| + |
PKNOX1 | up-regulates activity 
binding
|
HOXA1 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-220242 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9582372 |
Our results are consistent with a primary interaction of the YPWM motif of HOXA1 with the homeodomain of PBX. HOX proteins are dependent upon cofactors of the PBX family for specificity of DNA binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKNOX1 | up-regulates activity
binding
|
HOXB1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241215 |
|
|
in vitro |
|
| pmid |
sentence |
| 9482740 |
we observe the formation of a ternary Prep1-Pbx1-HOXB1 complex on a HOXB1-responsive target in vitro. Interaction with Prep1 enhances the ability of the HOXB1-Pbx1 complex to activate transcription in a cooperative fashion from the same target. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PKNOX1 | up-regulates quantity by expression 
transcriptional regulation
|
SYP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254923 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20864515 |
Prep1 overexpression in HepG2 liver cells upregulated SYP and SHP1 and inhibited insulin-induced IR and IRS1/2 phosphorylation and was accompanied by reduced glycogen content. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKNOX1 | up-regulates quantity by expression
transcriptional regulation
|
PTPN6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254924 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 20864515 |
Prep1 overexpression in HepG2 liver cells upregulated SYP and SHP1 and inhibited insulin-induced IR and IRS1/2 phosphorylation and was accompanied by reduced glycogen content. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKNOX1 | up-regulates activity
binding
|
PBX1 |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241212 |
|
|
in vitro |
|
| pmid |
sentence |
| 9482740 |
we show that Pbx proteins exist as stable heterodimers with a novel homeodomain protein, Prep1. Here we show that Prep1-Pbx interaction presents novel structural features: it is independent of DNA binding and of the integrity of their respective homeodomains, and requires sequences in the N-terminal portions of both proteins. The Prep1-Pbx protein-protein interaction is essential for DNA-binding activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PKNOX1
- 
- 