EC Number   |
Posttranslational Modification |
Reference |
|---|
    3.1.3.4 | glycoprotein |
glycosylation is not required for activity |
649679 |
| 3.1.3.4 | glycoprotein |
N-glycosylation |
665805 |
| 3.1.3.4 | glycoprotein |
the anionic and the cationic enzyme form are glycoproteins |
134885 |
| 3.1.3.4 | glycoprotein |
the enzyme is partially N-glycosylated |
751935 |
| 3.1.3.4 | glycoprotein |
the glycosylation is not required for catalytic activity, no glycosylation of PRG-1 |
666926 |
| 3.1.3.4 | glycoprotein |
the two Mg2+-independent isoenzymes, PAP-2a and PAP-2b are glycoproteins |
134884 |
| 3.1.3.4 | phosphoprotein |
- |
-, 694357, 749525, 751097, 751135 |
| 3.1.3.4 | phosphoprotein |
identification of fifteen phosphorylation sites by mass spectrometric analysis |
680814 |
| 3.1.3.4 | phosphoprotein |
insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720 |
714316 |
| 3.1.3.4 | phosphoprotein |
lipin is phosphorylated by human Dullard, a protein that participates in a unique phosphatase cascade regulating nuclear membrane biogenesis, and this cascade is conserved from yeast to mammals |
682573 |
