+ |
MAX | up-regulates activity
binding
|
MXI1 |
0.575 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240314 |
|
|
Homo sapiens |
|
pmid |
sentence |
7954804 |
The role MAX plays in transcription is thought to be primarily as a cofactor for DNA binding. In this capacity, however, it appears to be essential for most, if not all, the known biological activities of MYC. MAX also functions as a cofactor for DNA binding for a group of bHLHZip proteins related to MYC, including MNT, MXD1-4 (formerly Mad1, Mxi1, Mad3 and Mad4), and MGA. Like MYC, these proteins do not homodimerize and appear to be incapable of binding DNA on their own, but when bound to MAX, they recognize E-box sequences. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MXI1 | down-regulates quantity by repression
transcriptional regulation
|
CCNB1 |
0.269 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266064 |
|
|
Homo sapiens |
U-87MG Cell |
pmid |
sentence |
11875718 |
Mxi1 inhibits the proliferation of U87 glioma cells through down-regulation of cyclin B1 gene expression | Mxi1 inhibits the promoter activity of the cyclin B1 gene. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMC3 | down-regulates activity
binding
|
MXI1 |
0.413 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241223 |
|
|
Chlorocebus aethiops |
CV-1 Cell |
pmid |
sentence |
9528857 |
We identified a novel ZIP-containing protein, Mmip1 (Mad member interacting protein 1) that strongly dimerizes with all four Mad members, but not with c-myc. Mmip1 can inhibit DNA binding by Max-Mad heterodimers and, in vivo, can reverse the suppressive eects of Mad proteins on c-myc functions. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |