BRD4_DANRE
ID BRD4_DANRE Reviewed; 1444 AA.
AC F1R5H6; A8WE74;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Bromodomain-containing protein 4;
GN Name=brd4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18498094; DOI=10.1002/dvdy.21576;
RA Toyama R., Rebbert M.L., Dey A., Ozato K., Dawid I.B.;
RT "Brd4 associates with mitotic chromosomes throughout early zebrafish
RT embryogenesis.";
RL Dev. Dyn. 237:1636-1644(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Chromatin reader protein that recognizes and binds acetylated
CC histones and plays a key role in transmission of epigenetic memory
CC across cell divisions and transcription regulation. Remains associated
CC with acetylated chromatin throughout the entire cell cycle and provides
CC epigenetic memory for postmitotic G1 gene transcription by preserving
CC acetylated chromatin status and maintaining high-order chromatin
CC structure. During interphase, plays a key role in regulating the
CC transcription of signal-inducible genes by associating with the P-TEFb
CC complex and recruiting it to promoters (By similarity).
CC {ECO:0000250|UniProtKB:O60885}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18498094}. Chromosome
CC {ECO:0000269|PubMed:18498094}. Note=Associates with acetylated
CC chromatin.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18498094}.
CC -!- DEVELOPMENTAL STAGE: Detected at all stages tested, including the
CC fertilized egg stage (at protein level). Present in the fertilized egg
CC before mid-blastula transition, and is expressed ubiquitously at
CC relatively high levels from gastrulation to mid-somitogenesis stages.
CC At the 20-somite stage, expression starts to decrease in the notochord,
CC but remains high in the head and central nervous system. This
CC expression pattern persists until approximately 24 hours post-
CC fertilization (hpf). At 48 hpf, expression is dramatically reduced in
CC the posterior part of the body, and becomes restricted to the head
CC area. {ECO:0000269|PubMed:18498094}.
CC -!- DOMAIN: The 2 bromo domains mediate specific binding to acetylated
CC histones. The exact combination of modified histone tails required to
CC recruit brd4 to target genes is still unclear. The first bromo domain
CC has high affinity for acetylated histone H4 tail, whereas the second
CC bromo domain recognizes multiply acetylated marks in histone H3 (By
CC similarity). {ECO:0000250|UniProtKB:O60885}.
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DR EMBL; EU236152; ABW97742.1; -; mRNA.
DR EMBL; AL954361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001104751.1; NM_001111281.1.
DR AlphaFoldDB; F1R5H6; -.
DR SMR; F1R5H6; -.
DR STRING; 7955.ENSDARP00000101616; -.
DR PaxDb; F1R5H6; -.
DR PRIDE; F1R5H6; -.
DR Ensembl; ENSDART00000115117; ENSDARP00000101616; ENSDARG00000078904.
DR GeneID; 570531; -.
DR KEGG; dre:570531; -.
DR CTD; 23476; -.
DR ZFIN; ZDB-GENE-030131-267; brd4.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000162790; -.
DR HOGENOM; CLU_001499_0_3_1; -.
DR InParanoid; F1R5H6; -.
DR OMA; ERMRWAR; -.
DR OrthoDB; 619848at2759; -.
DR TreeFam; TF317345; -.
DR PRO; PR:F1R5H6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000078904; Expressed in early embryo and 28 other tissues.
DR ExpressionAtlas; F1R5H6; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:ZFIN.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0002574; P:thrombocyte differentiation; IMP:ZFIN.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR031354; BRD4_CDT.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF17105; BRD4_CDT; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Chromatin regulator; Chromosome; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1444
FT /note="Bromodomain-containing protein 4"
FT /id="PRO_0000423294"
FT DOMAIN 60..132
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 378..450
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 633..730
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..517
FT /note="NPS region"
FT /evidence="ECO:0000250"
FT REGION 538..610
FT /note="BID region"
FT /evidence="ECO:0000250"
FT REGION 540..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1444
FT /note="C-terminal (CTD) region"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 125
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000250|UniProtKB:O60885"
FT SITE 443
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000250|UniProtKB:O60885"
FT CONFLICT 1001
FT /note="M -> K (in Ref. 1; ABW97742)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="N -> H (in Ref. 1; ABW97742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1444 AA; 159675 MW; 47A145D499DCCB11 CRC64;
MGDGLDAVQM SGSSSSQGQP SSQAPSSFNP NPPETSNPTR PKRQTNQLQY LLKVVLKSLW
KHQFAWPFHA PVDAVKLNLP DYYKIIKNPM DMGTIKKRLE SAFYTSAQEC IQDFNTMFTN
CYIYNKPGDD IVLMAEALEK VFLTKISEMP QQEVEISTTA GKGRGRGRRD PDMNMKVGPV
LEPLTASPQT RGLSNLTPGP QTRGPPQGPP TLPPQPIVQI QALPPRVPPS LPTIPLHAPQ
LGPPFSLGPT DCNPPAPIIT AVPPPTQTAL PPVHIQQSAA PPILQTPISI PNKRKSQKRK
ADTTTPTAND QLNESSPAES KSGKTLPRRD NTRPSKLPKK EAPDSQHHWT AAPGTPSPKQ
QEQLRYCSGI VKDMFAKKHA AYAWPFYKPV DVDTLGLHDY HDIIKHPMDL STIKDKLETR
QYREAQEFAA DVRLMFSNCY KYNPPDHEVV AMARKLQDVF EMRFAKMPDE PEEMLAPAPA
PVLHPAPVKT QPVMATASSS DTSSDSSSES ESSTDDSEEE RAQRLAELQE QLKAVHEQLA
ALSQPQASKP KKKEKEKKEK KKDKHKKKAG VMPALEEILE PPPALKPQGK PKNKDPLPKK
SKKLSKKEGG KSNRSMAPPG AAPPTLQPVP GLDTEEDLGL TGGAAMAGMA AGEKCKPMSY
EEKRQLSLDI NKLPGDKLGR VVHIIQSREP SLKNSNPDEI EIDFETLKPS TLRELERYVS
SCLRKKKKPA VPEKSMEAIS AVKTKGTSSD SGSSSESSSS ESEDSETGMA SKPKKRGRGE
GKKAHHQTTA PGMPLPQVPL QPQTPALQPS IQLKQQQPQH PSPAAYMPPP VTALEPSQLL
ENPFDPLAHF MHLPHHANDS SSPAPPHLNA HPPGGPVSPE THPFLNQHPI LPSPALHNAL
PQQPSRPSNR AAPLPPKPLQ QSTSQQQPPP QQTLVPPQQL QPQQQQPAPP QQQHLPHHPL
HAPQQMRPRP LSPPTLTPQG LLSSQPPQML LEDDEEPVPS MSLPMYLQHL QPNRLQATPT
SLMQSLQSRP QPPGQPSLLQ SVQVQSHLPP PQLPVQTQVQ PQQPAPHQPS PQLSQHQARH
MQQLGFPQGP LQTAQTQPGQ HKVSMPSTKA QQIIQQQQAT QHHSPRQHKA DSYNSAHLRD
NPSPLMMHSP QIPQYSLVHQ SPSQDKKEPQ RGPSALGGIK EEKLPPSPVM RGEPFSPAMR
PESHKHPDSK PTMPGHSQQR ADMKPLEMSR PVIRSSEQSG PPPSMQDKEK FKQEPKTPSA
PKKVQDVKFK NMGSWASLAQ KSSTTPSSGL KSSSDSFEQF RRAAREKEER EKALKAQVEQ
AEKDRLRKEQ EKLRGRDEED SIEPPRRPLE EPRRRQEPQQ VQPPPQQHQT QAQAQTLNPA
QSPSASQPTQ APPQSPASSQ SALDQQREMA RRREQERRRR EAMAATIDMN FQSDLMAIFE
ENLF
