| + |
PLK1 | up-regulates activity 
phosphorylation
|
RIOK2 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262937 |
Ser335 |
TKEGSEFsFSDGEVA |
in vitro |
|
| pmid |
sentence |
| 21880710 |
Here, we report that the atypical protein kinase Rio2 is a novel substrate of Plk1 and can be phosphorylated by Plk1 at Ser-335, Ser-380, and Ser-548. Overexpression of Rio2 causes a prolonged mitotic exit whereas knockdown of Rio2 accelerates mitotic progression, suggesting that Rio2 is required for the proper mitotic progression. F urthermore, time-lapse imaging data show that overexpression of Rio2 but not Rio2 S3A results in a slowed metaphase-anaphase transition. Collectively, these findings strongly indicate that the Plk1-mediated phosphorylation of Rio2 regulates metaphase-anaphase transition during mitotic progression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262938 |
Ser380 |
PEQIKEDsLSEESAD |
in vitro |
|
| pmid |
sentence |
| 21880710 |
Here, we report that the atypical protein kinase Rio2 is a novel substrate of Plk1 and can be phosphorylated by Plk1 at Ser-335, Ser-380, and Ser-548. Overexpression of Rio2 causes a prolonged mitotic exit whereas knockdown of Rio2 accelerates mitotic progression, suggesting that Rio2 is required for the proper mitotic progression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262939 |
Ser548 |
KSSLEAAsFWGE |
in vitro |
|
| pmid |
sentence |
| 21880710 |
Here, we report that the atypical protein kinase Rio2 is a novel substrate of Plk1 and can be phosphorylated by Plk1 at Ser-335, Ser-380, and Ser-548. Overexpression of Rio2 causes a prolonged mitotic exit whereas knockdown of Rio2 accelerates mitotic progression, suggesting that Rio2 is required for the proper mitotic progression. |
|
| Publications: |
3 |
Organism: |
In Vitro |
3.0
RIOK2
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