| + |
PKN3 | up-regulates activity 
phosphorylation
|
ARHGAP18 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264571 |
Ser156 |
QKRVETVsQTLRKKN |
in vitro |
|
| pmid |
sentence |
| 33092266 |
We present strong evidence that PKN3-ARHGAP18 interaction is increased upon ARHGAP18 phosphorylation and that the phosphorylation of ARHGAP18 by PKN3 enhances its GAP domain activity and contributes to negative regulation of active RhoA.|These results support our data from phosphoproteomic screen and suggest that ARHGAP18 can be phosphorylated by PKN3 on Thr154, Ser156 and Thr158. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264570 |
Thr154 |
AVQKRVEtVSQTLRK |
in vitro |
|
| pmid |
sentence |
| 33092266 |
We present strong evidence that PKN3-ARHGAP18 interaction is increased upon ARHGAP18 phosphorylation and that the phosphorylation of ARHGAP18 by PKN3 enhances its GAP domain activity and contributes to negative regulation of active RhoA.|These results support our data from phosphoproteomic screen and suggest that ARHGAP18 can be phosphorylated by PKN3 on Thr154, Ser156 and Thr158. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264572 |
Thr158 |
RVETVSQtLRKKNKQ |
in vitro |
|
| pmid |
sentence |
| 33092266 |
We present strong evidence that PKN3-ARHGAP18 interaction is increased upon ARHGAP18 phosphorylation and that the phosphorylation of ARHGAP18 by PKN3 enhances its GAP domain activity and contributes to negative regulation of active RhoA.|These results support our data from phosphoproteomic screen and suggest that ARHGAP18 can be phosphorylated by PKN3 on Thr154, Ser156 and Thr158. |
|
| Publications: |
3 |
Organism: |
In Vitro |
3.0
ARHGAP18
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