GSTP1

Protein-coding gene in the species Homo sapiens
GSTP1
Available structures
PDBHuman UniProt 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
AliasesGSTP1, DFN7, FAEES3, GST3, GSTP, HEL-S-22, PI, glutathione S-transferase pi 1
External IDsOMIM: 134660; MGI: 3782108; HomoloGene: 660; GeneCards: GSTP1; OMA:GSTP1 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for GSTP1
Genomic location for GSTP1
Band11q13.2Start67,583,742 bp[1]
End67,586,656 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • olfactory zone of nasal mucosa

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • ectocervix

  • skin of abdomen

  • skin of leg

  • right lung

  • upper lobe of left lung

  • anterior pituitary
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • JUN kinase binding
  • kinase regulator activity
  • glutathione binding
  • nitric oxide binding
  • protein binding
  • S-nitrosoglutathione binding
  • dinitrosyl-iron complex binding
  • glutathione transferase activity
  • protein kinase binding
  • glutathione peroxidase activity
Cellular component
  • vesicle
  • TRAF2-GSTP1 complex
  • plasma membrane
  • intracellular anatomical structure
  • mitochondrion
  • extracellular exosome
  • nucleus
  • extracellular region
  • extracellular space
  • cytoplasm
  • cytosol
  • secretory granule lumen
  • ficolin-1-rich granule lumen
Biological process
  • negative regulation of monocyte chemotactic protein-1 production
  • cellular response to cell-matrix adhesion
  • response to amino acid
  • response to estradiol
  • negative regulation of interleukin-1 beta production
  • negative regulation of acute inflammatory response
  • glutathione metabolic process
  • negative regulation of tumor necrosis factor-mediated signaling pathway
  • negative regulation of leukocyte proliferation
  • common myeloid progenitor cell proliferation
  • nitric oxide storage
  • negative regulation of extrinsic apoptotic signaling pathway
  • negative regulation of apoptotic process
  • response to L-ascorbic acid
  • negative regulation of I-kappaB kinase/NF-kappaB signaling
  • cellular response to epidermal growth factor stimulus
  • central nervous system development
  • cellular response to glucocorticoid stimulus
  • response to nutrient levels
  • negative regulation of MAP kinase activity
  • animal organ regeneration
  • regulation of ERK1 and ERK2 cascade
  • cellular response to insulin stimulus
  • negative regulation of MAPK cascade
  • negative regulation of ERK1 and ERK2 cascade
  • negative regulation of stress-activated MAPK cascade
  • oligodendrocyte development
  • positive regulation of superoxide anion generation
  • negative regulation of tumor necrosis factor production
  • metabolism
  • response to ethanol
  • cellular response to lipopolysaccharide
  • negative regulation of JUN kinase activity
  • negative regulation of fibroblast proliferation
  • negative regulation of nitric-oxide synthase biosynthetic process
  • glutathione derivative biosynthetic process
  • response to toxic substance
  • regulation of stress-activated MAPK cascade
  • negative regulation of biosynthetic process
  • cellular oxidant detoxification
  • negative regulation of protein kinase activity
  • xenobiotic metabolic process
  • negative regulation of smooth muscle cell chemotaxis
  • linoleic acid metabolic process
  • negative regulation of vascular associated smooth muscle cell proliferation
  • neutrophil degranulation
  • response to reactive oxygen species
  • cellular response to oxidative stress
  • xenobiotic catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2950

100042625

Ensembl

ENSG00000084207

n/a

UniProt

P09211

n/a

RefSeq (mRNA)

NM_000852

XM_036155425

RefSeq (protein)

NP_000843

n/a

Location (UCSC)Chr 11: 67.58 – 67.59 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.[4][5]

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 four 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.[6]

Interactions

GSTP1 has been shown to interact with Fanconi anemia, complementation group C[7][8] and MAPK8.[9]

GST-Pi is expressed in many human tissues, particularly in the biliary tree, renal distal convoluted tubules and lungs.[10]

Possible drug target

Triple-negative breast cancer cells rely on glutathione-S-transferase Pi1, and inhibitors are being studied.[11] Piperlongumine has been found to silence the gene.[12]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084207 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Bora PS, Bora NS, Wu XL, Lange LG (October 1991). "Molecular cloning, sequencing, and expression of human myocardial fatty acid ethyl ester synthase-III cDNA". J. Biol. Chem. 266 (25): 16774–7. doi:10.1016/S0021-9258(18)55367-9. PMID 1885604.
  5. ^ Smith CM, Bora PS, Bora NS, Jones C, Gerhard DS (November 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.
  6. ^ "Entrez Gene: GSTP1 glutathione S-transferase pi".
  7. ^ Cumming RC, Lightfoot J, Beard K, Youssoufian H, O'Brien PJ, Buchwald M (July 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. S2CID 35177844.
  8. ^ Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (October 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.
  9. ^ Wang T, Arifoglu P, Ronai Z, Tew KD (15 June 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.
  10. ^ 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. PMC 1877535. PMID 1977319.
  11. ^ Triple-negative breast cancer target is found. May 2016
  12. ^ "Researchers uncover mechanism for cancer-killing properties of pepper plant".

Further reading

  • 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.
  • v
  • t
  • e
  • 10gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117
    10gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117
  • 11gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE (FORM II)
    11gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE (FORM II)
  • 12gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
    12gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
  • 13gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE
    13gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE
  • 14gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
    14gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
  • 16gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
    16gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
  • 17gs: GLUTATHIONE S-TRANSFERASE P1-1
    17gs: GLUTATHIONE S-TRANSFERASE P1-1
  • 18gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE
    18gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE
  • 19gs: GLUTATHIONE S-TRANSFERASE P1-1
    19gs: GLUTATHIONE S-TRANSFERASE P1-1
  • 1aqv: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE
    1aqv: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE
  • 1aqw: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE
    1aqw: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE
  • 1aqx: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX
    1aqx: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX
  • 1eog: CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE
    1eog: CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE
  • 1eoh: GLUTATHIONE TRANSFERASE P1-1
    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
    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
    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
    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
    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
    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
    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
    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
    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
    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
    20gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE
  • 21gs:
    21gs:
  • 22gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT
    22gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT
  • 2a2r: Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione
    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
    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
    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
    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
    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
    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
    3pgt: CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
  • 4gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT
    4gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT
  • 4pgt: CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE
    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
    5gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
  • 6gss: 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
    7gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE
  • 8gss: 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
    9gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH S-HEXYL GLUTATHIONE


Stub icon

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.

  • v
  • t
  • e