PGM3
Phosphoglucomutase 3: A Key Enzyme in Glycosylation and Immune Function
Gene Information Card
| Symbol | PGM3 |
|---|---|
| Full Name | Phosphoglucomutase 3 |
| Gene Type | Protein coding |
| Chromosomal Location | 6q14.1 |
| NCBI Gene ID | 5238 ncbi.nlm.nih.gov/gene/5238 |
| Ensembl ID | ENSG00000113319 |
| UniProt ID | O95394 |
| OMIM ID | 172100 |
| HGNC ID | 8907 |
| Aliases | AGM1, PAGM, PGM3 |
Description
PGM3 encodes phosphoglucomutase 3, an enzyme that catalyzes the interconversion of N-acetylglucosamine-6-phosphate and N-acetylglucosamine-1-phosphate, a critical step in the hexosamine biosynthetic pathway. This pathway is essential for the synthesis of UDP-N-acetylglucosamine, a key substrate for N-glycosylation and O-GlcNAcylation. Mutations in PGM3 cause a congenital disorder of glycosylation (CDG IIt) characterized by immune deficiency, intellectual disability, and skeletal abnormalities.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Congenital disorder of glycosylation type IIt (CDG IIt) | Loss-of-function mutations impair UDP-GlcNAc synthesis, disrupting N-glycosylation and O-GlcNAcylation, leading to multisystem defects. | ClinVar, OMIM |
| Immunodeficiency with hyper-IgE syndrome | PGM3 mutations reduce glycosylation of immune receptors, impairing T-cell and B-cell function. | ClinVar, OMIM |
| Myelodysplastic syndrome | Somatic PGM3 mutations may contribute to clonal hematopoiesis and dysplasia. | COSMIC |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Lymph node | 12.5 | Medium |
| Spleen | 10.8 | Medium |
| Bone marrow | 9.2 | Medium |
| Brain | 6.1 | Low |
| Liver | 4.3 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| K-562 | 14.7 | Leukemia cell line |
| HEK 293 | 11.2 | Embryonic kidney |
| HeLa | 9.8 | Cervical carcinoma |
| HepG2 | 7.5 | Hepatocellular carcinoma |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1000G>A (p.Glu334Lys) | Missense | Rare | Loss of function; reduces enzyme activity |
| c.1556T>C (p.Leu519Pro) | Missense | Rare | Loss of function; disrupts protein folding |
| c.1462C>T (p.Arg488Trp) | Missense | Rare | Loss of function; impairs substrate binding |
Mutation functional classification
Loss of Function (LOF)
Most PGM3 mutations are recessive loss-of-function, reducing enzyme activity and UDP-GlcNAc production.
Gain of Function (GOF)
Not reported.
Dominant Negative (DN)
Not reported.
View complete mutation data：
Gene Ontology (GO)
| • phosphoglucomutase activity | • N-acetylglucosamine metabolic process |
| • UDP-N-acetylglucosamine biosynthetic process | • protein glycosylation |
| • cytoplasm |
Pathways
• Hexosamine biosynthetic pathway
• O-GlcNAcylation
• N-glycan biosynthesis
Protein Summary
Phosphoglucomutase 3 (PGM3) is a 62 kDa cytoplasmic enzyme that converts N-acetylglucosamine-6-phosphate to N-acetylglucosamine-1-phosphate, a rate-limiting step in the hexosamine pathway. It is ubiquitously expressed with highest levels in lymphoid tissues. The protein contains a phosphoserine intermediate and requires magnesium ions for activity. Defects in PGM3 lead to reduced UDP-GlcNAc pools, impairing glycosylation of proteins critical for immune function and development.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID |
|---|
