EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.4.12 | glycoprotein |
- |
651148, 692274, 751328 |
| 3.1.4.12 | glycoprotein |
aSMase is an N-glycoprotein bearing 5 discrete asparagine-linked glycans with glycosylation of N395 and N520 being critical for normal secretion and function. SMPDL3A contains 7 potential N-linked glycosylation motifs (defined by the pattern NX[S|T], where X is any amino acid except proline). Notably, two of these motifs (N222 and N356) are perfectly aligned with the functionally important N395 and N520 N-linked sites of aSMase |
730060 |
| 3.1.4.12 | glycoprotein |
at least five of six potential glycosylation sites are utilized |
652444 |
| 3.1.4.12 | glycoprotein |
molecular mass reduction of approx. 8-9 kDA upon deglycosylation |
653119 |
| 3.1.4.12 | glycoprotein |
synthesis of a 78 kDA preproform of the enzyme which is glycosylated and proteolytically cleaved to a 72 kDa pre-form and subsequently to a 70 kDA mature enzyme |
714689 |
| 3.1.4.12 | glycoprotein |
the enzyme has seven sites for glycosylation |
750518 |
| 3.1.4.12 | glycoprotein |
the five potential N-glycosylation sites are all glycosylated, activity of the enzyme is severely affected by defective N-glycosylation |
663951 |
| 3.1.4.12 | glycoprotein |
the mature form and its precursors have six potential N-glycosylation sites, and at least five of them are important for proper folding, protection against proteolysis, and enzymatic activity of A-SMase. A-SMase has a mannose 6-phosphate residue that is required for lysosomal targetting of the enzyme via the mannose 6-phosphate receptor |
716445 |
| 3.1.4.12 | glycoprotein |
the protein has five sites of N-glycosylation |
751655 |
| 3.1.4.12 | lipoprotein |
neutral sphingomyelinase 2 is palmitoylated on multiple cysteine residues, palmitoylation of nSMase2 via thioester linkage, mutational analysis, overview |
680745 |
