+ |
MAF | down-regulates
binding
|
ETS1 |
0.436 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-56808 |
|
|
Homo sapiens |
|
pmid |
sentence |
9566892 |
Full-length c-maf binds to the c-myb and ets-1. / c-maf inhibits c-myb and ets-1 transcriptional activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAF | down-regulates
binding
|
MYB |
0.646 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-56811 |
|
|
Homo sapiens |
|
pmid |
sentence |
9566892 |
Full-length c-maf binds to the c-myb and ets-1. / c-maf inhibits c-myb and ets-1 transcriptional activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRRX1 | down-regulates activity
binding
|
MAF |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-221893 |
|
|
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 |
+ |
GSK3A | down-regulates
phosphorylation
|
MAF |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159361 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3B | up-regulates
phosphorylation
|
MAF |
0.264 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159435 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAF | up-regulates quantity by expression
transcriptional regulation
|
MMP13 |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254560 |
|
|
Homo sapiens |
|
pmid |
sentence |
20067416 |
MMP-13 gene expression is regulated primarily at the transcriptional level. In this study, we investigated the role of c-maf in regulating MMP-13 transcription. Using transient transfection system with an c-maf construct, and MMP-13 promoter-luciferase constructs with specific mutations in transcription factor binding sites, we found that c-maf can significantly enhance MMP-13 promoter activity via the AP-1 sitecv |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3A | up-regulates
phosphorylation
|
MAF |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159358 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3B | down-regulates
phosphorylation
|
MAF |
0.264 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159438 |
|
|
Homo sapiens |
|
pmid |
sentence |
18042454 |
We showed that c-maf and mafb, like mafa, are indeed phosphorylated by gsk-3/ we demonstrated that phosphorylation by gsk-3 is conserved among the large maf proteins. It couples ubiquitination/degradation and transcriptional activation and modulates maf biological activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |