Brd4
entrez
57261
canonical
uniprot
Q9ESU6
canonical
ensembl
ENSMUSG00000024002
resolver
ensp
ENSMUSP00000003726
resolver
ensp
ENSMUSP00000112474
resolver
ensp
ENSMUSP00000113070
resolver
ensp
ENSMUSP00000320613
resolver
ensp
ENSMUSP00000320614
resolver
ensp
ENSMUSP00000342274
resolver
ensp
ENSMUSP00000342275
resolver
ensp
ENSMUSP00000342277
resolver
ensp
ENSMUSP00000342278
resolver
ensp
ENSMUSP00000342280
resolver
enst
ENSMUST00000003726
resolver
genesymbol
Brd4
resolver
genesymbol_syn
Mcap
resolver
uniprot
B0V2V7
resolver
uniprot
B2RSE4
resolver
uniprot
F6WAL9
resolver
uniprot
Q3UH70
resolver
uniprot
Q8VHF7
resolver
uniprot
Q8VHF8
resolver
uniprot_entry
B2RSE4_MOUSE
resolver
uniprot_entry
BRD4_MOUSE
resolver
uniprot_entry
F6WAL9_MOUSE
resolver
uniprot_entry
Q3UH70_MOUSE
resolver
uniprot_sec
B0V2V7
resolver
uniprot_sec
Q8VHF7
resolver
uniprot_sec
Q8VHF8
resolver
amino_acid_sequence
MSTESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGAAKPGVSTVPNTTQASTSPQTQTPQQNPPPPVQATTHPFPAVTPDLIAQPPVMTMVPPQPLQTPSPVPPQPPPPPAPVPQPVQSHPPIIATTPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLAPEPKTAKLGPRRESSRPVKPPKKDVPDSQQHPGPEKSSKISEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLESREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVTVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKKKEEVEENKKSKTKELPPKKTKKNNSSNSNVSKKEPVPTKTKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESTSESSSSDSEDSETEMAPKSKKKGHTGRDQKKHHHHHHPQMQPAPAPVPQQPPPPPQQPPPPPPPQQQQQQPPPPPPPPSMPQQTAPAMKSSPPPFITAQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPTRPPAVSPALAQPPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQQLQPQPPPPPPPQPQPPPQQQHQPPPRPVHLPSMPFSAHIQQPPPPPGQQPTHPPPGQQPPPPQPAKPQQVIQHHPSPRHHKSDPYSAGHLREAPSPLMIHSPQMPQFQSLTHQSPPQQNVQPKKQVKGRAEPQPPGPVMGQGQGCPPASPAAVPMLSQELRPPSVVQPQPLVVVKEEKIHSPIIRSEPFSTSLRPEPPKHPENIKAPVHLPQRPEMKPVDIGRPVIRPPEQSAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEHFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQQQQRQEQQQQQQQAAAVAAASAPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF
uniprot
proteins
function
FUNCTION: Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:10938129, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:10938129). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters. Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6. BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (By similarity). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (PubMed:28262505). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidence in vivo. In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (By similarity). {ECO:0000250|UniProtKB:O60885, ECO:0000269|PubMed:10938129, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:29379197}.
uniprot
proteins
mass_dalton
155895
uniprot
proteins
mutagenesis
MUTAGEN 139; /note="Y->A: No effect on acetylated histone binding."; /evidence="ECO:0000269|PubMed:12840145"; MUTAGEN 146; /note="I->A: No effect on acetylated histone binding."; /evidence="ECO:0000269|PubMed:12840145"; MUTAGEN 431; /note="Y->C: Reduced acetylated histone binding. Reduced binding to promoters and enhancers of BRD4 target genes."; /evidence="ECO:0000269|PubMed:29379197"; MUTAGEN 433; /note="Y->A: No effect on acetylated histone binding."; /evidence="ECO:0000269|PubMed:12840145"; MUTAGEN 440; /note="V->A: No effect on acetylated histone binding."; /evidence="ECO:0000269|PubMed:12840145
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by CK2 disrupt the intramolecular binding between the bromo domain 2 and the NPS region and promotes binding between the NPS and the BID regions, leading to activate the protein and promote binding to acetylated histones. In absence of phosphorylation, BRD4 does not localize to p53/TP53 target gene promoters, phosphorylation promoting recruitment to p53/TP53 target promoters. {ECO:0000250|UniProtKB:O60885}.
uniprot
proteins
protein_family
BET family
uniprot
proteins
pubmed
10938129
uniprot
proteins
pubmed
11997514
uniprot
proteins
pubmed
12840145
uniprot
proteins
pubmed
16109376
uniprot
proteins
pubmed
17267518
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19828451
uniprot
proteins
pubmed
20715035
uniprot
proteins
pubmed
21814200
uniprot
proteins
pubmed
21964340
uniprot
proteins
pubmed
22567088
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28262505
uniprot
proteins
pubmed
29379197
uniprot
proteins
pubmed
29440723
uniprot
proteins
pubmed
31168063
uniprot
proteins
sequence_length
1400
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10938129, ECO:0000269|PubMed:12840145, ECO:0000269|PubMed:17267518, ECO:0000269|PubMed:22567088}. Chromosome {ECO:0000269|PubMed:10938129, ECO:0000269|PubMed:12840145, ECO:0000269|PubMed:17267518, ECO:0000269|PubMed:22567088}. Note=Associates with acetylated chromatin (PubMed:12840145). Released from chromatin upon deacetylation of histones that can be triggered by different signals such as activation of the JNK pathway or nocodazole treatment (PubMed:22567088). Preferentially localizes to mitotic chromosomes, while it does not localizes to meiotic chromosomes (PubMed:17267518). {ECO:0000269|PubMed:12840145, ECO:0000269|PubMed:17267518, ECO:0000269|PubMed:22567088}.
uniprot
proteins