TRIM8
Gene Ontology Biological Process
- innate immune response [IDA]
- negative regulation of viral release from host cell [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PIAS3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
TRIM8 modulates STAT3 activity through negative regulation of PIAS3.
TRIM8 is a member of the protein family defined by the presence of a common domain structure composed of a tripartite motif: a RING-finger, one or two B-box domains and a coiled-coil motif. Here, we show that TRIM8 interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. Ectopic expression of TRIM8 cancels the negative effect ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID