| + |
SOCS3 | up-regulates quantity 
binding
|
Elongin E3-Cul-5 |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272643 |
|
|
Mus musculus |
BA/F3 Cell |
| pmid |
sentence |
| 17138568 |
SOCS proteins can act as E3 ligases by forming a complex with Elongin B/C and Cul5/Rbx1/2.SOCS3 targets Siglec 7 for degradation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SPSB2 | up-regulates activity
binding
|
Elongin E3-Cul-5 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271899 |
|
|
in vitro |
|
| pmid |
sentence |
| 20603330 |
We have identified SPRY domain-containing SOCS (suppressor of cytokine signaling) box protein 2 (SPSB2) as a novel negative regulator that recruits an E3 ubiquitin ligase complex to polyubiquitinate iNOS, resulting in its proteasomal degradation. A cell-free ubiquitination assay was established to demonstrate SPSB2-dependent ubiquitination of iNOS. LPS/IFN-γ–stimulated macrophage lysates from Spsb2−/− mice were used as a source of iNOS and incubated with ubiquitin and a trimeric SPSB2/elongin BC complex in the presence of E1 and E2 (UbcH5a) enzymes, Rbx2, and Cullin5 for various times. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ASB2 | up-regulates activity
binding
|
Elongin E3-Cul-5 |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271800 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ELOC | form complex 
binding
|
Elongin E3-Cul-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271797 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Elongin E3-Cul-5 | down-regulates quantity by destabilization 
polyubiquitination
|
CLEC1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272783 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19785988 |
In this study, we reported that RACK1, the receptor for activated C-kinase 1, associated with the cytoplasmic tail of CLEC-2. Moreover, overexpression of RACK1 decreased the stability of CLEC-2 through promoting its ubiquitin-proteasome degradation, without impairing surface expression and downstream signaling of CLEC-2. Taken together, these results suggest RACK1 as a novel modulator of CLEC-2 expression.Previous reports indicated that RACK1 mediated ubiquitin–proteasome degradation of HIF-1a and BimEL by recruiting Elongin-C/B ubiquitin ligase complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Elongin E3-Cul-5 | down-regulates quantity by destabilization
polyubiquitination
|
NANOS2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271900 |
|
|
in vitro |
|
| pmid |
sentence |
| 20603330 |
We have identified SPRY domain-containing SOCS (suppressor of cytokine signaling) box protein 2 (SPSB2) as a novel negative regulator that recruits an E3 ubiquitin ligase complex to polyubiquitinate iNOS, resulting in its proteasomal degradation. A cell-free ubiquitination assay was established to demonstrate SPSB2-dependent ubiquitination of iNOS. LPS/IFN-γ–stimulated macrophage lysates from Spsb2−/− mice were used as a source of iNOS and incubated with ubiquitin and a trimeric SPSB2/elongin BC complex in the presence of E1 and E2 (UbcH5a) enzymes, Rbx2, and Cullin5 for various times. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RACK1 | up-regulates activity
binding
|
Elongin E3-Cul-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272782 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19785988 |
In this study, we reported that RACK1, the receptor for activated C-kinase 1, associated with the cytoplasmic tail of CLEC-2. Moreover, overexpression of RACK1 decreased the stability of CLEC-2 through promoting its ubiquitin-proteasome degradation, without impairing surface expression and downstream signaling of CLEC-2. Taken together, these results suggest RACK1 as a novel modulator of CLEC-2 expression.Previous reports indicated that RACK1 mediated ubiquitin–proteasome degradation of HIF-1a and BimEL by recruiting Elongin-C/B ubiquitin ligase complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ELOB | form complex
binding
|
Elongin E3-Cul-5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271796 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RNF7 | form complex
binding
|
Elongin E3-Cul-5 |
0.929 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271799 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
UBE2D1 | up-regulates activity
binding
|
Elongin E3-Cul-5 |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271898 |
|
|
in vitro |
|
| pmid |
sentence |
| 20603330 |
We have identified SPRY domain-containing SOCS (suppressor of cytokine signaling) box protein 2 (SPSB2) as a novel negative regulator that recruits an E3 ubiquitin ligase complex to polyubiquitinate iNOS, resulting in its proteasomal degradation. A cell-free ubiquitination assay was established to demonstrate SPSB2-dependent ubiquitination of iNOS. LPS/IFN-γ–stimulated macrophage lysates from Spsb2−/− mice were used as a source of iNOS and incubated with ubiquitin and a trimeric SPSB2/elongin BC complex in the presence of E1 and E2 (UbcH5a) enzymes, Rbx2, and Cullin5 for various times. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CUL5 | form complex
binding
|
Elongin E3-Cul-5 |
0.929 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271798 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Elongin E3-Cul-5 | down-regulates quantity by destabilization
polyubiquitination
|
FLNB |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271801 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19300455 |
Here, we provide the first evidence that a novel ASB2 isoform, ASB2beta, is important for muscle differentiation. ASB2beta is expressed in muscle cells during embryogenesis and in adult tissues. ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (FLNb) for proteasomal degradation. Altogether, our results indicated that ASB2β can assemble with elongin B, elongin C, Cullin 5 and Rbx2 to reconstitute an active E3 ubiquitin ligase complex.ASB2β induces polyubiquitylation of FLNb. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Elongin E3-Cul-5 | down-regulates quantity by destabilization
polyubiquitination
|
SIGLEC7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272644 |
|
|
Mus musculus |
BA/F3 Cell |
| pmid |
sentence |
| 17138568 |
SOCS proteins can act as E3 ligases by forming a complex with Elongin B/C and Cul5/Rbx1/2.SOCS3 targets Siglec 7 for degradation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
Elongin E3-Cul-5