EC Number   |
Posttranslational Modification |
Reference |
|---|
    1.2.1.12 | acetylation |
- |
743402 |
| 1.2.1.12 | acylation |
acetylation of lysine residues Lys115, -160, -225, and -252 as post-translational modification of glyceraldehyde-3-phosphate dehydrogenase. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice. Lys115, -225, and -252 are acetylated in a coordinated manner by the p300/cAMP response element-binding protein (CBP)-associated factor acetyltransferase, whereas Lys160 is acetylated by the p300/CBP acetyltransferase |
-, 742477 |
| 1.2.1.12 | alkylation |
methylation on residues Lys213 and Asp242, site specific alterations in methylation sites suggests that the stable changes observed in kinetic and structural GAPDH properties may be due to posttranslational modification of this enzyme during torpor |
743402 |
| 1.2.1.12 | glutathionylation |
- |
673587 |
| 1.2.1.12 | glycoprotein |
N-glycosylated |
674688 |
| 1.2.1.12 | more |
4-hydroxy-2-nonenal-modified GAPDH is degraded by cathepsin G |
686867 |
| 1.2.1.12 | more |
GAPDH of enterohemorrhagic and enteropathogenic Escherichia coli-strains is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification involving residue C149 at the active site, reaction requires NAD+ |
698374 |
| 1.2.1.12 | more |
no signal peptide is found in the deduced protein |
725632 |
| 1.2.1.12 | more |
O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme |
696464 |
| 1.2.1.12 | more |
Plasmodium yoelii, Gapdh undergoes multiple posttranslational modifications |
-, 743738 |
