Title : Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation.

Pub. Date : 2000 Nov

PMID : 11046142






6 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation. Lysine tumor protein p53 Homo sapiens
2 Simultaneous mutation of lysine residues 370, 372, 373, 381, 382, and 386 to arginine residues (6KR p53 mutant) generates a p53 molecule with potent transcriptional activity that is resistant to Mdm2-induced degradation and is refractory to Mdm2-mediated ubiquitination. Lysine tumor protein p53 Homo sapiens
3 Simultaneous mutation of lysine residues 370, 372, 373, 381, 382, and 386 to arginine residues (6KR p53 mutant) generates a p53 molecule with potent transcriptional activity that is resistant to Mdm2-induced degradation and is refractory to Mdm2-mediated ubiquitination. Lysine tumor protein p53 Homo sapiens
4 Those differences are also manifest in HeLa cells which express the human papillomavirus E6 protein, suggesting that p53 C-terminal lysine residues are also implicated in E6-AP-mediated ubiquitination. Lysine tumor protein p53 Homo sapiens
5 These data suggest that p53 C-terminal lysine residues are the main sites of ubiquitin ligation, which target p53 for proteasome-mediated degradation. Lysine tumor protein p53 Homo sapiens
6 These data suggest that p53 C-terminal lysine residues are the main sites of ubiquitin ligation, which target p53 for proteasome-mediated degradation. Lysine tumor protein p53 Homo sapiens