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
UBE2N
Gene Ontology Biological Process
- DNA double-strand break processing [IMP]
- Fc-epsilon receptor signaling pathway [TAS]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- T cell receptor signaling pathway [IMP, TAS]
- cellular protein modification process [TAS]
- cytokine-mediated signaling pathway [TAS]
- double-strand break repair via homologous recombination [IMP]
- histone ubiquitination [IMP]
- innate immune response [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of DNA repair [IMP]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of histone modification [IMP]
- positive regulation of ubiquitin-protein transferase activity [IMP]
- postreplication repair [IMP]
- protein K63-linked ubiquitination [IDA]
- protein ubiquitination [IMP, TAS]
- proteolysis [TAS]
- regulation of DNA repair [TAS]
- regulation of histone ubiquitination [IMP]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor 5 signaling pathway [TAS]
- toll-like receptor 9 signaling pathway [TAS]
- toll-like receptor TLR1:TLR2 signaling pathway [TAS]
- toll-like receptor TLR6:TLR2 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
TRIM25-mediated ubiquitination of G3BP1 regulates the proliferation and migration of human neuroblastoma cells.
Neuroblastoma is one of the most severe malignant tumors and accounts for substantial cancer-related mortality in children. Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is highly expressed in various cancers and acts as an important biomarker of poor prognosis. The ablation of G3BP1 inhibited the proliferation and migration of human SHSY5Y cells. Because of its important role in neuroblastoma, the ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM25 UBE2N | 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 | - | |
| TRIM25 UBE2N | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| TRIM25 UBE2N | 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 | - | |
| TRIM25 UBE2N | 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 | 2207963 | |
| UBE2N TRIM25 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | 4 | BioGRID | - |
Curated By
- BioGRID