IndraLab

Statements


USP28 is phosphorylated. 4 / 4
| 4

rlimsp
"ATM/IR-Dependent Phosphorylation of USP28."

rlimsp
"Based on these and other data, it has been proposed that DDR-induced phosphorylation of USP28 leads to its dissociation from the Fbw7 ubiquitin ligase complex, allowing unchecked Myc degradation, and its subsequent association with DDR components, such as 53BP1, claspin, Nbs1, and Chk2, to promote their stabilization (Popov et al., 2007a)."

rlimsp
"To monitor phosphorylation of USP28, the above reaction was carried out using 10 µM substrate (peptides corresponding to amino acids 543–557 [TCLQRWRSEIEQDIQ] or 892–906 [YSLFRKVSVYLLTGL] in USP28) diluted in 1X kinase buffer."

rlimsp
"Phosphorylated USP28 removes a ubiquitin group from a transcription factor called ZNF304, thus increasing its concentration in the nucleus."