TRIM32
Gene Ontology Biological Process
- actin ubiquitination [IDA]
- innate immune response [ISO]
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [ISO]
- negative regulation of keratinocyte apoptotic process [NAS]
- negative regulation of viral release from host cell [ISO]
- negative regulation of viral transcription [ISO]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [ISO]
- positive regulation of NF-kappaB transcription factor activity [IDA, ISO]
- positive regulation of cell cycle [ISO]
- positive regulation of cell growth [ISO]
- positive regulation of cell migration [ISO]
- positive regulation of cell motility [IDA]
- positive regulation of neurogenesis [IDA]
- positive regulation of neuron differentiation [IDA]
- positive regulation of protein catabolic process [IDA]
- positive regulation of proteolysis [ISO]
- positive regulation of sequence-specific DNA binding transcription factor activity [ISO]
- protein polyubiquitination [ISO]
- protein ubiquitination [IDA, ISO]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [ISO]
- response to UV [IDA]
- response to tumor necrosis factor [IDA]
Gene Ontology Molecular Function
ACTN3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy.
During muscle atrophy, myofibrillar proteins are degraded in an ordered process in which MuRF1 catalyzes ubiquitylation of thick filament components (Cohen et al. 2009. J. Cell Biol. http://dx.doi.org/10.1083/jcb.200901052). Here, we show that another ubiquitin ligase, Trim32, ubiquitylates thin filament (actin, tropomyosin, troponins) and Z-band (α-actinin) components and promotes their degradation. Down-regulation of Trim32 during fasting reduced fiber atrophy and the ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TRIM32 ACTN3 | 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 | 2207955 |
Curated By
- BioGRID