| + |
Cullin 7-RBX1-Skp1 | down-regulates quantity by destabilization 
polyubiquitination
|
CCND1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271633 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1. We next investigated whether in vitro ubiquitination of cyclin D1 through the SCF-like (SCFL) complex FBXW8 (SKP1-CUL7-FBXW8-RBX1/SCFLFBXW8) requires phosphorylation of cyclin D1 at Thr286 (Fig. 3F). Polyubiquitination through SCFLFBXW8 was dramatically reduced by the depletion of ERK2 (lane 2). Furthermore, cyclin D1 polyubiquitination was largely prevented by the alanine-for-Thr286 substitution (T286A, lane 3), suggesting that phosphorylation of cyclin D1 at Thr286 is necessary for ubiquitination by SCFLFBXW8. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 7-RBX1-Skp1 | down-regulates quantity by destabilization
ubiquitination
|
AICDA |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272026 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31092637 |
Further analysis indicated that CUL7 mediated AID ubiquitination by forming a complex with FBXW11. In a CUL7 fl/fl CD19 cre+ mouse model, we demonstrated that CUL7 knockout significantly enhanced AID protein levels in B cells in the germinal center and increased both the IgG1 and IgA class switching. Collectively, our results reveal a subtle regulation mechanism for tightly controlling AID protein levels. F-box proteins are components of SCF ubiquitin-ligase complexes that contain Skp1, CUL1, or CUL7, and an F-box protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 7-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
IRS1 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271941 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 23142081 |
We provide evidence that mTORC2 can stabilize Fbw8, the substrate-targeting subunit of the CUL7 E3 ligase complex that has been shown to mediate degradation of IRS-1 . |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FBXO31 | up-regulates activity 
binding
|
Cullin 7-RBX1-Skp1 |
0.54 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277381 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 29343641 |
FBXO31 serves as the substrate-recognition component of the SKP/Cullin/F-box protein class of E3 ubiquitin ligases and has been shown to direct degradation of pivotal cell-cycle regulatory proteins including cyclin D1 and the p53 antagonist MDM2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RBX1 | form complex 
binding
|
Cullin 7-RBX1-Skp1 |
0.851 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271626 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW8 | up-regulates activity
binding
|
Cullin 7-RBX1-Skp1 |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271942 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23142081 |
Defective IRS-1 degradation was due to attenuated expression and phosphorylation of the ubiquitin ligase substrate-targeting subunit, Fbw8. mTORC2 stabilizes Fbw8 by phosphorylation at Ser86, allowing the insulin-induced translocation of Fbw8 to the cytosol where it mediates IRS-1 degradation. We provide evidence that mTORC2 can stabilize Fbw8, the substrate-targeting subunit of the CUL7 E3 ligase complex that has been shown to mediate degradation of IRS-1 . |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271631 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1. We next investigated whether in vitro ubiquitination of cyclin D1 through the SCF-like (SCFL) complex FBXW8 (SKP1-CUL7-FBXW8-RBX1/SCFLFBXW8) requires phosphorylation of cyclin D1 at Thr286 (Fig. 3F). Polyubiquitination through SCFLFBXW8 was dramatically reduced by the depletion of ERK2 (lane 2). Furthermore, cyclin D1 polyubiquitination was largely prevented by the alanine-for-Thr286 substitution (T286A, lane 3), suggesting that phosphorylation of cyclin D1 at Thr286 is necessary for ubiquitination by SCFLFBXW8. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
Cullin 7-RBX1-Skp1 | down-regulates quantity by destabilization
ubiquitination
|
NCOA3 |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272837 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUL7 | form complex
binding
|
Cullin 7-RBX1-Skp1 |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271625 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SKP1 | form complex
binding
|
Cullin 7-RBX1-Skp1 |
0.845 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271627 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 17205132 |
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW11 | up-regulates activity
binding
|
Cullin 7-RBX1-Skp1 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272025 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31092637 |
Further analysis indicated that CUL7 mediated AID ubiquitination by forming a complex with FBXW11. In a CUL7 fl/fl CD19 cre+ mouse model, we demonstrated that CUL7 knockout significantly enhanced AID protein levels in B cells in the germinal center and increased both the IgG1 and IgA class switching. Collectively, our results reveal a subtle regulation mechanism for tightly controlling AID protein levels. F-box proteins are components of SCF ubiquitin-ligase complexes that contain Skp1, CUL1, or CUL7, and an F-box protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Cullin 7-RBX1-Skp1