BRD3_HUMAN
ID BRD3_HUMAN Reviewed; 726 AA.
AC Q15059; B1APD9; Q4G5Y3; Q5T1R7; Q8N5M3; Q92645;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Bromodomain-containing protein 3;
DE AltName: Full=RING3-like protein;
GN Name=BRD3; Synonyms=KIAA0043, RING3L;
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 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16008511; DOI=10.1089/dna.2005.24.432;
RA Ishii H., Mimori K., Mori M., Vecchione A.;
RT "Differentially expressed genes in endothelial differentiation.";
RL DNA Cell Biol. 24:432-437(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 [GENOMIC DNA] OF 363-726.
RX PubMed=9373153; DOI=10.1016/s0378-1119(97)00415-0;
RA Thorpe K.L., Gorman P., Thomas C., Sheer D., Trowsdale J., Beck S.;
RT "Chromosomal localization, gene structure and transcription pattern of the
RT ORFX gene, a homologue of the MHC-linked RING3 gene.";
RL Gene 200:177-183(1997).
RN [7]
RP FUNCTION, AND INTERACTION WITH ACETYLATED CHROMATIN.
RX PubMed=18406326; DOI=10.1016/j.molcel.2008.01.018;
RA LeRoy G., Rickards B., Flint S.J.;
RT "The double bromodomain proteins Brd2 and Brd3 couple histone acetylation
RT to transcription.";
RL Mol. Cell 30:51-60(2008).
RN [8]
RP CHROMOSOMAL TRANSLOCATION WITH NUTM1.
RX PubMed=17934517; DOI=10.1038/sj.onc.1210852;
RA French C.A., Ramirez C.L., Kolmakova J., Hickman T.T., Cameron M.J.,
RA Thyne M.E., Kutok J.L., Toretsky J.A., Tadavarthy A.K., Kees U.R.,
RA Fletcher J.A., Aster J.C.;
RT "BRD-NUT oncoproteins: a family of closely related nuclear proteins that
RT block epithelial differentiation and maintain the growth of carcinoma
RT cells.";
RL Oncogene 27:2237-2242(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-563, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-563, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-414, 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 [17]
RP STRUCTURE BY NMR OF 25-415.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and second bromodomain from human
RT bromodomain containing protein 3.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 24-416, SUBUNIT, AND DOMAIN.
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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 307-416 IN COMPLEX WITH
RP ACETYLATED HISTONE H3 PEPTIDE, FUNCTION, AND DOMAIN.
RX PubMed=27105114; DOI=10.1016/j.molcel.2016.03.028;
RA Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L.,
RA Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.;
RT "Molecular coupling of histone crotonylation and active transcription by
RT AF9 YEATS domain.";
RL Mol. Cell 62:181-193(2016).
RN [20]
RP VARIANTS [LARGE SCALE ANALYSIS] ASN-36; THR-161; VAL-172; GLN-435; HIS-441
RP AND PRO-447.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Chromatin reader that recognizes and binds hyperacetylated
CC chromatin and plays a role in the regulation of transcription, probably
CC by chromatin remodeling and interaction with transcription factors
CC (PubMed:18406326, PubMed:27105114). Regulates transcription by
CC promoting the binding of the transcription factor GATA1 to its targets
CC (By similarity). {ECO:0000250|UniProtKB:Q8K2F0,
CC ECO:0000269|PubMed:18406326, ECO:0000269|PubMed:27105114}.
CC -!- SUBUNIT: Interacts (via bromo domain 1) with GATA1 acetylated at 'Lys-
CC 312' and 'Lys-315'. Interacts (via bromo domain 1) with GATA2
CC acetylated on lysine residues (By similarity). Interacts (via bromo
CC domains) with acetylated lysine residues on the N-terminus of histone
CC H2A, H2B, H3 and H4 (in vitro). {ECO:0000250|UniProtKB:Q8K2F0,
CC ECO:0000269|PubMed:18406326, ECO:0000269|PubMed:22464331}.
CC -!- INTERACTION:
CC Q15059; P01106: MYC; NbExp=3; IntAct=EBI-1383460, EBI-447544;
CC Q15059-2; O00505: KPNA3; NbExp=3; IntAct=EBI-13468085, EBI-358297;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8K2F0}.
CC Note=Detected on chromatin. {ECO:0000250|UniProtKB:Q8K2F0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15059-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15059-2; Sequence=VSP_010247, VSP_010248;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The Bromo domains specifically recognize and bind acetylated
CC histones. {ECO:0000269|PubMed:27105114}.
CC -!- DISEASE: Note=A chromosomal aberration involving BRD3 is found in a
CC rare, aggressive, and lethal carcinoma arising in midline organs of
CC young people. Translocation t(15;9)(q14;q34) with NUTM1 which produces
CC a BRD3-NUTM1 fusion protein. {ECO:0000269|PubMed:17934517}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05393.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D26362; BAA05393.2; ALT_INIT; mRNA.
DR EMBL; AY513270; AAS82952.1; -; mRNA.
DR EMBL; AL445931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88113.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88114.1; -; Genomic_DNA.
DR EMBL; BC032124; AAH32124.1; -; mRNA.
DR EMBL; Z81330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS6980.1; -. [Q15059-1]
DR RefSeq; NP_031397.1; NM_007371.3. [Q15059-1]
DR RefSeq; XP_006717354.1; XM_006717291.2. [Q15059-1]
DR RefSeq; XP_011517354.1; XM_011519052.2. [Q15059-1]
DR PDB; 2E7N; NMR; -; A=306-415.
DR PDB; 2NXB; X-ray; 1.40 A; A/B=24-144.
DR PDB; 2OO1; X-ray; 1.70 A; A/B/C/D=307-416.
DR PDB; 2YW5; NMR; -; A=25-155.
DR PDB; 3S91; X-ray; 2.06 A; A=24-144.
DR PDB; 3S92; X-ray; 1.36 A; A=306-416.
DR PDB; 5A7C; X-ray; 1.90 A; A/B/C/D=306-416.
DR PDB; 5HFR; X-ray; 1.70 A; A/B/C/D=306-416.
DR PDB; 5HJC; X-ray; 2.60 A; A=307-416.
DR PDB; 6BGG; NMR; -; B=557-644.
DR PDB; 6BGH; NMR; -; A=557-643.
DR PDB; 6I41; X-ray; 1.90 A; B=245-253.
DR PDB; 6I5P; X-ray; 1.81 A; B/D/F/H=245-253.
DR PDB; 6I68; X-ray; 1.85 A; B/D/F/H=245-253.
DR PDB; 6I7A; X-ray; 2.20 A; B/D/F/H=245-253.
DR PDB; 6QJU; X-ray; 1.20 A; A/B=24-144.
DR PDB; 6U4A; X-ray; 1.88 A; A/B=25-147.
DR PDB; 6ULP; X-ray; 2.80 A; A/B=307-419.
DR PDB; 7JMY; NMR; -; A=554-640.
DR PDB; 7JQ8; NMR; -; A=554-640.
DR PDB; 7JYN; NMR; -; A=554-640.
DR PDB; 7JYZ; NMR; -; B=554-640.
DR PDB; 7L72; X-ray; 1.50 A; A=306-416.
DR PDB; 7L9L; X-ray; 1.55 A; A=306-416.
DR PDB; 7LAY; X-ray; 1.45 A; A/B=24-144.
DR PDB; 7LAZ; X-ray; 2.30 A; A/B=24-144.
DR PDB; 7LB4; X-ray; 2.00 A; A/B=306-416.
DR PDB; 7LBT; X-ray; 2.70 A; A/B/C/D=306-416.
DR PDBsum; 2E7N; -.
DR PDBsum; 2NXB; -.
DR PDBsum; 2OO1; -.
DR PDBsum; 2YW5; -.
DR PDBsum; 3S91; -.
DR PDBsum; 3S92; -.
DR PDBsum; 5A7C; -.
DR PDBsum; 5HFR; -.
DR PDBsum; 5HJC; -.
DR PDBsum; 6BGG; -.
DR PDBsum; 6BGH; -.
DR PDBsum; 6I41; -.
DR PDBsum; 6I5P; -.
DR PDBsum; 6I68; -.
DR PDBsum; 6I7A; -.
DR PDBsum; 6QJU; -.
DR PDBsum; 6U4A; -.
DR PDBsum; 6ULP; -.
DR PDBsum; 7JMY; -.
DR PDBsum; 7JQ8; -.
DR PDBsum; 7JYN; -.
DR PDBsum; 7JYZ; -.
DR PDBsum; 7L72; -.
DR PDBsum; 7L9L; -.
DR PDBsum; 7LAY; -.
DR PDBsum; 7LAZ; -.
DR PDBsum; 7LB4; -.
DR PDBsum; 7LBT; -.
DR AlphaFoldDB; Q15059; -.
DR SASBDB; Q15059; -.
DR SMR; Q15059; -.
DR BioGRID; 113715; 478.
DR DIP; DIP-39755N; -.
DR IntAct; Q15059; 25.
DR MINT; Q15059; -.
DR STRING; 9606.ENSP00000305918; -.
DR BindingDB; Q15059; -.
DR ChEMBL; CHEMBL1795186; -.
DR GuidetoPHARMACOLOGY; 2725; -.
DR GlyGen; Q15059; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q15059; -.
DR PhosphoSitePlus; Q15059; -.
DR BioMuta; BRD3; -.
DR DMDM; 12643726; -.
DR EPD; Q15059; -.
DR jPOST; Q15059; -.
DR MassIVE; Q15059; -.
DR MaxQB; Q15059; -.
DR PaxDb; Q15059; -.
DR PeptideAtlas; Q15059; -.
DR PRIDE; Q15059; -.
DR ProteomicsDB; 60414; -. [Q15059-1]
DR ProteomicsDB; 60415; -. [Q15059-2]
DR ABCD; Q15059; 1 sequenced antibody.
DR Antibodypedia; 31966; 404 antibodies from 34 providers.
DR DNASU; 8019; -.
DR Ensembl; ENST00000303407.12; ENSP00000305918.6; ENSG00000169925.17. [Q15059-1]
DR Ensembl; ENST00000371834.6; ENSP00000360900.2; ENSG00000169925.17. [Q15059-2]
DR GeneID; 8019; -.
DR KEGG; hsa:8019; -.
DR MANE-Select; ENST00000303407.12; ENSP00000305918.6; NM_007371.4; NP_031397.1.
DR UCSC; uc004cew.4; human. [Q15059-1]
DR CTD; 8019; -.
DR DisGeNET; 8019; -.
DR GeneCards; BRD3; -.
DR HGNC; HGNC:1104; BRD3.
DR HPA; ENSG00000169925; Low tissue specificity.
DR MIM; 601541; gene.
DR neXtProt; NX_Q15059; -.
DR OpenTargets; ENSG00000169925; -.
DR PharmGKB; PA25415; -.
DR VEuPathDB; HostDB:ENSG00000169925; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR HOGENOM; CLU_001499_0_4_1; -.
DR InParanoid; Q15059; -.
DR OMA; CYAFNPD; -.
DR PhylomeDB; Q15059; -.
DR TreeFam; TF317345; -.
DR PathwayCommons; Q15059; -.
DR SignaLink; Q15059; -.
DR SIGNOR; Q15059; -.
DR BioGRID-ORCS; 8019; 17 hits in 1097 CRISPR screens.
DR ChiTaRS; BRD3; human.
DR EvolutionaryTrace; Q15059; -.
DR GeneWiki; BRD3; -.
DR GenomeRNAi; 8019; -.
DR Pharos; Q15059; Tchem.
DR PRO; PR:Q15059; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15059; protein.
DR Bgee; ENSG00000169925; Expressed in nipple and 218 other tissues.
DR ExpressionAtlas; Q15059; baseline and differential.
DR Genevisible; Q15059; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR DisProt; DP03059; -.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
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; 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 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; Chromosomal rearrangement; Coiled coil;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..726
FT /note="Bromodomain-containing protein 3"
FT /id="PRO_0000211181"
FT DOMAIN 51..123
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 326..398
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 562..644
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..80
FT /note="Acetylated histone H3 binding"
FT /evidence="ECO:0000269|PubMed:27105114"
FT REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..524
FT /evidence="ECO:0000255"
FT COILED 645..684
FT /evidence="ECO:0000255"
FT COMPBIAS 14..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 647..648
FT /note="Breakpoint for translocation to form BDR3-NUTM1
FT fusion protein"
FT /evidence="ECO:0000269|PubMed:17934517"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 549..556
FT /note="QLKKGGKQ -> DHFLTCGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010247"
FT VAR_SEQ 557..726
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010248"
FT VARIANT 36
FT /note="T -> N (in a renal clear cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041913"
FT VARIANT 161
FT /note="A -> T (in a gastric adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041914"
FT VARIANT 172
FT /note="A -> V (in dbSNP:rs34609592)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041915"
FT VARIANT 435
FT /note="K -> Q (in dbSNP:rs36093130)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041916"
FT VARIANT 441
FT /note="R -> H (in dbSNP:rs56017928)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041917"
FT VARIANT 447
FT /note="S -> P (in dbSNP:rs55754444)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041918"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2YW5"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6QJU"
FT TURN 65..69
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:6QJU"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3S92"
FT TURN 340..344
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 373..390
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 396..413
FT /evidence="ECO:0007829|PDB:3S92"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:6BGH"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:6BGG"
FT HELIX 574..585
FT /evidence="ECO:0007829|PDB:6BGG"
FT HELIX 589..602
FT /evidence="ECO:0007829|PDB:6BGG"
FT HELIX 604..608
FT /evidence="ECO:0007829|PDB:6BGG"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:6BGH"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:6BGG"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:6BGG"
FT HELIX 623..636
FT /evidence="ECO:0007829|PDB:6BGG"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:6BGG"
SQ SEQUENCE 726 AA; 79542 MW; 64F526FC3C1033AA CRC64;
MSTATTVAPA GIPATPGPVN PPPPEVSNPS KPGRKTNQLQ YMQNVVVKTL WKHQFAWPFY
QPVDAIKLNL PDYHKIIKNP MDMGTIKKRL ENNYYWSASE CMQDFNTMFT NCYIYNKPTD
DIVLMAQALE KIFLQKVAQM PQEEVELLPP APKGKGRKPA AGAQSAGTQQ VAAVSSVSPA
TPFQSVPPTV SQTPVIAATP VPTITANVTS VPVPPAAAPP PPATPIVPVV PPTPPVVKKK
GVKRKADTTT PTTSAITASR SESPPPLSDP KQAKVVARRE SGGRPIKPPK KDLEDGEVPQ
HAGKKGKLSE HLRYCDSILR EMLSKKHAAY AWPFYKPVDA EALELHDYHD IIKHPMDLST
VKRKMDGREY PDAQGFAADV RLMFSNCYKY NPPDHEVVAM ARKLQDVFEM RFAKMPDEPV
EAPALPAPAA PMVSKGAESS RSSEESSSDS GSSDSEEERA TRLAELQEQL KAVHEQLAAL
SQAPVNKPKK KKEKKEKEKK KKDKEKEKEK HKVKAEEEKK AKVAPPAKQA QQKKAPAKKA
NSTTTAGRQL KKGGKQASAS YDSEEEEEGL PMSYDEKRQL SLDINRLPGE KLGRVVHIIQ
SREPSLRDSN PDEIEIDFET LKPTTLRELE RYVKSCLQKK QRKPFSASGK KQAAKSKEEL
AQEKKKELEK RLQDVSGQLS SSKKPARKEK PGSAPSGGPS RLSSSSSSES GSSSSSGSSS
DSSDSE
