Relation Results

Summary

Name ASB3
Full Name Ankyrin repeat and SOCS box protein 3
Synonyms ASB-3 |
Primary ID Q9Y575
Links - -
Type protein
Relations 2
Function Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ub ...
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Type: Score: Layout: SPV 
0.290.403ASB3VCB-Cul2TNFRSF1B

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Relations
Regulator
Mechanism
target
score ℹ
+ ASB3up-regulates activity img/direct-activation.png binding VCB-Cul2 0.29
Identifier Residue Sequence Organism Cell Line
SIGNOR-271544 Homo sapiens HEK-293 Cell
pmid sentence
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
+ ASB3down-regulates quantity by destabilization img/direct_inhibition.png binding TNFRSF1B 0.403
Identifier Residue Sequence Organism Cell Line
SIGNOR-271546 Homo sapiens HEK-293 Cell
pmid sentence
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
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