Details for: BRD4
Associated with
Other Information
Genular Protein ID: 2301593749
Symbol: BRD4_HUMAN
Name: Bromodomain-containing protein 4
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11733348
Title: BRD4 bromodomain gene rearrangement in aggressive carcinoma with translocation t(15;19).
PubMed ID: 11733348
PubMed ID: 15057824
Title: The DNA sequence and biology of human chromosome 19.
PubMed ID: 15057824
DOI: 10.1038/nature02399
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 12543779
Title: BRD4-NUT fusion oncogene: a novel mechanism in aggressive carcinoma.
PubMed ID: 12543779
PubMed ID: 16109376
Title: The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription.
PubMed ID: 16109376
PubMed ID: 16109377
Title: Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4.
PubMed ID: 16109377
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16940503
Title: Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen interacts with bromodomain protein Brd4 on host mitotic chromosomes.
PubMed ID: 16940503
DOI: 10.1128/jvi.00502-06
PubMed ID: 17189189
Title: ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes and viral genome maintenance.
PubMed ID: 17189189
PubMed ID: 18922874
Title: The EBNA1 protein of Epstein-Barr virus functionally interacts with Brd4.
PubMed ID: 18922874
DOI: 10.1128/jvi.01680-08
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19596240
Title: Control of inducible gene expression by signal-dependent transcriptional elongation.
PubMed ID: 19596240
PubMed ID: 19103749
Title: Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA.
PubMed ID: 19103749
DOI: 10.1128/mcb.01365-08
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21555454
Title: The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3.
PubMed ID: 21555454
DOI: 10.1128/mcb.01341-10
PubMed ID: 21890894
Title: Signal-induced Brd4 release from chromatin is essential for its role transition from chromatin targeting to transcriptional regulation.
PubMed ID: 21890894
DOI: 10.1093/nar/gkr698
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22334664
Title: Bromodomain protein Brd4 associated with acetylated chromatin is important for maintenance of higher-order chromatin structure.
PubMed ID: 22334664
PubMed ID: 23086925
Title: Bromodomain-containing protein 4 (BRD4) regulates RNA polymerase II serine 2 phosphorylation in human CD4+ T cells.
PubMed ID: 23086925
PubMed ID: 22509028
Title: BRD4 is an atypical kinase that phosphorylates serine2 of the RNA polymerase II carboxy-terminal domain.
PubMed ID: 22509028
PubMed ID: 24360279
Title: Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release.
PubMed ID: 24360279
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23317504
Title: Phospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targeting.
PubMed ID: 23317504
PubMed ID: 23589332
Title: BRD4 coordinates recruitment of pause release factor P-TEFb and the pausing complex NELF/DSIF to regulate transcription elongation of interferon-stimulated genes.
PubMed ID: 23589332
DOI: 10.1128/mcb.01180-12
PubMed ID: 23728299
Title: The bromodomain protein Brd4 insulates chromatin from DNA damage signalling.
PubMed ID: 23728299
DOI: 10.1038/nature12147
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25593309
Title: Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination.
PubMed ID: 25593309
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 29374058
Title: Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.
PubMed ID: 29374058
PubMed ID: 17344846
Title: Patterns of somatic mutation in human cancer genomes.
PubMed ID: 17344846
DOI: 10.1038/nature05610
PubMed ID: 18500820
Title: Structural basis and binding properties of the second bromodomain of Brd4 with acetylated histone tails.
PubMed ID: 18500820
DOI: 10.1021/bi8001659
PubMed ID: 20871596
PubMed ID: 21068722
Title: Suppression of inflammation by a synthetic histone mimic.
PubMed ID: 21068722
DOI: 10.1038/nature09589
PubMed ID: 21568322
Title: Discovery and characterization of small molecule inhibitors of the BET family bromodomains.
PubMed ID: 21568322
DOI: 10.1021/jm200108t
PubMed ID: 21964340
Title: Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia.
PubMed ID: 21964340
DOI: 10.1038/nature10509
PubMed ID: 22137933
Title: Benzodiazepines and benzotriazepines as protein interaction inhibitors targeting bromodomains of the BET family.
PubMed ID: 22137933
PubMed ID: 22645123
Title: Down-regulation of NF-kappaB transcriptional activity in HIV-associated kidney disease by BRD4 inhibition.
PubMed ID: 22645123
PubMed ID: 22136404
Title: Fragment-based discovery of bromodomain inhibitors part 1: inhibitor binding modes and implications for lead discovery.
PubMed ID: 22136404
DOI: 10.1021/jm201320w
PubMed ID: 23095041
Title: Identification of a chemical probe for bromo and extra C-terminal bromodomain inhibition through optimization of a fragment-derived hit.
PubMed ID: 23095041
DOI: 10.1021/jm3010515
PubMed ID: 22464331
Title: Histone recognition and large-scale structural analysis of the human bromodomain family.
PubMed ID: 22464331
PubMed ID: 23517011
Title: Optimization of 3,5-dimethylisoxazole derivatives as potent bromodomain ligands.
PubMed ID: 23517011
DOI: 10.1021/jm301588r
PubMed ID: 23530754
Title: Fragment-based drug discovery of 2-thiazolidinones as inhibitors of the histone reader BRD4 bromodomain.
PubMed ID: 23530754
DOI: 10.1021/jm301793a
PubMed ID: 29176719
Title: Structural Mechanism of the Oxygenase JMJD6 Recognition by the Extraterminal (ET) Domain of BRD4.
PubMed ID: 29176719
Sequence Information:
- Length: 1362
- Mass: 152219
- Checksum: D52EFE1CF9960907
- Sequence:
MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET SNPNKPKRQT NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI IKTPMDMGTI KKRLENNYYW NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK INELPTEETE IMIVQAKGRG RGRKETGTAK PGVSTVPNTT QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT VVPPQPLQTP PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV SEQLKCCSGI LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM STIKSKLEAR EYRDAQEFGA DVRLMFSNCY KYNPPDHEVV AMARKLQDVF EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV APPSSSDSSS DSSSDSDSST DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE KDKKEKKKEK HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD EIEIDFETLK PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS SESESSSESS SSDSEDSETE MAPKSKKKGH PGREQKKHHH HHHQQMQQAP APVPQQPPPP PQQPPPPPPP QQQQQPPPPP PPPSMPQQAA PAMKSSPPPF IATQVPVLEP QLPGSVFDPI GHFTQPILHL PQPELPPHLP QPPEHSTPPH LNQHAVVSPP ALHNALPQQP SRPSNRAAAL PPKPARPPAV SPALTQTPLL PQPPMAQPPQ VLLEDEEPPA PPLTSMQMQL YLQQLQKVQP PTPLLPSVKV QSQPPPPLPP PPHPSVQQQL QQQPPPPPPP QPQPPPQQQH QPPPRPVHLQ PMQFSTHIQQ PPPPQGQQPP HPPPGQQPPP PQPAKPQQVI QHHHSPRHHK SDPYSTGHLR EAPSPLMIHS PQMSQFQSLT HQSPPQQNVQ PKKQELRAAS VVQPQPLVVV KEEKIHSPII RSEPFSPSLR PEPPKHPESI KAPVHLPQRP EMKPVDVGRP VIRPPEQNAP PPGAPDKDKQ KQEPKTPVAP KKDLKIKNMG SWASLVQKHP TTPSSTAKSS SDSFEQFRRA AREKEEREKA LKAQAEHAEK EKERLRQERM RSREDEDALE QARRAHEEAR RRQEQQQQQR QEQQQQQQQQ AAAVAAAATP QAQSSQPQSM LDQQRELARK REQERRRREA MAATIDMNFQ SDLLSIFEEN LF
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.