Glutathione S-transferase Mu 2 (GSTM2)
The protein contains 218 amino acids for an estimated molecular weight of 25745 Da.
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). (updated: June 17, 2020)
Protein identification was indicated in the following studies:
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
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| Variant | Description |
|---|---|
| dbSNP:rs2229050 |
No binding partner found
Biological Process
Cellular detoxification of nitrogen compound
Cellular response to caffeine
Glutathione derivative biosynthetic process
Glutathione metabolic process
Hepoxilin biosynthetic process
Linoleic acid metabolic process
Negative regulation of ryanodine-sensitive calcium-release channel activity
Nitrobenzene metabolic process
Positive regulation of ryanodine-sensitive calcium-release channel activity
Regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
Regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
Regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
Relaxation of cardiac muscle
Xenobiotic catabolic process
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Intercellular bridge
Obsolete cell
Sarcoplasmic reticulum
The reference OMIM entry for this protein is 138380
Glutathione s-transferase, mu-2; gstm2
Glutathione s-transferase 4; gst4
Glutathione s-transferase m2
Gst, muscle; gstm
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). This enzyme catalyzes the reaction of glutathione with a wide variety of organic compounds to form thioethers, a reaction that is sometimes a first step in a detoxification process leading to mercapturic acid formation. Based on amino acid sequence similarities and antibody cross-reactivities, 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 (134660), omega (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
In muscle extracts, Van Cong et al. (1984) observed a novel GST band (called GST4, or GSTM2), which migrated between GST3 (GSTP1; 134660) and GST1 (GSTM1; 138350). No polymorphism was noted. The formation of heterodimeric bands with GSTM1 indicated that GSTM2 is a dimeric enzyme and that it is controlled by a separate gene. GSTM1, GSTM2, and GSTM3 (138390) are class mu isoenzymes. GSTM1 encodes an enzyme expressed in liver and peripheral blood, while the products of GSTM2 and GSTM3 are expressed in muscle and brain, respectively. Vorachek et al. (1991) isolated a cDNA for GSTM2 from a human myoblast cDNA library and determined its sequence. The deduced 217-amino acid protein has a molecular mass of 25,599 Da. It shares 84.8% sequence identity with the GSTM1 protein.MAPPING
Taylor et al. (1991) demonstrated that GSTM2 and GSTM4 (138333) are located on the same cosmid. Pearson et al. (1993) isolated a YAC clone containing all 5 GSTM genes, GSTM1-5; using this clone, they mapped all of these genes to 1p13.3 by fluorescence in situ hybridization. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 138380 was added.
June 29, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).