GSTP1_HUMAN
ID GSTP1_HUMAN Reviewed; 210 AA.
AC P09211; O00460; Q15690; Q5TZY3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 242.
DE RecName: Full=Glutathione S-transferase P {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000269|PubMed:1540159, ECO:0000269|PubMed:1567427, ECO:0000269|PubMed:8433974};
DE AltName: Full=GST class-pi;
DE AltName: Full=GSTP1-1;
GN Name=GSTP1 {ECO:0000312|HGNC:HGNC:4638}; Synonyms=FAEES3, GST3;
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].
RX PubMed=3664469;
RA Kano T., Sakai M., Muramatsu M.;
RT "Structure and expression of a human class pi glutathione S-transferase
RT messenger RNA.";
RL Cancer Res. 47:5626-5630(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3196325; DOI=10.1042/bj2550079;
RA Cowell I.G., Dixon K.H., Pemble S.E., Ketterer B., Taylor J.B.;
RT "The structure of the human glutathione S-transferase pi gene.";
RL Biochem. J. 255:79-83(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2542132; DOI=10.1016/0378-1119(89)90377-6;
RA Morrow C.S., Cowan K.H., Goldsmith M.E.;
RT "Structure of the human genomic glutathione S-transferase-pi gene.";
RL Gene 75:3-11(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2466554;
RA Moscow J.A., Fairchild C.R., Madden M.J., Ransom D.T., Wieand H.S.,
RA O'Brien E.E., Poplack D.G., Cossman J., Myers C.E., Cowan K.H.;
RT "Expression of anionic glutathione-S-transferase and P-glycoprotein genes
RT in human tissues and tumors.";
RL Cancer Res. 49:1422-1428(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bora P.S., Smith C., Lange L.G., Bora N.S., Jones C., Gerhard D.S.;
RT "Human fatty acid ethyl ester synthase III gene: genomic organization,
RT nucleotide sequence, genetic and chromosomal sublocalization.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-105 AND VAL-114.
RX PubMed=9092542; DOI=10.1074/jbc.272.15.10004;
RA Ali-Osman F., Akande O., Antoun G., Mao J.X., Buolamwini J.;
RT "Molecular cloning, characterization, and expression in Escherichia coli of
RT full-length cDNAs of three human glutathione S-transferase Pi gene
RT variants. Evidence for differential catalytic activity of the encoded
RT proteins.";
RL J. Biol. Chem. 272:10004-10012(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-105 AND VAL-114.
RG NIEHS SNPs program;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-105.
RC TISSUE=Urinary bladder;
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 [11]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=3979555; DOI=10.1016/0014-5793(85)80324-0;
RA Alin P., Mannervik B., Joernvall H.;
RT "Structural evidence for three different types of glutathione transferase
RT in human tissues.";
RL FEBS Lett. 182:319-322(1985).
RN [12]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M.,
RA Joernvall H.;
RT "Identification of three classes of cytosolic glutathione transferase
RT common to several mammalian species: correlation between structural data
RT and enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
RN [13]
RP PROTEIN SEQUENCE OF 2-14.
RX PubMed=3395118; DOI=10.1016/0003-9861(88)90564-4;
RA Singh S.V., Ahmad H., Kurosky A., Awasthi Y.C.;
RT "Purification and characterization of unique glutathione S-transferases
RT from human muscle.";
RL Arch. Biochem. Biophys. 264:13-22(1988).
RN [14]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP PROTEIN SEQUENCE OF 2-12; 20-71; 76-101; 104-141; 122-141 AND 192-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [16]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [17]
RP PRIMARY AND SECONDARY STRUCTURAL ANALYSES.
RX PubMed=2327795; DOI=10.1016/0003-9861(90)90277-6;
RA Ahmad H., Wilson D.E., Fritz R.R., Singh S.V., Medh R.D., Nagle G.T.,
RA Awasthi Y.C., Kurosky A.;
RT "Primary and secondary structural analyses of glutathione S-transferase pi
RT from human placenta.";
RL Arch. Biochem. Biophys. 278:398-408(1990).
RN [18]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-8.
RX PubMed=1567427; DOI=10.1016/0006-291x(92)91177-r;
RA Kong K.H., Takasu K., Inoue H., Takahashi K.;
RT "Tyrosine-7 in human class Pi glutathione S-transferase is important for
RT lowering the pKa of the thiol group of glutathione in the enzyme-
RT glutathione complex.";
RL Biochem. Biophys. Res. Commun. 184:194-197(1992).
RN [19]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-8.
RX PubMed=1540159; DOI=10.1016/0006-291x(92)91848-k;
RA Kong K.H., Nishida M., Inoue H., Takahashi K.;
RT "Tyrosine-7 is an essential residue for the catalytic activity of human
RT class PI glutathione S-transferase: chemical modification and site-directed
RT mutagenesis studies.";
RL Biochem. Biophys. Res. Commun. 182:1122-1129(1992).
RN [20]
RP MUTAGENESIS OF ASP-99, AND CATALYTIC ACTIVITY.
RX PubMed=8433974; DOI=10.1093/protein/6.1.93;
RA Kong K.-H., Inoue H., Takahashi K.;
RT "Site-directed mutagenesis study on the roles of evolutionally conserved
RT aspartic acid residues in human glutathione S-transferase P1-1.";
RL Protein Eng. 6:93-99(1993).
RN [21]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9084911; DOI=10.1021/tx9601770;
RA Bogaards J.J., Venekamp J.C., van Bladeren P.J.;
RT "Stereoselective conjugation of prostaglandin A2 and prostaglandin J2 with
RT glutathione, catalyzed by the human glutathione S-transferases A1-1, A2-2,
RT M1a-1a, and P1-1.";
RL Chem. Res. Toxicol. 10:310-317(1997).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=19269317; DOI=10.1016/j.freeradbiomed.2009.02.025;
RA Goto S., Kawakatsu M., Izumi S., Urata Y., Kageyama K., Ihara Y., Koji T.,
RA Kondo T.;
RT "Glutathione S-transferase pi localizes in mitochondria and protects
RT against oxidative stress.";
RL Free Radic. Biol. Med. 46:1392-1403(2009).
RN [23]
RP PHOSPHORYLATION AT TYR-4 AND TYR-199.
RX PubMed=19254954; DOI=10.1074/jbc.m808153200;
RA Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H., Bigner D.,
RA Ali-Osman F.;
RT "Tyrosine phosphorylation of the human glutathione S-transferase P1 by
RT epidermal growth factor receptor.";
RL J. Biol. Chem. 284:16979-16989(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY MASS
RP 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 [25]
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 [26]
RP CATALYTIC ACTIVITY.
RX PubMed=21046276; DOI=10.1007/s11745-010-3485-1;
RA Brunnstroem A., Hamberg M., Griffiths W.J., Mannervik B., Claesson H.E.;
RT "Biosynthesis of 14,15-hepoxilins in human l1236 Hodgkin lymphoma cells and
RT eosinophils.";
RL Lipids 46:69-79(2011).
RN [27]
RP FUNCTION, AND INTERACTION WITH CDK5.
RX PubMed=21668448; DOI=10.1111/j.1471-4159.2011.07343.x;
RA Sun K.H., Chang K.H., Clawson S., Ghosh S., Mirzaei H., Regnier F.,
RA Shah K.;
RT "Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase
RT activity.";
RL J. Neurochem. 118:902-914(2011).
RN [28]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [31]
RP IDENTIFICATION 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., 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 [32]
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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) COMPLEX WITH S-HEXYLGLUTATHIONE.
RX PubMed=1522586; DOI=10.1016/0022-2836(92)90692-d;
RA Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M., Federici G.,
RA Parker M.W.;
RT "Three-dimensional structure of class pi glutathione S-transferase from
RT human placenta in complex with S-hexylglutathione at 2.8-A resolution.";
RL J. Mol. Biol. 227:214-226(1992).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP ETHACRYNIC ACID AND GLUTATHIONE.
RX PubMed=9012673; DOI=10.1021/bi962316i;
RA Oakley A.J., Rossjohn J., Lo Bello M., Caccuri A.M., Federici G.,
RA Parker M.W.;
RT "The three-dimensional structure of the human Pi class glutathione
RT transferase P1-1 in complex with the inhibitor ethacrynic acid and its
RT glutathione conjugate.";
RL Biochemistry 36:576-585(1997).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND
RP INHIBITOR.
RX PubMed=9245401; DOI=10.1021/bi970805s;
RA Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B., Gilliland G.L.,
RA Zimniak P.;
RT "Structure and function of the xenobiotic substrate-binding site and
RT location of a potential non-substrate-binding site in a class pi
RT glutathione S-transferase.";
RL Biochemistry 36:9690-9702(1997).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE.
RX PubMed=9398518; DOI=10.1006/jmbi.1997.1364;
RA Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J.,
RA Villar H.O., Parker M.W.;
RT "The structures of human glutathione transferase P1-1 in complex with
RT glutathione and various inhibitors at high resolution.";
RL J. Mol. Biol. 274:84-100(1997).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=9351803; DOI=10.1016/s0969-2126(97)00281-5;
RA Prade L., Huber R., Manoharan T.H., Fahl W.E., Reuter W.;
RT "Structures of class pi glutathione S-transferase from human placenta in
RT complex with substrate, transition-state analogue and inhibitor.";
RL Structure 5:1287-1295(1997).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10441116; DOI=10.1021/bi990668u;
RA Ji X., Blaszczyk J., Xiao B., O'Donnell R., Hu X., Herzog C., Singh S.V.,
RA Zimniak P.;
RT "Structure and function of residue 104 and water molecules in the
RT xenobiotic substrate-binding site in human glutathione S-transferase P1-
RT 1.";
RL Biochemistry 38:10231-10238(1999).
RN [39]
RP STRUCTURE BY NMR.
RX PubMed=9485454; DOI=10.1021/bi971902o;
RA Nicotra M., Paci M., Sette M., Oakley A.J., Parker M.W., Lo Bello M.,
RA Caccuri A.M., Federici G., Ricci G.;
RT "Solution structure of glutathione bound to human glutathione transferase
RT P1-1: comparison of NMR measurements with the crystal structure.";
RL Biochemistry 37:3020-3027(1998).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=19396894; DOI=10.1002/anie.200900185;
RA Ang W.H., Parker L.J., De Luca A., Juillerat-Jeanneret L., Morton C.J.,
RA Lo Bello M., Parker M.W., Dyson P.J.;
RT "Rational design of an organometallic glutathione transferase inhibitor.";
RL Angew. Chem. Int. Ed. 48:3854-3857(2009).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 2-210 IN COMPLEX WITH
RP GLUTATHIONE.
RX PubMed=19808963; DOI=10.1158/0008-5472.can-09-1314;
RA Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F.,
RA Federici G., Caccuri A.M.;
RT "Structural basis for the binding of the anticancer compound 6-(7-nitro-
RT 2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases.";
RL Cancer Res. 69:8025-8034(2009).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Involved in the
CC formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation
CC of novel hepoxilin regioisomers (PubMed:21046276). Regulates negatively
CC CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
CC {ECO:0000269|PubMed:21046276, ECO:0000269|PubMed:21668448,
CC ECO:0000269|PubMed:9084911}.
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; Evidence={ECO:0000269|PubMed:1540159,
CC ECO:0000269|PubMed:1567427, ECO:0000269|PubMed:8433974};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133772;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133769;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000269|PubMed:21046276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000305|PubMed:21046276};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=395 uM for prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC KM=201 uM for prostaglandin J2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC Vmax=267 nmol/min/mg enzyme for the formation of the glutathione-S-
CC conjugate of prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC Vmax=105 nmol/min/mg enzyme for the formation of the glutathione-S-
CC conjugate of prostaglandin J2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC -!- SUBUNIT: Homodimer. Interacts with CDK5. {ECO:0000269|PubMed:21668448,
CC ECO:0000269|PubMed:9012673}.
CC -!- INTERACTION:
CC P09211; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-353467, EBI-10173507;
CC P09211; Q92624: APPBP2; NbExp=6; IntAct=EBI-353467, EBI-743771;
CC P09211; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-353467, EBI-3866279;
CC P09211; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-353467, EBI-3867333;
CC P09211; Q5TD97: FHL5; NbExp=3; IntAct=EBI-353467, EBI-750641;
CC P09211; P49639: HOXA1; NbExp=3; IntAct=EBI-353467, EBI-740785;
CC P09211; Q15323: KRT31; NbExp=6; IntAct=EBI-353467, EBI-948001;
CC P09211; Q14525: KRT33B; NbExp=3; IntAct=EBI-353467, EBI-1049638;
CC P09211; O76011: KRT34; NbExp=3; IntAct=EBI-353467, EBI-1047093;
CC P09211; P78385: KRT83; NbExp=3; IntAct=EBI-353467, EBI-10221390;
CC P09211; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-353467, EBI-11959885;
CC P09211; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-353467, EBI-11749135;
CC P09211; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-353467, EBI-10172290;
CC P09211; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-353467, EBI-10172052;
CC P09211; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-353467, EBI-9996449;
CC P09211; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-353467, EBI-3957694;
CC P09211; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-353467, EBI-11962084;
CC P09211; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-353467, EBI-18273118;
CC P09211; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-353467, EBI-11522433;
CC P09211; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-353467, EBI-945833;
CC P09211; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-353467, EBI-22310682;
CC P09211; P22735: TGM1; NbExp=3; IntAct=EBI-353467, EBI-2562368;
CC P09211; Q12933: TRAF2; NbExp=5; IntAct=EBI-353467, EBI-355744;
CC P09211; Q8N720: ZNF655; NbExp=3; IntAct=EBI-353467, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19269317}.
CC Mitochondrion {ECO:0000269|PubMed:19269317}. Nucleus
CC {ECO:0000269|PubMed:19269317}. Note=The 83 N-terminal amino acids
CC function as un uncleaved transit peptide, and arginine residues within
CC it are crucial for mitochondrial localization.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gstp1/";
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DR EMBL; X06547; CAA29794.1; -; mRNA.
DR EMBL; M24485; AAA56823.1; -; Genomic_DNA.
DR EMBL; X08058; CAA30847.1; -; Genomic_DNA.
DR EMBL; X08094; CAA30894.1; -; Genomic_DNA.
DR EMBL; X08095; CAA30894.1; JOINED; Genomic_DNA.
DR EMBL; X08096; CAA30894.1; JOINED; Genomic_DNA.
DR EMBL; X15480; CAA33508.1; -; mRNA.
DR EMBL; U12472; AAA64919.1; -; Genomic_DNA.
DR EMBL; U30897; AAC51280.1; -; mRNA.
DR EMBL; U62589; AAC51237.1; -; mRNA.
DR EMBL; U21689; AAC13869.1; -; Genomic_DNA.
DR EMBL; BT019949; AAV38752.1; -; mRNA.
DR EMBL; BT019950; AAV38753.1; -; mRNA.
DR EMBL; CR450361; CAG29357.1; -; mRNA.
DR EMBL; AY324387; AAP72967.1; -; Genomic_DNA.
DR EMBL; BC010915; AAH10915.1; -; mRNA.
DR CCDS; CCDS41679.1; -.
DR PIR; A41177; A41177.
DR PIR; JS0153; A37378.
DR RefSeq; NP_000843.1; NM_000852.3.
DR PDB; 10GS; X-ray; 2.20 A; A/B=2-210.
DR PDB; 11GS; X-ray; 2.30 A; A/B=1-210.
DR PDB; 12GS; X-ray; 2.10 A; A/B=1-210.
DR PDB; 13GS; X-ray; 1.90 A; A/B=1-210.
DR PDB; 14GS; X-ray; 2.80 A; A/B=1-210.
DR PDB; 16GS; X-ray; 1.90 A; A/B=1-210.
DR PDB; 17GS; X-ray; 1.90 A; A/B=1-210.
DR PDB; 18GS; X-ray; 1.90 A; A/B=1-210.
DR PDB; 19GS; X-ray; 1.90 A; A/B=2-210.
DR PDB; 1AQV; X-ray; 1.94 A; A/B=2-210.
DR PDB; 1AQW; X-ray; 1.80 A; A/B/C/D=2-210.
DR PDB; 1AQX; X-ray; 2.00 A; A/B/C/D=2-210.
DR PDB; 1EOG; X-ray; 2.10 A; A/B=3-210.
DR PDB; 1EOH; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-210.
DR PDB; 1GSS; X-ray; 2.80 A; A/B=2-210.
DR PDB; 1KBN; X-ray; 2.00 A; A/B=2-210.
DR PDB; 1LBK; X-ray; 1.86 A; A/B=2-203.
DR PDB; 1MD3; X-ray; 2.03 A; A/B=2-210.
DR PDB; 1MD4; X-ray; 2.10 A; A/B=2-210.
DR PDB; 1PGT; X-ray; 1.80 A; A/B=1-210.
DR PDB; 1PX6; X-ray; 2.10 A; A/B=2-210.
DR PDB; 1PX7; X-ray; 2.03 A; A/B=2-210.
DR PDB; 1ZGN; X-ray; 2.10 A; A/B=2-210.
DR PDB; 20GS; X-ray; 2.45 A; A/B=2-210.
DR PDB; 22GS; X-ray; 1.90 A; A/B=1-210.
DR PDB; 2A2R; X-ray; 1.40 A; A/B=1-210.
DR PDB; 2A2S; X-ray; 1.70 A; A/B=1-210.
DR PDB; 2GSS; X-ray; 1.90 A; A/B=2-210.
DR PDB; 2J9H; X-ray; 2.40 A; A/B=2-210.
DR PDB; 2PGT; X-ray; 1.90 A; A/B=1-210.
DR PDB; 3CSH; X-ray; 1.55 A; A/B=2-210.
DR PDB; 3CSI; X-ray; 1.90 A; A/B/C/D=2-210.
DR PDB; 3CSJ; X-ray; 1.90 A; A/B=2-210.
DR PDB; 3DD3; X-ray; 2.25 A; A/B=1-210.
DR PDB; 3DGQ; X-ray; 1.60 A; A/B=1-210.
DR PDB; 3GSS; X-ray; 1.90 A; A/B=2-210.
DR PDB; 3GUS; X-ray; 1.53 A; A/B=2-210.
DR PDB; 3HJM; X-ray; 2.10 A; A/B/C/D=2-210.
DR PDB; 3HJO; X-ray; 1.95 A; A/B=2-210.
DR PDB; 3HKR; X-ray; 1.80 A; A/B=2-210.
DR PDB; 3IE3; X-ray; 1.80 A; A/B=2-210.
DR PDB; 3KM6; X-ray; 2.10 A; A/B=2-210.
DR PDB; 3KMN; X-ray; 1.80 A; A/B=2-210.
DR PDB; 3KMO; X-ray; 2.60 A; A/B=2-210.
DR PDB; 3N9J; X-ray; 1.85 A; A/B=1-210.
DR PDB; 3PGT; X-ray; 2.14 A; A/B=1-210.
DR PDB; 4GSS; X-ray; 2.50 A; A/B=2-210.
DR PDB; 4PGT; X-ray; 2.10 A; A/B=1-210.
DR PDB; 5DAK; X-ray; 2.11 A; A/B=1-210.
DR PDB; 5DAL; X-ray; 1.50 A; A/B=1-210.
DR PDB; 5DCG; X-ray; 2.01 A; A/B=1-210.
DR PDB; 5DDL; X-ray; 1.98 A; A/B=1-210.
DR PDB; 5DJL; X-ray; 1.80 A; A/B=1-210.
DR PDB; 5DJM; X-ray; 1.90 A; A/B=1-210.
DR PDB; 5GSS; X-ray; 1.95 A; A/B=2-210.
DR PDB; 5J41; X-ray; 1.19 A; A/B=2-210.
DR PDB; 5JCW; X-ray; 1.95 A; A/B=1-210.
DR PDB; 5L6X; X-ray; 2.00 A; A/B=1-210.
DR PDB; 5X79; X-ray; 1.90 A; A/B=1-210.
DR PDB; 6AP9; X-ray; 1.55 A; A/B=1-210.
DR PDB; 6GSS; X-ray; 1.90 A; A/B=2-210.
DR PDB; 6LLX; X-ray; 1.58 A; A/B=1-210.
DR PDB; 6Y1E; X-ray; 1.40 A; A/B/C/D=1-210.
DR PDB; 7BIA; X-ray; 1.73 A; A/B=1-210.
DR PDB; 7GSS; X-ray; 2.20 A; A/B=2-210.
DR PDB; 8GSS; X-ray; 1.90 A; A/B/C=2-210.
DR PDB; 9GSS; X-ray; 1.97 A; A/B=2-210.
DR PDBsum; 10GS; -.
DR PDBsum; 11GS; -.
DR PDBsum; 12GS; -.
DR PDBsum; 13GS; -.
DR PDBsum; 14GS; -.
DR PDBsum; 16GS; -.
DR PDBsum; 17GS; -.
DR PDBsum; 18GS; -.
DR PDBsum; 19GS; -.
DR PDBsum; 1AQV; -.
DR PDBsum; 1AQW; -.
DR PDBsum; 1AQX; -.
DR PDBsum; 1EOG; -.
DR PDBsum; 1EOH; -.
DR PDBsum; 1GSS; -.
DR PDBsum; 1KBN; -.
DR PDBsum; 1LBK; -.
DR PDBsum; 1MD3; -.
DR PDBsum; 1MD4; -.
DR PDBsum; 1PGT; -.
DR PDBsum; 1PX6; -.
DR PDBsum; 1PX7; -.
DR PDBsum; 1ZGN; -.
DR PDBsum; 20GS; -.
DR PDBsum; 22GS; -.
DR PDBsum; 2A2R; -.
DR PDBsum; 2A2S; -.
DR PDBsum; 2GSS; -.
DR PDBsum; 2J9H; -.
DR PDBsum; 2PGT; -.
DR PDBsum; 3CSH; -.
DR PDBsum; 3CSI; -.
DR PDBsum; 3CSJ; -.
DR PDBsum; 3DD3; -.
DR PDBsum; 3DGQ; -.
DR PDBsum; 3GSS; -.
DR PDBsum; 3GUS; -.
DR PDBsum; 3HJM; -.
DR PDBsum; 3HJO; -.
DR PDBsum; 3HKR; -.
DR PDBsum; 3IE3; -.
DR PDBsum; 3KM6; -.
DR PDBsum; 3KMN; -.
DR PDBsum; 3KMO; -.
DR PDBsum; 3N9J; -.
DR PDBsum; 3PGT; -.
DR PDBsum; 4GSS; -.
DR PDBsum; 4PGT; -.
DR PDBsum; 5DAK; -.
DR PDBsum; 5DAL; -.
DR PDBsum; 5DCG; -.
DR PDBsum; 5DDL; -.
DR PDBsum; 5DJL; -.
DR PDBsum; 5DJM; -.
DR PDBsum; 5GSS; -.
DR PDBsum; 5J41; -.
DR PDBsum; 5JCW; -.
DR PDBsum; 5L6X; -.
DR PDBsum; 5X79; -.
DR PDBsum; 6AP9; -.
DR PDBsum; 6GSS; -.
DR PDBsum; 6LLX; -.
DR PDBsum; 6Y1E; -.
DR PDBsum; 7BIA; -.
DR PDBsum; 7GSS; -.
DR PDBsum; 8GSS; -.
DR PDBsum; 9GSS; -.
DR AlphaFoldDB; P09211; -.
DR SMR; P09211; -.
DR BioGRID; 109205; 162.
DR IntAct; P09211; 78.
DR MINT; P09211; -.
DR STRING; 9606.ENSP00000381607; -.
DR BindingDB; P09211; -.
DR ChEMBL; CHEMBL3902; -.
DR DrugBank; DB01834; (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB01008; Busulfan.
DR DrugBank; DB04972; Canfosfamide.
DR DrugBank; DB00958; Carboplatin.
DR DrugBank; DB00291; Chlorambucil.
DR DrugBank; DB02633; Cibacron Blue.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB01242; Clomipramine.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB11672; Curcumin.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR DrugBank; DB03619; Deoxycholic acid.
DR DrugBank; DB11831; Dinitrochlorobenzene.
DR DrugBank; DB00903; Etacrynic acid.
DR DrugBank; DB00773; Etoposide.
DR DrugBank; DB06246; Exisulind.
DR DrugBank; DB05460; Ezatiostat.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR DrugBank; DB03003; Glutathione sulfonic acid.
DR DrugBank; DB13014; Hypericin.
DR DrugBank; DB00526; Oxaliplatin.
DR DrugBank; DB08370; S-(4-BROMOBENZYL)CYSTEINE.
DR DrugBank; DB03686; S-(4-nitrobenzyl)glutathione.
DR DrugBank; DB04132; S-Hexylglutathione.
DR DrugBank; DB01915; S-Hydroxycysteine.
DR DrugBank; DB07849; S-NONYL-CYSTEINE.
DR DrugBank; DB00197; Troglitazone.
DR DrugBank; DB00163; Vitamin E.
DR DrugCentral; P09211; -.
DR SwissLipids; SLP:000001615; -.
DR GlyGen; P09211; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09211; -.
DR MetOSite; P09211; -.
DR PhosphoSitePlus; P09211; -.
DR SwissPalm; P09211; -.
DR BioMuta; GSTP1; -.
DR DOSAC-COBS-2DPAGE; P09211; -.
DR OGP; P09211; -.
DR REPRODUCTION-2DPAGE; IPI00219757; -.
DR SWISS-2DPAGE; P09211; -.
DR UCD-2DPAGE; P09211; -.
DR CPTAC; CPTAC-1412; -.
DR CPTAC; CPTAC-1413; -.
DR CPTAC; CPTAC-1414; -.
DR CPTAC; CPTAC-1415; -.
DR CPTAC; CPTAC-212; -.
DR CPTAC; CPTAC-213; -.
DR CPTAC; CPTAC-3231; -.
DR CPTAC; CPTAC-701; -.
DR EPD; P09211; -.
DR jPOST; P09211; -.
DR MassIVE; P09211; -.
DR PaxDb; P09211; -.
DR PeptideAtlas; P09211; -.
DR PRIDE; P09211; -.
DR ProteomicsDB; 52207; -.
DR TopDownProteomics; P09211; -.
DR ABCD; P09211; 1 sequenced antibody.
DR Antibodypedia; 7688; 901 antibodies from 47 providers.
DR CPTC; P09211; 1 antibody.
DR DNASU; 2950; -.
DR Ensembl; ENST00000398606.10; ENSP00000381607.3; ENSG00000084207.18.
DR GeneID; 2950; -.
DR KEGG; hsa:2950; -.
DR MANE-Select; ENST00000398606.10; ENSP00000381607.3; NM_000852.4; NP_000843.1.
DR CTD; 2950; -.
DR DisGeNET; 2950; -.
DR GeneCards; GSTP1; -.
DR HGNC; HGNC:4638; GSTP1.
DR HPA; ENSG00000084207; Tissue enhanced (esophagus).
DR MIM; 134660; gene.
DR neXtProt; NX_P09211; -.
DR OpenTargets; ENSG00000084207; -.
DR PharmGKB; PA29028; -.
DR VEuPathDB; HostDB:ENSG00000084207; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000162460; -.
DR InParanoid; P09211; -.
DR OMA; IKPKMIF; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P09211; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P09211; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; P09211; -.
DR SignaLink; P09211; -.
DR SIGNOR; P09211; -.
DR BioGRID-ORCS; 2950; 27 hits in 1075 CRISPR screens.
DR ChiTaRS; GSTP1; human.
DR EvolutionaryTrace; P09211; -.
DR GeneWiki; GSTP1; -.
DR GenomeRNAi; 2950; -.
DR Pharos; P09211; Tchem.
DR PRO; PR:P09211; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P09211; protein.
DR Bgee; ENSG00000084207; Expressed in lower esophagus mucosa and 204 other tissues.
DR ExpressionAtlas; P09211; baseline and differential.
DR Genevisible; P09211; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0097057; C:TRAF2-GSTP1 complex; IDA:BHF-UCL.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0035731; F:dinitrosyl-iron complex binding; IDA:BHF-UCL.
DR GO; GO:0005504; F:fatty acid binding; IPI:BHF-UCL.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0008432; F:JUN kinase binding; ISS:BHF-UCL.
DR GO; GO:0019207; F:kinase regulator activity; ISS:BHF-UCL.
DR GO; GO:0070026; F:nitric oxide binding; NAS:BHF-UCL.
DR GO; GO:0035730; F:S-nitrosoglutathione binding; IDA:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:BHF-UCL.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; NAS:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0009890; P:negative regulation of biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:BHF-UCL.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0070664; P:negative regulation of leukocyte proliferation; ISS:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; NAS:BHF-UCL.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:BHF-UCL.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IC:BHF-UCL.
DR GO; GO:0035732; P:nitric oxide storage; NAS:BHF-UCL.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:BHF-UCL.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0000302; P:response to reactive oxygen species; ISS:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
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; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:3395118, ECO:0000269|PubMed:3864155,
FT ECO:0000269|PubMed:3979555, ECO:0000269|Ref.15,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..210
FT /note="Glutathione S-transferase P"
FT /id="PRO_0000185900"
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT DOMAIN 83..204
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:1522586,
FT ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963,
FT ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401,
FT ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
FT BINDING 14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:1522586,
FT ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963,
FT ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401,
FT ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:1522586,
FT ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963,
FT ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401,
FT ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
FT BINDING 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:1522586,
FT ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963,
FT ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401,
FT ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
FT BINDING 52..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:1522586,
FT ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963,
FT ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401,
FT ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:1522586,
FT ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963,
FT ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401,
FT ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
FT MOD_RES 4
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:19254954"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19157"
FT MOD_RES 116
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19157"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 199
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:19254954"
FT VARIANT 105
FT /note="I -> V (in allele GSTP1*B and allele GSTP1*C;
FT dbSNP:rs1695)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9092542, ECO:0000269|Ref.9"
FT /id="VAR_014499"
FT VARIANT 114
FT /note="A -> V (in allele GSTP1*C; dbSNP:rs1138272)"
FT /evidence="ECO:0000269|PubMed:9092542, ECO:0000269|Ref.9"
FT /id="VAR_014500"
FT VARIANT 169
FT /note="G -> D (in dbSNP:rs41462048)"
FT /id="VAR_049493"
FT MUTAGEN 8
FT /note="Y->F: Reduces catalytic activity about 50-fold."
FT /evidence="ECO:0000269|PubMed:1540159,
FT ECO:0000269|PubMed:1567427"
FT MUTAGEN 99
FT /note="D->A: Reduces affinity for glutathione. Slightly
FT reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:8433974"
FT CONFLICT 186
FT /note="A -> P (in Ref. 2; CAA30894)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5J41"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:5J41"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:5J41"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3KMN"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5J41"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 84..110
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 112..135
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5J41"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5JCW"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:5J41"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:5J41"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5J41"
SQ SEQUENCE 210 AA; 23356 MW; 409E33FFAA338396 CRC64;
MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVTVETWQ EGSLKASCLY GQLPKFQDGD
LTLYQSNTIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL RCKYISLIYT NYEAGKDDYV
KALPGQLKPF ETLLSQNQGG KTFIVGDQIS FADYNLLDLL LIHEVLAPGC LDAFPLLSAY
VGRLSARPKL KAFLASPEYV NLPINGNGKQ
