+ |
PLK1 | up-regulates activity
phosphorylation
|
USP16 |
0.344 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274016 |
Ser330 |
ILKAFGNsTEKLDEE |
in vitro |
|
pmid |
sentence |
26323689 |
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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274015 |
Ser386 |
HESFLDLsLPVLDDQ |
in vitro |
|
pmid |
sentence |
26323689 |
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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-274017 |
Ser486 |
SEYEAEMsLQGEVNI |
in vitro |
|
pmid |
sentence |
26323689 |
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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278270 |
Ser486 |
SEYEAEMsLQGEVNI |
Homo sapiens |
|
pmid |
sentence |
26323689 |
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. |
|
Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens |
+ |
TTK | down-regulates quantity by destabilization
phosphorylation
|
USP16 |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277350 |
Ser415 |
VEDEDQDsEEEKDND |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
28380042 |
Usp16 is a TTK phosphorylation substrate. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277351 |
Thr554 |
EVLTSSPtRNLNGAY |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
28380042 |
Usp16 is a TTK phosphorylation substrate. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK1 | up-regulates
phosphorylation
|
USP16 |
0.457 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202678 |
Ser552 |
DLEVLTSsPTRNLNG |
Homo sapiens |
|
pmid |
sentence |
24013421 |
Here, we report that cyclin-dependent kinase 1 (cdk1) phosphorylates the histone h2a deubiquitinase ubp-m at serine 552 (s552p), and, importantly, this phosphorylation is required for cell cycle progression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
USP16 | down-regulates activity
deubiquitination
|
Histone H2A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277348 |
|
|
Homo sapiens |
|
pmid |
sentence |
17914355 |
Here we report the identification and functional characterization of the major deubiquitinase for histone H2A, Ubp-M (also called USP16). Ubp-M prefers nucleosomal substrates in vitro, and specifically deubiquitinates histone H2A but not H2B in vitro and in vivo. This study identifies the major deubiquitinase for histone H2A and demonstrates that H2A deubiquitination is critically involved in cell cycle progression and gene expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |