| + |
Ub:E2 | up-regulates activity 
ubiquitination
|
CHFR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271061 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization 
ubiquitination
|
CHFR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271461 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17442268 |
In this study, we identified USP7 (also known as HAUSP), which is a member of a family of proteins that cleave polyubiquitin chains and/or ubiquitin precursors, as an interacting protein with Chfr by immunoaffinity purification and mass spectrometry, and their interaction greatly increases the stability of Chfr. In fact, USP7 can remove ubiquitin moiety from the autoubiquitinated Chfr both in vivo and in vitro, which results in the accumulation of Chfr in the cell. USP7 mediates deubiquitination of Chfr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
PBK |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271471 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24012691 |
CHFR ubiquitinates and degrades TOPK. Our in vivo ubiquitination assays revealed that the polyubiquitination of TOPK occurs only in the presence of full length CHFR but not with the ΔRING or Δcysteine-rich domain deletion mutants (Fig. 2a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
SMARCD1 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271459 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 22285184 |
Here we report that CHFR interacts with BRG1, SNF5, and BAF60a of the SWI/SNF-like BAF complex and ubiquitinates them to target for degradation through a proteasome-mediated pathway, and that SRG3/mBAF155 stabilizes these components by blocking their interaction with CHFR. These results suggest that CHFR enhances the degradation of the components of the SWI/SNF-like BAF complex by inducing their poly-ubiquitination. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
SMARCB1 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271458 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 22285184 |
Here we report that CHFR interacts with BRG1, SNF5, and BAF60a of the SWI/SNF-like BAF complex and ubiquitinates them to target for degradation through a proteasome-mediated pathway, and that SRG3/mBAF155 stabilizes these components by blocking their interaction with CHFR. These results suggest that CHFR enhances the degradation of the components of the SWI/SNF-like BAF complex by inducing their poly-ubiquitination. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
USP7 | up-regulates quantity by stabilization
deubiquitination
|
CHFR |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271462 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17442268 |
In this study, we identified USP7 (also known as HAUSP), which is a member of a family of proteins that cleave polyubiquitin chains and/or ubiquitin precursors, as an interacting protein with Chfr by immunoaffinity purification and mass spectrometry, and their interaction greatly increases the stability of Chfr. In fact, USP7 can remove ubiquitin moiety from the autoubiquitinated Chfr both in vivo and in vitro, which results in the accumulation of Chfr in the cell. USP7 mediates deubiquitination of Chfr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
SMARCA4 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271457 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 22285184 |
Here we report that CHFR interacts with BRG1, SNF5, and BAF60a of the SWI/SNF-like BAF complex and ubiquitinates them to target for degradation through a proteasome-mediated pathway, and that SRG3/mBAF155 stabilizes these components by blocking their interaction with CHFR. These results suggest that CHFR enhances the degradation of the components of the SWI/SNF-like BAF complex by inducing their poly-ubiquitination. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
HLTF |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271460 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20388495 |
CHFR functions as a ubiquitin ligase for HLTF to regulate its stability and functions. CHFR negatively regulates and ubiquitinates HLTF. Taken together, this is the first report identifying the regulatory mechanism of HLTF by CHFR, suggesting that CHFR-mediated downregulation of HLTF may help protect against cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
HDAC1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271465 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19182791 |
Histone deacetylase 1 (HDAC1), which represses transcription by deacetylating histones, was newly isolated as a Chfr-interacting protein. Chfr binds and downregulates HDAC1 by inducing its polyubiquitylation, both in vitro and in vivo. Together, these results suggest that the ubiquitin ligase activity of Chfr targets HDAC1 for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
ubiquitination
|
KIF22 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271469 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19321445 |
Chfr ubiquitinates Kif22 and promotes its degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
PLK1 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271464 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17442268 |
Chfr, a mitotic stress checkpoint, plays an important role in cell cycle progression, tumor suppression and the processes that require the E3 ubiquitin ligase activity mediated by the RING finger domain. Chfr stimulates the formation of polyubiquitin chains by ub-conjugating enzymes, and induces the proteasome-dependent degradation of a number of cellular proteins including Plk1 and Aurora A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
AURKA |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271463 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17442268 |
Chfr, a mitotic stress checkpoint, plays an important role in cell cycle progression, tumor suppression and the processes that require the E3 ubiquitin ligase activity mediated by the RING finger domain. Chfr stimulates the formation of polyubiquitin chains by ub-conjugating enzymes, and induces the proteasome-dependent degradation of a number of cellular proteins including Plk1 and Aurora A. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
PARP1 |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271470 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 23268447 |
Here, we show that checkpoint with Forkhead-associated (FHA) and RING finger domain protein (CHFR), an E3 ubiquitin ligase, is recruited to DSBs by poly(ADP-ribose) (PAR). Moreover, CHFR ubiquitinates PAR polymerase 1 (PARP1) and regulates chromatin-associated PARP1 in vivo. Moreover, the poly-ubiquitin chain on PARP1 could be recognized by both anti-K48 and K63-linked poly-ubiquitin chain antibodies, suggesting that CHFR mediates a mixed poly-ubiquitin chain linkage on PARP1. With MG132 treatment, ubiquitinated PARP1 was significantly accumulated (Figure 4D), suggesting that the ubiquitination of PARP1 is likely involved in protein degradation. Consistently, we found that following DNA damage, PARP1 quickly dissociated from the chromatin in the wild-type cells (Figure 4F). However, in the Chfr−/− cells, the dissociation of PARP1 from the chromatin was significantly delayed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CHFR
- 
- 