Glutathione S-transferase P (GSTP1)

The protein contains 210 amino acids for an estimated molecular weight of 23356 Da.

 

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. (updated: June 17, 2020)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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VariantDescription
allele GSTP1*B and allele GSTP1*C
allele GSTP1*C
dbSNP:rs41462048

Biological Process

Animal organ regeneration GO Logo
Cellular response to cell-matrix adhesion GO Logo
Cellular response to epidermal growth factor stimulus GO Logo
Cellular response to glucocorticoid stimulus GO Logo
Cellular response to insulin stimulus GO Logo
Cellular response to lipopolysaccharide GO Logo
Cellular response to oxidative stress GO Logo
Central nervous system development GO Logo
Common myeloid progenitor cell proliferation GO Logo
Glutathione derivative biosynthetic process GO Logo
Glutathione metabolic process GO Logo
Hepoxilin biosynthetic process GO Logo
Linoleic acid metabolic process GO Logo
Negative regulation of acute inflammatory response GO Logo
Negative regulation of apoptotic process GO Logo
Negative regulation of biosynthetic process GO Logo
Negative regulation of ERK1 and ERK2 cascade GO Logo
Negative regulation of extrinsic apoptotic signaling pathway GO Logo
Negative regulation of fibroblast proliferation GO Logo
Negative regulation of I-kappaB kinase/NF-kappaB signaling GO Logo
Negative regulation of interleukin-1 beta production GO Logo
Negative regulation of JUN kinase activity GO Logo
Negative regulation of leukocyte proliferation GO Logo
Negative regulation of MAP kinase activity GO Logo
Negative regulation of MAPK cascade GO Logo
Negative regulation of monocyte chemotactic protein-1 production GO Logo
Negative regulation of nitric-oxide synthase biosynthetic process GO Logo
Negative regulation of protein kinase activity GO Logo
Negative regulation of smooth muscle cell chemotaxis GO Logo
Negative regulation of stress-activated MAPK cascade GO Logo
Negative regulation of tumor necrosis factor production GO Logo
Negative regulation of tumor necrosis factor-mediated signaling pathway GO Logo
Negative regulation of vascular associated smooth muscle cell proliferation GO Logo
Neutrophil degranulation GO Logo
Nitric oxide storage GO Logo
Oligodendrocyte development GO Logo
Positive regulation of superoxide anion generation GO Logo
Prostaglandin metabolic process GO Logo
Regulation of ERK1 and ERK2 cascade GO Logo
Regulation of stress-activated MAPK cascade GO Logo
Response to amino acid GO Logo
Response to estradiol GO Logo
Response to ethanol GO Logo
Response to L-ascorbic acid GO Logo
Response to reactive oxygen species GO Logo
Small molecule metabolic process GO Logo
Xenobiotic catabolic process GO Logo
Xenobiotic metabolic process GO Logo

The reference OMIM entry for this protein is 134660

Glutathione s-transferase, pi; gstp1
Glutathione s-transferase 3; gst3
Gst, class pi
Fatty acid ethyl ester synthase iii, myocardial; faees3 glutathione s-transferase pi pseudogene, included; gstpp, included

DESCRIPTION

Glutathione S-transferases (GSTs; EC 2.5.1.18) 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 mammalian cytosolic GSTs are divided into several classes, including alpha (e.g., 138359), mu (e.g., 138350), kappa (602321), theta (e.g., 600436), pi, omega (e.g., 605482), and zeta (e.g., 603758). In addition, there is a class of microsomal GSTs (e.g., 138330). Each class is encoded by a single gene or a gene family.

CLONING

By screening a human placenta cDNA library with a rat placenta GST (GSTP) cDNA, Kano et al. (1987) isolated GST-pi cDNAs. The predicted 209-amino acid protein shares 86% sequence identity with GSTP. However, GST-pi has a pI of 5.5, while that of GSTP is 6.9. Northern hybridization revealed that GST-pi is expressed as a 750-nucleotide mRNA in liver. Moscow et al. (1988) cloned cDNA corresponding to the anionic isozyme of glutathione S-transferase (GST-pi), one of the drug-detoxifying enzymes overexpressed in multidrug-resistant cells. Board et al. (1989) isolated a partial cDNA clone of GST3 from a human lung cDNA library using antiserum to human lung GST3. The sequence showed 2 base differences from that of GST3 isolated from a human placenta cDNA library. Kingsley et al. (1989) and Seldin et al. (1991) concluded that Gsta of the mouse is homologous to human GST2 (138360), not GST3.

GENE STRUCTURE

Morrow et al. (1989) reported that the GST-pi gene contains 7 exons and spans approximately 2.8 kb.

MAPPING

Using an X;11 translocation segregating in hybrids, Silberstein et al. (1982) and Silberstein and Shows (1982) showed that the GST3 gene, which they called GST1, is located in the p13-qter region of chromosome 11. Laisney et al. (1983) concluded that the GST gene localized to chromosome 11 by Silberstein and Shows (1982) was GST3. They assigned the gene to 11q13-q22. Suzuki and Board (1984) also stated that the glutathione S-transferase gene that was mapped to chromosome 11 was GST3, not GST1. Moscow et al. (1988) and Board et al. (1989) mapped the GST-pi gene to 11q13 using in situ hybridization. Using a panel of human-rodent somatic cell hybrids and a DNA probe specific for the class, Islam et al. (1989) mapped GST3, called by them a class pi gene, to chromosome 11. By study of somatic cell hybrids, Konohana et al. (1990) confirmed the assignment of the GST3 gene to 11q. Smith et al. (1995) refined the localization of the GSTP1 gene by study of radiation-reduced somatic cell hybrids. They identified a tandem repeat polymorphism in the 5-prime region and used it for linkage analysis to demonstrate that GSTP1 is 5 cM distal to PYGM (608455) and 4 cM proximal to FGF3 (164950). Rochelle et al. (1992) indicated that the mouse Gst3 locus is on proximal chromosome 19. - Pseudogenes In in situ hybridization studies that assigned the GSTP1 gene to 11q13, Board et al. (1989) found an additional hybridizing locus at 12q13-q14. Board et al. (1992) demonstrated that this closely related Pi class glutathione S-transferase gene is, in fact, a partial reverse-transcribed pseudogene.

GENE FUNCTION

Laisney et al. (1984) stated that GST3 is present in all tissues and cells, with the exception of red cells, in which only erythrocyte GST (GSTe) is observed. Furthermore, GSTe, the ... More on the omim web site

Subscribe to this protein entry history

June 29, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 134660 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed