EC Number   |
General Information |
Reference |
|---|
   2.4.1.41 | malfunction |
aberrant mucin O-glycosylation is often observed in cancer and is characterized by the expression of immature simple mucin-type carbohydrate antigens. Altered expression of ppGalNAc-Ts can be one of the mechanisms that explain the changes in mucin O-glycosylation during malignant transformation |
704935 |
| 2.4.1.41 | malfunction |
knockdown of the isoform GALNT3 expression in epithelial ovarian cancer cells leads to sharp decrease of cell proliferation and induced S-phase cell cycle arrest. Additionally, GALNT3 suppression significantly inhibits epithelial ovarian cancer cell migration and invasion. GALNT3 knockdown is also accompanied with increase of the cell adhesion molecules beta-catenin and E-cadherin |
736918 |
| 2.4.1.41 | malfunction |
mutation of the enzyme might be involved in development of cancer |
706506 |
| 2.4.1.41 | malfunction |
Overexpression of polypeptide N-acetylgalactosaminyltransferase 6 induces epithelial-to-mesenchymal transition-like morphologic alterations |
720549 |
| 2.4.1.41 | metabolism |
GalNAc-type protein O-glycosylation is important in modulating protein processing, O-linked glycans have important biological functions |
718991 |
| 2.4.1.41 | metabolism |
the enzyme catalyzes the first step in mucin-type O-glycosylation |
736207 |
| 2.4.1.41 | physiological function |
both GalNAc-T1 and -T4 isoforms are highly expressed during osteogenesis of MC3T3-E1 pre-osteoblasts and their knockdown by short hairpin RNA decreases osteoblast formation and bone mineralization. Knockdown of GalNAc-T1 or -T4 decreases mRNA and protein levels of bone sialoprotein. Knockdown of GalNAc-T1 decreases mRNA levels of osteocalcin and osteoprotegerin. Knockdown of T1 or T4 isoforms does not change the expression of osteopontin, COLLI, receptor activator for nuclear factor-kappaB ligand and transforming growth factor-beta |
755948 |
| 2.4.1.41 | physiological function |
both GalNAc-T1 and -T4 isoforms are highly expressed during osteogenesis of MC3T3-E1 pre-osteoblasts and their knockdown by short hairpin RNA decreases osteoblast formation and bone mineralization. Knockdown of GalNAc-T1 or -T4 decreases mRNA and protein levels of bone sialoprotein. Knockdown of GalNAc-T4 decreases mRNA levels osteocalcin, osteoprotegerin and vitamin D receptor. Knockdown of T1 or T4 isoforms does not change the expression of osteopontin, COLLI, receptor activator for nuclear factor-kappaB ligand and transforming growth factor-beta |
755948 |
| 2.4.1.41 | physiological function |
GalNAc-T18 silencing in cells decreases O-glycosylation levels and activates ER stress leading to apoptosis. After treatment with chaperone 4-phenylbutyric acid or forced expression of GalNAc-T18 in the GalNAc-T18 knockdown cell, these defects can be significantly alleviated. GalNAc-T18 exerts its functions in O-glycosylation and ER stress via a non-catalytic mechanism. Both wild-type GalNT18 and mutant H253D show no catalytic activity in vitro, but both of them can rescue the O-glycosylation defect of GalNAc-T18 knockdown cells |
756092 |
| 2.4.1.41 | physiological function |
isoform GalNAc-T1 is largely required for the Ebola virus surface glycoprotein-mediated adhesion defects. Despite its profound effect on surface glycoprotein function, the absence of GalNAc-T1 only modestly reduces the O-glycan mass of surface glycoprotein. A small segment of the mucin-like domain of the surface glycoprotein is critical for function and mutation of five glycan acceptor sites within this segment are sufficient to abrogate surface glycoprotein function |
757208 |
