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Glutathione S-transferase P (EC 2.5.1.18) (GST class-pi) (GSTP1-1)

 GSTP1_HUMAN             Reviewed;         210 AA.
P09211; O00460; Q15690; Q5TZY3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 210.
RecName: Full=Glutathione S-transferase P;
EC=2.5.1.18;
AltName: Full=GST class-pi;
AltName: Full=GSTP1-1;
Name=GSTP1; Synonyms=FAEES3, GST3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3664469;
Kano T., Sakai M., Muramatsu M.;
"Structure and expression of a human class pi glutathione S-
transferase messenger RNA.";
Cancer Res. 47:5626-5630(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3196325; DOI=10.1042/bj2550079;
Cowell I.G., Dixon K.H., Pemble S.E., Ketterer B., Taylor J.B.;
"The structure of the human glutathione S-transferase pi gene.";
Biochem. J. 255:79-83(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2542132; DOI=10.1016/0378-1119(89)90377-6;
Morrow C.S., Cowan K.H., Goldsmith M.E.;
"Structure of the human genomic glutathione S-transferase-pi gene.";
Gene 75:3-11(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2466554;
Moscow J.A., Fairchild C.R., Madden M.J., Ransom D.T., Wieand H.S.,
O'Brien E.E., Poplack D.G., Cossman J., Myers C.E., Cowan K.H.;
"Expression of anionic glutathione-S-transferase and P-glycoprotein
genes in human tissues and tumors.";
Cancer Res. 49:1422-1428(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Bora P.S., Smith C., Lange L.G., Bora N.S., Jones C., Gerhard D.S.;
"Human fatty acid ethyl ester synthase III gene: genomic organization,
nucleotide sequence, genetic and chromosomal sublocalization.";
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-105 AND VAL-114.
PubMed=9092542; DOI=10.1074/jbc.272.15.10004;
Ali-Osman F., Akande O., Antoun G., Mao J.X., Buolamwini J.;
"Molecular cloning, characterization, and expression in Escherichia
coli of full-length cDNAs of three human glutathione S-transferase Pi
gene variants. Evidence for differential catalytic activity of the
encoded proteins.";
J. Biol. Chem. 272:10004-10012(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-105 AND VAL-114.
NIEHS SNPs program;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-105.
TISSUE=Urinary bladder;
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).
[11]
PROTEIN SEQUENCE OF 2-24.
PubMed=3979555; DOI=10.1016/0014-5793(85)80324-0;
Alin P., Mannervik B., Joernvall H.;
"Structural evidence for three different types of glutathione
transferase in human tissues.";
FEBS Lett. 182:319-322(1985).
[12]
PROTEIN SEQUENCE OF 2-24.
PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K.,
Warholm M., Joernvall H.;
"Identification of three classes of cytosolic glutathione transferase
common to several mammalian species: correlation between structural
data and enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
[13]
PROTEIN SEQUENCE OF 2-14.
PubMed=3395118; DOI=10.1016/0003-9861(88)90564-4;
Singh S.V., Ahmad H., Kurosky A., Awasthi Y.C.;
"Purification and characterization of unique glutathione S-
transferases from human muscle.";
Arch. Biochem. Biophys. 264:13-22(1988).
[14]
PROTEIN SEQUENCE OF 2-12.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[15]
PROTEIN SEQUENCE OF 2-12; 20-71; 76-101; 104-141; 122-141 AND 192-209,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[16]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[17]
PRIMARY AND SECONDARY STRUCTURAL ANALYZES.
PubMed=2327795; DOI=10.1016/0003-9861(90)90277-6;
Ahmad H., Wilson D.E., Fritz R.R., Singh S.V., Medh R.D., Nagle G.T.,
Awasthi Y.C., Kurosky A.;
"Primary and secondary structural analyses of glutathione S-
transferase pi from human placenta.";
Arch. Biochem. Biophys. 278:398-408(1990).
[18]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-8.
PubMed=1567427; DOI=10.1016/0006-291X(92)91177-R;
Kong K.H., Takasu K., Inoue H., Takahashi K.;
"Tyrosine-7 in human class Pi glutathione S-transferase is important
for lowering the pKa of the thiol group of glutathione in the enzyme-
glutathione complex.";
Biochem. Biophys. Res. Commun. 184:194-197(1992).
[19]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-8.
PubMed=1540159; DOI=10.1016/0006-291X(92)91848-K;
Kong K.H., Nishida M., Inoue H., Takahashi K.;
"Tyrosine-7 is an essential residue for the catalytic activity of
human class PI glutathione S-transferase: chemical modification and
site-directed mutagenesis studies.";
Biochem. Biophys. Res. Commun. 182:1122-1129(1992).
[20]
MUTAGENESIS OF ASP-99, AND CATALYTIC ACTIVITY.
PubMed=8433974; DOI=10.1093/protein/6.1.93;
Kong K.-H., Inoue H., Takahashi K.;
"Site-directed mutagenesis study on the roles of evolutionally
conserved aspartic acid residues in human glutathione S-transferase
P1-1.";
Protein Eng. 6:93-99(1993).
[21]
SUBCELLULAR LOCATION.
PubMed=19269317; DOI=10.1016/j.freeradbiomed.2009.02.025;
Goto S., Kawakatsu M., Izumi S., Urata Y., Kageyama K., Ihara Y.,
Koji T., Kondo T.;
"Glutathione S-transferase pi localizes in mitochondria and protects
against oxidative stress.";
Free Radic. Biol. Med. 46:1392-1403(2009).
[22]
PHOSPHORYLATION AT TYR-4 AND TYR-199.
PubMed=19254954; DOI=10.1074/jbc.M808153200;
Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H.,
Bigner D., Ali-Osman F.;
"Tyrosine phosphorylation of the human glutathione S-transferase P1 by
epidermal growth factor receptor.";
J. Biol. Chem. 284:16979-16989(2009).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
FUNCTION, AND INTERACTION WITH CDK5.
PubMed=21668448; DOI=10.1111/j.1471-4159.2011.07343.x;
Sun K.H., Chang K.H., Clawson S., Ghosh S., Mirzaei H., Regnier F.,
Shah K.;
"Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase
activity.";
J. Neurochem. 118:902-914(2011).
[26]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
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).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[31]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) COMPLEX WITH S-HEXYLGLUTATHIONE.
PubMed=1522586; DOI=10.1016/0022-2836(92)90692-D;
Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M.,
Federici G., Parker M.W.;
"Three-dimensional structure of class pi glutathione S-transferase
from human placenta in complex with S-hexylglutathione at 2.8-A
resolution.";
J. Mol. Biol. 227:214-226(1992).
[32]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
ETHACRYNIC ACID AND GLUTATHIONE.
PubMed=9012673; DOI=10.1021/bi962316i;
Oakley A.J., Rossjohn J., Lo Bello M., Caccuri A.M., Federici G.,
Parker M.W.;
"The three-dimensional structure of the human Pi class glutathione
transferase P1-1 in complex with the inhibitor ethacrynic acid and its
glutathione conjugate.";
Biochemistry 36:576-585(1997).
[33]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
AND INHIBITOR.
PubMed=9245401; DOI=10.1021/bi970805s;
Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B.,
Gilliland G.L., Zimniak P.;
"Structure and function of the xenobiotic substrate-binding site and
location of a potential non-substrate-binding site in a class pi
glutathione S-transferase.";
Biochemistry 36:9690-9702(1997).
[34]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE.
PubMed=9398518; DOI=10.1006/jmbi.1997.1364;
Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J.,
Villar H.O., Parker M.W.;
"The structures of human glutathione transferase P1-1 in complex with
glutathione and various inhibitors at high resolution.";
J. Mol. Biol. 274:84-100(1997).
[35]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
PubMed=9351803; DOI=10.1016/S0969-2126(97)00281-5;
Prade L., Huber R., Manoharan T.H., Fahl W.E., Reuter W.;
"Structures of class pi glutathione S-transferase from human placenta
in complex with substrate, transition-state analogue and inhibitor.";
Structure 5:1287-1295(1997).
[36]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=10441116; DOI=10.1021/bi990668u;
Ji X., Blaszczyk J., Xiao B., O'Donnell R., Hu X., Herzog C.,
Singh S.V., Zimniak P.;
"Structure and function of residue 104 and water molecules in the
xenobiotic substrate-binding site in human glutathione S-transferase
P1-1.";
Biochemistry 38:10231-10238(1999).
[37]
STRUCTURE BY NMR.
PubMed=9485454; DOI=10.1021/bi971902o;
Nicotra M., Paci M., Sette M., Oakley A.J., Parker M.W., Lo Bello M.,
Caccuri A.M., Federici G., Ricci G.;
"Solution structure of glutathione bound to human glutathione
transferase P1-1: comparison of NMR measurements with the crystal
structure.";
Biochemistry 37:3020-3027(1998).
[38]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
PubMed=19396894; DOI=10.1002/anie.200900185;
Ang W.H., Parker L.J., De Luca A., Juillerat-Jeanneret L.,
Morton C.J., Lo Bello M., Parker M.W., Dyson P.J.;
"Rational design of an organometallic glutathione transferase
inhibitor.";
Angew. Chem. Int. Ed. 48:3854-3857(2009).
[39]
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 2-210 IN COMPLEX WITH
GLUTATHIONE.
PubMed=19808963; DOI=10.1158/0008-5472.CAN-09-1314;
Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F.,
Federici G., Caccuri A.M.;
"Structural basis for the binding of the anticancer compound 6-(7-
nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-
transferases.";
Cancer Res. 69:8025-8034(2009).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. Regulates
negatively CDK5 activity via p25/p35 translocation to prevent
neurodegeneration. {ECO:0000269|PubMed:21668448}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:1540159, ECO:0000269|PubMed:1567427,
ECO:0000269|PubMed:8433974}.
-!- SUBUNIT: Homodimer. Interacts with CDK5.
{ECO:0000269|PubMed:21668448, ECO:0000269|PubMed:9012673}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=5; IntAct=EBI-353467, EBI-743771;
Q15323:KRT31; NbExp=5; IntAct=EBI-353467, EBI-948001;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-353467, EBI-10172290;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-353467, EBI-10172052;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-353467, EBI-945833;
P30041:PRDX6; NbExp=2; IntAct=EBI-353467, EBI-2255129;
Q12933:TRAF2; NbExp=5; IntAct=EBI-353467, EBI-355744;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19269317}.
Mitochondrion {ECO:0000269|PubMed:19269317}. Nucleus
{ECO:0000269|PubMed:19269317}. Note=The 83 N-terminal amino acids
function as un uncleaved transit peptide, and arginine residues
within it are crucial for mitochondrial localization.
-!- SIMILARITY: Belongs to the GST superfamily. Pi family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gstp1/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=GSTP1";
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EMBL; X06547; CAA29794.1; -; mRNA.
EMBL; M24485; AAA56823.1; -; Genomic_DNA.
EMBL; X08058; CAA30847.1; -; Genomic_DNA.
EMBL; X08094; CAA30894.1; -; Genomic_DNA.
EMBL; X08095; CAA30894.1; JOINED; Genomic_DNA.
EMBL; X08096; CAA30894.1; JOINED; Genomic_DNA.
EMBL; X15480; CAA33508.1; -; mRNA.
EMBL; U12472; AAA64919.1; -; Genomic_DNA.
EMBL; U30897; AAC51280.1; -; mRNA.
EMBL; U62589; AAC51237.1; -; mRNA.
EMBL; U21689; AAC13869.1; -; Genomic_DNA.
EMBL; BT019949; AAV38752.1; -; mRNA.
EMBL; BT019950; AAV38753.1; -; mRNA.
EMBL; CR450361; CAG29357.1; -; mRNA.
EMBL; AY324387; AAP72967.1; -; Genomic_DNA.
EMBL; BC010915; AAH10915.1; -; mRNA.
CCDS; CCDS41679.1; -.
PIR; A41177; A41177.
PIR; JS0153; A37378.
RefSeq; NP_000843.1; NM_000852.3.
UniGene; Hs.523836; -.
PDB; 10GS; X-ray; 2.20 A; A/B=2-210.
PDB; 11GS; X-ray; 2.30 A; A/B=1-210.
PDB; 12GS; X-ray; 2.10 A; A/B=1-210.
PDB; 13GS; X-ray; 1.90 A; A/B=1-210.
PDB; 14GS; X-ray; 2.80 A; A/B=1-210.
PDB; 16GS; X-ray; 1.90 A; A/B=1-210.
PDB; 17GS; X-ray; 1.90 A; A/B=1-210.
PDB; 18GS; X-ray; 1.90 A; A/B=1-210.
PDB; 19GS; X-ray; 1.90 A; A/B=2-210.
PDB; 1AQV; X-ray; 1.94 A; A/B=2-210.
PDB; 1AQW; X-ray; 1.80 A; A/B/C/D=2-210.
PDB; 1AQX; X-ray; 2.00 A; A/B/C/D=2-210.
PDB; 1EOG; X-ray; 2.10 A; A/B=3-210.
PDB; 1EOH; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-210.
PDB; 1GSS; X-ray; 2.80 A; A/B=2-210.
PDB; 1KBN; X-ray; 2.00 A; A/B=2-210.
PDB; 1LBK; X-ray; 1.86 A; A/B=2-203.
PDB; 1MD3; X-ray; 2.03 A; A/B=2-210.
PDB; 1MD4; X-ray; 2.10 A; A/B=2-210.
PDB; 1PGT; X-ray; 1.80 A; A/B=1-210.
PDB; 1PX6; X-ray; 2.10 A; A/B=2-210.
PDB; 1PX7; X-ray; 2.03 A; A/B=2-210.
PDB; 1ZGN; X-ray; 2.10 A; A/B=2-210.
PDB; 20GS; X-ray; 2.45 A; A/B=2-210.
PDB; 22GS; X-ray; 1.90 A; A/B=1-210.
PDB; 2A2R; X-ray; 1.40 A; A/B=1-210.
PDB; 2A2S; X-ray; 1.70 A; A/B=1-210.
PDB; 2GSS; X-ray; 1.90 A; A/B=2-210.
PDB; 2J9H; X-ray; 2.40 A; A/B=2-210.
PDB; 2PGT; X-ray; 1.90 A; A/B=1-210.
PDB; 3CSH; X-ray; 1.55 A; A/B=2-210.
PDB; 3CSI; X-ray; 1.90 A; A/B/C/D=2-210.
PDB; 3CSJ; X-ray; 1.90 A; A/B=2-210.
PDB; 3DD3; X-ray; 2.25 A; A/B=1-210.
PDB; 3DGQ; X-ray; 1.60 A; A/B=1-210.
PDB; 3GSS; X-ray; 1.90 A; A/B=2-210.
PDB; 3GUS; X-ray; 1.53 A; A/B=2-210.
PDB; 3HJM; X-ray; 2.10 A; A/B/C/D=2-210.
PDB; 3HJO; X-ray; 1.95 A; A/B=2-210.
PDB; 3HKR; X-ray; 1.80 A; A/B=2-210.
PDB; 3IE3; X-ray; 1.80 A; A/B=2-210.
PDB; 3KM6; X-ray; 2.10 A; A/B=2-210.
PDB; 3KMN; X-ray; 1.80 A; A/B=2-210.
PDB; 3KMO; X-ray; 2.60 A; A/B=2-210.
PDB; 3N9J; X-ray; 1.85 A; A/B=1-210.
PDB; 3PGT; X-ray; 2.14 A; A/B=1-210.
PDB; 4GSS; X-ray; 2.50 A; A/B=2-210.
PDB; 4PGT; X-ray; 2.10 A; A/B=1-210.
PDB; 5DAK; X-ray; 2.11 A; A/B=1-210.
PDB; 5DAL; X-ray; 1.50 A; A/B=1-210.
PDB; 5DCG; X-ray; 2.01 A; A/B=1-210.
PDB; 5DDL; X-ray; 1.98 A; A/B=1-210.
PDB; 5DJL; X-ray; 1.80 A; A/B=1-210.
PDB; 5DJM; X-ray; 1.90 A; A/B=1-210.
PDB; 5GSS; X-ray; 1.95 A; A/B=2-210.
PDB; 5J41; X-ray; 1.19 A; A/B=2-210.
PDB; 5JCW; X-ray; 1.95 A; A/B=1-210.
PDB; 5L6X; X-ray; 2.00 A; A/B=1-210.
PDB; 5X79; X-ray; 1.90 A; A/B=1-210.
PDB; 6GSS; X-ray; 1.90 A; A/B=2-210.
PDB; 7GSS; X-ray; 2.20 A; A/B=2-210.
PDB; 8GSS; X-ray; 1.90 A; A/B/C=2-210.
PDB; 9GSS; X-ray; 1.97 A; A/B=2-210.
PDBsum; 10GS; -.
PDBsum; 11GS; -.
PDBsum; 12GS; -.
PDBsum; 13GS; -.
PDBsum; 14GS; -.
PDBsum; 16GS; -.
PDBsum; 17GS; -.
PDBsum; 18GS; -.
PDBsum; 19GS; -.
PDBsum; 1AQV; -.
PDBsum; 1AQW; -.
PDBsum; 1AQX; -.
PDBsum; 1EOG; -.
PDBsum; 1EOH; -.
PDBsum; 1GSS; -.
PDBsum; 1KBN; -.
PDBsum; 1LBK; -.
PDBsum; 1MD3; -.
PDBsum; 1MD4; -.
PDBsum; 1PGT; -.
PDBsum; 1PX6; -.
PDBsum; 1PX7; -.
PDBsum; 1ZGN; -.
PDBsum; 20GS; -.
PDBsum; 22GS; -.
PDBsum; 2A2R; -.
PDBsum; 2A2S; -.
PDBsum; 2GSS; -.
PDBsum; 2J9H; -.
PDBsum; 2PGT; -.
PDBsum; 3CSH; -.
PDBsum; 3CSI; -.
PDBsum; 3CSJ; -.
PDBsum; 3DD3; -.
PDBsum; 3DGQ; -.
PDBsum; 3GSS; -.
PDBsum; 3GUS; -.
PDBsum; 3HJM; -.
PDBsum; 3HJO; -.
PDBsum; 3HKR; -.
PDBsum; 3IE3; -.
PDBsum; 3KM6; -.
PDBsum; 3KMN; -.
PDBsum; 3KMO; -.
PDBsum; 3N9J; -.
PDBsum; 3PGT; -.
PDBsum; 4GSS; -.
PDBsum; 4PGT; -.
PDBsum; 5DAK; -.
PDBsum; 5DAL; -.
PDBsum; 5DCG; -.
PDBsum; 5DDL; -.
PDBsum; 5DJL; -.
PDBsum; 5DJM; -.
PDBsum; 5GSS; -.
PDBsum; 5J41; -.
PDBsum; 5JCW; -.
PDBsum; 5L6X; -.
PDBsum; 5X79; -.
PDBsum; 6GSS; -.
PDBsum; 7GSS; -.
PDBsum; 8GSS; -.
PDBsum; 9GSS; -.
ProteinModelPortal; P09211; -.
SMR; P09211; -.
BioGrid; 109205; 46.
IntAct; P09211; 55.
MINT; MINT-4998983; -.
STRING; 9606.ENSP00000381607; -.
BindingDB; P09211; -.
ChEMBL; CHEMBL3902; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB01008; Busulfan.
DrugBank; DB04972; Canfosfamide.
DrugBank; DB04339; Carbocisteine.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00291; Chlorambucil.
DrugBank; DB02633; Cibacron Blue.
DrugBank; DB00515; Cisplatin.
DrugBank; DB01242; Clomipramine.
DrugBank; DB00773; Etoposide.
DrugBank; DB00143; Glutathione.
DrugBank; DB03003; Glutathione Sulfonic Acid.
DrugBank; DB04077; Glycerol.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB08370; S-(4-BROMOBENZYL)CYSTEINE.
DrugBank; DB03686; S-(P-Nitrobenzyl)Glutathione.
DrugBank; DB04132; S-Hexylglutathione.
DrugBank; DB01915; S-Hydroxycysteine.
DrugBank; DB07849; S-NONYL-CYSTEINE.
DrugBank; DB05460; TLK-199.
DrugBank; DB00163; Vitamin E.
SwissLipids; SLP:000001615; -.
iPTMnet; P09211; -.
PhosphoSitePlus; P09211; -.
SwissPalm; P09211; -.
BioMuta; GSTP1; -.
DOSAC-COBS-2DPAGE; P09211; -.
OGP; P09211; -.
REPRODUCTION-2DPAGE; IPI00219757; -.
SWISS-2DPAGE; P09211; -.
UCD-2DPAGE; P09211; -.
EPD; P09211; -.
PaxDb; P09211; -.
PeptideAtlas; P09211; -.
PRIDE; P09211; -.
TopDownProteomics; P09211; -.
DNASU; 2950; -.
Ensembl; ENST00000398606; ENSP00000381607; ENSG00000084207.
GeneID; 2950; -.
KEGG; hsa:2950; -.
CTD; 2950; -.
DisGeNET; 2950; -.
EuPathDB; HostDB:ENSG00000084207.15; -.
GeneCards; GSTP1; -.
HGNC; HGNC:4638; GSTP1.
HPA; HPA019779; -.
HPA; HPA019869; -.
MIM; 134660; gene.
neXtProt; NX_P09211; -.
OpenTargets; ENSG00000084207; -.
PharmGKB; PA29028; -.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115733; -.
HOVERGEN; HBG108324; -.
InParanoid; P09211; -.
KO; K00799; -.
OMA; LRCKYAT; -.
OrthoDB; EOG091G0K2E; -.
PhylomeDB; P09211; -.
TreeFam; TF105321; -.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P09211; -.
SIGNOR; P09211; -.
ChiTaRS; GSTP1; human.
EvolutionaryTrace; P09211; -.
GeneWiki; GSTP1; -.
GenomeRNAi; 2950; -.
PMAP-CutDB; P09211; -.
PRO; PR:P09211; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000084207; -.
CleanEx; HS_GSTP1; -.
ExpressionAtlas; P09211; baseline and differential.
Genevisible; P09211; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005622; C:intracellular; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0097057; C:TRAF2-GSTP1 complex; IDA:BHF-UCL.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0035731; F:dinitrosyl-iron complex binding; IDA:BHF-UCL.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0043295; F:glutathione binding; IEA:Ensembl.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0008432; F:JUN kinase binding; ISS:BHF-UCL.
GO; GO:0019207; F:kinase regulator activity; ISS:BHF-UCL.
GO; GO:0070026; F:nitric oxide binding; NAS:BHF-UCL.
GO; GO:0035730; F:S-nitrosoglutathione binding; IDA:BHF-UCL.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0071460; P:cellular response to cell-matrix adhesion; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:BHF-UCL.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:BHF-UCL.
GO; GO:0002674; P:negative regulation of acute inflammatory response; NAS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0009890; P:negative regulation of biosynthetic process; IDA:BHF-UCL.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:BHF-UCL.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:BHF-UCL.
GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0070664; P:negative regulation of leukocyte proliferation; ISS:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0043409; P:negative regulation of MAPK cascade; NAS:BHF-UCL.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:BHF-UCL.
GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IEA:Ensembl.
GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IC:BHF-UCL.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0035732; P:nitric oxide storage; NAS:BHF-UCL.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:BHF-UCL.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; ISS:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003082; GST_pi.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01268; GSTRNSFRASEP.
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; Mitochondrion; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:3395118,
ECO:0000269|PubMed:3864155,
ECO:0000269|PubMed:3979555,
ECO:0000269|Ref.15}.
CHAIN 2 210 Glutathione S-transferase P.
/FTId=PRO_0000185900.
DOMAIN 2 81 GST N-terminal.
DOMAIN 83 204 GST C-terminal.
REGION 52 53 Glutathione binding.
{ECO:0000269|PubMed:1522586,
ECO:0000269|PubMed:19396894,
ECO:0000269|PubMed:19808963,
ECO:0000269|PubMed:9012673,
ECO:0000269|PubMed:9245401,
ECO:0000269|PubMed:9351803,
ECO:0000269|PubMed:9398518}.
REGION 65 66 Glutathione binding.
{ECO:0000269|PubMed:1522586,
ECO:0000269|PubMed:19396894,
ECO:0000269|PubMed:19808963,
ECO:0000269|PubMed:9012673,
ECO:0000269|PubMed:9245401,
ECO:0000269|PubMed:9351803,
ECO:0000269|PubMed:9398518}.
BINDING 8 8 Glutathione. {ECO:0000269|PubMed:1522586,
ECO:0000269|PubMed:19396894,
ECO:0000269|PubMed:19808963,
ECO:0000269|PubMed:9012673,
ECO:0000269|PubMed:9245401,
ECO:0000269|PubMed:9351803,
ECO:0000269|PubMed:9398518}.
BINDING 14 14 Glutathione. {ECO:0000269|PubMed:1522586,
ECO:0000269|PubMed:19396894,
ECO:0000269|PubMed:19808963,
ECO:0000269|PubMed:9012673,
ECO:0000269|PubMed:9245401,
ECO:0000269|PubMed:9351803,
ECO:0000269|PubMed:9398518}.
BINDING 39 39 Glutathione. {ECO:0000269|PubMed:1522586,
ECO:0000269|PubMed:19396894,
ECO:0000269|PubMed:19808963,
ECO:0000269|PubMed:9012673,
ECO:0000269|PubMed:9245401,
ECO:0000269|PubMed:9351803,
ECO:0000269|PubMed:9398518}.
BINDING 45 45 Glutathione. {ECO:0000269|PubMed:1522586,
ECO:0000269|PubMed:19396894,
ECO:0000269|PubMed:19808963,
ECO:0000269|PubMed:9012673,
ECO:0000269|PubMed:9245401,
ECO:0000269|PubMed:9351803,
ECO:0000269|PubMed:9398518}.
MOD_RES 4 4 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:19254954}.
MOD_RES 62 62 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 103 103 N6-succinyllysine.
{ECO:0000250|UniProtKB:P19157}.
MOD_RES 116 116 N6-succinyllysine.
{ECO:0000250|UniProtKB:P19157}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 199 199 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:19254954}.
VARIANT 105 105 I -> V (in allele GSTP1*B and allele
GSTP1*C; dbSNP:rs1695).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9092542,
ECO:0000269|Ref.9}.
/FTId=VAR_014499.
VARIANT 114 114 A -> V (in allele GSTP1*C;
dbSNP:rs1138272).
{ECO:0000269|PubMed:9092542,
ECO:0000269|Ref.9}.
/FTId=VAR_014500.
VARIANT 169 169 G -> D (in dbSNP:rs41462048).
/FTId=VAR_049493.
MUTAGEN 8 8 Y->F: Reduces catalytic activity about
50-fold. {ECO:0000269|PubMed:1540159,
ECO:0000269|PubMed:1567427}.
MUTAGEN 99 99 D->A: Reduces affinity for glutathione.
Slightly reduced catalytic activity.
{ECO:0000269|PubMed:8433974}.
CONFLICT 186 186 A -> P (in Ref. 2; CAA30894).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:5J41}.
STRAND 10 12 {ECO:0000244|PDB:5J41}.
HELIX 13 15 {ECO:0000244|PDB:5J41}.
HELIX 16 24 {ECO:0000244|PDB:5J41}.
STRAND 29 33 {ECO:0000244|PDB:5J41}.
HELIX 36 41 {ECO:0000244|PDB:5J41}.
HELIX 43 47 {ECO:0000244|PDB:5J41}.
STRAND 48 51 {ECO:0000244|PDB:3KMN}.
STRAND 55 58 {ECO:0000244|PDB:5J41}.
STRAND 61 65 {ECO:0000244|PDB:5J41}.
HELIX 66 77 {ECO:0000244|PDB:5J41}.
HELIX 84 110 {ECO:0000244|PDB:5J41}.
HELIX 112 135 {ECO:0000244|PDB:5J41}.
HELIX 138 140 {ECO:0000244|PDB:5J41}.
STRAND 144 148 {ECO:0000244|PDB:5JCW}.
HELIX 151 166 {ECO:0000244|PDB:5J41}.
HELIX 170 173 {ECO:0000244|PDB:5J41}.
HELIX 175 185 {ECO:0000244|PDB:5J41}.
HELIX 188 195 {ECO:0000244|PDB:5J41}.
HELIX 197 200 {ECO:0000244|PDB:5J41}.
STRAND 204 208 {ECO:0000244|PDB:5J41}.
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


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