| + |
MSX2 | down-regulates activity 
binding
|
DLX5 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240990 |
|
|
Mus musculus |
Neuronal Cell Line |
| 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 |
| + |
DLX2 | down-regulates activity
binding
|
MSX2 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240911 |
|
|
Mus musculus |
|
| 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 |
| + |
TBX22 | down-regulates quantity by repression
transcriptional regulation
|
MSX2 |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265567 |
|
|
Gallus gallus |
UMNSAH/DF-1 Cell |
| pmid |
sentence |
| 20033915 |
the main function of TBX22 as shown in misexpression experiments is to decrease proliferation. We subsequently uncovered three targets of TBX22, DLX5, MSX2, and TBX22 itself. All are downregulated in the presence of viral-derived hTBX22. |
|
| Publications: |
1 |
Organism: |
Gallus Gallus |
| + |
DLX5 | down-regulates activity
binding
|
MSX2 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240925 |
|
|
Mus musculus |
Neuronal Cell Line |
| 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 |
| + |
MSX2 | down-regulates activity
binding
|
DLX2 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240932 |
|
|
Mus musculus |
CAL-51 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 |
| + |
FBXW2 | down-regulates quantity by destabilization
binding
|
MSX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272259 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31548378 |
Mechanistic studies revealed that MSX2 is a new substrate of SCFFBXW2 E3 ubiquitin ligase. Taken together, our combined results showed that MSX2 is a substrate of the SCFFBXW2 E3 ligase, which ubiquitylates it and targets it for proteasome degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MSX2 | up-regulates 
binding
|
SPEN |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188572 |
|
|
Homo sapiens |
T-lymphocyte, Leukemia Cell, JURKAT Cell |
| pmid |
sentence |
| 19835636 |
Furthermore, in addition to msx2, both tlx1 and nkx2-5 proteins interacted with notch-pathway repressors, spen/mint/sharp and tle1/grg1, representing a potential mechanism for (de)regulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
MSX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272261 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31548378 |
Mechanistic studies revealed that MSX2 is a new substrate of SCFFBXW2 E3 ubiquitin ligase. Taken together, our combined results showed that MSX2 is a substrate of the SCFFBXW2 E3 ligase, which ubiquitylates it and targets it for proteasome degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MSX2
- 
- 