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.

Ichimura T, Taoka M, Shoji I, Kato H, Sato T, Hatakeyama S, Isobe T, Hachiya N

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

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
CAMKK1 YWHAQ	Affinity Capture-MS 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.	Buljan M (2020)	High	94.7143	BioGRID	3484975

Curated By

BioGRID

Interaction Summary

YWHAQ

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein N-terminus binding [IPI]protein binding [IPI]

Gene Ontology Cellular Component

CAMKK1