+ |
RPS6KB1 | down-regulates
phosphorylation
|
MXD1 |
0.309 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178590 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
pmid |
sentence |
18451027 |
Both rsk and s6k phosphorylate serine 145 of mad1 upon serum or insulin stimulation. Ser-145 phosphorylation of mad1 accelerates the ubiquitination and degradation of mad1 through the 26s proteasome pathway, which in turn promotes the transcriptional activity of myc. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | down-regulates
phosphorylation
|
MXD1 |
0.369 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252525 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
pmid |
sentence |
19526459 |
Here, we present evidence that akt inhibits mad1-mediated transcription repression by physical interaction with and phosphorylation of mad1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT | down-regulates
phosphorylation
|
MXD1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-186130 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
pmid |
sentence |
19526459 |
Here, we present evidence that akt inhibits mad1-mediated transcription repression by physical interaction with and phosphorylation of mad1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA1 | down-regulates
phosphorylation
|
MXD1 |
0.32 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178586 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
pmid |
sentence |
18451027 |
In this study, we showed that mad1 is a substrate of p90 ribosomal kinase (rsk) and p70 s6 kinase (s6k). Both rsk and s6k phosphorylate serine 145 of mad1 upon serum or insulin stimulation. Ser-145 phosphorylation of mad1 accelerates the ubiquitination and degradation of mad1 through the 26s proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6K | down-regulates
phosphorylation
|
MXD1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252811 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
pmid |
sentence |
18451027 |
In this study, we showed that mad1 is a substrate of p90 ribosomal kinase (rsk) and p70 s6 kinase (s6k). Both rsk and s6k phosphorylate serine 145 of mad1 upon serum or insulin stimulation. Ser-145 phosphorylation of mad1 accelerates the ubiquitination and degradation of mad1 through the 26s proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KB2 | down-regulates
phosphorylation
|
MXD1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178594 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
pmid |
sentence |
18451027 |
In this study, we showed that mad1 is a substrate of p90 ribosomal kinase (rsk) and p70 s6 kinase (s6k). Both rsk and s6k phosphorylate serine 145 of mad1 upon serum or insulin stimulation. Ser-145 phosphorylation of mad1 accelerates the ubiquitination and degradation of mad1 through the 26s proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MXD1 | down-regulates quantity by repression
transcriptional regulation
|
UBTF |
0.368 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269646 |
|
|
Homo sapiens |
Granulocyte |
pmid |
sentence |
15282543 |
MAD1 and c-MYC regulate UBF and rDNA transcription during granulocyte differentiation|MAD1 repressed and c-MYC activated rDNA transcription in nuclear run-on assays. Repression of rDNA transcription by MAD1 was associated with its ability to interact directly with the promoter of upstream binding factor (UBF), an rDNA regulatory factor. Conversely, c-MYC activated transcription from the UBF promoter. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMC3 | down-regulates activity
binding
|
MXD1 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241278 |
|
|
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 |