EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.8.17 | glycoprotein |
- |
645375 |
| 2.7.8.17 | glycoprotein |
an N-linked glycoprotein |
739732 |
| 2.7.8.17 | glycoprotein |
an N-linked oligosaccharide, hydrolysis by peptide-N-glycosidase F (PNGase F) |
738351 |
| 2.7.8.17 | glycoprotein |
enzyme contains N-glycosylation sites at position 88 and 115. N-glycosylation is important for intracellular trafficking of the gamma subunit |
725457 |
| 2.7.8.17 | glycoprotein |
the gamma subunit of GlcNAc-1-phosphotransferase is a soluble glycoprotein |
738354 |
| 2.7.8.17 | glycoprotein |
the wild-type inactive alphabeta precursor protein contains a very low amount of complex-type glycans, all of the N-linked glycans are of the high mannose-type, which is consistent with its endoplasmic reticulum localization. The mutant K4Q alphabeta phosphotransferase contains increased complex-type N-linked glycans |
739540 |
| 2.7.8.17 | proteolytic modification |
proteolytic cleavage of the alpha/beta enzyme precursor |
739527 |
| 2.7.8.17 | proteolytic modification |
upon arrival in the Golgi apparatus, the newly synthesized alpha/beta subunit precursor is catalytically activated by site-1 protease (S1P). A stretch of amino acids in the N-terminus of the beta-subunit is essential for precise S1P-mediated cleavage and activity of theGlcNAc-1-phosphotransferase. The proteolytic cleavage of the alpha/beta-subunit precursor protein is a prerequisite for the catalytic activity of the GlcNAc-1-phosphotransferase and therefore plays an important role in the biogenesis of lysosomes. Proteolytic S1P-mediated activation of the alpha/beta-subunit precursor of GlcNAc-1-phosphotransferase into mature subunits occurs in the cis-Golgi apparatus |
738351 |
