IndraLab

Statements

USP15 is phosphorylated on S678. 12 / 12
| 5 7
sparser
"Mechanistically, USP15 is recruited to DNA double-strand breaks (DSBs) by MDC1, which requires the FHA domain of MDC1 and phosphorylated Ser678 of USP15."
30874560
rlimsp
"USP15 Ser678 phosphorylation is essential for its function in homologous recombination (HR)."
30874560
rlimsp
"We also found that MDC1-FHA domain bound phosphorylated USP15, and Ser678 phosphorylation was essential for this binding (Fig. 4i, j)."
30874560
rlimsp
"Mechanistically, USP15 is recruited to DNA double-strand breaks (DSBs) by MDC1, which requires the FHA domain of MDC1 and phosphorylated Ser678 of USP15."
30874560
rlimsp
"These results clearly indicate that USP15 Ser678 phosphorylation is required for its function in HR."
30874560
sparser
"These results clearly indicate that USP15 Ser678 phosphorylation is required for its function in HR."
30874560
sparser
"USP15 is phosphorylated at Ser678 and recruited to DSBs."
30874560
rlimsp
"We confirmed that USP15 S678 phosphorylation is essential for its functions in HR and genome stability."
30874560
sparser
"We confirmed that USP15 S678 phosphorylation is essential for its functions in HR and genome stability."
30874560
rlimsp
"Previous large-scale proteomic studies also demonstrated that Ser678 of USP15 is phosphorylated by ATM following DNA damage."
30874560
rlimsp
"As shown in Fig. 4c, mutation at Ser678 abolished ATM-dependent USP15 phosphorylation, indicating that Ser678 is the major ATM phosphorylation site of USP15."
30874560
sparser
"As shown in Fig.  xref , mutation at Ser678 abolished ATM-dependent USP15 phosphorylation, indicating that Ser678 is the major ATM phosphorylation site of USP15."
30874560