BPGM

Protein identityUniProt · HPA

UniProt accession

P07738

Gene

BPGM

Ensembl

ENSG00000172331

Chromosome

7

Canonical length

259 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Nucleoplasm,Nucleoli,Nucleoli rim

Quaternary structure

Homodimer

OverviewNCBI Gene

2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. This gene encodes a multifunctional enzyme that catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. The enzyme also has phosphoglycerate phosphomutase activity. Deficiency of this enzyme increases the affinity of cells for oxygen. Mutations in this gene result in hemolytic anemia. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2009]

Canonical amino-acid sequenceUniProt

259 residues, UniProt reviewed canonical sequence.

>P07738|BPGM
     1  MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL
    61  NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN
   121  VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
   181  KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA
   241  IQAAIKKVED QGKVKQAKK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against BPGM can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.23

Highest tissue expression

82 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about BPGM.

Disease | AllUniProt

Conditions BPGM is implicated in, by any mechanism.

• Erythrocytosis, familial, 8 (ECYT8) MIM:222800

Disease | GeneticClinVar

4 pathogenic / likely-pathogenic of 60 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Deficiency of bisphosphoglycerate mutase

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1

gnomAD pLI

0.02

gnomAD missense Z

0.7

DepMap mean gene effect

0.05

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• carbohydrate metabolic process
• cellular response to stress
• defense response to protozoan
• erythrocyte development
• establishment of blood-brain barrier
• glycolytic process
• neuroinflammatory response
• oxygen transport
• respiratory gaseous exchange by respiratory system
• carbohydrate derivative catabolic process

Molecular functions

• bisphosphoglycerate mutase activity
• hydrolase activity
• phosphoglycerate mutase activity

Cellular components

• cytosol
• extracellular exosome

Protein domainsUniProt · Pfam · InterPro

• Phosphoglycerate/bisphosphoglycerate mutase, active site
• Phosphoglycerate mutase 1
• Histidine phosphatase superfamily, clade-1
• Histidine phosphatase superfamily
• Histidine phosphatase superfamily (branch 1)

KeywordsUniProt

• Acetylation
• Congenital erythrocytosis
• Glycation
• Glycolysis
• Glycoprotein
• Hereditary hemolytic anemia
• Hydrolase
• Isomerase
• Phosphoprotein

InteractionsUniProt · HPA

Protein binding partners of BPGM in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• PGAM2