Title : Detection of Non-Canonical N-Glycosylationat
N274
Abstract :
- A small percentage of peptides (<1%) containingthe noncanonical N-glycosylation site NVV at N274 were occupied inboth serum and recombinant ITIH4
- Noncanonical N-glycosylation hasrecently been described in immunoglobulins and a recent report alsodescribes high-mannose glycoforms at noncanonical N-glycosylationsites on several murine proteins
- Using CID MS/MS, we found high-mannoseN-glycopeptides on the NVVFVIDK peptide in both serum and cell-derived ITIH4
- As we find only high-mannose N-glycans at this site, its accessibilityto glycosidases and glycosyltransferases during protein maturationin the Golgi may be limited
- The N274site is near the beginning of the von Willebrand factor type A ( vWF ) domain of ITIH4 , which spans residues 272–432
- Protein vWFdomains are typically involved in protein–protein interactions,and glycosylation at this site could potentially affect ITIH4 interactionswith other proteins
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. N-glycosylation, , -, -, site
- 3. high-mannoseN-glycopeptides, , -, the NVVFVIDK peptide, peptide
- 6. glycosylation, , -, -, site
- 6. glycosylation, , ITIH4, -, site
Output(Part-Of) (sent_index,
protein,
site):
- 2. proteins, N-glycosylationsites
- 3. ITIH4, peptide
- 5. ITIH4, domain
- 5. vWF, domain
- 5. von Willebrand factor, domain
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):