Glutathione S-transferase A2 (GSTA2)

The protein contains 222 amino acids for an estimated molecular weight of 25664 Da.

 

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

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.

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

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VariantDescription
dbSNP:rs2234951
dbSNP:rs2180314
dbSNP:rs2266631
dbSNP:rs6577

No binding partner found

The reference OMIM entry for this protein is 138360

Glutathione s-transferase, alpha-2; gsta2
Glutathione s-transferase a2
Glutathione s-transferase 2; gst2
Liver gst2
Gst, class alpha, 2

DESCRIPTION

The glutathione S-transferases (GST; EC 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens (Mannervik, 1985). Based on amino acid sequence similarities and antibody cross-reactivities, the cytosolic glutathione S-transferases (GSTs) are grouped into several classes termed alpha (e.g., GSTA1; 138359), mu (e.g., 138350), kappa (602321), theta (e.g., 600436), pi (134660), sigma, omega (e.g., 605482), and zeta (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

Board and Webb (1987) isolated a cDNA clone containing the entire coding sequence of human GST2. The subunit is composed of 221 amino acids with a molecular mass of 25,425 before posttranslational modification. By searching a genomic sequence database with the GSTA1 and GSTA4 (605450) sequences, Morel et al. (2002) identified 1 BAC and 3 PAC clones covering more than 400 kb and containing the entire GST-alpha gene cluster. The cluster consists of 5 genes, GSTA1, GSTA2, GSTA3 (605449), GSTA4, and GSTA5 (607605), as well as 7 pseudogenes. The deduced GSTA2 protein contains 222 amino acids. By RT-PCR using gene-specific probes, Morel et al. (2002) demonstrated that GSTA1, GSTA2, and GSTA4 transcripts are widely expressed in human tissues, whereas the GSTA3 transcript appears to be a rare message subject to splicing defects. Although GSTA5 appears to be a functional gene, expression of GSTA5 could not be detected in any tissues examined.

GENE FUNCTION

Board and Webb (1987) pointed out that deficiencies of GST had been implicated in the etiology of nonhemolytic unconjugated hyperbilirubinemia in the newborn. The GSTs are involved not only in the metabolism of a broad range of xenobiotics but also in the binding and possible transport of some endogenous anionic compounds such as bilirubin and heme.

GENE STRUCTURE

Suzuki et al. (1993) isolated and characterized genomic DNA encoding several human alpha class GST genes and pseudogenes. They found that all the genes are composed of 7 exons with boundaries identical to those of the alpha class genes in rats. The GSTA1 gene was approximately 12 kb long and was closely flanked by other alpha class sequences. Several pseudogenes with single-base and/or complete exon deletions were identified in the same chromosomal region, but no reverse-transcribed pseudogenes were detected. Suzuki et al. (1993) concluded that the multiple genes and pseudogenes on a single fragment of cloned genomic DNA represented a closely linked gene family that evolved by duplication and gene conversion events.

MAPPING

Board and Webb (1987) showed that in situ hybridization of the cloned GST2 cDNA to human chromosomes produced intense labeling only over 6p12. Using in situ chromosomal hybridization, Chow et al. (1988) confirmed the location of the GST2 gene in 6p12. Using a panel of human-rodent somatic cell hybrids and a DNA probe specific for the gene, Islam et al. (1989) assigned GST2, called by them an alpha class gene, to chromosome 6. The human genome contains multiple copies of GST2 genes, all of which map to 6p12. In the mouse, by use of recombinant inbred strains, Kasahara et al. (1990) mapped the Gst-2 gene to chromosome 9. Three genes in the pericentric area of human chromosome 6 show homology to mouse chromosome 9: GST2, ME1 (154250), and PGM3 (172100 ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 138360 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).