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
YWHAQ
Gene Ontology Biological Process
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
14-3-3 proteins sequester a pool of soluble TRIM32 ubiquitin ligase to repress autoubiquitination and cytoplasmic body formation.
Deregulated expression of tripartite-motif protein 32 (TRIM32, an E3 ubiquitin-protein ligase) contributes to various diseases. Here we report, using quantitative proteomics and biochemistry, that 14-3-3 proteins bind to phosphorylated TRIM32 and prevent TRIM32 autoubiquitination and the formation of TRIM32-containing cytoplasmic bodies, potential autoregulatory mechanisms that can reduce the concentration of soluble free TRIM32. The 14-3-3-TRIM32 interaction was dependent on protein ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID