EC Number |
Posttranslational Modification |
Reference |
---|
3.4.21.41 | glycoprotein |
- |
683195 |
3.4.21.41 | glycoprotein |
carbohydrate content of C1r fragments |
652176 |
3.4.21.41 | proteolytic modification |
- |
81389 |
3.4.21.41 | proteolytic modification |
activation of C1r involves cleavage of a single peptide bond which converts the proenzyme into active enzyme. Activation of the serine-proteinase domain of C1r is controlled by a Ca2+-dependent intramolecular mechanism involving the Ca2+-binding alpha-region. This control is released in C1 by a signal originating in C1q and transmitted through the C1q/C1r interface |
81388 |
3.4.21.41 | proteolytic modification |
activation of the proenzyme C1r can be mimicked under certain conditions by digestion of C1r with trypsin or plasmin |
81395 |
3.4.21.41 | proteolytic modification |
autoactivation of C1r as part of the C1 complex |
683195 |
3.4.21.41 | proteolytic modification |
autoactivation of C1r as part of the C1 complex, modeling, overview |
683889 |
3.4.21.41 | proteolytic modification |
autolytic proteolysis involves cleavage of the Arg279-Gly280 bond in the sequence Asp-Ser-Arg-Gly-Trp-Lys |
81403 |
3.4.21.41 | proteolytic modification |
binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar |
81390 |
3.4.21.41 | proteolytic modification |
the proenzyme C1r is not autoactivatable but undergoes proteolysis by exogenous C1rbar |
81397 |