| + |
MDM2 | down-regulates quantity by destabilization 
polyubiquitination
|
EID1 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272582 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11073989 |
Degradation of EID-1 occurs via ubiquitin-dependent proteolysis and correlates with MDM2 binding. These results are consistent with a model wherein destruction of EID-1 is linked to its ability to interact with MDM2 via either p300 or pRB. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
EID1 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272431 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26085330 |
SCFFBXO21 ubiquitylates and thereby targets EID1 for degradation.We have now applied this approach to an uncharacterized human F-box protein, FBXO21, which serves as the substrate-recognition subunit of a SKP1-CUL1-F-box protein (SCF)-type E3, thereby identifying EID1 (EP300-interacting inhibitor of differentiation 1) as a candidate substrate.Over-expression of FBXO21 resulted in the down-regulation of EID1, whereas disruption of the FBXO21 gene with the CRISPR/Cas9 system stabilized EID1 and led to its accumulation in both the cytoplasm and nucleus. An in vitro ubiquitylation assay showed that EID1 is a direct substrate of SCF(FBXO) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EID1 | down-regulates activity
binding
|
CREBBP |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253380 |
|
|
|
|
| pmid |
sentence |
| 11073989 |
Here, we show that EID-1 is a potent inhibitor of differentiation and link this activity to its ability to inhibit p300 (and the highly related molecule, CREB-binding protein, or CBP) histone acetylation activity. |
|
| Publications: |
1 |
| + |
EID1 | down-regulates activity
binding
|
EP300 |
0.434 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253377 |
|
|
|
|
| pmid |
sentence |
| 11073990 |
Inhibition of MyoD may be explained by EID-1's ability to bind and inhibit p300's histone acetylase activity, an essential MyoD coactivator. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253379 |
|
|
|
|
| pmid |
sentence |
| 11073989 |
Here, we show that EID-1 is a potent inhibitor of differentiation and link this activity to its ability to inhibit p300 (and the highly related molecule, CREB-binding protein, or CBP) histone acetylation activity. |
|
| Publications: |
2 |
| + |
FBXO21 | down-regulates quantity by destabilization
binding
|
EID1 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272429 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26085330 |
SCFFBXO21 ubiquitylates and thereby targets EID1 for degradation.We have now applied this approach to an uncharacterized human F-box protein, FBXO21, which serves as the substrate-recognition subunit of a SKP1-CUL1-F-box protein (SCF)-type E3, thereby identifying EID1 (EP300-interacting inhibitor of differentiation 1) as a candidate substrate.Over-expression of FBXO21 resulted in the down-regulation of EID1, whereas disruption of the FBXO21 gene with the CRISPR/Cas9 system stabilized EID1 and led to its accumulation in both the cytoplasm and nucleus. An in vitro ubiquitylation assay showed that EID1 is a direct substrate of SCF(FBXO) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EID1 | down-regulates 
|
MYOD1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253378 |
|
|
|
|
| pmid |
sentence |
| 11073990 |
Thus, EID-1 binds both Rb and p300 and is a novel repressor of MyoD function. |
|
| Publications: |
1 |
| + |
NDN | up-regulates activity 
binding
|
EID1 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-237614 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 18557765 |
The Prader-Willi syndrome protein necdin interacts with the E1A-like inhibitor of differentiation EID-1 and promotes myoblast differentiation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
EID1
- 
- 