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
MYLPF
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
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
Curated By
- BioGRID