| + |
SCF-FBW7 | down-regulates quantity by destabilization 
ubiquitination
|
DLGAP5 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271508 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15145941 |
We show here that Fbx7, an F-box protein without WD repeats and leucine-rich repeats, is required for the proteasome-mediated proteolysis of the hepatoma up-regulated protein (HURP).Thus, Fbx7 is a functional adaptor of the SCF complex with a proline-rich region as the substrate-binding module. Depletion of Fbx7 by small interfering RNA leads to depression of HURP ubiquitination and accumulation of HURP abundance. In the SCFFbx7 complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO7 | up-regulates activity 
binding
|
SCF-FBW7 |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271507 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15145941 |
We show here that Fbx7, an F-box protein without WD repeats and leucine-rich repeats, is required for the proteasome-mediated proteolysis of the hepatoma up-regulated protein (HURP).Thus, Fbx7 is a functional adaptor of the SCF complex with a proline-rich region as the substrate-binding module. Depletion of Fbx7 by small interfering RNA leads to depression of HURP ubiquitination and accumulation of HURP abundance. In the SCFFbx7 complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUL1 | form complex 
binding
|
SCF-FBW7 |
0.925 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243763 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
The F-box family of proteins which are the substrate-recognition components of the Skp1Cul1F-box-protein (SCF) ubiquitin ligase are important players in many mammalian functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP1 | form complex
binding
|
SCF-FBW7 |
0.935 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243760 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
The F-box family of proteins which are the substrate-recognition components of the Skp1Cul1F-box-protein (SCF) ubiquitin ligase are important players in many mammalian functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
MED13L |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266689 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23322298 |
The SCF-Fbw7 ubiquitin ligase degrades MED13 and MED13L and regulates CDK8 module association with Mediator. We show that Fbw7, a tumor suppressor and ubiquitin ligase, binds to CDK8-Mediator and targets MED13/13L for degradation. MED13/13L physically link the CDK8 module to Mediator, and Fbw7 loss increases CDK8 module-Mediator association. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
NCOA3 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276066 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 17574025 |
We identified SCFFbw7α as an E3 ligase that binds to SRC-3 in an S505 phosphorylation-dependent manner (Figure 4Ci) and that is responsible for the further ubiquitination of SRC-3 (Figure 4A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
TOP2A |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276302 |
|
|
Homo sapiens |
PLC-PRF-5 Cell |
| pmid |
sentence |
| 21254166 |
Evidence that Fbw7 acts as the E3-ligase mediating the degradation of topoIIα in HDAC inhibitor-treated PLC5 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
DEK |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276304 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21282377 |
These data suggest that the E3 ligase SCFFbxw7-α degrades p-DEK in a GSK-3β–dependent manner.Therefore, the phosphorylation of DEK by GSK-3β is a crucial step to mediate Tpm RNA splicing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity
ubiquitination
|
MYC |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243757 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20852628 |
We now show that the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1. Whereas wild-type Fbw7 promoted c-Myc turnover in cells, an Fbw7 mutant lacking the F-box domain delayed it. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | form complex
binding
|
SCF-FBW7 |
0.902 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
The F-box family of proteins which are the substrate-recognition components of the Skp1Cul1F-box-protein (SCF) ubiquitin ligase are important players in many mammalian functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
MED13 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266691 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23322298 |
The SCF-Fbw7 ubiquitin ligase degrades MED13 and MED13L and regulates CDK8 module association with Mediator. We show that Fbw7, a tumor suppressor and ubiquitin ligase, binds to CDK8-Mediator and targets MED13/13L for degradation. MED13/13L physically link the CDK8 module to Mediator, and Fbw7 loss increases CDK8 module-Mediator association. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
BIRC2 |
0.315 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271553 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16510124 |
Since Fbxo7 is one component of the SCF complex, we tried to determine whether overexpression of Fbxo7 could promote cIAP1 ubiquitination in the hope to reveal functional aspects of the cIAP1–Fbxo7 interaction. cIAP1-Flag was co-expressed with or without Fbxo7 in 293T cells. In conclusion, our results show that overexpression of Fbxo7 promotes the ubiquitination of cIAP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SCF-FBW7