EC Number |
Posttranslational Modification |
Reference |
---|
3.4.21.B24 | glycoprotein |
- |
718107 |
3.4.21.B24 | glycoprotein |
glycosylation sites are at N465 and N629 |
718107 |
3.4.21.B24 | glycoprotein |
the enzyme contains two putative N-glycosylation sites |
692581 |
3.4.21.B24 | proteolytic modification |
activation |
29874 |
3.4.21.B24 | proteolytic modification |
after cotranslational removal of the signal peptide, the resulting proPCSK undergoes maturation by autocatalytic cleavage between the pro and the catalytic domains, within a cleavage motif that is also recognized by the fully activated enzyme in the primary sequence of its physiological substrates, mechanism |
692581 |
3.4.21.B24 | proteolytic modification |
after cotranslational removal of the signal peptide, the resulting proPCSK undergoes maturation by autocatalytic cleavage between the pro and the catalytic domains, within a cleavage motif that is also recognized by the fully activated enzyme in the primary sequence of its physiological substrates, mechanism, overview |
692581 |