BRD9_HUMAN
ID BRD9_HUMAN Reviewed; 597 AA.
AC Q9H8M2; A6NFY8; B4DMQ2; B4DR93; Q2XUS1; Q6UWU9; Q8IUS4; Q9H5Q5; Q9H7R9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Bromodomain-containing protein 9;
DE AltName: Full=Rhabdomyosarcoma antigen MU-RMS-40.8;
GN Name=BRD9; ORFNames=UNQ3040/PRO9856;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 235-597 (ISOFORM 3).
RC TISSUE=Brain, Lung, Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 171-597 (ISOFORM 3).
RC TISSUE=Embryonic carcinoma;
RA Behrends U., Gotz C., Mautner J.;
RT "Serological identification of rhabdomyosarcoma antigens.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-373, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-373, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
RN [15]
RP FUNCTION, AND INTERACTION WITH RAD51 AND RAD54.
RX PubMed=32457312; DOI=10.1038/s41467-020-16443-x;
RA Zhou Q., Huang J., Zhang C., Zhao F., Kim W., Tu X., Zhang Y., Nowsheen S.,
RA Zhu Q., Deng M., Chen Y., Qin B., Luo K., Liu B., Lou Z., Mutter R.W.,
RA Yuan J.;
RT "The bromodomain containing protein BRD-9 orchestrates RAD51-RAD54 complex
RT formation and regulates homologous recombination-mediated repair.";
RL Nat. Commun. 11:2639-2639(2020).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 134-239, SUBUNIT, DOMAIN, AND
RP FUNCTION.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
RN [17] {ECO:0007744|PDB:4YY4, ECO:0007744|PDB:4YY6, ECO:0007744|PDB:4YYD, ECO:0007744|PDB:4YYG, ECO:0007744|PDB:4YYH, ECO:0007744|PDB:4YYI, ECO:0007744|PDB:4YYJ, ECO:0007744|PDB:4YYK}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 134-239 IN COMPLEX WITH
RP ACETYLATED OR BUTYRYLATED HISTONE H4, SUBUNIT, DOMAIN, AND FUNCTION.
RX PubMed=26365797; DOI=10.1016/j.str.2015.08.004;
RA Flynn E.M., Huang O.W., Poy F., Oppikofer M., Bellon S.F., Tang Y.,
RA Cochran A.G.;
RT "A subset of human bromodomains recognizes butyryllysine and crotonyllysine
RT histone peptide modifications.";
RL Structure 23:1801-1814(2015).
CC -!- FUNCTION: Plays a role in chromatin remodeling and regulation of
CC transcription (PubMed:22464331, PubMed:26365797). Acts as a chromatin
CC reader that recognizes and binds acylated histones: binds histones that
CC are acetylated and/or butyrylated (PubMed:26365797). Component of
CC SWI/SNF chromatin remodeling subcomplex GBAF that carries out key
CC enzymatic activities, changing chromatin structure by altering DNA-
CC histone contacts within a nucleosome in an ATP-dependent manner
CC (PubMed:29374058). Orchestrates also the RAD51-RAD54 complex formation
CC and thereby plays a role in homologous recombination (HR)
CC (PubMed:32457312). {ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797, ECO:0000269|PubMed:29374058,
CC ECO:0000269|PubMed:32457312}.
CC -!- SUBUNIT: Binds acetylated histones H3 and H4 (PubMed:22464331,
CC PubMed:26365797). Binds butyrylated histone H4 (PubMed:26365797).
CC Component of the multiprotein chromatin-remodeling subcomplex SWI/SNF
CC called GBAF, which includes at least BICRA or BICRAL (mutually
CC exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A
CC (PubMed:29374058). Interacts (via N-terminal bromodomain) with
CC acteylated RAD54 (PubMed:32457312). Interacts (via C-terminus) with
CC RAD51 (PubMed:32457312). {ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797, ECO:0000269|PubMed:29374058,
CC ECO:0000269|PubMed:32457312}.
CC -!- INTERACTION:
CC Q9H8M2; Q7Z7H3: CATIP; NbExp=3; IntAct=EBI-10258305, EBI-10258233;
CC Q9H8M2-3; Q7Z7H3: CATIP; NbExp=3; IntAct=EBI-12834120, EBI-10258233;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9H8M2-5; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8M2-2; Sequence=VSP_019112;
CC Name=3;
CC IsoId=Q9H8M2-3; Sequence=VSP_037493, VSP_037494;
CC Name=4;
CC IsoId=Q9H8M2-4; Sequence=VSP_037493, VSP_037494, VSP_019114,
CC VSP_019115;
CC Name=5;
CC IsoId=Q9H8M2-1; Sequence=VSP_037493, VSP_037494, VSP_019113;
CC Name=6;
CC IsoId=Q9H8M2-6; Sequence=VSP_037493, VSP_043234;
CC -!- DOMAIN: The Bromo domain mediates interaction with histones that have
CC acetylated lysine residues at specific positions (PubMed:22464331).
CC Also recognizes and binds histones that are butyrylated
CC (PubMed:26365797). {ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15565.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY358630; AAQ88993.1; -; mRNA.
DR EMBL; AK023503; BAB14591.1; -; mRNA.
DR EMBL; AK024392; BAB14907.1; -; mRNA.
DR EMBL; AK026830; BAB15565.1; ALT_INIT; mRNA.
DR EMBL; AK297573; BAG59964.1; -; mRNA.
DR EMBL; AK299157; BAG61205.1; -; mRNA.
DR EMBL; AC122719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471102; EAX08192.1; -; Genomic_DNA.
DR EMBL; BC041590; AAH41590.1; -; mRNA.
DR EMBL; DQ248311; ABB55266.1; -; mRNA.
DR CCDS; CCDS34127.2; -. [Q9H8M2-5]
DR CCDS; CCDS34128.2; -. [Q9H8M2-6]
DR RefSeq; NP_001009877.2; NM_001009877.2. [Q9H8M2-6]
DR RefSeq; NP_001304880.1; NM_001317951.1. [Q9H8M2-1]
DR RefSeq; NP_076413.3; NM_023924.4. [Q9H8M2-5]
DR PDB; 3HME; X-ray; 2.23 A; A/B=134-239.
DR PDB; 4NQN; X-ray; 1.73 A; A=134-239.
DR PDB; 4UIT; X-ray; 1.30 A; A=134-238.
DR PDB; 4UIU; X-ray; 1.64 A; A=134-238.
DR PDB; 4UIV; X-ray; 1.72 A; A=134-238.
DR PDB; 4UIW; X-ray; 1.73 A; A=134-238.
DR PDB; 4XY8; X-ray; 1.70 A; A=134-239.
DR PDB; 4YY4; X-ray; 1.47 A; A=134-239.
DR PDB; 4YY6; X-ray; 1.45 A; A=134-239.
DR PDB; 4YYD; X-ray; 1.52 A; A=134-239.
DR PDB; 4YYG; X-ray; 2.10 A; A=134-239.
DR PDB; 4YYH; X-ray; 1.74 A; A/B=134-239.
DR PDB; 4YYI; X-ray; 1.50 A; A/B/D/E=134-239.
DR PDB; 4YYJ; X-ray; 1.85 A; A/B/D/E=134-239.
DR PDB; 4YYK; X-ray; 1.79 A; A/B/D/E=134-239.
DR PDB; 4Z6H; X-ray; 1.80 A; A/B=134-239.
DR PDB; 4Z6I; X-ray; 1.95 A; A/B=134-239.
DR PDB; 5E9V; X-ray; 1.80 A; A/B=134-239.
DR PDB; 5EU1; X-ray; 1.60 A; A/B=134-239.
DR PDB; 5F1H; X-ray; 1.82 A; A/B=134-239.
DR PDB; 5F1L; X-ray; 2.30 A; A/B=134-239.
DR PDB; 5F25; X-ray; 1.68 A; A/B=134-239.
DR PDB; 5F2P; X-ray; 1.80 A; A/B=134-239.
DR PDB; 5I40; X-ray; 1.04 A; A=138-239.
DR PDB; 5I7X; X-ray; 1.18 A; A=138-238.
DR PDB; 5I7Y; X-ray; 1.45 A; A=138-238.
DR PDB; 5IGM; X-ray; 1.60 A; A/B=134-239.
DR PDB; 5IGN; X-ray; 1.70 A; A/B=134-239.
DR PDB; 5JI8; X-ray; 1.42 A; A=137-239.
DR PDB; 5MKY; X-ray; 1.67 A; A=134-238.
DR PDB; 5TWX; X-ray; 2.55 A; A/B/C/D=134-250.
DR PDB; 6BQA; X-ray; 1.03 A; A=138-239.
DR PDB; 6HM0; X-ray; 2.40 A; A/B=134-243.
DR PDB; 6UZF; X-ray; 1.75 A; A=134-243.
DR PDB; 6V0S; X-ray; 2.40 A; A/B=134-243.
DR PDB; 6V0X; X-ray; 1.50 A; A=134-243.
DR PDB; 6V14; X-ray; 1.70 A; A=134-243.
DR PDB; 6V1B; X-ray; 1.35 A; A/B=134-243.
DR PDB; 6Y7H; X-ray; 1.80 A; A/B=134-243.
DR PDB; 6Y7I; X-ray; 1.60 A; A/B=134-243.
DR PDB; 6Y7J; X-ray; 1.60 A; A/B=134-243.
DR PDB; 6Y7K; X-ray; 1.20 A; A=134-243.
DR PDB; 6Y7L; X-ray; 1.80 A; A=134-243.
DR PDB; 6YQR; X-ray; 1.68 A; AAA=134-238.
DR PDB; 6YQS; X-ray; 1.68 A; AAA=134-238.
DR PDB; 6YQW; X-ray; 1.50 A; A=134-238.
DR PDBsum; 3HME; -.
DR PDBsum; 4NQN; -.
DR PDBsum; 4UIT; -.
DR PDBsum; 4UIU; -.
DR PDBsum; 4UIV; -.
DR PDBsum; 4UIW; -.
DR PDBsum; 4XY8; -.
DR PDBsum; 4YY4; -.
DR PDBsum; 4YY6; -.
DR PDBsum; 4YYD; -.
DR PDBsum; 4YYG; -.
DR PDBsum; 4YYH; -.
DR PDBsum; 4YYI; -.
DR PDBsum; 4YYJ; -.
DR PDBsum; 4YYK; -.
DR PDBsum; 4Z6H; -.
DR PDBsum; 4Z6I; -.
DR PDBsum; 5E9V; -.
DR PDBsum; 5EU1; -.
DR PDBsum; 5F1H; -.
DR PDBsum; 5F1L; -.
DR PDBsum; 5F25; -.
DR PDBsum; 5F2P; -.
DR PDBsum; 5I40; -.
DR PDBsum; 5I7X; -.
DR PDBsum; 5I7Y; -.
DR PDBsum; 5IGM; -.
DR PDBsum; 5IGN; -.
DR PDBsum; 5JI8; -.
DR PDBsum; 5MKY; -.
DR PDBsum; 5TWX; -.
DR PDBsum; 6BQA; -.
DR PDBsum; 6HM0; -.
DR PDBsum; 6UZF; -.
DR PDBsum; 6V0S; -.
DR PDBsum; 6V0X; -.
DR PDBsum; 6V14; -.
DR PDBsum; 6V1B; -.
DR PDBsum; 6Y7H; -.
DR PDBsum; 6Y7I; -.
DR PDBsum; 6Y7J; -.
DR PDBsum; 6Y7K; -.
DR PDBsum; 6Y7L; -.
DR PDBsum; 6YQR; -.
DR PDBsum; 6YQS; -.
DR PDBsum; 6YQW; -.
DR AlphaFoldDB; Q9H8M2; -.
DR SMR; Q9H8M2; -.
DR BioGRID; 122430; 112.
DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR IntAct; Q9H8M2; 13.
DR MINT; Q9H8M2; -.
DR STRING; 9606.ENSP00000419765; -.
DR BindingDB; Q9H8M2; -.
DR ChEMBL; CHEMBL3108640; -.
DR GuidetoPHARMACOLOGY; 2728; -.
DR iPTMnet; Q9H8M2; -.
DR PhosphoSitePlus; Q9H8M2; -.
DR BioMuta; BRD9; -.
DR DMDM; 239938605; -.
DR EPD; Q9H8M2; -.
DR jPOST; Q9H8M2; -.
DR MassIVE; Q9H8M2; -.
DR MaxQB; Q9H8M2; -.
DR PaxDb; Q9H8M2; -.
DR PeptideAtlas; Q9H8M2; -.
DR PRIDE; Q9H8M2; -.
DR ProteomicsDB; 81218; -. [Q9H8M2-5]
DR ProteomicsDB; 81219; -. [Q9H8M2-1]
DR ProteomicsDB; 81220; -. [Q9H8M2-2]
DR ProteomicsDB; 81221; -. [Q9H8M2-3]
DR ProteomicsDB; 81222; -. [Q9H8M2-4]
DR ProteomicsDB; 81223; -. [Q9H8M2-6]
DR TopDownProteomics; Q9H8M2-1; -. [Q9H8M2-1]
DR TopDownProteomics; Q9H8M2-4; -. [Q9H8M2-4]
DR Antibodypedia; 8843; 163 antibodies from 26 providers.
DR DNASU; 65980; -.
DR Ensembl; ENST00000467963.6; ENSP00000419765.1; ENSG00000028310.18. [Q9H8M2-5]
DR Ensembl; ENST00000483173.5; ENSP00000419845.1; ENSG00000028310.18. [Q9H8M2-6]
DR GeneID; 65980; -.
DR KEGG; hsa:65980; -.
DR MANE-Select; ENST00000467963.6; ENSP00000419765.1; NM_023924.5; NP_076413.3.
DR UCSC; uc003jbq.4; human. [Q9H8M2-5]
DR CTD; 65980; -.
DR DisGeNET; 65980; -.
DR GeneCards; BRD9; -.
DR HGNC; HGNC:25818; BRD9.
DR HPA; ENSG00000028310; Low tissue specificity.
DR MIM; 618465; gene.
DR neXtProt; NX_Q9H8M2; -.
DR OpenTargets; ENSG00000028310; -.
DR PharmGKB; PA134866578; -.
DR VEuPathDB; HostDB:ENSG00000028310; -.
DR eggNOG; KOG1828; Eukaryota.
DR GeneTree; ENSGT00950000183170; -.
DR HOGENOM; CLU_020704_2_0_1; -.
DR InParanoid; Q9H8M2; -.
DR OMA; ICDMQMS; -.
DR OrthoDB; 439339at2759; -.
DR PhylomeDB; Q9H8M2; -.
DR TreeFam; TF106439; -.
DR PathwayCommons; Q9H8M2; -.
DR SignaLink; Q9H8M2; -.
DR BioGRID-ORCS; 65980; 52 hits in 1098 CRISPR screens.
DR ChiTaRS; BRD9; human.
DR EvolutionaryTrace; Q9H8M2; -.
DR GenomeRNAi; 65980; -.
DR Pharos; Q9H8M2; Tchem.
DR PRO; PR:Q9H8M2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H8M2; protein.
DR Bgee; ENSG00000028310; Expressed in sural nerve and 196 other tissues.
DR ExpressionAtlas; Q9H8M2; baseline and differential.
DR Genevisible; Q9H8M2; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; NAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
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; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..597
FT /note="Bromodomain-containing protein 9"
FT /id="PRO_0000239219"
FT DOMAIN 153..223
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..216
FT /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT binding"
FT /evidence="ECO:0000269|PubMed:26365797"
FT REGION 536..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 169
FT /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT binding"
FT /evidence="ECO:0000269|PubMed:26365797"
FT SITE 222
FT /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT binding"
FT /evidence="ECO:0000269|PubMed:26365797"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQU0"
FT MOD_RES 373
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..391
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_019112"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_037493"
FT VAR_SEQ 117..155
FT /note="EVEPPPDRPVRACRTQPAENESTPIQQLLEHFLRQLQRK -> MMTGQTMSE
FT RGTKKRKRRRRRSPRRRSIWTMRKEGSERKRRSGSERGSTVTRRERLTTLILGRRWRWS
FT RPQIGQSERAGHSQPKMRAHLFSNSWNTSSASFR (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043234"
FT VAR_SEQ 117..133
FT /note="EVEPPPDRPVRACRTQP -> MKGYQSLVFNFFFLKLS (in isoform
FT 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_037494"
FT VAR_SEQ 239
FT /note="K -> KERLLALKRSMSFMQDMDFSQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019113"
FT VAR_SEQ 323..349
FT /note="MGYLKRNGDGSLLYSVVNTAEPDADEE -> VVLCGHRERVPRGPRLSVCLS
FT FWVGAV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019114"
FT VAR_SEQ 350..597
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019115"
FT VARIANT 170
FT /note="A -> T (in dbSNP:rs34292369)"
FT /id="VAR_059143"
FT VARIANT 266
FT /note="A -> T (in dbSNP:rs34292369)"
FT /id="VAR_033635"
FT VARIANT 389
FT /note="A -> T (in dbSNP:rs414349)"
FT /id="VAR_033636"
FT CONFLICT 146
FT /note="E -> D (in Ref. 2; BAB14907)"
FT /evidence="ECO:0000305"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:6BQA"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4YYK"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6BQA"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6BQA"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:6BQA"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:6BQA"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6V0X"
FT HELIX 221..238
FT /evidence="ECO:0007829|PDB:6BQA"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:6Y7K"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:5TWX"
SQ SEQUENCE 597 AA; 67000 MW; 3B248FA97948266E CRC64;
MGKKHKKHKA EWRSSYEDYA DKPLEKPLKL VLKVGGSEVT ELSGSGHDSS YYDDRSDHER
ERHKEKKKKK KKKSEKEKHL DDEERRKRKE EKKRKREREH CDTEGEADDF DPGKKVEVEP
PPDRPVRACR TQPAENESTP IQQLLEHFLR QLQRKDPHGF FAFPVTDAIA PGYSMIIKHP
MDFGTMKDKI VANEYKSVTE FKADFKLMCD NAMTYNRPDT VYYKLAKKIL HAGFKMMSKQ
AALLGNEDTA VEEPVPEVVP VQVETAKKSK KPSREVISCM FEPEGNACSL TDSTAEEHVL
ALVEHAADEA RDRINRFLPG GKMGYLKRNG DGSLLYSVVN TAEPDADEEE THPVDLSSLS
SKLLPGFTTL GFKDERRNKV TFLSSATTAL SMQNNSVFGD LKSDEMELLY SAYGDETGVQ
CALSLQEFVK DAGSYSKKVV DDLLDQITGG DHSRTLFQLK QRRNVPMKPP DEAKVGDTLG
DSSSSVLEFM SMKSYPDVSV DISMLSSLGK VKKELDPDDS HLNLDETTKL LQDLHEAQAE
RGGSRPSSNL SSLSNASERD QHHLGSPSRL SVGEQPDVTH DPYEFLQSPE PAASAKT
