+ |
FBXO22 | down-regulates quantity by destabilization
ubiquitination
|
KDM4A |
0.347 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273442 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
pmid |
sentence |
21768309 |
SCF(FBXO22) regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitin-mediated proteasomal degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity by destabilization
ubiquitination
|
SNAI1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273446 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
pmid |
sentence |
29945959 |
FBXO22 elicits its antimetastatic effects by targeting SNAIL, a master regulator of EMT and breast cancer metastasis, for ubiquitin-mediated proteasomal degradation in a glycogen synthase kinase 3β phosphorylation-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | up-regulates
binding
|
Cullin 1-RBX1-Skp1 |
0.569 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272788 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28117675 |
FBXO22 mediates poly-ubiquitination and degradation of CD147. Classically, F-box protein together with Skp1 and Cullin 1 constitute Skp-Cullin-F box ubiquitin E3 ligase (SCFs) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity by destabilization
ubiquitination, binding
|
BSG |
0.438 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273452 |
|
|
Homo sapiens |
HEK-293 Cell, SMMC-7721 Cell, A549-CR Cell |
pmid |
sentence |
28117675 |
F-Box Protein FBXO22 Mediates Polyubiquitination and Degradation of CD147 to Reverse Cisplatin Resistance of Tumor Cells |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272787 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28117675 |
FBXO22 mediates poly-ubiquitination and degradation of CD147. Classically, F-box protein together with Skp1 and Cullin 1 constitute Skp-Cullin-F box ubiquitin E3 ligase (SCFs) |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
heme | up-regulates activity
chemical activation
|
FBXO22 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259332 |
|
|
Homo sapiens |
|
pmid |
sentence |
31257023 |
Here, we show that heme triggers the degradation of Bach1, a pro-metastatic transcription factor, by promoting its interaction with the ubiquitin ligase Fbxo22. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity by destabilization
ubiquitination
|
TP53 |
0.346 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273448 |
|
|
Homo sapiens |
HCA-7 Cell |
pmid |
sentence |
26868148 |
We demonstrate here that SCFFbxo22-KDM4A is a senescence-associated E3 ligase targeting methylated p53 for degradation. We find that Fbxo22 is highly expressed in senescent cells in a p53-dependent manner, and that SCFFbxo22 ubiquitylated p53 and formed a complex with a lysine demethylase, KDM4A. |SCFFbxo22 forms a ternary complex with p53 and KDM4A that targets methylated p53 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity by destabilization
ubiquitination
|
KLF4 |
0.372 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273444 |
|
|
Homo sapiens |
Liver Cancer Cell |
pmid |
sentence |
26087183 |
F-box protein FBXO22 mediates polyubiquitination and degradation of KLF4 to promote hepatocellular carcinoma progression |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity by destabilization
ubiquitination
|
MDM2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273440 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
pmid |
sentence |
31138683 |
SCFFBXO22 targets HDM2 for degradation and modulates breast cancer cell invasion and metastasis|we discovered Skp1-Cullin 1-FBXO22-ROC1 (SCFFBXO22) as the most dominating HDM2 E3 ubiquitin ligase from human proteome. The results of protein decay rate analysis, ubiquitination, siRNA-mediated silencing, and coimmunoprecipitation experiments support a hypothesis that FBXO22 targets cellular HDM2 for ubiquitin-dependent degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity
ubiquitination
|
BACH1 |
0.285 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259331 |
|
|
Homo sapiens |
|
pmid |
sentence |
31257023 |
Here, we show that heme triggers the degradation of Bach1, a pro-metastatic transcription factor, by promoting its interaction with the ubiquitin ligase Fbxo22. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO22 | down-regulates quantity by destabilization
binding
|
BAG3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277319 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
34215846 |
We further demonstrated BAG3, a HSP70 co-chaperone, is a bona fide substrate of SCFFBXO22. FBXO22 mediates BAG3 ubiquitination and degradation that requires ERK-dependent BAG3 phosphorylation at S377. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |