Article
Mutation of aspartic acid 199 in USP1 disrupts its deubiquitinating activity and impairs DNA repair.
FEBS letters - 1 Aug 2021
Jang Seok Won, Kim Jung Min
Abstract excerpt
The deubiquitinating enzyme USP1 contains highly conserved motifs forming its catalytic center. Recently, the COSMIC mutation database identified a mutation in USP1 at Asp-199 in endometrial cancer. Here, we investigated the role of Asp-199 for USP1 function. The mutation of aspartic acid to alanine (D199A) resulted in failure of USP1 to undergo autocleavage and form a complex with ubiquitin, indicating D199A...
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