Predicate | Object |
---|---|
rdf:type | |
biopax3:controlType |
INHIBITION
|
biopax3:controlled | |
biopax3:comment |
ISG15 is a ubiquitin (Ub)-like protein which is conjugated to intracellular proteins via an isopeptide bond. Similar to ubiquitination, the conjugation of ISG15 (ISGylation) requires a three-step process, involving an E1 activating enzyme (UBE1L), an E2 conjugating enzyme (UbcM8/H8), and HERC5/Ceb1 an IFN-inducible ISG15-specific E3 ligase. ISG15 conjugation may play an important regulatory role in IFN-mediated antiviral responses. IFN induces ISG15 conjugation to RIG-I protein and lowers cellular levels of unconjugated RIG-I protein and, thus, negatively regulates RIG-I-mediated antiviral signaling. ISGylated RIG-I protein becomes subject to an irreversible biochemical process, such as proteolysis or proteasomeal degradation.
|
biopax3:xref | |
biopax3:controller | |
biopax3:dataSource | |
biopax3:displayName |
'ISG15:RIG-I conjugate [cytosol]' negatively regulates 'dsRNA binds to RIG-I'
|