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BMI1 — H2AFX

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: H2AFX — BMI1 (direct interaction, enzymatic study) Pan et al., J Biol Chem 2011*
• IRef Biogrid Interaction: H2AFX — BMI1 (physical association, affinity chromatography technology) Pan et al., J Biol Chem 2011*
• IRef Biogrid Interaction: H2AFX — BMI1 (colocalization, imaging technique) Ginjala et al., Mol Cell Biol 2011*

Text-mined interactions from Literome

Ginjala et al., Mol Cell Biol 2011 : The sustained localization of BMI1 to damage sites is dependent on intact ATM and ATR and requires H2AX phosphorylation and recruitment of RNF8
Pan et al., J Biol Chem 2011 : Here we show that monoubiquitination of H2AX mediated by the RNF2-BMI1 complex is critical for the efficient formation of ?-H2AX and functions as a proximal regulator in DDR ( DNA damage response ) ... Additionally, the regulatory effect of RNF2-BMI1 on ?-H2AX formation is dependent on ATM. Lacking their ability to properly activate the DNA damage signaling pathway, RNF2-BMI1 complex depleted cells exhibit impaired DNA repair and increased sensitivity to ionizing radiation