BRD8_HUMAN
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 03-AUG-2022, entry version 177.
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 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 [26]
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.
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};
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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; 133.
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 GlyGen; Q9H0E9; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q9H0E9; -.
DR PhosphoSitePlus; Q9H0E9; -.
DR BioMuta; BRD8; -.
DR DMDM; 313104080; -.
DR EPD; Q9H0E9; -.
DR jPOST; Q9H0E9; -.
DR MassIVE; Q9H0E9; -.
DR MaxQB; Q9H0E9; -.
DR PaxDb; Q9H0E9; -.
DR PeptideAtlas; Q9H0E9; -.
DR PRIDE; Q9H0E9; -.
DR ProteomicsDB; 80265; -. [Q9H0E9-1]
DR ProteomicsDB; 80266; -. [Q9H0E9-2]
DR ProteomicsDB; 80267; -. [Q9H0E9-3]
DR ProteomicsDB; 80268; -. [Q9H0E9-4]
DR Antibodypedia; 678; 197 antibodies from 28 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 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; IQTGHMD; -.
DR OrthoDB; 1509761at2759; -.
DR PhylomeDB; Q9H0E9; -.
DR TreeFam; TF106422; -.
DR PathwayCommons; Q9H0E9; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9H0E9; -.
DR BioGRID-ORCS; 10902; 264 hits in 1104 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 208 other tissues.
DR ExpressionAtlas; Q9H0E9; baseline and differential.
DR Genevisible; Q9H0E9; HS.
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: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:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
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:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd05507; Bromo_brd8_like; 2.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR038002; BRD8.
DR InterPro; IPR037966; Brd8_Bromo_dom.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR PANTHER; PTHR15398:SF6; PTHR15398:SF6; 2.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
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
