EC Number   |
Posttranslational Modification |
Reference |
|---|
    3.1.2.22 | glycoprotein |
- |
651450, 653345 |
| 3.1.2.22 | glycoprotein |
heterogenous glycosylation is the major cause of multiple bands observed in SDS-PAGE |
23911 |
| 3.1.2.22 | glycoprotein |
mannose-6-phosphorylated glycoprotein |
23917 |
| 3.1.2.22 | glycoprotein |
N-glycosylation at Asn232, Asn197, and Asn212, essential for activity |
653651 |
| 3.1.2.22 | glycoprotein |
N-glycosylation of N197 and N232, but not N212, is essential for enzyme activity and intracellular transport. Deglycosylation of overexpressed PPT1 produced in neurons and fibroblasts demonstrates differentially modified PPT1 in different cell types |
678930 |
| 3.1.2.22 | glycoprotein |
the enzyme is N-glycosylated at residues 197, 212, and 232 |
751407 |
| 3.1.2.22 | glycoprotein |
three potential asparagine-linked glycosylation sites are found near the carboxyl terminus of the protein at positions 199, 214, and 234. Glycosylation of the amino acid 234 demonstrated experimentally |
23913 |
| 3.1.2.22 | palmitoylation |
the enzyme is palmitoylated at Cys-6 by DHHC3 and DHHC7 |
751937 |
| 3.1.2.22 | proteolytic modification |
enzyme contains 2 putative cleavage sites for the kex-related endopeptidase Krp1p, the precursor is proteolytically processed to form distinct Ppt1p and Dolpp1p domains, Arg354 is crucial for the processing |
651030 |
