| + |
CDK2 | up-regulates 
phosphorylation
|
DLG1 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182761 |
Ser158 |
FVSHSHIsPIKPTEA |
Homo sapiens |
|
| pmid |
sentence |
| 19066288 |
We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. phosphorylation on ser158 and ser442 enhances nuclear expression of dlg1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182765 |
Ser443 |
FLGQTPAsPARYSPV |
Homo sapiens |
|
| pmid |
sentence |
| 19066288 |
We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. phosphorylation on ser158 and ser442 enhances nuclear expression of dlg1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK1 |
phosphorylation
|
DLG1 |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182753 |
Ser158 |
FVSHSHIsPIKPTEA |
Homo sapiens |
|
| pmid |
sentence |
| 19066288 |
We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182757 |
Ser443 |
FLGQTPAsPARYSPV |
Homo sapiens |
|
| pmid |
sentence |
| 19066288 |
We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK2A | down-regulates activity 
phosphorylation
|
DLG1 |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250618 |
Ser232 |
ITLERGNsGLGFSIA |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12933808 |
Synapse-associated protein 97 (SAP97), a member of membrane-associated guanylate kinase protein family, has been implicated in the processes of targeting ionotropic glutamate receptors at postsynaptic sites. | We show here that SAP97 is directly associated with NR2A through its PDZ1 domain, and CaMKII-dependent phosphorylation of SAP97-Ser-232 disrupts NR2A interaction both in an in vitro pull-out assay and in transfected COS-7 cells. Moreover, expression of SAP97(S232D) mutant has effects similar to those observed upon constitutively activating CaMKII. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
DLG1 | up-regulates activity
phosphorylation
|
ZAP70 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274142 |
Tyr493 |
LGADDSYyTARSAGK |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 34960191 |
Immunoblot analysis showed that phosphorylation of the activating ZAP70 kinase domain residue Tyr 493 was decreased in the DLG1 KD cells. Similarly, the Tyr 319 residue of ZAP70 and Tyr 83 residue of TCR- ζ also showed reduced phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPB41 | up-regulates activity
relocalization
|
DLG1 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266011 |
|
|
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 12807908 |
Together, our results demonstrate that in addition to the N-terminal targeting domain, the alternatively spliced I3 insertion plays a critical role in recruiting hDlg to the lateral membrane in epithelial cells via its interaction with protein 4.1R. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
DLG1 | form complex 
binding
|
Scribble_complex_DLG1-LLGL1_variant |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270913 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG1 | up-regulates activity
binding
|
p38 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274143 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 17187070 |
Dlgh1 immunoprecipitates were specifically enriched for activated p38 phosphorylated at Thr180 and Tyr182; phosphorylated p38 was not detected in the unbound fraction from stimulated samples |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DLG1
- 
- 