| + |
HOXD12 | down-regulates activity 
binding
|
MAF |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-221887 |
|
|
in vitro |
|
| pmid |
sentence |
| 11036080 |
Hoxd12 and MHox, that interact with v-/c-Maf, using the phage display method. The Hox proteins also could associate with the other Maf protein family members, MafB, MafK, MafF, and MafG, but not with Jun and Fos. The Hox proteins negatively regulated the DNA binding, transactivation and cell-transforming abilities of Maf. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HOXD12 | down-regulates activity
binding
|
MAFK |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-221929 |
|
|
in vitro |
|
| pmid |
sentence |
| 11036080 |
Hoxd12 and MHox, that interact with v-/c-Maf, using the phage display method. The Hox proteins also could associate with the other Maf protein family members, MafB, MafK, MafF, and MafG, but not with Jun and Fos. The Hox proteins negatively regulated the DNA binding, transactivation and cell-transforming abilities of Maf. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HOXD12 | down-regulates activity
binding
|
MAFG |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-221958 |
|
|
in vitro |
|
| pmid |
sentence |
| 11036080 |
Hoxd12 and MHox, that interact with v-/c-Maf, using the phage display method. The Hox proteins also could associate with the other Maf protein family members, MafB, MafK, MafF, and MafG, but not with Jun and Fos. The Hox proteins negatively regulated the DNA binding, transactivation and cell-transforming abilities of Maf. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HOXD12 | down-regulates activity
binding
|
MAFF |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-221884 |
|
|
in vitro |
|
| pmid |
sentence |
| 11036080 |
Hoxd12 and MHox, that interact with v-/c-Maf, using the phage display method. The Hox proteins also could associate with the other Maf protein family members, MafB, MafK, MafF, and MafG, but not with Jun and Fos. The Hox proteins negatively regulated the DNA binding, transactivation and cell-transforming abilities of Maf. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HOXD12 | up-regulates activity 
binding
|
MEIS1 |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241232 |
|
|
in vitro |
|
| pmid |
sentence |
| 9343407 |
We now show that the Hoxa-9 protein physically interacts with Meis1 proteins. Hox proteins from the other AbdB-like paralogs, Hoxa-10, Hoxa-11, Hoxd-12, and Hoxb-13, also form DNA binding complexes with Meis1b. DNA binding complexes formed by Meis1 with Hox proteins dissociate much more slowly than DNA complexes with Meis1 alone, suggesting that Hox proteins stabilize the interactions of Meis1 proteins with their DNA targets. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HOXD12 | down-regulates activity
binding
|
MAFB |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-221896 |
|
|
in vitro |
|
| pmid |
sentence |
| 11036080 |
Hoxd12 and MHox, that interact with v-/c-Maf, using the phage display method. The Hox proteins also could associate with the other Maf protein family members, MafB, MafK, MafF, and MafG, but not with Jun and Fos. The Hox proteins negatively regulated the DNA binding, transactivation and cell-transforming abilities of Maf. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
HOXD12
- 
- 