+ |
FBXO2 | up-regulates activity
binding
|
Cullin 1-RBX1-Skp1 |
0.678 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271902 |
|
|
Mus musculus |
Neuron |
pmid |
sentence |
20854419 |
SCFFbx2-E3-ligase-mediated degradation of BACE1 attenuates Alzheimer’s disease amyloidosis and improves synaptic function. We report that the SCF(Fbx2) -E3 ligase is involved in the binding and ubiquitination of BACE1 via its Trp 280 residue of F-box-associated domain. we found that overexpression of Fbx2 in the primary cortical and hippocampal neurons derived from Tg2576 transgenic mice significantly promoted BACE1 degradation and reduced β-amyloid production. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271937 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23604317 |
FBXL2 interacts with the pool of p85β that is free of p110 PI(3)K catalytic subunits and targets this pool for ubiquitylation and subsequent proteasomal degradation.This result suggests that FBXL2 localization to cell membranes facilitates substrate binding, which in turn stimulates CUL1 neddylation and activation of ubiquitin ligase activity. |
|
Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
+ |
FBXO2 | up-regulates activity
binding
|
STUB1 |
0.573 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271589 |
|
|
Rattus norvegicus |
PC-12 Cell |
pmid |
sentence |
16682404 |
Through this novel interaction, which is mediated by the TPR domain of CHIP and an N-terminal PEST domain of Fbx2, CHIP facilitates the ubiquitination and degradation of Fbx2-bound glycoproteins. This study highlights a novel mechanism of F-box protein-mediated ubiquitination that contributes to glycoprotein homeostasis. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
FBXO2 | down-regulates quantity by destabilization
binding
|
BACE1 |
0.538 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271904 |
|
|
Mus musculus |
Neuron |
pmid |
sentence |
20854419 |
SCFFbx2-E3-ligase-mediated degradation of BACE1 attenuates Alzheimer’s disease amyloidosis and improves synaptic function. We report that the SCF(Fbx2) -E3 ligase is involved in the binding and ubiquitination of BACE1 via its Trp 280 residue of F-box-associated domain. we found that overexpression of Fbx2 in the primary cortical and hippocampal neurons derived from Tg2576 transgenic mice significantly promoted BACE1 degradation and reduced β-amyloid production. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
FBXO2 | down-regulates quantity by destabilization
binding
|
PIK3R2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271936 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23604317 |
FBXL2 interacts with the pool of p85β that is free of p110 PI(3)K catalytic subunits and targets this pool for ubiquitylation and subsequent proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |