BAIT

TP53

Trp53, p53
tumor protein p53
GO Process (119)
GO Function (32)
GO Component (17)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Rattus norvegicus
PREY

HSP90AA1

Hsp86, Hsp90, Hspca
heat shock protein 90, alpha (cytosolic), class A member 1
GO Process (16)
GO Function (20)
GO Component (18)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Rattus norvegicus

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

The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent.

Whitesell L, Sutphin PD, Pulcini EJ, Martinez JD, Cook PH

Wild-type p53 is a short-lived protein which turns over very rapidly via selective proteolysis in the ubiquitin-proteasome pathway. Most p53 mutations, however, encode for protein products which display markedly increased intracellular levels and are associated with positive tumor-promoting activity. The mechanism by which mutation leads to impairment of ubiquitination and proteasome-mediated degradation is unknown, but it has been noted that ... [more]

Mol. Cell. Biol. Mar. 01, 1998; 18(3);1517-24 [Pubmed: 9488468]

Throughput

  • Low Throughput

Curated By

  • BioGRID