BPGM (Bisphosphoglycerate Mutase) Gene
Key regulator of erythrocyte oxygen affinity via 2,3-BPG synthesis
Gene Information Card
| Symbol | BPGM |
|---|---|
| Full Name | Bisphosphoglycerate Mutase |
| Gene Type | Protein coding |
| Chromosomal Location | 7q33 |
| NCBI Gene ID | 669 ncbi.nlm.nih.gov/gene/669 |
| Ensembl ID | ENSG00000172331 |
| UniProt ID | P07738 |
| OMIM ID | 222800 |
| HGNC ID | 1093 |
| Aliases | BPG-dependent mutase, 2,3-bisphosphoglycerate mutase, 2,3-BPG mutase, DPGM |
Description
The BPGM gene encodes bisphosphoglycerate mutase, an erythrocyte-specific enzyme that catalyzes the synthesis and degradation of 2,3-bisphosphoglycerate (2,3-BPG). 2,3-BPG is a key allosteric regulator of hemoglobin oxygen affinity, binding to deoxyhemoglobin and promoting oxygen release to tissues. BPGM also possesses phosphatase and mutase activities, maintaining 2,3-BPG homeostasis in red blood cells. Mutations in BPGM can lead to altered oxygen affinity and erythrocytosis.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Erythrocytosis, familial, 8 (Erythrocytosis due to bisphosphoglycerate mutase deficiency) | Loss-of-function mutations reduce 2,3-BPG levels, increasing hemoglobin oxygen affinity and impairing oxygen delivery, leading to compensatory erythrocytosis. | ClinVar, OMIM #222800 |
| Polycythemia (secondary) | BPGM deficiency causes decreased 2,3-BPG, shifting the oxygen dissociation curve leftward, resulting in tissue hypoxia and increased erythropoietin-driven red cell mass. | OMIM, NCBI Gene |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Bone Marrow | 0.0 | Not detected |
| Whole Blood | 0.0 | Not detected |
| Erythrocytes (red blood cells) | High (enzymatic activity) | High expression (protein level) |
| Spleen | 0.0 | Not detected |
| Liver | 0.0 | Not detected |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| K-562 (erythroleukemia) | 0.0 | Low/undetectable in undifferentiated; induced upon erythroid differentiation |
| HEL (erythroleukemia) | 0.0 | Similar to K-562 |
| Erythroid progenitor cells (CD34+ derived) | High (upon differentiation) | Upregulated during erythropoiesis |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.268C>T (p.Arg90Cys) | Missense | Rare | Reduces enzyme activity; associated with erythrocytosis |
| c.206A>G (p.Tyr69Cys) | Missense | Rare | Decreased 2,3-BPG levels; left-shifted oxygen dissociation curve |
| c.418G>A (p.Gly140Arg) | Missense | Rare | Loss of function; familial erythrocytosis |
Mutation functional classification
Loss of Function (LOF)
Most BPGM mutations are loss-of-function, reducing 2,3-BPG synthesis and increasing hemoglobin oxygen affinity.
Gain of Function (GOF)
No gain-of-function mutations reported.
Dominant Negative (DN)
Not described; inheritance is typically autosomal recessive.
View complete mutation data：
Gene Ontology (GO)
Pathways
• ['2
• 3-bisphosphoglycerate metabolic process (R-HSA-6806664)']
• ['Glycolysis / Gluconeogenesis (KEGG: hsa00010)']
• ['Metabolism of carbohydrates (Reactome: R-HSA-71387)']
• ['Erythrocyte oxygen transport (Reactome: R-HSA-1247673)']
Protein Summary
Bisphosphoglycerate mutase (BPGM) is a homodimeric enzyme predominantly expressed in erythrocytes. It catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate (2,3-BPG), the major allosteric effector of hemoglobin. BPGM also has phosphatase activity converting 2,3-BPG to 3-phosphoglycerate, and mutase activity interconverting 2,3-BPG and 3-phosphoglycerate. The enzyme is essential for regulating oxygen release from hemoglobin in peripheral tissues. Deficiency leads to increased hemoglobin oxygen affinity and compensatory erythrocytosis.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| BPGM Knockout HEK293 Cell Line | EDJ-KQ4143 | Human | 669 | Details Get a Quote |
| BPGM Knockout A-549 Cell Line | EDJ-KQ26572 | Human | 669 | Details Get a Quote |
| BPGM Knockout HCT 116 Cell Line | EDJ-KQ26573 | Human | 669 | Details Get a Quote |
| BPGM Knockout HeLa Cell Line | EDJ-KQ26574 | Human | 669 | Details Get a Quote |
