BAIT
YWHAQ
14-3-3, 1C5, HS1
tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta
GO Process (6)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
SMURF1
SMAD specific E3 ubiquitin protein ligase 1
GO Process (14)
GO Function (5)
GO Component (6)
Gene Ontology Biological Process
- BMP signaling pathway [IDA, TAS]
- cell differentiation [IDA]
- ectoderm development [TAS]
- negative regulation of BMP signaling pathway [TAS]
- negative regulation of transforming growth factor beta receptor signaling pathway [IDA, TAS]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein export from nucleus [IDA]
- protein localization to cell surface [IDA]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA]
- protein ubiquitination involved in ubiquitin-dependent protein catabolic process [IDA]
- receptor catabolic process [IDA]
- transforming growth factor beta receptor signaling pathway [TAS]
- ubiquitin-dependent SMAD protein catabolic process [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Affinity Capture-MS
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 is identified by mass spectrometric methods.
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]
J. Cell. Sci. Feb. 26, 2013; 0(0); [Pubmed: 23444366]
Throughput
- Low Throughput
Curated By
- BioGRID