ID BRD8_HUMAN Reviewed; 1235 AA. AC Q9H0E9; O43178; Q15355; Q58AB0; Q59GN0; Q969M9; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Bromodomain-containing protein 8; DE AltName: Full=Skeletal muscle abundant protein; DE AltName: Full=Skeletal muscle abundant protein 2; DE AltName: Full=Thyroid hormone receptor coactivating protein of 120 kDa; DE Short=TrCP120; DE AltName: Full=p120; GN Name=BRD8; Synonyms=SMAP, SMAP2; 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 [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND VARIANT RP ARG-1198. RX PubMed=8611617; DOI=10.1016/0167-4781(95)00239-1; RA Nielsen M.S., Petersen C.M., Gliemann J., Madsen P.; RT "Cloning and sequencing of a human cDNA encoding a putative transcription RT factor containing a bromodomain."; RL Biochim. Biophys. Acta 1306:14-16(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-1198. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-490 RP AND ARG-1198. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1235 (ISOFORM 2), AND VARIANT RP ARG-1198. RC TISSUE=Muscle; 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 6-1235 (ISOFORM 2), INTERACTION WITH THRB, RP AND VARIANT ARG-1198. RC TISSUE=Brain; RX PubMed=9368056; DOI=10.1074/jbc.272.47.29834; RA Monden T., Wondisford F.E., Hollenberg A.N.; RT "Isolation and characterization of a novel ligand-dependent thyroid hormone RT receptor-coactivating protein."; RL J. Biol. Chem. 272:29834-29841(1997). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1235 (ISOFORM 4), AND VARIANT ARG-1198. RC TISSUE=Skin; RA Nielsen M.S.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [8] RP PROTEIN SEQUENCE OF 34-44; 63-79; 83-98; 125-137; 138-148; 150-159; RP 270-295; 385-399; 485-493; 541-565; 576-604 AND 625-646, IDENTIFICATION IN RP NUA4 COMPLEX (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12963728; DOI=10.1074/jbc.c300389200; RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., RA Conaway R.C., Conaway J.W.; RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60- RT containing histone acetyltransferase complex."; RL J. Biol. Chem. 278:42733-42736(2003). RN [9] RP FUNCTION, AND INTERACTION WITH RXRA. RX PubMed=10517671; DOI=10.1210/mend.13.10.0353; RA Monden T., Kishi M., Hosoya T., Satoh T., Wondisford F.E., Hollenberg A.N., RA Yamada M., Mori M.; RT "p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) RT on peroxisome proliferator-activated receptor-gamma/RXR heterodimers."; RL Mol. Endocrinol. 13:1695-1703(1999). RN [10] RP REVIEW ON NUA4 COMPLEX. RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009; RA Doyon Y., Cote J.; RT "The highly conserved and multifunctional NuA4 HAT complex."; RL Curr. Opin. Genet. Dev. 14:147-154(2004). RN [11] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 RP COMPLEX (ISOFORMS 1 AND 2), AND IDENTIFICATION IN NUA4-RELATED RP SRCAP-CONTAINING COMPLEX. RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004; RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.; RT "Structural and functional conservation of the NuA4 histone RT acetyltransferase complex from yeast to humans."; RL Mol. Cell. Biol. 24:1884-1896(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637 AND SER-641, AND 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264; SER-268 AND SER-284 RP (ISOFORMS 2 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124; RP SER-128 AND SER-144 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264 AND SER-268 (ISOFORMS 2 RP AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND SER-128 RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-481, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-641, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924 (ISOFORM 2), AND RP IDENTIFICATION BY 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-579 AND SER-621, AND RP IDENTIFICATION BY 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637 AND SER-641, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264 AND SER-268 (ISOFORMS 2 RP AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND SER-128 RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481; LYS-509; LYS-575 AND RP LYS-612, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [22] RP FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX. RX PubMed=24463511; DOI=10.1038/nature12922; RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., RA Hamiche A.; RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin."; RL Nature 505:648-653(2014). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481 AND LYS-612, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [25] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-469; LYS-481; LYS-509; LYS-575 RP AND LYS-612, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). CC -!- FUNCTION: May act as a coactivator during transcriptional activation by CC hormone-activated nuclear receptors (NR). Isoform 2 stimulates CC transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and CC THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 CC histone acetyltransferase (HAT) complex which is involved in CC transcriptional activation of select genes principally by acetylation CC of nucleosomal histones H4 and H2A. This modification may both alter CC nucleosome - DNA interactions and promote interaction of the modified CC histones with other proteins which positively regulate transcription. CC This complex may be required for the activation of transcriptional CC programs associated with oncogene and proto-oncogene mediated growth CC induction, tumor suppressor mediated growth arrest and replicative CC senescence, apoptosis, and DNA repair. NuA4 may also play a direct role CC in DNA repair when recruited to sites of DNA damage. Component of a CC SWR1-like complex that specifically mediates the removal of histone CC H2A.Z/H2AZ1 from the nucleosome. {ECO:0000269|PubMed:10517671, CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:24463511}. CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400, CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, CC YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC CC and the adenovirus E1A protein. Component of a NuA4-related complex CC which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and CC YEATS4/GAS41. BRD8 isoform 2 interacts with RXRA/NR2B1 and THRB/ERBA2 CC (By similarity). Component of a SWR1-like complex. {ECO:0000250, CC ECO:0000269|PubMed:10517671, ECO:0000269|PubMed:14966270, CC ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:9368056}. CC -!- INTERACTION: CC Q9H0E9; Q9H2F5: EPC1; NbExp=5; IntAct=EBI-769266, EBI-769270; CC Q9H0E9-2; A0A0A0MR80: EP400; NbExp=3; IntAct=EBI-10304361, EBI-12089140; CC Q9H0E9-2; A1L4K1: FSD2; NbExp=6; IntAct=EBI-10304361, EBI-5661036; CC Q9H0E9-2; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-10304361, EBI-348259; CC Q9H0E9-2; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-10304361, EBI-1104552; CC Q9H0E9-2; Q13526: PIN1; NbExp=3; IntAct=EBI-10304361, EBI-714158; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25593309}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9H0E9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H0E9-2; Sequence=VSP_012880, VSP_012883, VSP_012884; CC Name=3; CC IsoId=Q9H0E9-3; Sequence=VSP_012879, VSP_012880, VSP_012881, CC VSP_012882, VSP_012883, VSP_012884; CC Name=4; CC IsoId=Q9H0E9-4; Sequence=VSP_012880, VSP_023187, VSP_023188, CC VSP_023189, VSP_023190, VSP_023191; CC -!- TISSUE SPECIFICITY: Expressed in adipose tissue, brain, heart, kidney, CC liver, lung, pancreas, placenta and skeletal muscle. CC {ECO:0000269|PubMed:8611617}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB87858.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH08039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH08076.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA63925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; X87613; CAA60949.1; -; mRNA. DR EMBL; AL136823; CAB66757.1; -; mRNA. DR EMBL; AB209079; BAD92316.1; -; mRNA. DR EMBL; AC109442; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113382; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008039; AAH08039.1; ALT_INIT; mRNA. DR EMBL; BC008076; AAH08076.1; ALT_INIT; mRNA. DR EMBL; AF016270; AAB87858.1; ALT_INIT; mRNA. DR EMBL; X94234; CAA63925.1; ALT_INIT; mRNA. DR CCDS; CCDS34241.1; -. [Q9H0E9-2] DR CCDS; CCDS4198.1; -. [Q9H0E9-1] DR CCDS; CCDS54907.1; -. [Q9H0E9-4] DR PIR; S58225; S58225. DR PIR; S68142; S68142. DR RefSeq; NP_001157798.1; NM_001164326.1. [Q9H0E9-4] DR RefSeq; NP_001287890.1; NM_001300961.1. DR RefSeq; NP_001287891.1; NM_001300962.1. DR RefSeq; NP_001287895.1; NM_001300966.1. [Q9H0E9-3] DR RefSeq; NP_006687.3; NM_006696.3. [Q9H0E9-2] DR RefSeq; NP_631938.1; NM_139199.1. [Q9H0E9-1] DR AlphaFoldDB; Q9H0E9; -. DR SMR; Q9H0E9; -. DR BioGRID; 116108; 143. DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex. DR CORUM; Q9H0E9; -. DR DIP; DIP-31762N; -. DR IntAct; Q9H0E9; 53. DR MINT; Q9H0E9; -. DR STRING; 9606.ENSP00000254900; -. DR BindingDB; Q9H0E9; -. DR ChEMBL; CHEMBL3588731; -. DR GlyCosmos; Q9H0E9; 7 sites, 2 glycans. DR GlyGen; Q9H0E9; 10 sites, 2 O-linked glycans (10 sites). DR iPTMnet; Q9H0E9; -. DR PhosphoSitePlus; Q9H0E9; -. DR SwissPalm; Q9H0E9; -. DR BioMuta; BRD8; -. DR DMDM; 313104080; -. DR EPD; Q9H0E9; -. DR jPOST; Q9H0E9; -. DR MassIVE; Q9H0E9; -. DR MaxQB; Q9H0E9; -. DR PaxDb; 9606-ENSP00000254900; -. DR PeptideAtlas; Q9H0E9; -. DR ProteomicsDB; 80265; -. [Q9H0E9-1] DR ProteomicsDB; 80266; -. [Q9H0E9-2] DR ProteomicsDB; 80267; -. [Q9H0E9-3] DR ProteomicsDB; 80268; -. [Q9H0E9-4] DR Pumba; Q9H0E9; -. DR Antibodypedia; 678; 221 antibodies from 29 providers. DR DNASU; 10902; -. DR Ensembl; ENST00000230901.9; ENSP00000230901.5; ENSG00000112983.18. [Q9H0E9-2] DR Ensembl; ENST00000254900.10; ENSP00000254900.5; ENSG00000112983.18. [Q9H0E9-1] DR Ensembl; ENST00000411594.6; ENSP00000394330.2; ENSG00000112983.18. [Q9H0E9-4] DR GeneID; 10902; -. DR KEGG; hsa:10902; -. DR MANE-Select; ENST00000254900.10; ENSP00000254900.5; NM_139199.2; NP_631938.2. DR UCSC; uc003lcf.2; human. [Q9H0E9-1] DR AGR; HGNC:19874; -. DR CTD; 10902; -. DR DisGeNET; 10902; -. DR GeneCards; BRD8; -. DR HGNC; HGNC:19874; BRD8. DR HPA; ENSG00000112983; Low tissue specificity. DR MIM; 602848; gene. DR neXtProt; NX_Q9H0E9; -. DR OpenTargets; ENSG00000112983; -. DR PharmGKB; PA134923194; -. DR VEuPathDB; HostDB:ENSG00000112983; -. DR eggNOG; ENOG502QRPS; Eukaryota. DR GeneTree; ENSGT00530000064262; -. DR InParanoid; Q9H0E9; -. DR OMA; AYKPHTT; -. DR OrthoDB; 2919186at2759; -. DR PhylomeDB; Q9H0E9; -. DR TreeFam; TF106422; -. DR PathwayCommons; Q9H0E9; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; Q9H0E9; -. DR SIGNOR; Q9H0E9; -. DR BioGRID-ORCS; 10902; 291 hits in 1183 CRISPR screens. DR ChiTaRS; BRD8; human. DR GeneWiki; BRD8; -. DR GenomeRNAi; 10902; -. DR Pharos; Q9H0E9; Tbio. DR PRO; PR:Q9H0E9; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9H0E9; Protein. DR Bgee; ENSG00000112983; Expressed in right testis and 210 other cell types or tissues. DR ExpressionAtlas; Q9H0E9; baseline and differential. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:ARUK-UCL. DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:ARUK-UCL. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:ARUK-UCL. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal. DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR CDD; cd05507; Bromo_brd8_like; 2. DR Gene3D; 1.20.920.10; Bromodomain-like; 2. DR InterPro; IPR037966; Brd8_Bromo_dom. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR PANTHER; PTHR15398; BROMODOMAIN-CONTAINING PROTEIN 8; 1. DR PANTHER; PTHR15398:SF4; BROMODOMAIN-CONTAINING PROTEIN 8; 1. DR Pfam; PF00439; Bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SUPFAM; SSF47370; Bromodomain; 2. DR PROSITE; PS50014; BROMODOMAIN_2; 2. DR Genevisible; Q9H0E9; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; KW Coiled coil; Direct protein sequencing; Growth regulation; Isopeptide bond; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1235 FT /note="Bromodomain-containing protein 8" FT /id="PRO_0000211185" FT DOMAIN 724..794 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1120..1190 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT REGION 186..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 551..597 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 621..672 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 827..848 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 903..940 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 966..999 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 97..171 FT /evidence="ECO:0000255" FT COMPBIAS 572..589 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 639..653 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 981..999 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 85 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8R3B7" FT MOD_RES 383 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R3B7" FT MOD_RES 387 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:23186163" FT MOD_RES 481 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 579 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 621 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 637 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT CROSSLNK 469 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 481 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 481 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 509 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 575 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 612 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..147 FT /note="MATGTGKHKLLSTGPTEPWSIREKLCLASSVMRSGDQNWVSVSRAIKPFAEP FT GRPPDWFSQKHCASQYSELLETTETPKRKRGEKGEVVETVEDVIVRKLTAERVEELKKV FT IKETQERYRRLKRDAELIQAGHMDSRLDELCNDIAT -> MSFAMTL (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:8611617" FT /id="VSP_012879" FT VAR_SEQ 215 FT /note="V -> VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQ FT KATPPPSPLLSELLKKGSLLPTSPRLV (in isoform 2, isoform 3 and FT isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8611617, ECO:0000303|PubMed:9368056, FT ECO:0000303|Ref.3, ECO:0000303|Ref.7" FT /id="VSP_012880" FT VAR_SEQ 263..332 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_023187" FT VAR_SEQ 263..301 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8611617" FT /id="VSP_012881" FT VAR_SEQ 845..859 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8611617" FT /id="VSP_012882" FT VAR_SEQ 846 FT /note="S -> G (in isoform 4)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_023188" FT VAR_SEQ 847..975 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_023189" FT VAR_SEQ 860..878 FT /note="MGHEWVWLDSEQDHPNDSE -> DGGTRGRRCAIEADMKMKK (in FT isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8611617, ECO:0000303|PubMed:9368056, FT ECO:0000303|Ref.3" FT /id="VSP_012883" FT VAR_SEQ 879..1235 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8611617, ECO:0000303|PubMed:9368056, FT ECO:0000303|Ref.3" FT /id="VSP_012884" FT VAR_SEQ 979..992 FT /note="QEGREIKASEGERE -> GRRCAIEADMKMKK (in isoform 4)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_023190" FT VAR_SEQ 993..1235 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_023191" FT VARIANT 490 FT /note="T -> M (in dbSNP:rs11750814)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_030695" FT VARIANT 896 FT /note="L -> P (in dbSNP:rs6883021)" FT /id="VAR_048428" FT VARIANT 1198 FT /note="Q -> R (in dbSNP:rs412051)" FT /evidence="ECO:0000269|PubMed:11230166, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8611617, FT ECO:0000269|PubMed:9368056, ECO:0000269|Ref.3, FT ECO:0000269|Ref.7" FT /id="VAR_048429" FT CONFLICT 306 FT /note="Q -> H (in Ref. 6; AAB87858)" FT /evidence="ECO:0000305" FT CONFLICT 557 FT /note="V -> L (in Ref. 1; CAA60949 and 7; CAA63925)" FT /evidence="ECO:0000305" FT MOD_RES Q9H0E9-2:264 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES Q9H0E9-2:268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES Q9H0E9-2:284 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q9H0E9-2:924 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES Q9H0E9-3:124 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES Q9H0E9-3:128 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES Q9H0E9-3:144 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q9H0E9-4:264 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES Q9H0E9-4:268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES Q9H0E9-4:284 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 1235 AA; 135336 MW; 3738078C77FC17D1 CRC64; MATGTGKHKL LSTGPTEPWS IREKLCLASS VMRSGDQNWV SVSRAIKPFA EPGRPPDWFS QKHCASQYSE LLETTETPKR KRGEKGEVVE TVEDVIVRKL TAERVEELKK VIKETQERYR RLKRDAELIQ AGHMDSRLDE LCNDIATKKK LEEEEAEVKR KATDAAYQAR QAVKTPPRRL PTVMVRSPID SASPGGDYPL GDLTPTTMEE ATSGVNESEM AVASGHLNST GVLLEVGGVL PMIHGGEIQQ TPNTVAASPA ASGAPTLSRL LEAGPTQFTT PLASFTTVAS EPPVKLVPPP VESVSQATIV MMPALPAPSS APAVSTTESV APVSQPDNCV PMEAVGDPHT VTVSMDSSEI SMIINSIKEE CFRSGVAEAP VGSKAPSIDG KEELDLAEKM DIAVSYTGEE LDFETVGDII AIIEDKVDDH PEVLDVAAVE AALSFCEEND DPQSLPGPWE HPIQQERDKP VPLPAPEMTV KQERLDFEET ENKGIHELVD IREPSAEIKV EPAEPEPVIS GAEIVAGVVP ATSMEPPELR SQDLDEELGS TAAGEIVEAD VAIGKGDETP LTNVKTEASP ESMLSPSHGS NPIEDPLEAE TQHKFEMSDS LKEESGTIFG SQIKDAPGED EEEDGVSEAA SLEEPKEEDQ GEGYLSEMDN EPPVSESDDG FSIHNATLQS HTLADSIPSS PASSQFSVCS EDQEAIQAQK IWKKAIMLVW RAAANHRYAN VFLQPVTDDI APGYHSIVQR PMDLSTIKKN IENGLIRSTA EFQRDIMLMF QNAVMYNSSD HDVYHMAVEM QRDVLEQIQQ FLATQLIMQT SESGISAKSL RGRDSTRKQD ASEKDSVPMG SPAFLLSLFM GHEWVWLDSE QDHPNDSELS NDCRSLFSSW DSSLDLDVGN WRETEDPEAE ELEESSPERE PSELLVGDGG SEESQEAARK ASHQNLLHFL SEVAYLMEPL CISSNESSEG CCPPSGTRQE GREIKASEGE RELCRETEEL SAKGDPLVAE KPLGENGKPE VASAPSVICT VQGLLTESEE GEAQQESKGE DQGEVYVSEM EDQPPSGECD DAFNIKETPL VDTLFSHATS SKLTDLSQDD PVQDHLLFKK TLLPVWKMIA SHRFSSPFLK PVSERQAPGY KDVVKRPMDL TSLKRNLSKG RIRTMAQFLR DLMLMFQNAV MYNDSDHHVY HMAVEMRQEV LEQIQVLNIW LDKRKGSSSL EGEPANPVDD GKPVF //