BRD4B_XENLA
ID BRD4B_XENLA Reviewed; 1362 AA.
AC Q6DFF2; A8WE75;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Bromodomain-containing protein 4B;
GN Name=brd4-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O60885}.
CC Chromosome {ECO:0000250|UniProtKB:O60885}. Note=Associates with
CC acetylated chromatin. {ECO:0000250|UniProtKB:O60885}.
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; EU236153; ABW97743.1; -; mRNA.
DR EMBL; BC076786; AAH76786.1; -; mRNA.
DR RefSeq; NP_001086546.1; NM_001093077.1.
DR AlphaFoldDB; Q6DFF2; -.
DR SMR; Q6DFF2; -.
DR BioGRID; 103241; 1.
DR IntAct; Q6DFF2; 1.
DR PRIDE; Q6DFF2; -.
DR DNASU; 446381; -.
DR GeneID; 446381; -.
DR CTD; 446381; -.
DR Xenbase; XB-GENE-5859154; brd4.L.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 446381; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 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; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 2: Evidence at transcript level;
KW Bromodomain; Chromatin regulator; Chromosome; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1362
FT /note="Bromodomain-containing protein 4B"
FT /id="PRO_0000423296"
FT DOMAIN 74..146
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 385..457
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 623..707
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 22..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..521
FT /note="NPS region"
FT /evidence="ECO:0000250"
FT REGION 542..597
FT /note="BID region"
FT /evidence="ECO:0000250"
FT REGION 699..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1361
FT /note="C-terminal (CTD) region"
FT /evidence="ECO:0000250"
FT COMPBIAS 38..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..905
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1098
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 139
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000250|UniProtKB:O60885"
FT SITE 450
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000250|UniProtKB:O60885"
FT CONFLICT 209
FT /note="P -> S (in Ref. 1; ABW97743)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="S -> T (in Ref. 1; ABW97743)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="Q -> P (in Ref. 1; ABW97743)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="S -> P (in Ref. 1; ABW97743)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="P -> PQQQ (in Ref. 1; ABW97743)"
FT /evidence="ECO:0000305"
FT CONFLICT 1269
FT /note="M -> MS (in Ref. 1; ABW97743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1362 AA; 152229 MW; AC9C90A6BD625BA2 CRC64;
MSAETGLGTR LRATSVMGDG VEGAQMSGQQ QPAQPQPQTP MMQTPPPEIA RPNQPKRQTN
QLQYLLKTVL KTLWKHQFAW PFQVPVDVVK LNLPDYYKII KTPMDMGTIK KRLENHFYWN
AQECIQDFNT MFTNCYIYNK PGDDIVLMAE ALEKLFLQKI SEMPQEETEL AVVQCKGRGR
ARKEQDASIT PMRTRVLSGS LGDKSAVKPP VTPVSKPATP TPPAVIRAPT PPQTKPQQAH
PPAITQAPIS FSPIISQDVV VPTTVVPTPV PQPLANHPAV IHTAAQPAKT KKGVKRKADT
TTPTTHDPLH ESSPLPSDPK PPKAGPRKES GRQIRPIKKT EVPDSQLPAP PDLHPQPAPI
AEKDSKTSEQ LRYCAGIVRE MFSKKHQAYA WPFYKPVDVE TLGLHDYCEI IKHPMDLGTI
KVKMENCDYK NAQDFASDVR LMFSNCYKYN PPDHEVVIMA RKLQDVFEMR FAKMPDEPEE
APAPVPSPAP GPPAPSIKIP PPTSSDTSSD SSSDSESSSD SEEERAQRLA ELQEQLKAVH
EQLAALSQPQ PNKPKKKERE KRKEKHKRKE EVEETRKGRI REPPAKKPKK SVQVSGGTPS
IKKEAPPPVT RPARPAPPPA PCESSEEDTQ RCRPMSYEEK RQLSLDINKL PGEKLGRVVH
IIQSREPSLK NSNPDEIEID FETLKPSTLR ELERYVTSCL RKKRKPQDKI EAPTSGIVKV
KSYSSSESES SSESSTSDSE ESDPETAPNQ KKKGHSGRES RKHHHPMQQP LIAPPPVMKP
PSPTLAPSYP PPSSLDSSHP SLHHPLHPAN VFEAVMQLPP DLPPHLAGQT EHCSPPHLNQ
HALTSPPALH NAMPQQPSRP SNRAAALPTK PARPPSASPP LPPPQPHHQP PAHVHHHHHH
HHHAQPPHVL LEDDGPPSPH TGLPSYLQQL HKSQQPPTQS PIHSLLTTVK VQSQAPMAAP
AQSMRHHQPL VYPPPSSSAS PAPSPASSHI HQMQSPPVVP QQQPAGQAPP PPQQQQQQQQ
QQQHPALQGT LVSSHQHHVQ HQQAKQQQVI QHHHHHHPSP RQQKQETYPG GHLREAPSPL
LLHSPQVPPY PGLTHPPSPQ SVQPKKQEMR GALVLQPQPL VMKEDKRHSP SVRPEGFSPG
MRPEPPKVPE VLKGPSHIQP RPDLKPMDGG RPVRPPDQSL PPQGMPEKEK QKQEPKTPVA
PKKDLKIKNM GSWAGLMQKP PVTPTSAGKS TSDSFELFRR QAREKEERER ALKHQAEQAE
RMRREQERMR TREDDDVQDQ TRKAHEEARR RQEQQQQQQQ QHVQSNLPAA PSPAQSSQPI
MDQREMARKR EQERRRRQAM APSIDMNFQS ELMEIFEQNL FS
