| + |
DLX2 | down-regulates activity 
binding
|
MSX1 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240918 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MSX1 | down-regulates activity
binding
|
TBP |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240401 |
|
|
in vitro |
|
| pmid |
sentence |
| 8700832 |
Msx-1 is a potent transcriptional repressor and that this activity is independent of its DNA binding function. Here we show that Msx-1 interacts directly with the TATA binding protein (TBP) but not with several other general transcription factors. This interaction is mediated by the Msx-1 homeodomain, specifically through residues in the N-terminal arm. These same N-terminal arm residues are required for repression by Msx-1, suggesting a functional relationship between TBP association and transcriptional repression. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MSX1 | down-regulates activity
binding
|
DLX2 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240929 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DLX5 | down-regulates activity
binding
|
MSX1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240921 |
|
|
Mus musculus |
NT2/D1 Cell |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
LHX2 | down-regulates activity
binding
|
MSX1 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241327 |
|
|
in vitro |
|
| pmid |
sentence |
| 9697309 |
Protein complex formation between Msx1 and Lhx2 homeoproteins is incompatible with DNA binding activity |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FOXE1 | up-regulates quantity by expression 
transcriptional regulation
|
MSX1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254173 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21177256 |
The MSX1 and TGF-β3 up-regulation in response to FOXE1 at both transcriptional and translational levels and the recruitment of FOXE1 to specific binding motifs, together with the transactivation of the promoters of these genes, indicate that MSX1 and TGF-β3 are direct FOXE1 targets. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MSX1 | down-regulates activity
binding
|
LHX2 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241330 |
|
|
in vitro |
|
| pmid |
sentence |
| 9697309 |
Protein complex formation between Msx1 and Lhx2 homeoproteins is incompatible with DNA binding activity |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MSX1 | down-regulates quantity by repression 
transcriptional regulation
|
MYOD1 |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15192231 |
We found that msx1 and h1b bind to a key regulatory element of myod, a central regulator of skeletal muscle differentiation, where they induce repressed chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
MSX1 | down-regulates activity
binding
|
DLX5 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240987 |
|
|
Mus musculus |
NT2/D1 Cell |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
MSX1
- 
- 