a DNA damage checkpoint protein that interacts with HDAC4 protein to mediate the DNA damage response. Inhibits E2F1-mediated apoptosis in prostate cancer cells. Recruited to double strand breaks via the binding of its Tudor domain to dimethylated H3 K20. Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. Binds to the central domain of p53. Interacts with Artemis. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on S139. Interacts with histone H4 that has been dimethylated at K20. Has low affinity for histone H4 containing monomethylated K20. Does not bind histone H4 containing unmethylated or trimethylated K20. Has low affinity for histone H3 that has been dimethylated on K79. Does not bind unmethylated histone H3. Phosphorylated at basal level in the absence of DNA damage. Hyper-phosphorylated in an ATM-dependent manner in response to DNA damage induced by ionizing radiation. Hyper-phosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation. Two alternatively spliced human isoforms have been observed. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; Transcription, coactivator/corepressor
Molecular Function: methylated histone residue binding; p53 binding; protein binding
Biological Process: DNA damage checkpoint; double-strand break repair via nonhomologous end joining; positive regulation of isotype switching; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; protein homooligomerization; protein sumoylation; response to DNA damage stimulus