EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.93 | glycoprotein |
N-glycosylated |
653715 |
| 3.4.21.93 | glycoprotein |
the catalytic domain of PC1 contains two N-glycosylation sites, the C-terminal domain contains one N-glycosylation site |
669648 |
| 3.4.21.93 | glycoprotein |
the catalytic domain of PC1 contains two potential N-glycosylation sites |
667660 |
| 3.4.21.93 | more |
the PC3 C-terminus is not accessible to cytosolic protein kinase, recombinant PC3 is not phosphorylated in transfected COS-1 cells at a C-terminal phosphorylation site |
667660 |
| 3.4.21.93 | proteolytic modification |
PC1 zymogen is activated by proteolytic cleavage of the signal and the propeptide and is processed at the C-terminal domain, which is regulated by the separate PC1 propeptide and the SAAS CT propeptide, overview |
669648 |
| 3.4.21.93 | proteolytic modification |
proteolytic activation occurs in secretory vesicles at pH 5.5. The pKa of the conserved histidine in proprotein convertase 1/3 is acid-shifted compared with furin and is consistent with its lower pH of activation |
752479 |
| 3.4.21.93 | proteolytic modification |
synthesized as preproenzyme proPC1/3 |
651902 |
