TRIM5
Gene Ontology Biological Process
- activation of innate immune response [IDA]
- defense response to virus [TAS]
- innate immune response [IDA]
- negative regulation of viral entry into host cell [IDA]
- negative regulation of viral release from host cell [IDA]
- pattern recognition receptor signaling pathway [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA, IMP]
- positive regulation of MAPK cascade [IMP]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of sequence-specific DNA binding transcription factor activity [IMP]
- protein K63-linked ubiquitination [IDA]
- protein trimerization [IDA]
- regulation of lipopolysaccharide-mediated signaling pathway [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
SUMO1
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular protein metabolic process [TAS]
- cytokine-mediated signaling pathway [TAS]
- interferon-gamma-mediated signaling pathway [TAS]
- negative regulation of DNA binding [IMP]
- negative regulation of sequence-specific DNA binding transcription factor activity [IMP]
- negative regulation of transcription, DNA-templated [IDA, IMP]
- palate development [ISS]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein complex assembly [IDA]
- post-translational protein modification [TAS]
- protein sumoylation [IDA, TAS]
- regulation of interferon-gamma-mediated signaling pathway [TAS]
- regulation of protein localization [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
Endogenous TRIM5α Function Is Regulated by SUMOylation and Nuclear Sequestration for Efficient Innate Sensing in Dendritic Cells.
During retroviral infection, viral capsids are subject to restriction by the cellular factor TRIM5α. Here, we show that dendritic cells (DCs) derived from human and non-human primate species lack efficient TRIM5α-mediated retroviral restriction. In DCs, endogenous TRIM5α accumulates in nuclear bodies (NB) that partly co-localize with Cajal bodies in a SUMOylation-dependent manner. Nuclear sequestration of TRIM5α allowed potent induction of ... [more]
Throughput
- Low Throughput
Additional Notes
- Proximity Ligation Assay.
- TRIM5a is known to both bind to SUMO as well as postranslationally modified by SUMO
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM5 SUMO1 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | 1510385 | |
| SUMO1 TRIM5 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 608528 |
Curated By
- BioGRID