EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.7.1.1 | glycoprotein |
glucokinase is modified by O-GlcNAcylation. siRNA-mediated O-linked N-acetylglucosamine transferase knock-down not only decreases O-GlcNAc content but also glucokinase protein level |
737623 |
| 2.7.1.1 | lipoprotein |
The N-terminal MGQICQ motif in the unique germ cell-specific domain of hexokinase acquires hydrophobicity by N-myristoylation and palmitoylation. The mutation of the myristoyl recipient Gly2 impedes plasma membrane association and relocates the enzyme to the cytosol but not the nucleus. Substitution of the putatively palmitoylated Cys5 is reflected in a similar loss of compartmentalization of the protein |
737798 |
| 2.7.1.1 | more |
a posttranslational modification leading to membrane binding may occur |
-, 640260 |
| 2.7.1.1 | more |
isoenzyme PIIM derives from PII by a posttranslational event |
640235 |
| 2.7.1.1 | more |
poly/multiubiquitination of glucokinase in vitro serves as a signal for proteasomal degradation of the newly synthesized protein |
674840 |
| 2.7.1.1 | phosphoprotein |
- |
722695 |
| 2.7.1.1 | phosphoprotein |
differential phosphorylation of hexokinase is responsible for altered kinetic properties: in control frogs, hexokinase is in a higher phosphate form and displays a high substrate affinity and high activity, whereas in frozen frogs hexokinase is less phosphorylated, with lower substrate affinity and lower activity |
722079 |
| 2.7.1.1 | side-chain modification |
the germ cell component of testis contains a unique tyrosine-phosphorylated form of hexokinase, hexokinase I of brain, kidney, spleen and heart are not phosphorylated |
640229 |
