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USP13 deubiquitinates TOPBP1. 3 / 4
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"Protein interaction experiments demonstrated that USP13 could co-immunoprecipitate with endogenous TopBP1, and in vitro deubiquitination enzyme experiments showed that WT-USP13 could deubiquitinate TopBP1, while CA-USP13 could not, highlighting the requirement for USP13 ubiquitination activity (Kim et al., 2021)."
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"USP13 can deubiquitinate DNA topoisomerase 2 binding protein 1 (TopBP1), influencing DNA chain breakage and repair processes."
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"For instance, studies have shown that TopBP1 is ubiquitinated by the E3 ubiquitin ligase hHYD and deubiquitinated by USP13, while its phosphorylation enhances its recruitment to DNA damage sites [18, 19]."
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