Relation Results

Summary

Name Cullin 7-RBX1-Skp1
Primary ID SIGNOR-C528
Type complex
Formed by RBX1, SKP1, CUL7
Relations 11

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Type: Score: Layout: SPV 
0.710.250.7680.7260.8380.8430.3490.2610.5150.46FBXW11Cullin 7-RBX1-Skp1AICDAFBXW8CUL7SKP1RBX1IRS1NCOA3FBXO31CCND1

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Relations
Regulator
Mechanism
target
score ℹ
+ FBXW11up-regulates activity img/direct-activation.png binding Cullin 7-RBX1-Skp1 0.71
Identifier Residue Sequence Organism Cell Line
SIGNOR-272025 Homo sapiens HEK-293 Cell
pmid sentence
 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-Skp1down-regulates quantity by destabilization img/direct_inhibition.png ubiquitination AICDA 0.25
Identifier Residue Sequence Organism Cell Line
SIGNOR-272026 Homo sapiens HEK-293 Cell
pmid sentence
 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
+ FBXW8up-regulates activity img/direct-activation.png binding Cullin 7-RBX1-Skp1 0.768
Identifier Residue Sequence Organism Cell Line
SIGNOR-271942 Mus musculus MEF Cell
pmid sentence
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
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
+ CUL7form complex img/form-complex.png binding Cullin 7-RBX1-Skp1 0.726
Identifier Residue Sequence Organism Cell Line
SIGNOR-271625 Homo sapiens HCT-116 Cell
pmid sentence
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 
Publications: 1 Organism: Homo Sapiens
+ SKP1form complex img/form-complex.png binding Cullin 7-RBX1-Skp1 0.838
Identifier Residue Sequence Organism Cell Line
SIGNOR-271627 Homo sapiens HCT-116 Cell
pmid sentence
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 
Publications: 1 Organism: Homo Sapiens
+ RBX1form complex img/form-complex.png binding Cullin 7-RBX1-Skp1 0.843
Identifier Residue Sequence Organism Cell Line
SIGNOR-271626 Homo sapiens HCT-116 Cell
pmid sentence
FBXW8 associates with CUL1 or CUL7 and forms a complex with SKP1 and RBX1 
Publications: 1 Organism: Homo Sapiens
+ Cullin 7-RBX1-Skp1down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination IRS1 0.349
Identifier Residue Sequence Organism Cell Line
SIGNOR-271941 Mus musculus
pmid sentence
 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
+ Cullin 7-RBX1-Skp1down-regulates quantity by destabilization img/direct_inhibition.png ubiquitination NCOA3 0.261
Identifier Residue Sequence Organism Cell Line
SIGNOR-272837 Homo sapiens HEK-293 Cell
pmid sentence
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
+ FBXO31up-regulates activity img/direct-activation.png binding Cullin 7-RBX1-Skp1 0.515
Identifier Residue Sequence Organism Cell Line
SIGNOR-277381 Homo sapiens HEK-293T Cell
pmid sentence
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
+ Cullin 7-RBX1-Skp1down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination CCND1 0.46
Identifier Residue Sequence Organism Cell Line
SIGNOR-271633 Homo sapiens HCT-116 Cell
pmid sentence
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
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