| + |
PRKD1 | down-regulates 
phosphorylation
|
DLC1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169994 |
Ser1244 |
NTLKRENsSPRVMQR |
Homo sapiens |
|
| pmid |
sentence |
| 21087603 |
The tumor suppressor protein dlc1 is regulated by pkd-mediated gap domain phosphorylation.Our results thus show that pkd-mediated phosphorylation of dlc1 on serine 807 negatively regulates dlc1 cellular function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates activity 
phosphorylation
|
DLC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276443 |
Ser557 |
LEEFDVFsPKQDLVP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276444 |
Ser642 |
DSFGSLPsPKELSSF |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276445 |
Ser859 |
RRENSSDsPKELKRR |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276446 |
Ser946 |
SVSPCPSsPKQIHLD |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25452387 |
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
AKT1 |
phosphorylation
|
DLC1 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252550 |
Ser766 |
VTRTRSLsACNKRVG |
Rattus norvegicus |
|
| pmid |
sentence |
| 16338927 |
We have demonstrated that Ser-322 is phosphorylated upon insulin stimulation of intact cells and that this site is directly phosphorylated in vitro by PKB and ribosomal S6 kinase, members of the AGC (protein kinases A, G, and C) family of insulin-stimulated protein kinases |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AKT |
phosphorylation
|
DLC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247997 |
Ser766 |
VTRTRSLsACNKRVG |
Rattus norvegicus |
Adipocyte |
| pmid |
sentence |
| 16338927 |
We have demonstrated that Ser-322 is phosphorylated upon insulin stimulation of intact cells and that this site is directly phosphorylated in vitro by PKB and ribosomal S6 kinase, members of the AGC (protein kinases A, G, and C) family of insulin-stimulated protein kinases |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
DLC1 | down-regulates activity
binding
|
MYH9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269283 |
|
|
Homo sapiens |
OC-3 Cell |
| pmid |
sentence |
| 26977077 |
Our study has shown that Dlc1 interacts with non-muscle myosin heavy chain II-A (Myh9), plectin and spectrin proteins in different multiprotein complexes. Overexpression of Dlc1 led to increased phosphorylation of Myh9 protein and activation of Rac1 GTPase. Dlc1 interacts with phosphorylated Myh9 (Ser-1943). This association of Dlc1 with S1943 phosphorylated Myh9, suggests that Dlc1 may be involved in reduced Myh9 filament stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DLC1
- 
- 