BRD8_MOUSE
ID BRD8_MOUSE Reviewed; 951 AA.
AC Q8R3B7; Q3TSZ2; Q8C049; Q8R583; Q8VDP0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Bromodomain-containing protein 8;
GN Name=Brd8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85 AND LYS-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May act as a coactivator during transcriptional activation by
CC hormone-activated nuclear receptors (NR). Stimulates transcriptional
CC activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. Component
CC of the NuA4 histone acetyltransferase (HAT) complex which is involved
CC in transcriptional activation of select genes principally by
CC acetylation of nucleosomal histones H4 and H2A. This modification may
CC both alter nucleosome - DNA interactions and promote interaction of the
CC modified histones with other proteins which positively regulate
CC transcription. This complex may be required for the activation of
CC transcriptional programs associated with oncogene and proto-oncogene
CC mediated growth induction, tumor suppressor mediated growth arrest and
CC replicative senescence, apoptosis, and DNA repair. NuA4 may also play a
CC direct role in DNA repair when recruited to sites of DNA damage.
CC Component of a SWR1-like complex that specifically mediates the removal
CC of histone H2A.Z/H2AZ1 from the nucleosome.
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. 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 Component of a SWR1-like complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3B7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3B7-2; Sequence=VSP_038218;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23160.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAH25644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27812.1; Type=Erroneous initiation; 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; AK032320; BAC27812.1; ALT_INIT; mRNA.
DR EMBL; AK161689; BAE36533.1; -; mRNA.
DR EMBL; BC023160; AAH23160.1; ALT_SEQ; mRNA.
DR EMBL; BC025644; AAH25644.1; ALT_INIT; mRNA.
DR CCDS; CCDS50248.1; -. [Q8R3B7-1]
DR CCDS; CCDS70879.1; -. [Q8R3B7-2]
DR RefSeq; NP_001276535.1; NM_001289606.1. [Q8R3B7-2]
DR RefSeq; NP_001276536.1; NM_001289607.1.
DR RefSeq; NP_084423.2; NM_030147.3. [Q8R3B7-1]
DR AlphaFoldDB; Q8R3B7; -.
DR SMR; Q8R3B7; -.
DR BioGRID; 219557; 5.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q8R3B7; 6.
DR MINT; Q8R3B7; -.
DR STRING; 10090.ENSMUSP00000003876; -.
DR iPTMnet; Q8R3B7; -.
DR PhosphoSitePlus; Q8R3B7; -.
DR EPD; Q8R3B7; -.
DR jPOST; Q8R3B7; -.
DR MaxQB; Q8R3B7; -.
DR PaxDb; Q8R3B7; -.
DR PeptideAtlas; Q8R3B7; -.
DR PRIDE; Q8R3B7; -.
DR ProteomicsDB; 273799; -. [Q8R3B7-1]
DR ProteomicsDB; 273800; -. [Q8R3B7-2]
DR Antibodypedia; 678; 197 antibodies from 28 providers.
DR DNASU; 78656; -.
DR Ensembl; ENSMUST00000003876; ENSMUSP00000003876; ENSMUSG00000003778. [Q8R3B7-1]
DR Ensembl; ENSMUST00000097626; ENSMUSP00000095229; ENSMUSG00000003778. [Q8R3B7-2]
DR GeneID; 78656; -.
DR KEGG; mmu:78656; -.
DR UCSC; uc008ekv.2; mouse. [Q8R3B7-1]
DR UCSC; uc008ekx.2; mouse. [Q8R3B7-2]
DR CTD; 10902; -.
DR MGI; MGI:1925906; Brd8.
DR VEuPathDB; HostDB:ENSMUSG00000003778; -.
DR eggNOG; ENOG502QRPS; Eukaryota.
DR GeneTree; ENSGT00530000064262; -.
DR InParanoid; Q8R3B7; -.
DR OMA; IQTGHMD; -.
DR PhylomeDB; Q8R3B7; -.
DR TreeFam; TF106422; -.
DR BioGRID-ORCS; 78656; 17 hits in 75 CRISPR screens.
DR ChiTaRS; Brd8; mouse.
DR PRO; PR:Q8R3B7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8R3B7; protein.
DR Bgee; ENSMUSG00000003778; Expressed in floor plate of midbrain and 264 other tissues.
DR ExpressionAtlas; Q8R3B7; baseline and differential.
DR Genevisible; Q8R3B7; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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; ISO:MGI.
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; 1.
DR Gene3D; 1.20.920.10; -; 1.
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; 1.
DR Pfam; PF00439; Bromodomain; 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 Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW Coiled coil; Growth regulation; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..951
FT /note="Bromodomain-containing protein 8"
FT /id="PRO_0000211186"
FT DOMAIN 797..867
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 161..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 97..171
FT /evidence="ECO:0000255"
FT COMPBIAS 206..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 554
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT CROSSLNK 542
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT CROSSLNK 685
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0E9"
FT VAR_SEQ 215..287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038218"
FT CONFLICT 811
FT /note="D -> G (in Ref. 1; BAC27812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 102610 MW; 133859691F7CCEFB CRC64;
MATGTGKHKL LSTGPTEPWS IREKLCLASS VMRSGDQNWV SVSRAIKPFA EPGRPPDWFS
QKHCASQYSE LLETTETPKR KRGEKGEVVE TVEDVIVRKL TAERVEELKK VIKETQERYR
RLKRDAELIQ AGHMDSRLDE LCNDIAMKKK LEEEEAEVKR KATDAAYQAR QAVKTPPRRL
PTVMVRSPVD SASPGGDYPL GDLTPTTMEE ATSGVTPGTL PSTPVTSFPG IPDTLPPGSA
PLEAPMTPIT DDSPQKKMLG QKATPPPSPL LSELLKKGSL LPTSPRLVNE SEMPVPPGHL
NSTGVLLEVG GVLPMIHGGE IQPTTSAVAA SPAASGAPTL SRLLEAGPTQ FTTPLPSFTT
VASEPPVKLV PPPVESVSQA TIVMMPALPA PSSAAAVSTS ESGAPVSQPE PCVPLEAVGD
PHTVTVSMDS NEISMIINSI KEECFRSGVA EAPGGSKAPS IDGKEDLDLA EKMDIAVSYT
GEELDFETVG DIIAIIEDKV DDHPEVLDVA AVEAALSFCE ENDDPQSLPG PWEHPIQQER
DKPVPLPAPE MTVKQERLDF EESENKGLHD LVDIRDSGVE IKVEPTEPEP GMSGAEIVAG
VGPVPSMEPP ELRSQDSDEE PRSSAAGDIG EADGSSGKGD ERPLSAVKTE ASPESMLSPS
HGSNLIEDPL EAETQHKFEM SDSLKEESGT IFGSQIKDAP GDDEEEDGVS EAASLEEPKE
EDQGEGYLSE MDNEPPVSES DDGFSIHNAT LQSHTLADSI PSSPASSQFS VCSEDQEAIQ
AQKIWKKAIM LVWRAAANHR YANVFLQPVT DDIAPGYHSI VQRPMDLSTI KKNIENGLIR
STAEFQRDIM LMFQNAVMYN SSDHDVYHMA VEMQRDVLEQ IQQFLATQLI MQTSESGISA
KSLRGRDSTR KQDASEKDSV PMGSPAFLLS LFDGGTRGRR CAIEADMKMK K
