| + |
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 |
| + |
PKN3 |
phosphorylation
|
BCAR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264574 |
Ser428 |
PAEGKRLsASSTGST |
in vitro |
|
| pmid |
sentence |
| 30422386 |
These results verified the presence of a PKN3 phosphorylation motif in the sequence surrounding Ser432 and indicated that PKN3 phosphorylates p130Cas on Ser432 in vitro.|Human Ser428 of p130Cas corresponds to mouse p130Cas Ser432| |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BCAR1 | up-regulates activity
binding
|
PKN3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264573 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 30422386 |
Taken together, the data suggest that p130Cas expression induces PKN3 activation and this activation is independent of p130Cas–PKN3 interaction. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
PKN3
- 
- 