| + |
SMAD6 | down-regulates quantity by destabilization 
binding
|
TBX6 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272785 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19561075 |
Smad6 mediates Tbx6 ubiquitination and proteasomal degradation. Tbx6 forms a ternary complex with Smad6 and Smurf1. Here, we report that Tbx6 interacts directly with Smad6, an inhibitory Smad that antagonizes the BMP signal. This interaction is mediated through the Mad homology 2 (MH2) domain of Smad6 and residues 90-180 of Tbx6. We demonstrate that Smad6 facilitates the degradation of Tbx6 protein through recruitment of Smurf1, a ubiquitin E3 ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF1 | down-regulates quantity by destabilization
polyubiquitination
|
TBX6 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272784 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19561075 |
Smad6 mediates Tbx6 ubiquitination and proteasomal degradation. Tbx6 forms a ternary complex with Smad6 and Smurf1. Here, we report that Tbx6 interacts directly with Smad6, an inhibitory Smad that antagonizes the BMP signal. This interaction is mediated through the Mad homology 2 (MH2) domain of Smad6 and residues 90-180 of Tbx6. We demonstrate that Smad6 facilitates the degradation of Tbx6 protein through recruitment of Smurf1, a ubiquitin E3 ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TBX6
- 
- 