EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.6.4.13 | acetylation |
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation |
757299 |
| 3.6.4.13 | phosphoprotein |
helicase activity of DDX5 is regulated by phosphorylation and calmodulin binding |
691843 |
| 3.6.4.13 | phosphoprotein |
phosphorylation at serine/threonine residues of both DDX3 and DDX5 affect the protein-protein interaction. During the G2/M phase, phosphorylation of DDX3 is decreased, whereas, the phosphorylation of DDX5 is, compared with the G1/S phase |
720096 |
| 3.6.4.13 | phosphoprotein |
phosphorylation of p68 RNA helicase at Y593 upregulates transcription of the Snail1 gene |
713159 |
| 3.6.4.13 | phosphoprotein |
phosphorylation of tyrosine in p68 enhances cell transformation and cancer cell migration. The Y593 phosphorylation of p68 promotes the detachment of histone deacetylase (HDAC) 1 from the Snail1 promoter, which leads to the expression of Snail1. The phosphorylation of particular sites (such as Y593 and Y595 induced by PDGF) in p68 can attenuate resistance to TRAIL-induced apoptosis. The phosphorylated p68 exerts a definite protective effect on the activities of cancer cells. Phosphorylated p68 can enter the cytoplasm, which leads to its interaction with beta-catenin and displacment of axin |
757299 |
| 3.6.4.13 | proteolytic modification |
enzyme contains a 58-amino acid transit peptide that is predicted to be targeted to the chloroplast |
720747 |
| 3.6.4.13 | sumoylation |
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation. P68 may be sumoylated on site K53 residue, which may be associated with transcriptional coactivation |
757299 |
| 3.6.4.13 | ubiquitination |
P68 may undergo various modifications such as ubiquitylation, sumoylation, and acetylation |
757299 |
