ID   BRD9_XENLA              Reviewed;         527 AA.
AC   Q6GLP7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Bromodomain-containing protein 9;
GN   Name=brd9;
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 [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in chromatin remodeling and regulation of
CC       transcription. Acts as a chromatin reader that recognizes and binds
CC       acylated histones: binds histones that are acetylated and/or
CC       butyrylated. {ECO:0000250|UniProtKB:Q9H8M2}.
CC   -!- SUBUNIT: Binds acetylated histones H3 and H4. Binds butyrylated histone
CC       H4. {ECO:0000250|UniProtKB:Q9H8M2}.
CC   -!- DOMAIN: The Bromo domain mediates interaction with histones that have
CC       acetylated lysine residues at specific positions. Also recognizes and
CC       binds histones that are butyrylated. {ECO:0000250|UniProtKB:Q9H8M2}.
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DR   EMBL; BC074412; AAH74412.1; -; mRNA.
DR   RefSeq; NP_001086274.1; NM_001092805.1.
DR   AlphaFoldDB; Q6GLP7; -.
DR   SMR; Q6GLP7; -.
DR   PRIDE; Q6GLP7; -.
DR   DNASU; 444703; -.
DR   GeneID; 444703; -.
DR   KEGG; xla:444703; -.
DR   CTD; 444703; -.
DR   Xenbase; XB-GENE-969476; brd9.L.
DR   OrthoDB; 439339at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 444703; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.920.10; -; 1.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR021900; DUF3512.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF12024; DUF3512; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   Bromodomain; Chromatin regulator; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..527
FT                   /note="Bromodomain-containing protein 9"
FT                   /id="PRO_0000239222"
FT   DOMAIN          95..165
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..158
FT                   /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT                   binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT   REGION          468..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            111
FT                   /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT                   binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT   SITE            164
FT                   /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT                   binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8M2"
SQ   SEQUENCE   527 AA;  60268 MW;  FBB8F72DFC2F0EBD CRC64;
     MNVSVTKRRK KKKKKKSEKE KDKYLDEDER RRRKEEKKRK REKEQCDSEG ETEVFESIRK
     DIEATDRPVR TCRTHPENES TPLQQLLEYF LRQLQRKDPN GFFAFPVTDQ IAPGYFMIIK
     NPMDFSTMKE KISQDEYKSV TEFKADFKLM CDNAMTYNRP ETVYYKLAKK LLHTGFKMMS
     KAALLGNEVT TTEEPIPEII MPTAAEVVKK SKKPSKDMFR VMEEDQSSIF EPEGNACSLT
     DSTAEEHVLA LVEHAADEAR DKLNQYFPNC RIGYLKKNTD GTLFYTVVNG DPDNEEDTHL
     VDLSSLSSKL LPSFTTLGFK EDRRHKVTFL NSTGTALSLQ NNTLFTNLKP DQIELMYAGY
     GDDTGIQCAL SLQEFVKDSG SFAKRMVNDL LDQITGGDHS RTIYQIKQMT GSEREGCSNS
     VLDFMTLKSY SDVSLDMSML SSLDKVKKEL EHEDSHLNLD DASKLLPDFH DVHNDRGGSR
     PSSSSSMSNN SERDHHLGSP SRISVGEQQD IHDPYEFLQS PETDNQN