| + |
PLK1 | down-regulates 
phosphorylation
|
PINX1 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166317 |
Ser110 |
SDKKEKKsFSLEEKS |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166321 |
Ser117 |
SFSLEEKsKISKNRV |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166325 |
Ser226 |
ATGKDVEsYLQPKAK |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166329 |
Thr141 |
DLSSRSKtDLDCIFG |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166333 |
Thr317 |
EDATLEEtLVKKKKK |
Homo sapiens |
|
| pmid |
sentence |
| 20573420 |
Here, we show that polo-like kinase 1 (plk1) is a novel interacting protein of pinx1. Plk1 interacts with and phosphorylates pinx1 in vivo and in vitro. Moreover, plk1-mediated phosphorylation of pinx1 at five phosphorylation sites is essential for its plk1-induced degradation. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
3.0
PINX1
- 
- 