P09211 (GSTP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 motochondrial 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 component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 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 cascade 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 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 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 necrotic cell death Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of nitric-oxide synthase biosynthetic process Inferred from direct assay PubMed 18962899. 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 response to reactive oxygen species Inferred from sequence or structural similarity. Source: BHF-UCL xenobiotic metabolic process Inferred from direct assay Ref.19. Source: UniProtKB
Cellular_component	TRAF2-GSTP1 complex Inferred from direct assay PubMed 16636664. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	JUN 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
TRAF2	Q12933	4	EBI-353467,EBI-355744

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Chain

2 – 210

209

Glutathione S-transferase P

PRO_0000185900

Regions

Domain

2 – 81

80

GST N-terminal

Domain

83 – 204

122

GST C-terminal

Region

52 – 53

2

Glutathione binding

Region

65 – 66

2

Glutathione binding

Sites

Binding site

8

1

Glutathione

Binding site

14

1

Glutathione

Binding site

39

1

Glutathione

Binding site

45

1

Glutathione By similarity

Amino acid modifications

Modified residue

4

1

Phosphotyrosine; by EGFR Ref.22

Modified residue

109

1

Phosphotyrosine By similarity

Modified residue

128

1

N6-acetyllysine Ref.23

Modified residue

199

1

Phosphotyrosine; by EGFR Ref.22

Natural variations

Natural variant

105

1

I → V in allele GSTP1*B and allele GSTP1*C. Ref.6 Ref.9 Ref.10
Corresponds to variant rs1695 [ dbSNP | Ensembl ].

VAR_014499

Natural variant

114

1

A → V in allele GSTP1*C. Ref.6 Ref.9
Corresponds to variant rs1138272 [ dbSNP | Ensembl ].

VAR_014500

Natural variant

169

1

G → D.
Corresponds to variant rs41462048 [ dbSNP | Ensembl ].

VAR_049493

Experimental info

Mutagenesis

8

1

Y → F: Reduces catalytic activity about 50-fold. Ref.18 Ref.19

Mutagenesis

99

1

D → A: Reduces affinity for glutathione. Slightly reduced catalytic activity. Ref.20

Sequence conflict

186

1

A → P in CAA30894. Ref.2

Secondary structure

1

.

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210

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Beta strand

10 – 12

3

Helix

13 – 15

3

Helix

16 – 24

9

Beta strand

29 – 33

5

Helix

36 – 41

6

Helix

43 – 47

5

Beta strand

48 – 51

4

Beta strand

55 – 58

4

Beta strand

61 – 64

4

Helix

66 – 76

11

Helix

84 – 110

27

Helix

112 – 135

24

Helix

138 – 140

3

Beta strand

144 – 148

5

Helix

151 – 166

16

Helix

170 – 173

4

Helix

175 – 185

11

Helix

188 – 195

8

Helix

197 – 200

4

Beta strand

204 – 208

5

Sequences

	Sequence		Length	Mass (Da)
	P09211 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 409E33FFAA338396	FASTA	210	23,356
	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

References

	« Hide 'large scale' referencesShow '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, 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, MASS SPECTROMETRY.
[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]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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).
[31]	"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).
[32]	"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.
[33]	"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).
[34]	"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.

IPI

IPI00219757.

PIR

A41177.
A37378. JS0153.

RefSeq

NP_000843.1. NM_000852.3.

UniGene

Hs.523836.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
10GS	X-ray	2.20	A/B	2-210	[»]
11GS	X-ray	2.30	A/B	1-210	[»]
12GS	X-ray	2.10	A/B	1-210	[»]
13GS	X-ray	1.90	A/B	1-210	[»]
14GS	X-ray	2.80	A/B	2-209	[»]
16GS	X-ray	1.90	A/B	2-209	[»]
17GS	X-ray	1.90	A/B	1-210	[»]
18GS	X-ray	1.90	A/B	2-209	[»]
19GS	X-ray	1.90	A/B	2-210	[»]
1AQV	X-ray	1.94	A/B	2-210	[»]
1AQW	X-ray	1.80	A/B/C/D	2-210	[»]
1AQX	X-ray	2.00	A/B/C/D	2-210	[»]
1EOG	X-ray	2.10	A/B	3-210	[»]
1EOH	X-ray	2.50	A/B/C/D/E/F/G/H	2-210	[»]
1GSS	X-ray	2.80	A/B	2-210	[»]
1KBN	X-ray	2.00	A/B	2-209	[»]
1LBK	X-ray	1.86	A/B	2-202	[»]
1MD3	X-ray	2.03	A/B	2-209	[»]
1MD4	X-ray	2.10	A/B	2-209	[»]
1PGT	X-ray	1.80	A/B	1-210	[»]
1PX6	X-ray	2.10	A/B	2-209	[»]
1PX7	X-ray	2.03	A/B	2-209	[»]
1ZGN	X-ray	2.10	A/B	2-209	[»]
20GS	X-ray	2.45	A/B	2-209	[»]
22GS	X-ray	1.90	A/B	1-210	[»]
2A2R	X-ray	1.40	A/B	2-209	[»]
2A2S	X-ray	1.70	A/B	2-209	[»]
2GSS	X-ray	1.90	A/B	2-210	[»]
2J9H	X-ray	2.40	A/B	2-210	[»]
2PGT	X-ray	1.90	A/B	1-210	[»]
3CSH	X-ray	1.55	A/B	2-210	[»]
3CSI	X-ray	1.90	A/B/C/D	2-210	[»]
3CSJ	X-ray	1.90	A/B	2-210	[»]
3DD3	X-ray	2.25	A/B	1-210	[»]
3DGQ	X-ray	1.60	A/B	1-210	[»]
3GSS	X-ray	1.90	A/B	2-210	[»]
3GUS	X-ray	1.53	A/B	2-210	[»]
3HJM	X-ray	2.10	A/B/C/D	2-210	[»]
3HJO	X-ray	1.95	A/B	2-210	[»]
3HKR	X-ray	1.80	A/B	2-210	[»]
3IE3	X-ray	1.80	A/B	2-210	[»]
3KM6	X-ray	2.10	A/B	2-210	[»]
3KMN	X-ray	1.80	A/B	2-210	[»]
3KMO	X-ray	2.60	A/B	2-210	[»]
3N9J	X-ray	1.85	A/B	1-210	[»]
3PGT	X-ray	2.14	A/B	1-210	[»]
4GSS	X-ray	2.50	A/B	2-209	[»]
4PGT	X-ray	2.10	A/B	1-210	[»]
5GSS	X-ray	1.95	A/B	2-210	[»]
6GSS	X-ray	1.90	A/B	2-210	[»]
7GSS	X-ray	2.20	A/B	2-210	[»]
8GSS	X-ray	1.90	A/B/C	2-210	[»]
9GSS	X-ray	1.97	A/B	2-210	[»]

ProteinModelPortal

P09211.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09211. 22 interactions.

MINT

MINT-4998983.

STRING

9606.ENSP00000381607.

PTM databases

PhosphoSite

P09211.

Polymorphism databases

DMDM

121746.

2D gel databases

DOSAC-COBS-2DPAGE

P09211.

OGP

P09211.

REPRODUCTION-2DPAGE

IPI00219757.

SWISS-2DPAGE

P09211.

UCD-2DPAGE

P09211.

Proteomic databases

PaxDb

P09211.

PRIDE

P09211.

Protocols and materials databases

DNASU

2950.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398606; ENSP00000381607; ENSG00000084207.

GeneID

2950.

KEGG

hsa:2950.

UCSC

uc001omf.3. human.

Organism-specific databases

CTD

2950.

GeneCards

GC11P067351.

HGNC

HGNC:4638. GSTP1.

HPA

CAB019298.
HPA019779.
HPA019869.

MIM

134660. gene.

neXtProt

NX_P09211.

PharmGKB

PA29028.

GenAtlas

Search...

Phylogenomic databases

eggNOG

KOG1695.

HOGENOM

HOG000115733.

HOVERGEN

HBG108324.

InParanoid

P09211.

KO

K00799.

OMA

YEAGKDD.

OrthoDB

EOG48SGTZ.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P09211.

Gene expression databases

ArrayExpress

P09211.

Bgee

P09211.

CleanEx

HS_GSTP1.

Genevestigator

P09211.

GermOnline

ENSG00000084207. Homo sapiens.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01268. GSTRNSFRASEP.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09211.

ChEMBL

CHEMBL3902.

ChiTaRS

GSTP1. human.

DrugBank

DB00903. Ethacrynic acid.
DB00143. Glutathione.

EvolutionaryTrace

P09211.

GenomeRNAi

2950.

NextBio

11692.

PMAP-CutDB

P09211.

SOURCE

Search...

Entry information

Entry name

GSTP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 163 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.