BAIT

ATP7A

DSMAX, MK, MNK, SMAX3, RP3-465G10.1
ATPase, Cu++ transporting, alpha polypeptide
GO Process (38)
GO Function (7)
GO Component (11)
Homo sapiens
PREY

CLU

APO-J, APOJ, CLI, CLU1, CLU2, KUB1, NA1/NA2, SGP-2, SGP2, SP-40, TRPM-2, TRPM2, AAG4
clusterin
GO Process (35)
GO Function (4)
GO Component (12)

Gene Ontology Biological Process

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

Clusterin (apolipoprotein J), a molecular chaperone that facilitates degradation of the copper-ATPases ATP7A and ATP7B.

Materia S, Cater MA, Klomp LW, Mercer JF, La Fontaine S

The copper-transporting P(1B)-type ATPases (Cu-ATPases) ATP7A and ATP7B are key regulators of physiological copper levels. They function to maintain intracellular copper homeostasis by delivering copper to secretory compartments and by trafficking toward the cell periphery to export excess copper. Mutations in the genes encoding ATP7A and ATP7B lead to copper deficiency and toxicity disorders, Menkes and Wilson diseases, respectively. This ... [more]

J. Biol. Chem. Mar. 25, 2011; 286(12);10073-83 [Pubmed: 21242307]

Throughput

  • Low Throughput

Curated By

  • BioGRID