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ATP5O — TOP2A

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Intact Interaction: Complex of 177 proteins (association, cross-linking study) Byron et al., Proteomics 2012

Text-mined interactions from Literome

Olland et al., J Biol Chem 1999 : Purified Top2- ( 1-660 ), a fragment containing the NH ( 2 ) -terminal 660 amino acid of the yeast enzyme, appears to be dimeric in the absence or presence of DNA, and the ATPase activity of the protein is significantly stimulated by DNA
Dykhuizen et al., Nature 2013 (Medulloblastoma) : Our results demonstrate that TOP2A chromatin binding is dependent on the ATPase activity of BRG1, which is compromised in oncogenic BRG1 mutants