| + |
ELOB | form complex 
binding
|
VCB-Cul2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271517 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VCB-Cul2 | down-regulates quantity by destabilization 
polyubiquitination
|
USP20 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272606 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12056827 |
VDU1 and VDU2 could be important substrates of pVHL E3 ligase complex. Finally, we demonstrate that VDU2 can also be ubiquitinated and degraded in a pVHL-dependent manner.pVHL mediates the degradation of hVDU2 by proteasome. we have demonstrated that both VDU1 and VDU2 also bind to the β-domain of pVHL and several naturally occurring mutations in the β-domain disrupt the interaction between VDU1/VDU2 and pVHL. If pVHL is mutated either in the α-domain or β-domain, VDU1 and VDU2 would not be ubiquitinated and degraded properly. This could lead to accumulation of these two proteins in the cells. Together, our results suggest that VDU1 and VDU2 might be relevent to pVHL-related tumorigenesis. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ELOC | form complex
binding
|
VCB-Cul2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271518 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VHL | form complex
binding
|
VCB-Cul2 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272585 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VCB-Cul2 | down-regulates quantity by destabilization
polyubiquitination
|
VAV1 |
0.246 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272563 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10747851 |
Recent evidence indicates that SOCS1 interacts with elongins B and C, which are components of a ubiquitin ligase complex, VCB (VHL/elonginC/B), based on the VHL (von Hippel Lindau) tumor suppressor protein. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
RBX1 | form complex
binding
|
VCB-Cul2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271520 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VCB-Cul2 | down-regulates quantity by destabilization
polyubiquitination
|
TNFRSF1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271545 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15899873 |
While the ankyrin repeats of ASB3 interact with the C-terminal 37 amino acids of TNF-R2, the SOCS box of ASB3 is responsible for recruiting the E3 ubiquitin ligase adaptors Elongins-B/C, leading to TNF-R2 ubiquitination on multiple lysine residues within its C-terminal region. Downregulation of ASB3 expression by a small interfering RNA inhibited TNF-R2 degradation and potentiated TNF-R2-mediated cytotoxicity. The data presented here implicate ASB3 as a negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of TNF-R2 for ubiquitination and proteasome-mediated degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VCB-Cul2 | down-regulates quantity by destabilization
polyubiquitination
|
USP33 |
0.461 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272623 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11739384 |
Finally, we demonstrate that VDU1 is able to be ubiquitinated via a pVHL-dependent pathway for proteasomal degradation, and VHL mutations that disrupt the interaction between VDU1 and pVHL abrogate the ubiquitination of VDU1. Our findings indicate that VDU1, a novel ubiquitin-specific processing protease, is a downstream target for ubiquitination and degradation by pVHL E3 ligase. Targeted degradation of VDU1 by pVHL could be crucial for regulating the ubiquitin-proteasome degradation pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272607 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12056827 |
VDU1 and VDU2 could be important substrates of pVHL E3 ligase complex. Finally, we demonstrate that VDU2 can also be ubiquitinated and degraded in a pVHL-dependent manner.pVHL mediates the degradation of hVDU2 by proteasome. we have demonstrated that both VDU1 and VDU2 also bind to the β-domain of pVHL and several naturally occurring mutations in the β-domain disrupt the interaction between VDU1/VDU2 and pVHL. If pVHL is mutated either in the α-domain or β-domain, VDU1 and VDU2 would not be ubiquitinated and degraded properly. This could lead to accumulation of these two proteins in the cells. Together, our results suggest that VDU1 and VDU2 might be relevent to pVHL-related tumorigenesis. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
SOCS5 | up-regulates activity 
binding
|
VCB-Cul2 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271522 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15590694 |
SOCS5 Can Physically Associate with the EGFR. The complex recruited by SOCS proteins is composed of ElonginBC, Cullin, and Roc1 (15, 16). Together, this complex has E3 ubiquitin ligase activity. We suspect that the role of the SB domain is to mediate coupling of EGFR with the Elongin-Cullin-Roc E3 ubiquitin ligase complex, resulting in enhanced EGFR degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VCB-Cul2 | down-regulates quantity by destabilization
polyubiquitination
|
PRKCI |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272591 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. we show that PKClambda can be ubiquitinated in vitro in a cell-free ubiquitination assay using purified recombinant components including VCB-Cul2. Given the known function of aPKC in the regulation of cell polarity and cell growth, PKClambda may be a target of pVHL in its function as a tumor suppressor.Degradation of the Ubiquitin-conjugated Active Form of PKCλ Is Blocked by a Proteasome Inhibitor in Vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ASB3 | up-regulates activity
binding
|
VCB-Cul2 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271544 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15899873 |
While the ankyrin repeats of ASB3 interact with the C-terminal 37 amino acids of TNF-R2, the SOCS box of ASB3 is responsible for recruiting the E3 ubiquitin ligase adaptors Elongins-B/C, leading to TNF-R2 ubiquitination on multiple lysine residues within its C-terminal region. Downregulation of ASB3 expression by a small interfering RNA inhibited TNF-R2 degradation and potentiated TNF-R2-mediated cytotoxicity. The data presented here implicate ASB3 as a negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of TNF-R2 for ubiquitination and proteasome-mediated degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUL2 | form complex
binding
|
VCB-Cul2 |
0.895 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271519 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11574546 |
The von Hippel-Lindau tumor-suppressor protein (pVHL) forms a protein complex (VCB-Cul2) with elongin C, elongin B, Cul-2, and Rbx1, which functions as a ubiquitin-protein ligase (E3). The alpha-subunits of the hypoxia-inducible factors have been identified as targets for the VCB-Cul2 ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOCS1 | up-regulates activity
binding
|
VCB-Cul2 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272564 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10747851 |
Recent evidence indicates that SOCS1 interacts with elongins B and C, which are components of a ubiquitin ligase complex, VCB (VHL/elonginC/B), based on the VHL (von Hippel Lindau) tumor suppressor protein. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
VCB-Cul2 | down-regulates quantity by destabilization
ubiquitination
|
EGFR |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271521 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15590694 |
SOCS5 Can Physically Associate with the EGFR. The complex recruited by SOCS proteins is composed of ElonginBC, Cullin, and Roc1 (15, 16). Together, this complex has E3 ubiquitin ligase activity. We suspect that the role of the SB domain is to mediate coupling of EGFR with the Elongin-Cullin-Roc E3 ubiquitin ligase complex, resulting in enhanced EGFR degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
VCB-Cul2