Phosphoglycerate mutase 1 (PGAM1)
The protein contains 254 amino acids for an estimated molecular weight of 28804 Da.
Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. (updated: Jan. 31, 2018)
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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Biological Process
Canonical glycolysis
Carbohydrate metabolic process
Gluconeogenesis
Glucose metabolic process
Glycolytic process
Neutrophil degranulation
Pathogenesis
Regulation of glycolytic process
Regulation of pentose-phosphate shunt
Respiratory burst
Small molecule metabolic process
The reference OMIM entry for this protein is 172250
Phosphoglycerate mutase 1; pgam1 phosphoglycerate mutase a; pgama
Phosphoglycerate mutase, brain; pgamb
DESCRIPTION
Phosphoglycerate mutase (PGAM; EC 5.4.2.1; formerly EC 2.7.5.3) is widely distributed in mammalian tissues where it catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway (summary by Chen et al., 1974).CLONING
Monophosphoglycerate mutase (PGAM) of human red cells has strikingly similar physicochemical and catalytic properties to 2,3-diphosphoglycerate mutase (613896) from the same source. However, by studies of inherited electrophoretic variation, Chen et al. (1977) showed that they are different. Sakoda et al. (1988) described the isolation, the complete nucleotide sequence, and a transcriptional, genomic, and evolutionary analysis of a full-length cDNA encoding human PGAM. The cDNA encodes a deduced protein of 254 amino acids, 79% identical to PGAM-M (612931) and containing a 913-nucleotide 3-prime untranslated region as compared to the unusually short 37-nucleotide 3-prime untranslated region of PGAM-M. Genomic Southern analysis implied the presence of a large PGAM family in the human genome. Most of the PGAM-hybridizing sequences in both the human and mouse genomes seem to be related to the B-isozyme gene; many members of the PGAM-B gene family in humans are apparently processed pseudogenes. The evolutionary analysis suggests that the PGAMB gene is the progenitor of the PGAMM gene. PGAM is a dimeric enzyme containing, in different tissues, different proportions of a muscle (MM) isozyme, a brain (BB) isozyme, and a hybrid form (MB). Electrophoresis of normal adult human muscle PGAM shows marked predominance of the MM band with only faint BB and MB bands; see 612931. In most other human tissues, including brain, liver, erythrocytes, and leukocytes, PGAM-BB is the only demonstrable isozyme. In cardiac muscle extracts, all 3 bands are seen, although PGAM-MM predominates. DiMauro et al. (1986) stated that PGAM-B is the same as PGAM-A. This situation is comparable to that of lactate dehydrogenase in which the subunits are referred to by the designations M and H, based on predominance in skeletal muscle or heart muscle, respectively, but the loci are referred to as A and B (see 150000, 150100).MAPPING
The study of rare genetic variants of PGAM in a family studied by Chen et al. (1974) failed to exclude X-linkage, but the finding of a heterozygous male indicated autosomal localization of the gene. By gene dosage studies, Junien et al. (1982) assigned phosphoglycerate mutase A (PGAMA) and GOT1 (138180) to chromosome 10 (10q26.1-q25.3). In view of previous regional localization, the position of both PGAMA and GOT1 may be 10q25.3 (Gerald and Grzeschik, 1984). The fact that the PGAMA and GOT1 loci are linked in the mouse (on chromosome 19) supports the assignment of PGAMA to human chromosome 10.BIOCHEMICAL FEATURES
The M2 isoform of pyruvate kinase (PKM2; 179050) promotes the metabolism of glucose by aerobic glycolysis and contributes to anabolic metabolism. Paradoxically, decreased pyruvate kinase enzyme activity accompanies the expression of PKM2 in rapidly dividing cancer cells and tissues. Vander Heiden et al. (2010) demonstrated that phosphoenolpyruvate (PEP), the substrate for pyruvate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells. Vander Heiden et al. (2010) used mass s ... More on the omim web site
Feb. 10, 2018: 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 172250 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed