TRIM32
Gene Ontology Biological Process
- fat cell differentiation [ISS]
- innate immune response [IDA, TAS]
- negative regulation of fibroblast proliferation [ISS]
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [IDA]
- negative regulation of viral release from host cell [IDA]
- negative regulation of viral transcription [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of NF-kappaB transcription factor activity [IDA, ISS]
- positive regulation of cell cycle [IDA]
- positive regulation of cell growth [IDA]
- positive regulation of cell migration [IDA]
- positive regulation of cell motility [ISS]
- positive regulation of neurogenesis [ISS]
- positive regulation of neuron differentiation [ISS]
- positive regulation of protein catabolic process [ISS]
- positive regulation of proteolysis [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of type I interferon production [TAS]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IMP]
- regulation of type I interferon production [TAS]
- response to UV [ISS]
- response to tumor necrosis factor [ISS]
Gene Ontology Molecular Function
UBE2D1
Gene Ontology Biological Process
- BMP signaling pathway [TAS]
- MyD88-independent toll-like receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- cellular response to hypoxia [TAS]
- gene expression [TAS]
- innate immune response [TAS]
- mitotic cell cycle [TAS]
- mitotic spindle assembly checkpoint [TAS]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- positive regulation of protein ubiquitination [IDA]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- protein K48-linked ubiquitination [IDA]
- protein polyubiquitination [IDA]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
- ubiquitin-dependent protein catabolic process [IDA]
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
Functional interactions between ubiquitin E2 enzymes and TRIM proteins.
The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite motif module, composed of a RING domain, one or two B-box domains and a coiled-coil region. TRIM proteins are involved in many cellular processes and represent the largest subfamily of RING-containing putative ubiquitin E3 ligases. Whereas their role as E3 ubiquitin ligases has been presumed, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM32 UBE2D1 | 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 | 1032756 | |
| TRIM32 UBE2D1 | 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 | 1521837 | |
| TRIM32 UBE2D1 | 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 | 823426 | |
| TRIM32 UBE2D1 | 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 | - |
Curated By
- BioGRID