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