EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.81 | glycoprotein |
ADAm10 possesses four potential N-glycosylation sites |
719416 |
| 3.4.24.81 | glycoprotein |
contained high-mannose as well as complex-type N-glycans |
696395 |
| 3.4.24.81 | glycoprotein |
contains high-mannose as well as complex-type N-glycans. Glycosylation sites: S269, T280, S441, T553 |
696395 |
| 3.4.24.81 | glycoprotein |
glycosylation sites in the catalytic and disintegrin domain contain high-mannose as well as complex type N-glycans |
708492 |
| 3.4.24.81 | glycoprotein |
the enzyme has four potential N-glycosylation sites (N267, N278, N439 and N551) |
753694 |
| 3.4.24.81 | glycoprotein |
transmembrane glycoprotein |
709083 |
| 3.4.24.81 | proteolytic modification |
ADAM10 itself is subject to ectodomain shedding via a mechanism which is inhibited by ADAM inhibitor (GW4023) and stimulated by phorbol ester treatment of cells. The treatment of cells with GW4023 causes a reciprocal accumulation of membrane-associated mature ADAM10 in both cell lysates and extracellular membrane vesicles. ADAM9 is, at least in part, responsible for the ectodomain shedding of ADAM10 |
699655 |
| 3.4.24.81 | proteolytic modification |
synthesized in an inactive form, which is proteolytically activated during its forward transport along the secretory pathway and at the plasma membrane |
709083 |
| 3.4.24.81 | proteolytic modification |
tetraspanin overexpression enhances ADAM10 prodomain maturation, whereas TSPAN12 ablation diminishes ADAM10 maturation. TSPAN12 serves as a robust partner for ADAM10 and promotes ADAM10 maturation, thereby facilitating ADAM10-dependent proteolysis of amyloid precursor protein |
708462 |
| 3.4.24.81 | proteolytic modification |
the enzyme has an inactive form that is activated by cleavage |
644072 |
