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
TPM1
Gene Ontology Biological Process
- actin filament capping [ISO]
- cardiac muscle contraction [IMP, ISO]
- embryo development [IMP]
- in utero embryonic development [IMP]
- muscle filament sliding [ISO]
- negative regulation of cell migration [ISO]
- positive regulation of ATPase activity [ISO]
- positive regulation of cell adhesion [ISO]
- positive regulation of heart rate by epinephrine [IMP]
- positive regulation of stress fiber assembly [ISO]
- regulation of ATPase activity [ISO]
- ruffle organization [ISO]
- ventricular cardiac muscle tissue morphogenesis [IMP]
- wound healing [ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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 TPM1 | 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 | 2207953 |
Curated By
- BioGRID