BRD4 and cancer: BDs bind acetylated lysine residues on target proteins, including histones.[3] BDs function primarily as readers of acetylated lysine residues on histone tails; however, recent evidence indicates that BRD4 has acetylation‐independent transcriptional functions as well as a non‐transcriptional function in controlling DNA damage checkpoint activation and repair.[3, 4, 5, 6] Through its interaction with transcription factors, coactivators, and chromatin‐modifying enzymes, BRD4 plays a crucial role in embryogenesis and cancer development.