Protein trafficking & glycosylation
Gene co-expression module in Goblet cells
| Category | Mucus production & secretion |
|---|---|
| Genes | 10 |
| Annotation certainty | 5 of 5 |
| Annotation consistency | 9 of 10 genes have a known function matching the annotation |
Why this annotation
GALNT7 and GALNT3 initiate O-linked GalNAc glycosylation of mucins. COPB2, COPB1, COPG1, COPA are all subunits of the COPI vesicle coat that mediates retrograde Golgi-to-ER and intra-Golgi trafficking essential for glycoprotein processing. EDEM3 supports ER-associated degradation of misfolded glycoproteins. TM9SF2/3 are Golgi/lysosomal membrane proteins involved in secretory protein trafficking. This module represents the Golgi COPI trafficking and mucin O-glycosylation initiation machinery. It is a neighbor to M61 (Golgi structure and exocytosis) and M89 (goblet secretory proteins), forming a coherent secretory pathway cluster. Mild upregulation in inflammation is consistent with increased secretory demand.
Genes
COPA, COPB1, COPB2, COPG1, EDEM3, FAM114A1, GALNT3, GALNT7, TM9SF2, TM9SF3
Most correlated modules
- N-Glycosylation ER Stress · correlation 0.91
- ER Targeting ERAD · correlation 0.91
- Golgi-Exocytosis Machinery · correlation 0.88
- Mucin O-Glycosylation · correlation 0.87
- ER Protein Translocation · correlation 0.87
- Goblet Secretory Identity · correlation 0.83
- UPR Chaperone Response · correlation 0.82
- Mucin Folding Machinery · correlation 0.82
Module annotations were drafted by a large language model from the module's genes, then reviewed and approved by a domain expert. See sources & licences.