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
PIAS4
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB.
Protein inhibitors of activated STATs (PIAS) family members are ubiquitin-protein isopeptide ligase-small ubiquitin-like modifier ligases for diverse transcription factors. However, the regulation of PIAS protein activity in cells is poorly understood. Previously, we reported that expression of Trim32, a RING domain ubiquitin-protein isopeptide ligase-ubiquitin ligase mutated in human limb-girdle muscular dystrophy type 2H (LGMD2H) and Bardet-Biedl syndrome, is elevated during ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM32 PIAS4 | 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 | 1032759 |
Curated By
- BioGRID