| + |
FBXL5 | down-regulates quantity by destabilization 
binding
|
NABP2 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272460 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25249620 |
Here, we report that hSSB1 is the bona fide substrate for an Fbxl5-containing SCF (Skp1-Cul1-F box) E3 ligase. Fbxl5 interacts with and targets hSSB1 for ubiquitination and degradation, which could be prevented by ATM-mediated hSSB1 T117 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271655 |
|
|
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 25249620 |
Here, we report that hSSB1 is the bona fide substrate for an Fbxl5-containing SCF (Skp1-Cul1-F box) E3 ligase. Fbxl5 interacts with and targets hSSB1 for ubiquitination and degradation, which could be prevented by ATM-mediated hSSB1 T117 phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FBXL5 | down-regulates quantity by destabilization
binding
|
IREB2 |
0.739 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271882 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19762596 |
We found that a SKP1-CUL1-FBXL5 ubiquitin ligase protein complex associates with and promotes the iron-dependent ubiquitination and degradation of IRP2. The F-box substrate adaptor protein FBXL5 was degraded upon iron and oxygen depletion in a process that required an iron-binding hemerythrin-like domain in its N terminus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXL5 | up-regulates activity 
binding
|
Cullin 1-RBX1-Skp1 |
0.642 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272136 |
|
|
in vitro |
|
| pmid |
sentence |
| 24157836 |
FBXL5 is located in the nucleus where it interacts with Snail1 promoting its polyubiquitination and affecting Snail1 protein stability and function by impairing DNA binding. Snail1 is ubiquitinated by the SCFFBXL5 complex. Snail1 downregulation by FBXL5 is prevented by Lats2, a protein kinase that phosphorylates Snail1 precluding its nuclear export but not its polyubiquitination. To demonstrate that FBXL5 has a direct activity on Snail1, we carried out polyubiquitination reactions in vitro. For this we purified Snail1 and the SCFFBXL5 complex from Sf9 insect cells infected with different baculoviruses corresponding to Flag-FBXL5, His-Skp1, HA-Cullin1 and Rbx1 (Supplementary Figure S3C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272461 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25249620 |
Here, we report that hSSB1 is the bona fide substrate for an Fbxl5-containing SCF (Skp1-Cul1-F box) E3 ligase. Fbxl5 interacts with and targets hSSB1 for ubiquitination and degradation, which could be prevented by ATM-mediated hSSB1 T117 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271884 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19762596 |
We found that a SKP1-CUL1-FBXL5 ubiquitin ligase protein complex associates with and promotes the iron-dependent ubiquitination and degradation of IRP2. The F-box substrate adaptor protein FBXL5 was degraded upon iron and oxygen depletion in a process that required an iron-binding hemerythrin-like domain in its N terminus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271654 |
|
|
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 25249620 |
Here, we report that hSSB1 is the bona fide substrate for an Fbxl5-containing SCF (Skp1-Cul1-F box) E3 ligase. Fbxl5 interacts with and targets hSSB1 for ubiquitination and degradation, which could be prevented by ATM-mediated hSSB1 T117 phosphorylation. |
|
| Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens |
| + |
FBXL5 | down-regulates quantity by destabilization
binding
|
DCTN1 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271652 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17532294 |
FBXL5 binds to p150(Glued)in vitro and in vivo. FBXL5 and p150(Glued) co-localize primarily in the cytoplasm with peri-nuclear enrichment in HeLa cells. Overexpression of FBXL5 promotes poly-ubiquitination of p150(Glued) and protein turnover of p150(Glued). Our findings provide a potential mechanism by which p150(Glued) protein function is regulated by SCFs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXL5 | down-regulates quantity by destabilization
binding
|
SNAI1 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272135 |
|
|
in vitro |
|
| pmid |
sentence |
| 24157836 |
FBXL5 is located in the nucleus where it interacts with Snail1 promoting its polyubiquitination and affecting Snail1 protein stability and function by impairing DNA binding. Snail1 is ubiquitinated by the SCFFBXL5 complex. Snail1 downregulation by FBXL5 is prevented by Lats2, a protein kinase that phosphorylates Snail1 precluding its nuclear export but not its polyubiquitination. To demonstrate that FBXL5 has a direct activity on Snail1, we carried out polyubiquitination reactions in vitro. For this we purified Snail1 and the SCFFBXL5 complex from Sf9 insect cells infected with different baculoviruses corresponding to Flag-FBXL5, His-Skp1, HA-Cullin1 and Rbx1 (Supplementary Figure S3C). |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
FBXL5
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- 