| + |
SCF-FBW7 | down-regulates quantity by destabilization 
polyubiquitination
|
PDCD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277606 |
Lys233 |
LDFQWREkTPEPPVP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 36104103 |
We identified FBW7 as a E3 ubiquitin ligase for PD-1 protein, in which FBW7 promotes the K48-linked polyubiquitination of PD-1 protein at Lys233 residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | up-regulates activity 
ubiquitination
|
XRCC4 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277200 |
Lys296 |
QENQLQEkENSRPDS |
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 26774286 |
In response to ionizing radiation, ATM phosphorylates FBXW7 at serine 26 to recruit it to DNA double-strand break (DSB) sites, whereas activated DNA-PKcs phosphorylates XRCC4 at serines 325/326, which promotes binding of XRCC4 to FBXW7. SCF(FBXW7) E3 ligase then promotes polyubiquitylation of XRCC4 at lysine 296 via lysine 63 linkage for enhanced association with the Ku70/80 complex to facilitate NHEJ repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC34 | up-regulates activity
binding
|
SCF-FBW7 |
0.802 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277333 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25425648 |
The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association.Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUL1 | form complex 
binding
|
SCF-FBW7 |
0.926 |
| 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
polyubiquitination
|
DEK |
0.294 |
| 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 by destabilization
ubiquitination
|
DLGAP5 |
0.277 |
| 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 |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
TOP2A |
0.345 |
| 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
ubiquitination
|
STAT2 |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276766 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
These results demonstrate that the interaction between STAT2 and FBXW7 is involved in the SCF complex containing cullin 1 and RBX1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
NCOA3 |
0.299 |
| 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
ubiquitination
|
MED13L |
0.363 |
| 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 |
| + |
FBXW7 | form complex
binding
|
SCF-FBW7 |
0.903 |
| 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
|
GATA2 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276885 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25670854 |
GATA2 contains a cell division control protein 4 (Cdc4) phosphodegron (CPD), a consensus motif for ubiquitylation by Fbw7, which includes Thr(176). Ectopic expression of Fbw7 destabilized GATA2 and promoted its proteasomal degradation. Substitution of threonine 176 to alanine in GATA2 inhibited binding with Fbw7, and the ubiquitylation and degradation of GATA2 by Fbw7 was suppressed. The CPD kinase, which mediates the phosphorylation of Thr(176), was cyclin B-cyclin-dependent kinase 1 (CDK1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
SMARCA4 |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277409 |
|
|
Homo sapiens |
MKN-45 Cell |
| pmid |
sentence |
| 30177679 |
We reveal that CK1δ phosphorylates Brg1 at Ser31/Ser35 residues to facilitate the binding of Brg1 to FBW7, leading to ubiquitination-mediated degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
BIRC2 |
0.312 |
| 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 |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
FOXM1 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277209 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26912724 |
GSK3 phosphorylates FoxM1 on serine 474 which induces FoxM1 ubiquitination mediated by FBXW7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
GFI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277467 |
|
|
Homo sapiens |
Gastric Cancer Cell |
| pmid |
sentence |
| 31289136 |
GSK3β-mediated GFI1 S94/S98 phosphorylation triggered its interaction with FBXW7, resulting in SCFFBXW7-mediated ubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
BLM |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276912 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
polyubiquitination
|
SHOC2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277444 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 30865892 |
Here, we showed that SHOC2, a RAS activator, is a FBXW7 substrate. Growth stimuli trigger SHOC2 phosphorylation on Thr507 by the mitogen-activated protein kinase (MAPK) signal, which facilitates FBXW7 binding for ubiquitylation and degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO7 | up-regulates activity
binding
|
SCF-FBW7 |
0.605 |
| 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 |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
MED13 |
0.299 |
| 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
ubiquitination
|
MYC |
0.582 |
| 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 |
4.0
SCF-FBW7