IndraLab

Statements


USP47 is ubiquitinated. 5 / 5
| 1 4

sparser
"Furthermore, USP47 deubiquitinates itself, whereas β-TrCP promotes USP47 ubiquitination through interaction with an atypical motif in USP47."

trips
"Furthermore, USP47 deubiquitinates itself, whereas β-TrCP promotes USP47 ubiquitination through interaction with an atypical motif in USP47."

sparser
"Finally, attempts to ubiquitylate USP47 in the presence of purified SCF β-Trcp , E1 and several E2s (UbcH5 and UbcH3) had negative results (data not shown)."

sparser
"This statement is based on the following evidences: (i) USP47 is a stable protein, with a half-life of over 8 h; (ii) proteasome activity does not regulate USP47 protein levels; (iii) silencing of β-Trcp does not induce stabilization of USP47; (iv) USP47 expression is constant during a variety of processes, such as cell-cycle progression, DNA damage checkpoint responses or TNF signaling; and (v) SCF β-Trcp is not able to mediate USP47 ubiquitylation in vitro ."

sparser
"Interestingly, β-TrCP directly binds to the USP47 motif at DSGXXXS and regulates USP47 ubiquitination [ xref ]."