EC Number   |
Posttranslational Modification |
Reference |
|---|
   7.6.2.2 | glycoprotein |
- |
210390, 657552, 684938, 697712, 711295 |
| 7.6.2.2 | glycoprotein |
glycosylation is not essential for ATPase or transport function, the N-linked oligosaccharides appear to influence the conformation of the protein in a subtle way |
210381 |
| 7.6.2.2 | glycoprotein |
MDR1, phosphorylated glycoprotein |
658514 |
| 7.6.2.2 | glycoprotein |
one glycosylation site is in the second half of the P-glycoprotein, the second glycosylation site links transmembrane domains 8 and 9 in the traditional model of the P-glycoprotein topology |
210387 |
| 7.6.2.2 | glycoprotein |
P-gp is a highly glycosylated plasma membrane protein that exists in several glycoforms, with different degrees of glycosylation |
695397 |
| 7.6.2.2 | glycoprotein |
protein contains putative glycosylation sites |
210389 |
| 7.6.2.2 | glycoprotein |
the enzyme is N-glycosylated at N596 |
748763 |
| 7.6.2.2 | phosphoprotein |
MDR1, phosphorylated glycoprotein |
658514 |
| 7.6.2.2 | side-chain modification |
contains putative phosphorylation and myristylation sites |
210389 |
| 7.6.2.2 | ubiquitination |
H1 prompts the degradation of Pgp and decreases Pgp protein half-life by enhancing the ubiquitination of Pgp |
711656 |
