TRIM27
Gene Ontology Biological Process
- Arp2/3 complex-mediated actin nucleation [IDA]
- cell proliferation [TAS]
- innate immune response [IDA]
- interferon-gamma secretion [IMP]
- negative regulation of adaptive immune response [IMP]
- negative regulation of calcium ion import [IMP]
- negative regulation of gene expression, epigenetic [IDA]
- negative regulation of interleukin-2 secretion [IMP]
- negative regulation of protein kinase activity [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of tumor necrosis factor production [IMP]
- negative regulation of viral transcription [IDA]
- peptidyl-tyrosine phosphorylation [TAS]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- protein K63-linked ubiquitination [IMP]
- protein trimerization [IDA]
- retrograde transport, endosome to Golgi [IDA]
- spermatogenesis [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
MDM2
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [IMP, TAS]
- Fc-epsilon receptor signaling pathway [TAS]
- cellular response to hypoxia [IEP]
- epidermal growth factor receptor signaling pathway [TAS]
- establishment of protein localization [IDA]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- negative regulation of DNA damage response, signal transduction by p53 class mediator [IDA]
- negative regulation of cell cycle arrest [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- neurotrophin TRK receptor signaling pathway [TAS]
- peptidyl-lysine modification [IMP]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of cell proliferation [TAS]
- positive regulation of mitotic cell cycle [IMP]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- protein complex assembly [IDA]
- protein destabilization [IDA]
- protein localization to nucleus [IDA]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IDA]
- regulation of protein catabolic process [IDA]
- response to antibiotic [IEP]
- synaptic transmission [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
SUMO E3 ligase activity of TRIM proteins.
SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM27 MDM2 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 608710 |
Curated By
- BioGRID