Hydroxyacylglutathione hydrolase, mitochondrial (HAGH)
The protein contains 308 amino acids for an estimated molecular weight of 33806 Da.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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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The reference OMIM entry for this protein is 138760
Hydroxyacyl glutathione hydrolase; hagh
Glyoxalase ii; glo2
DESCRIPTION
Glyoxalase II (EC 3.1.2.6), otherwise known as hydroxyacyl-glutathione hydrolase, converts the intermediate substrate S-lactoyl-glutathione to reduced glutathione and D-lactate (summary by Honey and Shows, 1981).CLONING
Ridderstrom et al. (1996) cloned a cDNA coding for glyoxalase II from human liver. The 1,011-bp sequence contains a full-length coding region of 780 basepairs, corresponding to a 260-amino acid polypeptide. The calculated molecular mass of the protein is 28,861 Da. They expressed the gene in bacteria and the recombinant enzyme showed a kinetic behavior indistinguishable from that of the native enzyme.MAPPING
By study of somatic cell hybrids, Honey and Shows (1981) concluded that the gene for glyoxalase II is on chromosome 16. Mulley and Callen (1986) confirmed the assignment of HAGH to chromosome 16 by studies of a human-mouse hybrid panel. They found that both HAGH and phosphoglycolate phosphatase (PGP; 172280) were present only in those cell lines containing 16p13. Mulley et al. (1990) assigned the HAGH locus to 16p13.3 by electrophoretic detection of enzymes from a mouse/human somatic cell panel, the members of which carried portions of human chromosome 16 with precisely defined breakpoints.MOLECULAR GENETICS
Board (1980) described rare polymorphism of glyoxalase II, observed only in a Micronesian population, in which a new variant allele had a frequency of 0.016. In the heterozygotes, the electrophoretic pattern was a double band, suggesting that the structure of glyoxalase II is monomeric. The enzyme shows a high degree of polymorphism in anthropoid primates (Board et al., 1981). Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988). ... More on the omim web site
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 138760 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed