Title : PHD3 Regulates p53 Protein Stability by Hydroxylating Proline 359.

Pub. Date : 2018 Jul 31

PMID : 30067985






7 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 PHD3 Regulates p53 Protein Stability by Hydroxylating Proline 359. Proline tumor protein p53 Homo sapiens
2 Here, we show that PHD3 hydroxylates p53 at proline 359, a residue that is in the p53-DUB binding domain. Proline tumor protein p53 Homo sapiens
3 Here, we show that PHD3 hydroxylates p53 at proline 359, a residue that is in the p53-DUB binding domain. Proline tumor protein p53 Homo sapiens
4 Hydroxylation of p53 upon proline 359 regulates its interaction with USP7 and USP10, and its inhibition decreases the association of p53 with USP7/USP10, increases p53 ubiquitination, and rapidly reduces p53 protein levels independently of mRNA expression. Proline tumor protein p53 Homo sapiens
5 Hydroxylation of p53 upon proline 359 regulates its interaction with USP7 and USP10, and its inhibition decreases the association of p53 with USP7/USP10, increases p53 ubiquitination, and rapidly reduces p53 protein levels independently of mRNA expression. Proline tumor protein p53 Homo sapiens
6 Hydroxylation of p53 upon proline 359 regulates its interaction with USP7 and USP10, and its inhibition decreases the association of p53 with USP7/USP10, increases p53 ubiquitination, and rapidly reduces p53 protein levels independently of mRNA expression. Proline tumor protein p53 Homo sapiens
7 Hydroxylation of p53 upon proline 359 regulates its interaction with USP7 and USP10, and its inhibition decreases the association of p53 with USP7/USP10, increases p53 ubiquitination, and rapidly reduces p53 protein levels independently of mRNA expression. Proline tumor protein p53 Homo sapiens