EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.17.21 | acetylation |
treatment with valproic acid increases the acetylation of glutamate carboxypeptidase II protein at the lysine residues and facilitates a decrease of the poly-ubiquitinated glutamate carboxypeptidase II level. Similarly, M344, a specific histone deacetylase 1/6 inhibitor, also increases the glutamate carboxypeptidase II protein level |
731257 |
| 3.4.17.21 | glycoprotein |
- |
137218, 670685 |
| 3.4.17.21 | glycoprotein |
10 possible N-glycosylation sites |
668408 |
| 3.4.17.21 | glycoprotein |
identification of the N-glycosylation sites, e.g. N121, N153, N195, N638, and N140, the enzyme is heavily glycosylated |
670817 |
| 3.4.17.21 | glycoprotein |
N-glycosylation, correct sorting into appropriate post-Golgi vesicles for targeting into the apical plasma membrane depends on the N-glycosylation of the enzyme, inhibition of N-glycosylation abolishes the polarized enzyme expression, overview |
670219 |
| 3.4.17.21 | glycoprotein |
PSMA is a transmembrane glycoprotein |
709649 |
| 3.4.17.21 | glycoprotein |
PSMA is a type II transmembrane glycoprotein |
708256 |
| 3.4.17.21 | glycoprotein |
the enzyme is a type II membrane glycoprotein |
669595 |
| 3.4.17.21 | glycoprotein |
the extracellular domain contains nine potential glycosylation sites |
137215 |
| 3.4.17.21 | glycoprotein |
type II membrane glycoprotein |
670363 |
