BRD4A_XENLA
ID BRD4A_XENLA Reviewed; 1351 AA.
AC Q08D75;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Bromodomain-containing protein 4A;
GN Name=brd4-a;
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 (SEP-2006) 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}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU236154; ABW97744.1; -; mRNA.
DR EMBL; BC123908; AAI23909.1; -; mRNA.
DR RefSeq; NP_001085290.1; NM_001091821.1.
DR RefSeq; XP_018109724.1; XM_018254235.1.
DR RefSeq; XP_018109725.1; XM_018254236.1.
DR RefSeq; XP_018109726.1; XM_018254237.1.
DR AlphaFoldDB; Q08D75; -.
DR SMR; Q08D75; -.
DR DNASU; 443648; -.
DR GeneID; 443648; -.
DR KEGG; xla:443648; -.
DR CTD; 443648; -.
DR Xenbase; XB-GENE-17330650; brd4.S.
DR OMA; ERMRWAR; -.
DR OrthoDB; 619848at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 443648; 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..1351
FT /note="Bromodomain-containing protein 4A"
FT /id="PRO_0000423295"
FT DOMAIN 75..147
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 386..458
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 624..708
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..522
FT /note="NPS region"
FT /evidence="ECO:0000250"
FT REGION 543..598
FT /note="BID region"
FT /evidence="ECO:0000250"
FT REGION 700..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1350
FT /note="C-terminal (CTD) region"
FT /evidence="ECO:0000250"
FT COMPBIAS 214..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 140
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000250|UniProtKB:O60885"
FT SITE 451
FT /note="Acetylated histone binding"
FT /evidence="ECO:0000250|UniProtKB:O60885"
SQ SEQUENCE 1351 AA; 150927 MW; 1F3986A2AF815F74 CRC64;
MSSETGLGTR LRATSGMGDG IEGAQMLGQH QPALPQPQAT VMNNPDPPEI TRPNQPKRQT
NQLQYLLKAV LKTLWKHQFA WPFQLPVDVV KLNLPDYHKI IKTPMDMGTI KKRLENHYYW
NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK ISEMPQEETE LTVVQSKGRG
RGRKEQDASI TPMRTRVLSG SLEDKSTVKP PVTPVSKPST PTPPTVTRAP TPPQTRPQQG
RPPAIAQAPI RFSPTISQDV VVPTTVAPTL VPPPLSNHPA VIHTAAQPAK TKKGVKRKAD
TTTPTTHDPL HESSPLPSDP KPPRAVPRKE NGRQIRPTKK TEVPDSQLPA PPVLHPQPAP
NAERDTKTSE QLRYCASIIR EMFSKKHQAY AWPFYKPVDV EALGLHDYCE IIKHPMDLGT
IKVKMENRDY KEAQEFASDV RLMFSNCYKY NPPDHEVVIM ARKLQDVFEM RFAKMPDEPE
EAPAPVPSLA PGPPAPSIKG PPPTSSDSSS DSTSDSESSS DSEEERAQRL AELQEQLKAV
HEQLAALSQP QPNKPKKKER EKRKEKHKRK EEVEEPRKGR IREPPAKKPK KSVQGSGGTP
SIKKEAPPPA PRPARPAPPS APCESSEEET QRCRPMSYEE KRQLSLDINK LPGEKLGRVV
HIIQSREPSL KNSNPDEIEI DFETLKPSTL RELERYVTSC LRKKRKSQDK IEAPTSGTVK
VKGYSSSESE SSSESSTSDS EESDSETAPN QKKKGHSGRE SRKHHHPMQQ PLAAQLPVMK
PPSPTIAPSY PLPSSLDSSH ISLHHPLHPA NVFDAVMQLP PDLPPHLTGQ TEHCSPPHLN
QHALTSPPAL HNAMPQQPSR PSNRAAALPT KPAMPPSASP PPPAPQPPQQ PHVHHHHHHH
AQPPHVLLED DEPPSPLTGL PPYLQPLQKS QQPPTQSPIH SLLTSVKVQS QTPMAAPPQS
MRHLQPLVYP PPPSTATTAP PPASSHIHQL QSSPVVPQQL PAGQAPPPPQ QQQQHPALQG
TLVSSHQQHV QHQHAKQQQV IQHHHHHPSP RQQKQETYPG GHLRDAPSPL LLHSPPVPPY
PGLTHPPSPQ SVQPKKQEIR GASVLQPQPV VMKEDKRHSP SIRPEGFSPG MRPEPQKVPE
VLKGPSHIQP RPDLKKMDGG RPIRLPDQSL PPQGMPEKEK QKQEPKTPVA PKKDIKIKNM
GSWAGLMQKP PVTPTSAGKS TSDSFELFRR QAREKEERER ALKLQAEQAE RVRREQDRMS
RTREDDEVQD QARKAHEEAR RRQEQQQQQQ HVQSNLPTAP SPAQSSQPMM DQREMARKRE
QERRRRQAMA PSIDMNFQSE LMEIFEQNLF S
