| + |
TRIM25 | down-regulates activity 
ubiquitination
|
FBXW7 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277457 |
Lys412 |
VWSAVTGkCLRTLVG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31186535 |
This newly stabilized TRIM25 then directly ubiquitinates Lys412 of FBXW7α, a core subunit of the SKP1-Cullin-F-box (SCF) ubiquitin ligase complex involved in Myc ubiquitination, thereby stabilizing Myc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK2 | down-regulates
phosphorylation
|
FBXW7 |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196448 |
Ser176 |
KRKLDHGsEVRSFSL |
Homo sapiens |
|
| pmid |
sentence |
| 22399798 |
Plk2 regulates centriole duplication through phosphorylation-mediated degradation of fbxw7 (human cdc4).Plk2 phosphorylates fbxw7 on serine 176 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCI | down-regulates activity
phosphorylation
|
FBXW7 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277250 |
Ser18 |
KRRRTGGsLRGNPSS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28850619 |
Here, we report that Fbw7α, the only Fbw7 isoform detected in eggs, is phosphorylated by PKC (protein kinase C) at a key residue (S18) in a manner coincident with Fbw7α inactivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates activity
phosphorylation
|
FBXW7 |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277249 |
Ser18 |
KRRRTGGsLRGNPSS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28850619 |
Here, we report that Fbw7α, the only Fbw7 isoform detected in eggs, is phosphorylated by PKC (protein kinase C) at a key residue (S18) in a manner coincident with Fbw7α inactivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates activity 
phosphorylation
|
FBXW7 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276328 |
Ser227 |
QQRRRITsVQPPTGL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21620836 |
A reciprocal immunoprecipiation with anti-phospho-Akt substrate antibody followed by immunoblotting with anti-FLAG antibodies confirmed these findings (Fig. 1C). We concluded that Fbw7 is phosphorylated at S227 in vivo. Phosphorylation of Fbw7 is required for its biological activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | up-regulates
phosphorylation
|
FBXW7 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170404 |
Ser227 |
QQRRRITsVQPPTGL |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 21147854 |
Here, we report that the serum- and glucocorticoid-inducible protein kinase sgk1 remarkably reduced the protein stability of the active form of notch1 through fbw7activated sgk1 phosphorylated fbw7 at serine 227 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates activity
phosphorylation
|
FBXW7 |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259942 |
Ser26 |
LRGNPSSsQVDEEQM |
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 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
GATA2 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256005 |
Thr176 |
HLFGFPPtPPKEVSP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25670854 |
Here, we demonstrate that F-box/WD repeat-containing protein 7 (Fbw7/Fbxw7), a component of Skp1, Cullin 1, F-box-containing complex (SCF)-type E3 ligase, is an E3 ligase for GATA2. 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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | up-regulates activity
binding
|
Cullin 1-RBX1-Skp1 |
0.888 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271640 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 17298674 |
Cdk2 (S384) and GSK3 (T380) prime cyclin E for destruction. The hyper-phosphorylated T380/S384 degron has high affinity for monomeric Fbw7α, which engages the remainder of the SCF to initiate cyclin E's ubiquitination by an E2 enzyme |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272908 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 22388891 |
Fbxw7α is a member of the F-box family of proteins, which function as the substrate-targeting subunits of SCF (Skp1/Cul1/F-box protein) ubiquitin ligase complexes. Using differential purifications and mass spectrometry, we identified p100, an inhibitor of NF-κB signalling, as an interactor of Fbxw7α. p100 is constitutively targeted in the nucleus for proteasomal degradation by Fbxw7α |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271641 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 17298674 |
Cdk2 (S384) and GSK3 (T380) prime cyclin E for destruction. The hyper-phosphorylated T380/S384 degron has high affinity for monomeric Fbw7α, which engages the remainder of the SCF to initiate cyclin E's ubiquitination by an E2 enzyme |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
MED13 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266690 |
|
|
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 | down-regulates quantity by destabilization
ubiquitination
|
NOTCH1 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130706 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15546612 |
Purified recombinant cycc:cdk8 phosphorylates the notch icd within the tad and pest domains, and expression of cycc:cdk8 strongly enhances notch icd hyperphosphorylation and pest-dependent degradation by the fbw7/sel10 ubiquitin ligase in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
STYX | down-regulates activity
binding
|
FBXW7 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251663 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28007894 |
STYX acts as a direct inhibitor of FBXW7, affecting the cellular levels of its substrates. Furthermore, we find that levels of STYX and FBXW7 are anti-correlated in breast cancer patients, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
EGLN2 |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261997 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28036276 |
Mechanistically, we further show that FBW7, an E3 ligase complex component that is frequently downregulated in TNBC, negatively regulates EglN2 protein stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
MED13L |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266688 |
|
|
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 | down-regulates quantity by destabilization
ubiquitination
|
GATA3 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276635 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24820417 |
Fbw7 promotes degradation of GATA3 in a Thr-156-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
DAB2IP |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254774 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27858941 |
DAB2IP protein levels can be negatively regulated by the activity of the E3-ubiquitin ligases Fbw7, Skp2, and Smurf1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
ZNF322 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264898 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 28581525 |
CK1delta and GSK3beta kinases sequentially phosphorylate ZNF322A at serine-396 and then serine-391. Moreover, the doubly phosphorylated ZNF322A protein creates a destruction motif for the ubiquitin ligase FBXW7alpha leading to ZNF322A protein destruction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates
ubiquitination
|
NOTCH4 |
0.514 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110955 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11585921 |
We show here that the f-box/wd40 repeat protein sel-10 negatively regulates notch receptor activity by targeting the intracellular domain of notch receptors for ubiquitin-mediated protein degradation. in conclusion, hsel-10 physically associates with mouse notch4(int-3) through the wd40 domain, whereas the f-box domain is not required for this interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NPM1 | up-regulates quantity
binding
|
FBXW7 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245084 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 18625840 |
We report here that NPM regulates turnover of the c-Myc oncoprotein by acting on the F-box protein Fbw7 , a component of the E3 ligase complex involved in the ubiquitination and proteasome degradation of c-Myc. NPM was required for nucleolar localization and stabili- zation of Fbw7 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, NPM1 in AML, AML_TRIPLETS, Triple mutant AML, NPM1_new |
| + |
FBXW7 | down-regulates quantity by destabilization
binding
|
JUN |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272950 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14739463 |
We report that in neurons the stability of c-Jun is regulated by the E3 ligase SCF(Fbw7), which ubiquitinates phosphorylated c-Jun and facilitates c-Jun degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
PPARGC1A |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253394 |
|
|
|
|
| pmid |
sentence |
| 26971449 |
We then examined the effect of necdin on ubiquitin-dependent degradation of PGC-1α using Rnf34, a PGC-1α E3 ubiquitin ligase22. Rnf34 reduced the PGC-1α level, and necdin completely inhibited the reduction (Fig. 4i). In addition, necdin strongly suppressed Rnf34-mediated ubiquitination of PGC-1α (Fig. 4j). Necdin also protected PGC-1α against ubiquitination mediated by Fbxw7, another PGC-1α E3 ubiquitin ligase23 (Fig. 4k). These data indicate that necdin stabilizes PGC-1α by inhibiting its degradation in the ubiquitin-proteasomal system. |
|
| Publications: |
1 |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
NOTCH |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254310 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15546612 |
Purified recombinant cycc:cdk8 phosphorylates the notch icd within the tad and pest domains, and expression of cycc:cdk8 strongly enhances notch icd hyperphosphorylation and pest-dependent degradation by the fbw7/sel10 ubiquitin ligase in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
FBXW7 | down-regulates quantity by destabilization
ubiquitination
|
MYC |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249638 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15103331 |
We now show that the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, NPM1 in AML, AML_TRIPLETS, Triple mutant AML, NPM1_new |
| + |
FBXW7 | down-regulates quantity by destabilization
binding
|
PSEN1 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272600 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12354302 |
SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-beta peptide production SEL-10 protein is a homologue of yeast Cdc4, a member of the SCF (Skp1-Cdc53/CUL1-F-box protein) E2-E3 ubiquitin ligase family. In this study, we show that human SEL-10 interacts with PS1 and enhances PS1 ubiquitination, thus altering cellular levels of unprocessed PS1 and its N- and C-terminal fragments. These observations suggest that SEL-10 mediated ubiquitination of PS1-CTF and PS1-NTF leads to their degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates
binding
|
CCDC6 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199279 |
|
|
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 23108047 |
Fbxw7 interacts with and targets ccdc6 for ubiquitin-mediated proteasomal degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
binding
|
CCNE2 |
0.447 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271642 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 17298674 |
Cdk2 (S384) and GSK3 (T380) prime cyclin E for destruction. The hyper-phosphorylated T380/S384 degron has high affinity for monomeric Fbw7α, which engages the remainder of the SCF to initiate cyclin E's ubiquitination by an E2 enzyme |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity by destabilization
binding
|
NFKB2 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272907 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 22388891 |
Fbxw7α is a member of the F-box family of proteins, which function as the substrate-targeting subunits of SCF (Skp1/Cul1/F-box protein) ubiquitin ligase complexes. Using differential purifications and mass spectrometry, we identified p100, an inhibitor of NF-κB signalling, as an interactor of Fbxw7α. p100 is constitutively targeted in the nucleus for proteasomal degradation by Fbxw7α |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FBXW7 | down-regulates quantity by destabilization
binding
|
CCNE1 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271643 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 17298674 |
Cdk2 (S384) and GSK3 (T380) prime cyclin E for destruction. The hyper-phosphorylated T380/S384 degron has high affinity for monomeric Fbw7α, which engages the remainder of the SCF to initiate cyclin E's ubiquitination by an E2 enzyme |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW7 | down-regulates quantity
ubiquitination
|
MYC |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243545 |
|
|
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 |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, NPM1 in AML, AML_TRIPLETS, Triple mutant AML, NPM1_new |
| + |
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 |
3.0
FBXW7
- 
- 