Phosphoglucomutase-2 (PGM2)
The protein contains 612 amino acids for an estimated molecular weight of 68283 Da.
Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity. (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.
- 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:rs17856324 | |
| dbSNP:rs10001580 |
Biological Process
Carbohydrate metabolic process
Deoxyribose phosphate catabolic process
Galactose catabolic process
Glucose metabolic process
Glycogen biosynthetic process
Glycogen catabolic process
Neutrophil degranulation
Pathogenesis
Pentose-phosphate shunt
Small molecule metabolic process
The reference OMIM entry for this protein is 172000
Phosphoglucomutase 2; pgm2
CLONING
Hopkinson and Harris (1965) presented evidence for a second structural locus controlling phosphoglucomutase; see PGM1 (171900). Maliekal et al. (2007) isolated phosphopentomutase from human erythrocytes and found that it copurified with a 68-kD (612-amino acid) protein that was identified by mass spectrometry as phosphoglucomutase-2 (PGM2), a protein of the alpha-D-phosphohexomutase family. The PGM2 protein shares about 20% identity with mammalian PGM1. Sequence analysis suggested that PGM2 is a cytosolic protein. Quantitative RT-PCR of mouse tissues detected the highest expression levels of PGM2 in lung, spleen, and thymus.GENE FUNCTION
Maliekal et al. (2007) overexpressed and purified PGM2 and PGM2L1 (611610) in E. coli and found that PGM2 acted more than 10-fold better as a phosphopentomutase (both on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a phosphoglucomutase. Maliekal et al. (2007) speculated that PGM2 may play a role in congenital immunodeficiencies. They noted that phosphopentomutase uses ribose 1-phosphate and deoxyribose 1-phosphate, which are formed by purine nucleoside phosphorylase and uridine phosphorylase, and that the absence of phosphopentomutase should result in the accumulation of ribose 1-phosphate and deoxyribose 1-phosphate and therefore in a functional block of purine nucleoside phosphorylase. Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).MAPPING
By cell hybrid studies, PGM2 was assigned to chromosome 4 (McAlpine et al., 1975). The smallest region of overlap (SRO) derived from hybrid cell studies by Francke and Brown (1978), Sparkes et al. (1978, 1978), and Wijnen et al. (1977) was 4p14-q12. ... 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 172000 was added.