PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24144283-1	2013	BRD4, characterized by two acetyl-lysine binding bromodomains and an extra-terminal (ET) domain, is a key chromatin organizer that directs gene activation in chromatin through transcription factor recruitment, enhancer assembly, and pause release of the RNA polymerase II complex for transcription elongation.	N(alpha)-acetyllysine	27-40	bromodomain containing 4	Mus musculus	0-4	
24144283-4	2013	Here, we report our structure-guided development of diazobenzene-based small-molecule inhibitors for the BRD4 bromodomains that have over 90% sequence identity at the acetyl-lysine binding site.	N(alpha)-acetyllysine	167-180	bromodomain containing 4	Mus musculus	105-109	
33094644-3	2020	BRD4, a member of the BET (Bromo- and Extra-Terminal domain) family of ubiquitously expressed acetyl-lysine reader proteins, plays a pivotal role as a coactivator of enhancer signaling across diverse tissue types in both health and disease, and has been implicated as a pharmacologic target in heart failure.	N(alpha)-acetyllysine	94-107	bromodomain containing 4	Mus musculus	0-4