PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25097667-6 2014 RESULTS: Mutation of a conserved asparagine crucial for binding to acetylated lysines in the bromodomains of BRD3, BRD4 and TRIM24 all resulted in reduction of FRAP recovery times, indicating loss of or significantly reduced binding to acetylated chromatin, as did the addition of known inhibitors. Lysine 78-85 bromodomain containing 3 Homo sapiens 109-113 31266503-2 2019 Bromodomain and extra-terminal (BET) proteins (BRD2, BRD3, BRD4 and BRDT) are chromatin readers essential for maintaining proper gene transcription by specifically binding acetylated lysine residues. Lysine 183-189 bromodomain containing 3 Homo sapiens 53-57 32895492-4 2020 BRD3 binds to histone H3 acetylated at lysine 18 (H3K18ac) in vitro and co-occupies the genome with H3K18ac. Lysine 39-45 bromodomain containing 3 Homo sapiens 0-4 32324495-3 2020 The BETs (bromodomain and extraterminal-containing protein family), which includes BRD2, BRD3, and BRD4 and the testis-restricted BRDT, are epigenetic reader proteins that bind to specific acetylated lysine residues on histone tails where they facilitate the assembly of transcription complexes including transcription factors and transcriptional machinery like RNA Polymerase II. Lysine 200-206 bromodomain containing 3 Homo sapiens 89-93 24733848-3 2014 The bromodomain and extraterminal (BET) proteins, Brd2, Brd3, Brd4, and BrdT, bind to acetylated lysine residues on histone or nonhistone proteins recruiting transcriptional regulators and thus activating or repressing gene transcription. Lysine 97-103 bromodomain containing 3 Homo sapiens 56-60