs.94107; -.
PDB; 1AGS; X-ray; 2.50 A; A/B=2-222.
PDB; 2VCT; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-222.
PDB; 2WJU; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-222.
PDB; 4ACS; X-ray; 2.10 A; A/B/C/D=1-221.
PDBsum; 1AGS; -.
PDBsum; 2VCT; -.
PDBsum; 2WJU; -.
PDBsum; 4ACS; -.
ProteinModelPortal; P09210; -.
SMR; P09210; -.
BioGrid; 109194; 5.
IntAct; P09210; 1.
STRING; 9606.ENSP00000420168; -.
BindingDB; P09210; -.
ChEMBL; CHEMBL2241; -.
DrugBank; DB00993; Azathioprine.
DrugBank; DB01008; Busulfan.
DrugBank; DB00608; Chloroquine.
DrugBank; DB00636; Clofibrate.
DrugBank; DB00903; Etacrynic acid.
DrugBank; DB00143; Glutathione.
DrugBank; DB00163; Vitamin E.
iPTMnet; P09210; -.
PhosphoSitePlus; P09210; -.
BioMuta; GSTA2; -.
DMDM; 126302551; -.
REPRODUCTION-2DPAGE; IPI00745233; -.
EPD; P09210; -.
MaxQB; P09210; -.
PaxDb; P09210; -.
PeptideAtlas; P09210; -.
PRIDE; P09210; -.
DNASU; 2939; -.
Ensembl; ENST00000493422; ENSP00000420168; ENSG00000244067.
GeneID; 2939; -.
KEGG; hsa:2939; -.
UCSC; uc003pay.4; human.
CTD; 2939; -.
DisGeNET; 2939; -.
EuPathDB; HostDB:ENSG00000244067.2; -.
GeneCards; GSTA2; -.
H-InvDB; HIX0200871; -.
HGNC; HGNC:4627; GSTA2.
HPA; HPA004342; -.
HPA; HPA048934; -.
HPA; HPA053817; -.
MIM; 138360; gene.
neXtProt; NX_P09210; -.
OpenTargets; ENSG00000244067; -.
PharmGKB; PA29017; -.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00670000097856; -.
HOGENOM; HOG000115734; -.
HOVERGEN; HBG053749; -.
InParanoid; P09210; -.
KO; K00799; -.
OMA; CPPAEKD; -.
OrthoDB; EOG091G0O3D; -.
PhylomeDB; P09210; -.
TreeFam; TF105321; -.
BioCyc; MetaCyc:HS01846-MONOMER; -.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SABIO-RK; P09210; -.
EvolutionaryTrace; P09210; -.
GeneWiki; GSTA2; -.
GenomeRNAi; 2939; -.
PRO; PR:P09210; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000244067; -.
CleanEx; HS_GSTA2; -.
ExpressionAtlas; P09210; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR003080; GST_alpha.
InterPro; IPR004046; GST_C.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01266; GSTRNSFRASEA.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Polymorphism; Reference proteome;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P30115,
ECO:0000269|PubMed:8431482}.
CHAIN 2 222 Glutathione S-transferase A2.
/FTId=PRO_0000185784.
DOMAIN 3 83 GST N-terminal.
DOMAIN 85 207 GST C-terminal.
REGION 54 55 Glutathione binding.
{ECO:0000269|PubMed:20083122}.
REGION 67 68 Glutathione binding.
{ECO:0000269|PubMed:20083122}.
BINDING 9 9 Glutathione.
{ECO:0000269|PubMed:20083122}.
BINDING 45 45 Glutathione.
{ECO:0000269|PubMed:20083122}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P30115}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P30115}.
VARIANT 110 110 P -> S (in dbSNP:rs2234951).
/FTId=VAR_014495.
VARIANT 112 112 S -> T (in dbSNP:rs2180314).
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11668220,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3036131}.
/FTId=VAR_012205.
VARIANT 149 149 V -> A (in dbSNP:rs2266631).
/FTId=VAR_014496.
VARIANT 210 210 E -> A (in dbSNP:rs6577).
{ECO:0000269|PubMed:11668220,
ECO:0000269|PubMed:1329668,
ECO:0000269|PubMed:1497629}.
/FTId=VAR_012206.
CONFLICT 10 12 SNI -> FNA (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 12 12 I -> T (in Ref. 3; CAA46642).
{ECO:0000305}.
CONFLICT 19 19 I -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 K -> R (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 128 128 T -> I (in Ref. 6; AA sequence).
{ECO:0000305}.
STRAND 6 9 {ECO:0000244|PDB:2VCT}.
STRAND 11 13 {ECO:0000244|PDB:4ACS}.
TURN 14 16 {ECO:0000244|PDB:2VCT}.
HELIX 17 25 {ECO:0000244|PDB:2VCT}.
STRAND 31 34 {ECO:0000244|PDB:2VCT}.
HELIX 38 46 {ECO:0000244|PDB:2VCT}.
STRAND 57 60 {ECO:0000244|PDB:2VCT}.
STRAND 63 67 {ECO:0000244|PDB:2VCT}.
HELIX 68 78 {ECO:0000244|PDB:2VCT}.
HELIX 86 108 {ECO:0000244|PDB:2VCT}.
HELIX 109 111 {ECO:0000244|PDB:2VCT}.
TURN 114 116 {ECO:0000244|PDB:2VCT}.
HELIX 117 130 {ECO:0000244|PDB:2VCT}.
HELIX 132 143 {ECO:0000244|PDB:2VCT}.
STRAND 146 149 {ECO:0000244|PDB:2VCT}.
HELIX 155 170 {ECO:0000244|PDB:2VCT}.
TURN 172 177 {ECO:0000244|PDB:2VCT}.
HELIX 179 190 {ECO:0000244|PDB:2VCT}.
HELIX 192 197 {ECO:0000244|PDB:2VCT}.
HELIX 210 220 {ECO:0000244|PDB:2VCT}.
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


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