BAIT

TRIM63

IRF, MURF1, MURF2, RNF28, SMRZ
tripartite motif containing 63, E3 ubiquitin protein ligase
UPS Project
GO Process (2)
GO Function (3)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

HSPA4

APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY
heat shock 70kDa protein 4
GO Process (3)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens

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

TRIM32-Cytoplasmic-Body Formation Is an ATP-Consuming Process Stimulated by HSP70 in Cells.

Kawaguchi Y, Taoka M, Takekiyo T, Uekita T, Shoji I, Hachiya N, Ichimura T

The spontaneous and energy-releasing reaction of protein aggregation is typically prevented by cellular quality control machinery (QC). TRIM32 is a member of the TRIM (tripartite motif-containing) ubiquitin E3 ligases, and when overexpressed in cultured cells, readily forms spherical inclusions designated as cytoplasmic bodies (CBs) even without proteasome inhibition. Here, we show that HSP70, a central QC component, is a primary ... [more]

PLoS ONE Jan. 05, 2017; 12(1);e0169436 [Pubmed: 28052117]

Throughput

  • Low Throughput

Curated By

  • BioGRID