TRIM25
Gene Ontology Biological Process
- innate immune response [IDA, TAS]
- negative regulation of type I interferon production [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of sequence-specific DNA binding transcription factor activity [IMP]
- regulation of viral entry into host cell [IDA]
- regulation of viral release from host cell [IMP]
Gene Ontology Molecular Function
MDH1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
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 is identified by mass spectrometric methods.
Publication
RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination.
TRIM25 is a novel RNA-binding protein and a member of the Tripartite Motif (TRIM) family of E3 ubiquitin ligases, which plays a pivotal role in the innate immune response. However, there is scarce knowledge about its RNA-related roles in cell biology. Furthermore, its RNA-binding domain has not been characterized.Here, we reveal that the RNA-binding activity of TRIM25 is mediated by ... [more]
Throughput
- High Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
TRIM25 MDH1 | Affinity Capture-RNA Affinity Capture-RNA An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis. | High | - | BioGRID | - |
Curated By
- BioGRID