Brd2
entrez
14312
canonical
uniprot
Q7JJ13
canonical
ensembl
ENSMUSG00000024335
resolver
ensp
ENSMUSP00000025193
resolver
ensp
ENSMUSP00000092990
resolver
ensp
ENSMUSP00000109880
resolver
ensp
ENSMUSP00000267553
resolver
ensp
ENSMUSP00000329019
resolver
genesymbol
Brd2
resolver
genesymbol_syn
Fsrg1
resolver
genesymbol_syn
Kiaa4005
resolver
genesymbol_syn
Ring3
resolver
uniprot
B2RS09
resolver
uniprot
O54795
resolver
uniprot
O88411
resolver
uniprot
Q3UGI0
resolver
uniprot
Q5DTS6
resolver
uniprot
Q794H7
resolver
uniprot
Q794H9
resolver
uniprot
Q99PC5
resolver
uniprot_entry
B2RS09_MOUSE
resolver
uniprot_entry
BRD2_MOUSE
resolver
uniprot_sec
O54795
resolver
uniprot_sec
O88411
resolver
uniprot_sec
Q3UGI0
resolver
uniprot_sec
Q5DTS6
resolver
uniprot_sec
Q794H7
resolver
uniprot_sec
Q794H9
resolver
uniprot_sec
Q99PC5
resolver
amino_acid_sequence
MLQNVTPHKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLAPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSITSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVSAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTALPPGLTKSSSESSSEESSSESSSEEEEEEEEDEDEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRIGIDEDDKGPRAPRPPQPKKSKKAGGGGSNATTLSHPGFGTSGGSSNKLPKKSQKTAPPVLPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIRKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKASEKTESSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG
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:14731392). Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation (By similarity). 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:28388437). 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 (By similarity). Specifically binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (By similarity). {ECO:0000250|UniProtKB:P25440, ECO:0000269|PubMed:14731392, ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:28388437}.
uniprot
proteins
mass_dalton
88067
uniprot
proteins
mutagenesis
MUTAGEN 102; /note="V->A: In BD1-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-112, A-154 and A-161. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-112, A-154, A-161, A-375, A-385, A-427 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 112; /note="Y->A: In BD1-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-154 and A-161. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-154, A-161, A-375, A-385, A-427 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 154; /note="Y->A: In BD1-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112 and A-161. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112, A-161, A-375, A-385, A-427 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 154; /note="Y->F: Abolished interaction with acetylated STAT3."; /evidence="ECO:0000269|PubMed:28262505"; MUTAGEN 161; /note="I->A: In BD1-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112 and A-154. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112, A-161, A-375, A-385, A-427 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 375; /note="V->A: In BD2-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-385, A-427 and A-434. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112, A-154, A-161, A-385, A-427 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 385; /note="Y->A: In BD2-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-375, A-427 and A-434. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112, A-154, A-161, A-375, A-427 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 427; /note="Y->A: In BD2-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-375, A-385 and A-434. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112, A-154, A-161, A-375, A-385 and A-434."; /evidence="ECO:0000269|PubMed:14731392"; MUTAGEN 427; /note="Y->F: Abolished interaction with acetylated STAT3."; /evidence="ECO:0000269|PubMed:28262505"; MUTAGEN 434; /note="V->A: In BD2-m4 mutant; reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-375, A-385 and A-427. In m8 mutant; abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac); when associated with A-102, A-112, A-154, A-161, A-375, A-385, and A-427434."; /evidence="ECO:0000269|PubMed:14731392
uniprot
proteins
protein_family
BET family
uniprot
proteins
pubmed
14731392
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19301389
uniprot
proteins
pubmed
19883376
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
28262505
uniprot
proteins
pubmed
28388437
uniprot
proteins
pubmed
9601950
uniprot
proteins
pubmed
9693039
uniprot
proteins
pubmed
9811568
uniprot
proteins
sequence_length
798
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}. Chromosome {ECO:0000269|PubMed:28388437}. Note=Detected on chromatin and nucleosomes. {ECO:0000269|PubMed:28388437}.
uniprot
proteins