Bisphosphoglycerate mutase (BPGM)
The protein contains 259 amino acids for an estimated molecular weight of 30005 Da.
Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. (updated: March 28, 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.
- 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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
The reference OMIM entry for this protein is 222800
Bisphosphoglycerate mutase deficiency
Bisphosphoglyceromutase deficiency
Bpgm deficiency
Diphosphoglycerate mutase deficiency of erythrocyte
Dpgm deficiency
A number sign (#) is used with this entry because erythrocyte bisphosphoglycerate mutase deficiency can be caused by compound heterozygous mutation in the BPGM gene (613896), which encodes a multifunctional enzyme, on chromosome 7q31-q34.
CLINICAL FEATURES
Schroter (1965) described severe hemolytic anemia in an infant. Although the proband's blood could not be studied because of multiple transfusions, the erythrocytes of the consanguineous parents, the sister and the father's mother showed activity of 2,3-diphosphoglycerate mutase about half of normal. The family of Bowdler and Prankerd (1964) is puzzling in that father and son had hemolytic anemia for which splenectomy was performed. In father and son, Labie et al. (1970) found a decrease in DPGM by about 50%. An increase in oxygen affinity of hemoglobin was observed. Schroter (1965) observed heterozygotes in 3 generations including both parents of a homozygous child with hemolytic anemia. Rosa et al. (1978) described a French family in which a man and his 3 sisters had erythrocytosis and complete deficiency of bisphosphoglycerate mutase. As a consequence, the affinity of his red cells for oxygen was increased. Hemoglobin concentration was 19.0 g per dl. The morphology of his red cells was normal and there was no evidence of hemolysis. Low levels of red cell 2,3-DPG prompted assay of the enzyme. Scott and Wright (1982) found DPGM to be polymorphic in 4 Alaskan ethnic groups. Hemoglobin and hematocrit were elevated in all deficient persons. Thus, both hemolytic anemia and polycythemia have been observed with deficiency of DPGM. Galacteros et al. (1984) reported 2 families; in one, 3 sisters and a brother were homozygotes and all 3 offspring of 2 of them were heterozygotes with male-to-male transmission. Diphosphoglycerate phosphatase activity paralleled DPGM activity in all subjects.MOLECULAR GENETICS
In a patient with complete deficiency of erythrocyte BPGM reported by Rosa et al. (1978), Rosa et al. (1989) identified a heterozygous missense mutation in the BPGM gene (613896.0001). Lemarchandel et al. (1992) studied further the family originally reported by Rosa et al. (1978). They found that the affected individuals were, in fact, compound heterozygous for the R89C mutation and a deletion of nucleotide 205C or 206C (amino acid 19) (613896.0002). ... More on the omim web site
April 12, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 5, 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 222800 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed