EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.5.1.26 | glycoprotein |
- |
735290 |
| 3.5.1.26 | glycoprotein |
AGA contains two glycosylation sites at Asn38 and Asn308 |
753910 |
| 3.5.1.26 | glycoprotein |
Aurelia AGA possesses potential N-glycosylation sites, Asn36, Asn48, Asn168, and Asn213 |
753910 |
| 3.5.1.26 | glycoprotein |
each polypeptide N-glycosylated |
209056, 209057 |
| 3.5.1.26 | glycoprotein |
mannose-glycosyl groups at N38, T310 and N308 |
209052 |
| 3.5.1.26 | glycoprotein |
only the alpha AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview |
755152 |
| 3.5.1.26 | glycoprotein |
only the beta AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview |
755152 |
| 3.5.1.26 | glycoprotein |
two potential N-glycosylation sites are detected along the sequence at Asn52 and Asn153 |
712162 |
| 3.5.1.26 | phosphoprotein |
phosphate on high-mannose type glycosyl groups |
209052 |
| 3.5.1.26 | proteolytic modification |
Asp-151 plays a dual role in the autoproteolytic processing mechanism, acting as the general base to activate the nucleophile and holding the distorted trans conformation that is critical for initiating an N-O acyl shift, generation of a mature/active enzyme from a single-chain precursor, autoproteolysis into two subunits: alpha and beta, mechanism |
657367 |
