EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.4.1.41 | glycoprotein |
- |
757631 |
| 2.4.1.41 | glycoprotein |
2 N-linked oligosaccharides, on most enzyme molecules both oligosaccharides are of the complex type, but some molecules contain one complex type and one high mannose type |
489172 |
| 2.4.1.41 | glycoprotein |
contains 3 N- and 1 O-linked oligosaccharide structures per molecule, soluble enzyme contains N-acetylglucosamine, N-acetylgalactosamine, mannose, galactose and fucose, N-linked structures are likely to be of the truncated high-mannose type |
489175 |
| 2.4.1.41 | glycoprotein |
enzyme contains more than one N-linked oligosaccharide |
489170 |
| 2.4.1.41 | glycoprotein |
full length GalNAc-T18 carries high-mannose N-glycan |
756092 |
| 2.4.1.41 | glycoprotein |
isoform GlaNac-T6 contains two potential N-glycosylation sites |
735979 |
| 2.4.1.41 | glycoprotein |
residues Asn-95 and Asn-552 of the recombinant enzyme are occupied by N-linked sugars in Cos7 cells |
489198 |
| 2.4.1.41 | glycoprotein |
the enzyme is O-glycosylated but does not have any putative N-glycosylation sites |
736207 |
| 2.4.1.41 | more |
enzyme activity is reduced up to 95% by in vitro acetylation of residue K103, S109, K111, K363, S373, K521 and S529 |
718747 |
| 2.4.1.41 | proteolytic modification |
assumed due to detection in supernatants of dissociated ectodermal cells at slightly lower molecular weight |
686299 |
