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P09211 (GSTP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase P

EC=2.5.1.18
Alternative name(s):
GST class-pi
GSTP1-1
Gene names
Name:GSTP1
Synonyms:FAEES3, GST3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.25

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.18 Ref.19 Ref.20

Subunit structure

Homodimer. Interacts with CDK5. Ref.25

Subcellular location

Cytoplasm. Mitochondrion. Nucleus. Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. Ref.21

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: BHF-UCL

central nervous system development

Traceable author statement PubMed 9802272. Source: ProtInc

common myeloid progenitor cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

glutathione metabolic process

Inferred from direct assay Ref.19. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 11408560. Source: BHF-UCL

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of JUN kinase activity

Inferred from direct assay PubMed 16636664. Source: BHF-UCL

negative regulation of MAP kinase activity

Inferred from direct assay PubMed 11408560. Source: BHF-UCL

negative regulation of MAPK cascade

Non-traceable author statement PubMed 18962899. Source: BHF-UCL

negative regulation of acute inflammatory response

Non-traceable author statement PubMed 18962899. Source: BHF-UCL

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of biosynthetic process

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 16636664. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of interleukin-1 beta production

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of leukocyte proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of monocyte chemotactic protein-1 production

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of nitric-oxide synthase biosynthetic process

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of protein kinase activity

Inferred from direct assay PubMed 16636664. Source: BHF-UCL

negative regulation of stress-activated MAPK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of tumor necrosis factor production

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred by curator PubMed 16636664. Source: BHF-UCL

nitric oxide storage

Non-traceable author statement PubMed 12871931. Source: BHF-UCL

positive regulation of superoxide anion generation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of stress-activated MAPK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

response to reactive oxygen species

Inferred from sequence or structural similarity. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Inferred from direct assay Ref.19. Source: UniProtKB

   Cellular_componentTRAF2-GSTP1 complex

Inferred from direct assay PubMed 16636664. Source: BHF-UCL

cytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

intracellular

Inferred from direct assay PubMed 18962899. Source: BHF-UCL

mitochondrion

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionJUN kinase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

S-nitrosoglutathione binding

Inferred from direct assay PubMed 11533048. Source: BHF-UCL

dinitrosyl-iron complex binding

Inferred from direct assay PubMed 11533048PubMed 12871945. Source: BHF-UCL

glutathione transferase activity

Inferred from direct assay Ref.19. Source: UniProtKB

kinase regulator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

nitric oxide binding

Non-traceable author statement PubMed 11533048. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRAF2Q129334EBI-353467,EBI-355744

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Chain2 – 210209Glutathione S-transferase P
PRO_0000185900

Regions

Domain2 – 8180GST N-terminal
Domain83 – 204122GST C-terminal
Region52 – 532Glutathione binding
Region65 – 662Glutathione binding

Sites

Binding site81Glutathione
Binding site141Glutathione
Binding site391Glutathione
Binding site451Glutathione By similarity

Amino acid modifications

Modified residue41Phosphotyrosine; by EGFR Ref.22
Modified residue1031N6-succinyllysine By similarity
Modified residue1161N6-succinyllysine By similarity
Modified residue1281N6-acetyllysine Ref.23
Modified residue1991Phosphotyrosine; by EGFR Ref.22

Natural variations

Natural variant1051I → V in allele GSTP1*B and allele GSTP1*C. Ref.6 Ref.9 Ref.10
Corresponds to variant rs1695 [ dbSNP | Ensembl ].
VAR_014499
Natural variant1141A → V in allele GSTP1*C. Ref.6 Ref.9
Corresponds to variant rs1138272 [ dbSNP | Ensembl ].
VAR_014500
Natural variant1691G → D.
Corresponds to variant rs41462048 [ dbSNP | Ensembl ].
VAR_049493

Experimental info

Mutagenesis81Y → F: Reduces catalytic activity about 50-fold. Ref.18 Ref.19
Mutagenesis991D → A: Reduces affinity for glutathione. Slightly reduced catalytic activity. Ref.20
Sequence conflict1861A → P in CAA30894. Ref.2

Secondary structure

........................................ 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09211 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 409E33FFAA338396

FASTA21023,356
        10         20         30         40         50         60 
MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVTVETWQ EGSLKASCLY GQLPKFQDGD 

        70         80         90        100        110        120 
LTLYQSNTIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL RCKYISLIYT NYEAGKDDYV 

       130        140        150        160        170        180 
KALPGQLKPF ETLLSQNQGG KTFIVGDQIS FADYNLLDLL LIHEVLAPGC LDAFPLLSAY 

       190        200        210 
VGRLSARPKL KAFLASPEYV NLPINGNGKQ 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of a human class pi glutathione S-transferase messenger RNA."
Kano T., Sakai M., Muramatsu M.
Cancer Res. 47:5626-5630(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The structure of the human glutathione S-transferase pi gene."
Cowell I.G., Dixon K.H., Pemble S.E., Ketterer B., Taylor J.B.
Biochem. J. 255:79-83(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure of the human genomic glutathione S-transferase-pi gene."
Morrow C.S., Cowan K.H., Goldsmith M.E.
Gene 75:3-11(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors."
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.
Cancer Res. 49:1422-1428(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Human fatty acid ethyl ester synthase III gene: genomic organization, nucleotide sequence, genetic and chromosomal sublocalization."
Bora P.S., Smith C., Lange L.G., Bora N.S., Jones C., Gerhard D.S.
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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."
Ali-Osman F., Akande O., Antoun G., Mao J.X., Buolamwini J.
J. Biol. Chem. 272:10004-10012(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-105 AND VAL-114.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]NIEHS SNPs program
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-105 AND VAL-114.
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-105.
Tissue: Urinary bladder.
[11]"Structural evidence for three different types of glutathione transferase in human tissues."
Alin P., Mannervik B., Joernvall H.
FEBS Lett. 182:319-322(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
[12]"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
[13]"Purification and characterization of unique glutathione S-transferases from human muscle."
Singh S.V., Ahmad H., Kurosky A., Awasthi Y.C.
Arch. Biochem. Biophys. 264:13-22(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
[14]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Tissue: Platelet.
[15]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 20-71; 76-101; 104-141; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]"A two-dimensional gel database of human colon carcinoma proteins."
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Colon carcinoma.
[17]"Primary and secondary structural analyses of glutathione S-transferase pi from human placenta."
Ahmad H., Wilson D.E., Fritz R.R., Singh S.V., Medh R.D., Nagle G.T., Awasthi Y.C., Kurosky A.
Arch. Biochem. Biophys. 278:398-408(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PRIMARY AND SECONDARY STRUCTURAL ANALYZES.
[18]"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."
Kong K.H., Takasu K., Inoue H., Takahashi K.
Biochem. Biophys. Res. Commun. 184:194-197(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-8.
[19]"Tyrosine-7 is an essential residue for the catalytic activity of human class PI glutathione S-transferase: chemical modification and site-directed mutagenesis studies."
Kong K.H., Nishida M., Inoue H., Takahashi K.
Biochem. Biophys. Res. Commun. 182:1122-1129(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-8.
[20]"Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1."
Kong K.-H., Inoue H., Takahashi K.
Protein Eng. 6:93-99(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-99, CATALYTIC ACTIVITY.
[21]"Glutathione S-transferase pi localizes in mitochondria and protects against oxidative stress."
Goto S., Kawakatsu M., Izumi S., Urata Y., Kageyama K., Ihara Y., Koji T., Kondo T.
Free Radic. Biol. Med. 46:1392-1403(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[22]"Tyrosine phosphorylation of the human glutathione S-transferase P1 by epidermal growth factor receptor."
Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H., Bigner D., Ali-Osman F.
J. Biol. Chem. 284:16979-16989(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-4 AND TYR-199.
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity."
Sun K.H., Chang K.H., Clawson S., Ghosh S., Mirzaei H., Regnier F., Shah K.
J. Neurochem. 118:902-914(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDK5.
[26]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8-A resolution."
Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M.W.
J. Mol. Biol. 227:214-226(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) COMPLEX WITH S-HEXYLGLUTATHIONE.
[28]"The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate."
Oakley A.J., Rossjohn J., Lo Bello M., Caccuri A.M., Federici G., Parker M.W.
Biochemistry 36:576-585(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR ETHACRYNIC ACID AND GLUTATHIONE.
[29]"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."
Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B., Gilliland G.L., Zimniak P.
Biochemistry 36:9690-9702(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND INHIBITOR.
[30]"The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution."
Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J., Villar H.O., Parker M.W.
J. Mol. Biol. 274:84-100(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE.
[31]"Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor."
Prade L., Huber R., Manoharan T.H., Fahl W.E., Reuter W.
Structure 5:1287-1295(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[32]"Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1."
Ji X., Blaszczyk J., Xiao B., O'Donnell R., Hu X., Herzog C., Singh S.V., Zimniak P.
Biochemistry 38:10231-10238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[33]"Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure."
Nicotra M., Paci M., Sette M., Oakley A.J., Parker M.W., Lo Bello M., Caccuri A.M., Federici G., Ricci G.
Biochemistry 37:3020-3027(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[34]"Rational design of an organometallic glutathione transferase inhibitor."
Ang W.H., Parker L.J., De Luca A., Juillerat-Jeanneret L., Morton C.J., Lo Bello M., Parker M.W., Dyson P.J.
Angew. Chem. Int. Ed. 48:3854-3857(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[35]"Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases."
Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., Caccuri A.M.
Cancer Res. 69:8025-8034(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 2-210.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06547 mRNA. Translation: CAA29794.1.
M24485 Genomic DNA. Translation: AAA56823.1.
X08058 Genomic DNA. Translation: CAA30847.1.
X08094, X08095, X08096 Genomic DNA. Translation: CAA30894.1.
X15480 mRNA. Translation: CAA33508.1.
U12472 Genomic DNA. Translation: AAA64919.1.
U30897 mRNA. Translation: AAC51280.1.
U62589 mRNA. Translation: AAC51237.1.
U21689 Genomic DNA. Translation: AAC13869.1.
BT019949 mRNA. Translation: AAV38752.1.
BT019950 mRNA. Translation: AAV38753.1.
CR450361 mRNA. Translation: CAG29357.1.
AY324387 Genomic DNA. Translation: AAP72967.1.
BC010915 mRNA. Translation: AAH10915.1.
PIRA41177.
A37378. JS0153.
RefSeqNP_000843.1. NM_000852.3.
UniGeneHs.523836.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
10GSX-ray2.20A/B2-210[»]
11GSX-ray2.30A/B1-210[»]
12GSX-ray2.10A/B1-210[»]
13GSX-ray1.90A/B1-210[»]
14GSX-ray2.80A/B2-209[»]
16GSX-ray1.90A/B2-209[»]
17GSX-ray1.90A/B1-210[»]
18GSX-ray1.90A/B2-209[»]
19GSX-ray1.90A/B2-210[»]
1AQVX-ray1.94A/B2-210[»]
1AQWX-ray1.80A/B/C/D2-210[»]
1AQXX-ray2.00A/B/C/D2-210[»]
1EOGX-ray2.10A/B3-210[»]
1EOHX-ray2.50A/B/C/D/E/F/G/H2-210[»]
1GSSX-ray2.80A/B2-210[»]
1KBNX-ray2.00A/B2-209[»]
1LBKX-ray1.86A/B2-202[»]
1MD3X-ray2.03A/B2-209[»]
1MD4X-ray2.10A/B2-209[»]
1PGTX-ray1.80A/B1-210[»]
1PX6X-ray2.10A/B2-209[»]
1PX7X-ray2.03A/B2-209[»]
1ZGNX-ray2.10A/B2-209[»]
20GSX-ray2.45A/B2-209[»]
22GSX-ray1.90A/B1-210[»]
2A2RX-ray1.40A/B2-209[»]
2A2SX-ray1.70A/B2-209[»]
2GSSX-ray1.90A/B2-210[»]
2J9HX-ray2.40A/B2-210[»]
2PGTX-ray1.90A/B1-210[»]
3CSHX-ray1.55A/B2-210[»]
3CSIX-ray1.90A/B/C/D2-210[»]
3CSJX-ray1.90A/B2-210[»]
3DD3X-ray2.25A/B1-210[»]
3DGQX-ray1.60A/B1-210[»]
3GSSX-ray1.90A/B2-210[»]
3GUSX-ray1.53A/B2-210[»]
3HJMX-ray2.10A/B/C/D2-210[»]
3HJOX-ray1.95A/B2-210[»]
3HKRX-ray1.80A/B2-210[»]
3IE3X-ray1.80A/B2-210[»]
3KM6X-ray2.10A/B2-210[»]
3KMNX-ray1.80A/B2-210[»]
3KMOX-ray2.60A/B2-210[»]
3N9JX-ray1.85A/B1-210[»]
3PGTX-ray2.14A/B1-210[»]
4GSSX-ray2.50A/B2-209[»]
4PGTX-ray2.10A/B1-210[»]
5GSSX-ray1.95A/B2-210[»]
6GSSX-ray1.90A/B2-210[»]
7GSSX-ray2.20A/B2-210[»]
8GSSX-ray1.90A/B/C2-210[»]
9GSSX-ray1.97A/B2-210[»]
ProteinModelPortalP09211.
SMRP09211. Positions 1-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109205. 26 interactions.
IntActP09211. 23 interactions.
MINTMINT-4998983.
STRING9606.ENSP00000381607.

Chemistry

BindingDBP09211.
ChEMBLCHEMBL3902.
DrugBankDB00903. Ethacrynic acid.
DB00143. Glutathione.

PTM databases

PhosphoSiteP09211.

2D gel databases

DOSAC-COBS-2DPAGEP09211.
OGPP09211.
REPRODUCTION-2DPAGEIPI00219757.
SWISS-2DPAGEP09211.
UCD-2DPAGEP09211.

Proteomic databases

PaxDbP09211.
PRIDEP09211.

Protocols and materials databases

DNASU2950.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398606; ENSP00000381607; ENSG00000084207.
GeneID2950.
KEGGhsa:2950.
UCSCuc001omf.3. human.

Organism-specific databases

CTD2950.
GeneCardsGC11P067351.
HGNCHGNC:4638. GSTP1.
HPACAB019298.
HPA019779.
HPA019869.
MIM134660. gene.
neXtProtNX_P09211.
PharmGKBPA29028.
GenAtlasSearch...

Phylogenomic databases

eggNOGKOG1695.
HOGENOMHOG000115733.
HOVERGENHBG108324.
InParanoidP09211.
KOK00799.
OMADLRCKYV.
OrthoDBEOG7KH9M3.
PhylomeDBP09211.
TreeFamTF105321.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_120956. Cellular responses to stress.
SABIO-RKP09211.

Gene expression databases

ArrayExpressP09211.
BgeeP09211.
CleanExHS_GSTP1.
GenevestigatorP09211.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01268. GSTRNSFRASEP.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSTP1. human.
EvolutionaryTraceP09211.
GeneWikiGSTP1.
GenomeRNAi2950.
NextBio11692.
PMAP-CutDBP09211.
PROP09211.
SOURCESearch...

Entry information

Entry nameGSTP1_HUMAN
AccessionPrimary (citable) accession number: P09211
Secondary accession number(s): O00460, Q15690, Q5TZY3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM