BRD2
entrez
6046
canonical
uniprot
P25440
canonical
ensembl
ENSG00000204256
resolver
ensembl
ENSG00000215077
resolver
ensembl
ENSG00000234507
resolver
ensembl
ENSG00000234704
resolver
ensembl
ENSG00000235307
resolver
ensp
ENSP00000363958
resolver
ensp
ENSP00000363964
resolver
ensp
ENSP00000378702
resolver
ensp
ENSP00000391246
resolver
ensp
ENSP00000399009
resolver
ensp
ENSP00000409613
resolver
ensp
ENSP00000434978
resolver
ensp
ENSP00000435693
resolver
ensp
ENSP00000436322
resolver
ensp
ENSP00000475691
resolver
ensp
ENSP00000503515
resolver
enst
ENST00000414731
resolver
enst
ENST00000449118
resolver
enst
ENST00000486864
resolver
enst
ENST00000492172
resolver
enst
ENST00000495733
resolver
enst
ENST00000678778
resolver
genesymbol
BRD2
resolver
genesymbol_syn
KIAA9001
resolver
genesymbol_syn
RING3
resolver
hgnc
HGNC:1103
resolver
uniprot
A2AAU0
resolver
uniprot
B0S7P0
resolver
uniprot
B1AZT1
resolver
uniprot
E9PIQ3
resolver
uniprot
O00699
resolver
uniprot
O00700
resolver
uniprot
Q15310
resolver
uniprot
Q5STC9
resolver
uniprot
Q63HQ9
resolver
uniprot
Q658Y7
resolver
uniprot
Q6P3U2
resolver
uniprot
Q969U4
resolver
uniprot_entry
BRD2_HUMAN
resolver
uniprot_entry
E9PIQ3_HUMAN
resolver
uniprot_sec
A2AAU0
resolver
uniprot_sec
B0S7P0
resolver
uniprot_sec
B1AZT1
resolver
uniprot_sec
O00699
resolver
uniprot_sec
O00700
resolver
uniprot_sec
Q15310
resolver
uniprot_sec
Q5STC9
resolver
uniprot_sec
Q63HQ9
resolver
uniprot_sec
Q658Y7
resolver
uniprot_sec
Q6P3U2
resolver
uniprot_sec
Q969U4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by JQ1, a thieno-triazolo-1,4-diazepine derivative, which specifically inhibits members of the BET family (BRD2, BRD3 and BRD4) (PubMed:20871596). The first bromo domain is inhibited by GSK778 (iBET-BD1), which specifically inhibits the first bromo domain of members of the BET family (BRD2, BRD3 and BRD4) (PubMed:32193360). The second bromo domain is inhibited by ABBV-744, which specifically inhibits the second bromo domain of members of the BET family (BRD2, BRD3 and BRD4) (PubMed:31969702). The second bromo domain is inhibited by GSK046 (iBET-BD2), which specifically inhibits the second bromo domain of members of the BET family (BRD2, BRD3 and BRD4) (PubMed:32193360). {ECO:0000269|PubMed:20871596, ECO:0000269|PubMed:31969702, ECO:0000269|PubMed:32193360}.
uniprot
proteins
amino_acid_sequence
MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG
uniprot
proteins
function
FUNCTION: Chromatin reader protein that specifically recognizes and binds histone H4 acetylated at 'Lys-5' and 'Lys-12' (H4K5ac and H4K12ac, respectively), thereby controlling gene expression and remodeling chromatin structures (PubMed:17148447, PubMed:17848202, PubMed:18406326, PubMed:20048151, PubMed:20709061, PubMed:20871596). Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation (PubMed:28262505). Plays a key role in genome compartmentalization via its association with CTCF and cohesin: recruited to chromatin by CTCF and promotes formation of topologically associating domains (TADs) via its ability to bind acetylated histones, contributing to CTCF boundary formation and enhancer insulation (PubMed:35410381). Also recognizes and binds acetylated non-histone proteins, such as STAT3 (PubMed:28262505). Involved in inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17: recognizes and binds STAT3 acetylated at 'Lys-87', promoting STAT3 recruitment to chromatin (PubMed:28262505). In addition to acetylated lysines, also recognizes and binds lysine residues on histones that are both methylated and acetylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation (PubMed:37731000). Specifically binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000). {ECO:0000269|PubMed:17148447, ECO:0000269|PubMed:17848202, ECO:0000269|PubMed:18406326, ECO:0000269|PubMed:20048151, ECO:0000269|PubMed:20709061, ECO:0000269|PubMed:20871596, ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:35410381, ECO:0000269|PubMed:37731000}.
uniprot
proteins
mass_dalton
88061
uniprot
proteins
mutagenesis
MUTAGEN 78; /note="Q->A: Loss of homodimerization."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 111..112; /note="PD->AA: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 112..116; /note="DYHKI->AHYA: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 113; /note="Y->A: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 142..143; /note="MQ->AA: Loss of homodimerization."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 153; /note="Y->K: Loss of homodimerization."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 154; /note="I->A: Partial loss of homodimerization; when associated with A-182. Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:17148447, ECO:0000269|PubMed:20709061"; MUTAGEN 156..160; /note="NKPTD->AKPTA: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 156; /note="N->A: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac). Abolished binding to histone H4 acetyl-methylated."; /evidence="ECO:0000269|PubMed:20709061, ECO:0000269|PubMed:37731000"; MUTAGEN 157..160; /note="KPTD->APTA: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 158; /note="P->D: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 160; /note="D->A: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:20709061"; MUTAGEN 170; /note="E->A: Loss of homodimerization."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 174; /note="L->E: Loss of homodimerization."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 177; /note="V->E: Loss of homodimerization."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 182; /note="Q->A: Partial loss of homodimerization; when associated with A-154."; /evidence="ECO:0000269|PubMed:17148447"; MUTAGEN 376; /note="V->A: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:17848202"; MUTAGEN 381; /note="L->A: Reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:17848202"; MUTAGEN 383; /note="L->A: Reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:17848202"; MUTAGEN 429; /note="N->A: Abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)."; /evidence="ECO:0000269|PubMed:17848202
uniprot
proteins
protein_family
BET family
uniprot
proteins
pubmed
1352711
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16227282
uniprot
proteins
pubmed
17148447
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17848202
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18406326
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20048151
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20709061
uniprot
proteins
pubmed
20871596
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
28262505
uniprot
proteins
pubmed
31969702
uniprot
proteins
pubmed
32193360
uniprot
proteins
pubmed
35410381
uniprot
proteins
pubmed
37731000
uniprot
proteins
pubmed
8781126
uniprot
proteins
sequence_length
801
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18406326, ECO:0000269|PubMed:25593309}. Chromosome {ECO:0000269|PubMed:18406326, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:28262505}. Note=Detected on chromatin and nucleosomes. {ECO:0000269|PubMed:18406326}.
uniprot
proteins