IndraLab

Statements

PLK1 phosphorylates USP16 on S486. 5 / 5
1 2 | 2
signor
"In this study, we show that ubiquitin-specific peptidase 16 (Usp16) is a novel substrate for Plk1, and sequential phosphorylation by CDK1 and Plk1 activates Usp16, which, in turn, deubiquitinates Plk1 and promotes the recruitment of Plk1 to, and its retention on, the kinetochores for proper chromosome alignment.|In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig."
26323689
signor
"Plk1 phosphorylates and activates Usp16. In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig. S2 D)."
26323689
rlimsp
"By sequence analysis, we found three (S330, S386, and S486) potential Plk1 phosphorylation sites on Usp16 (Fig."
26323689
rlimsp
"In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig."
26323689
biopax:phosphositeplus
No evidence text available