GSTP1

Glutathione S-transferase pi 1

PDB rendering based on 10gs.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
10GS, 11GS, 12GS, 13GS, 14GS, 16GS, 17GS, 18GS, 19GS, 1AQV, 1AQW, 1AQX, 1EOG, 1EOH, 1GSS, 1KBN, 1LBK, 1MD3, 1MD4, 1PGT, 1PX6, 1PX7, 1ZGN, 20GS, 22GS, 2A2R, 2A2S, 2GSS, 2J9H, 2PGT, 3CSH, 3CSI, 3CSJ, 3DD3, 3DGQ, 3GSS, 3GUS, 3HJM, 3HJO, 3HKR, 3IE3, 3KM6, 3KMN, 3KMO, 3N9J, 3PGT, 4GSS, 4PGT, 5GSS, 6GSS, 7GSS, 8GSS, 9GSS

Identifiers

Symbols

GSTP1 ; DFN7; FAEES3; GST3; GSTP; HEL-S-22; PI

External IDs

OMIM: 134660 MGI: 95864 HomoloGene: 660 ChEMBL: 3902 GeneCards: GSTP1 Gene

EC number

2.5.1.18

Gene ontology
Molecular function	• glutathione transferase activity • protein binding • JUN kinase binding • kinase regulator activity • S-nitrosoglutathione binding • dinitrosyl-iron complex binding • nitric oxide binding
Cellular component	• extracellular space • intracellular • nucleus • cytoplasm • mitochondrion • cytosol • plasma membrane • vesicle • extracellular exosome • TRAF2-GSTP1 complex
Biological process	• response to reactive oxygen species • negative regulation of acute inflammatory response • negative regulation of protein kinase activity • glutathione metabolic process • xenobiotic metabolic process • central nervous system development • negative regulation of biosynthetic process • negative regulation of tumor necrosis factor-mediated signaling pathway • negative regulation of interleukin-1 beta production • negative regulation of tumor necrosis factor production • regulation of stress-activated MAPK cascade • negative regulation of stress-activated MAPK cascade • positive regulation of superoxide anion generation • common myeloid progenitor cell proliferation • nitric oxide storage • negative regulation of apoptotic process • negative regulation of I-kappaB kinase/NF-kappaB signaling • negative regulation of MAP kinase activity • negative regulation of MAPK cascade • negative regulation of JUN kinase activity • small molecule metabolic process • negative regulation of fibroblast proliferation • negative regulation of nitric-oxide synthase biosynthetic process • regulation of ERK1 and ERK2 cascade • negative regulation of ERK1 and ERK2 cascade • negative regulation of leukocyte proliferation • cellular response to lipopolysaccharide • negative regulation of monocyte chemotactic protein-1 production • glutathione derivative biosynthetic process • negative regulation of extrinsic apoptotic signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
67.58 – 67.59 Mb

Chr 19:
4.04 – 4.04 Mb

PubMed search

Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.^[1]^[2]

Function

Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into 4 main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.^[3]

Interactions

GSTP1 has been shown to interact with Fanconi anemia, complementation group C^[4]^[5] and MAPK8.^[6]

GST-Pi is expressed in many human tissues, particularly in the biliary tree and renal distal convoluted tubules.^[7]

References

↑ Bora PS, Bora NS, Wu XL, Lange LG (Oct 1991). "Molecular cloning, sequencing, and expression of human myocardial fatty acid ethyl ester synthase-III cDNA". J. Biol. Chem. 266 (25): 16774–7. PMID 1885604.
↑ Smith CM, Bora PS, Bora NS, Jones C, Gerhard DS (Nov 1995). "Genetic and radiation-reduced somatic cell hybrid sublocalization of the human GSTP1 gene". Cytogenet. Cell Genet. 71 (3): 235–9. doi:10.1159/000134117. PMID 7587384.
↑ "Entrez Gene: GSTP1 glutathione S-transferase pi".
↑ Cumming RC, Lightfoot J, Beard K, Youssoufian H, O'Brien PJ, Buchwald M (Jul 2001). "Fanconi anemia group C protein prevents apoptosis in hematopoietic cells through redox regulation of GSTP1". Nat. Med. 7 (7): 814–20. doi:10.1038/89937. PMID 11433346.
↑ Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (Oct 2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
↑ Wang T, Arifoglu P, Ronai Z, Tew KD (Jun 2001). "Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus". J. Biol. Chem. 276 (24): 20999–1003. doi:10.1074/jbc.M101355200. PMID 11279197.
↑ Terrier, P; Townsend, AJ; Coindre, JM; Triche, TJ; Cowan, KH (October 1990). "An immunohistochemical study of pi class glutathione S-transferase expression in normal human tissue.". The American Journal of Pathology 137 (4): 845–53. PMID 1977319.

Strange RC, Fryer AA (1999). "The glutathione S-transferases: influence of polymorphism on cancer susceptibility". IARC Sci. Publ. (148): 231–49. PMID 10493261.
Kellen E, Hemelt M, Broberg K, Golka K, Kristensen VN, Hung RJ, Matullo G, Mittal RD, Porru S, Povey A, Schulz WA, Shen J, Buntinx F, Zeegers MP, Taioli E (2007). "Pooled analysis and meta-analysis of the glutathione S-transferase P1 Ile 105Val polymorphism and bladder cancer: a HuGE-GSEC review". Am. J. Epidemiol. 165 (11): 1221–30. doi:10.1093/aje/kwm003. PMID 17404387.
Sekine I, Minna JD, Nishio K, Tamura T, Saijo N (2006). "A literature review of molecular markers predictive of clinical response to cytotoxic chemotherapy in patients with lung cancer". J Thorac Oncol 1 (1): 31–7. doi:10.1097/01243894-200601000-00008. PMID 17409824.

PDB gallery

10gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117

11gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE (FORM II)

12gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE

13gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE

14gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1

16gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3

17gs: GLUTATHIONE S-TRANSFERASE P1-1

18gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE

19gs: GLUTATHIONE S-TRANSFERASE P1-1

1aqv: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE

1aqw: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE

1aqx: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX

1eog: CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE

1eoh: GLUTATHIONE TRANSFERASE P1-1

1gss: THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION

1kbn: Glutathione transferase mutant

1lbk: Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

1md3: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to alanine

1md4: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine

1pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE

1px6: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine

1px7: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate

1zgn: Crystal Structure of the Glutathione Transferase Pi in Complex with Dinitrosyl-diglutathionyl Iron Complex

20gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE

21gs:

22gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT

2a2r: Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione

2a2s: Crystal Structure of Human Glutathione Transferase in complex with S-nitrosoglutathione in the absence of reducing agent

2gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID

2j9h: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE-S-TRANSFERASE P1-1 CYS-FREE MUTANT IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.4 A RESOLUTION

2pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE

3gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE

3pgt: CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE

4gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT

4pgt: CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE

5gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE

6gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE

7gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE

8gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE

9gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH S-HEXYL GLUTATHIONE

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GSTP1

Function

Interactions

References

Further reading