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 27-MAR-2024, entry version 251. 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 RT P1-1."; 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- RT nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s- RT 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). Negatively regulates 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 CC glutathione-S-conjugate of prostaglandin A2 (at pH 7.0 and 37 degrees CC Celsius) {ECO:0000269|PubMed:9084911}; CC Vmax=105 nmol/min/mg enzyme for the formation of the CC glutathione-S-conjugate of prostaglandin J2 (at pH 7.0 and 37 degrees CC Celsius) {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; Q9NRD0: FBXO8; NbExp=3; IntAct=EBI-353467, EBI-11615366; 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/"; 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; 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; 7XBA; X-ray; 2.83 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; 7XBA; -. DR PDBsum; 8GSS; -. DR PDBsum; 9GSS; -. DR AlphaFoldDB; P09211; -. DR SMR; P09211; -. DR BioGRID; 109205; 197. DR IntAct; P09211; 81. 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; DB00321; Amitriptyline. 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 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; 9606-ENSP00000381607; -. DR PeptideAtlas; P09211; -. DR PRIDE; P09211; -. DR ProteomicsDB; 52207; -. DR Pumba; P09211; -. DR TopDownProteomics; P09211; -. DR ABCD; P09211; 1 sequenced antibody. DR Antibodypedia; 7688; 973 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 AGR; HGNC:4638; -. DR CTD; 2950; -. DR DisGeNET; 2950; -. DR GeneCards; GSTP1; -. DR HGNC; HGNC:4638; GSTP1. DR HPA; ENSG00000084207; Tissue enhanced (choroid). 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; 5302341at2759; -. 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; 28 hits in 1156 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 206 other cell types or tissues. DR ExpressionAtlas; P09211; baseline and differential. 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:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS: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: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 CDD; cd03210; GST_C_Pi; 1. DR CDD; cd03076; GST_N_Pi; 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; IPR004046; GST_C. DR InterPro; IPR003082; GST_pi. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01268; GSTRNSFRASEP. 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. DR SWISS-2DPAGE; P09211; -. DR UCD-2DPAGE; P09211; -. DR Genevisible; P09211; HS. 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 //