BRD1_MOUSE
ID BRD1_MOUSE Reviewed; 1058 AA.
AC G5E8P1; E9PZ26; Q571F6; Q8BU83;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Bromodomain-containing protein 1 {ECO:0000303|PubMed:21753189};
DE AltName: Full=Bromodomain and PHD finger-containing protein 2 {ECO:0000303|PubMed:21753189};
GN Name=Brd1 {ECO:0000303|PubMed:21753189, ECO:0000312|MGI:MGI:1924161};
GN Synonyms=Brpf2 {ECO:0000303|PubMed:21753189}, Kiaa4191 {ECO:0000303|Ref.3};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-97.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC39779.1};
RC TISSUE=Lung {ECO:0000312|EMBL:BAC39779.1};
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 [3] {ECO:0000312|EMBL:BAD90158.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-1058 (ISOFORM 2).
RC TISSUE=Spleen {ECO:0000312|EMBL:BAD90158.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Kitamura H., Nagase T.,
RA Ohara O., Koga H.;
RT "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene. The
RT Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs Identified by
RT Screening of Terminal sequences of cDNA Clones Randomly Sampled from Size-
RT Fractionated Libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6]
RP FUNCTION, IDENTIFICATION IN THE HBO1 COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=21753189; DOI=10.1182/blood-2011-01-331892;
RA Mishima Y., Miyagi S., Saraya A., Negishi M., Endoh M., Endo T.A.,
RA Toyoda T., Shinga J., Katsumoto T., Chiba T., Yamaguchi N., Kitabayashi I.,
RA Koseki H., Iwama A.;
RT "The Hbo1-Brd1/Brpf2 complex is responsible for global acetylation of H3K14
RT and required for fetal liver erythropoiesis.";
RL Blood 118:2443-2453(2011).
RN [7] {ECO:0007744|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: Scaffold subunit of various histone acetyltransferase (HAT)
CC complexes, such as the MOZ/MORF and HBO1 complexes, that acts as a
CC regulator of hematopoiesis (PubMed:21753189). Plays a key role in HBO1
CC complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14'
CC acetylation (H3K14ac), thereby promoting erythroid differentiation
CC (PubMed:21753189). {ECO:0000269|PubMed:21753189}.
CC -!- SUBUNIT: Component of some HBO1 complexes composed of KAT7/HBO1, MEAF6,
CC ING4 and BRD1/BRPF2 (PubMed:21753189). Component of the MOZ/MORF
CC complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of
CC BRPF1, BRD1/BRPF2 and BRPF3 (By similarity). Interacts (via PHD-type
CC zinc finger domain) with unmodified histone H3 (By similarity).
CC Interacts (via PWWP domain) with dimethylated and trimethylated 'Lys-
CC 79' on histone H3 (By similarity). {ECO:0000250|UniProtKB:O95696,
CC ECO:0000269|PubMed:21753189}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95696}.
CC Chromosome {ECO:0000250|UniProtKB:O95696}. Note=Localizes to
CC transcription start sites. {ECO:0000250|UniProtKB:O95696}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G5E8P1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G5E8P1-2; Sequence=VSP_060568;
CC -!- DISRUPTION PHENOTYPE: Embryos die at mid-gestation because of anemia
CC and impaired fetal liver erythropoiesis. {ECO:0000269|PubMed:21753189}.
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DR EMBL; AC117700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220233; BAD90158.1; -; mRNA.
DR EMBL; AK086982; BAC39779.1; -; mRNA.
DR CCDS; CCDS27730.2; -. [G5E8P1-2]
DR RefSeq; NP_001028446.2; NM_001033274.3. [G5E8P1-2]
DR RefSeq; XP_006520898.1; XM_006520835.2. [G5E8P1-1]
DR AlphaFoldDB; G5E8P1; -.
DR SMR; G5E8P1; -.
DR ComplexPortal; CPX-801; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-805; MORF2 histone acetyltransferase complex.
DR STRING; 10090.ENSMUSP00000105007; -.
DR iPTMnet; G5E8P1; -.
DR PhosphoSitePlus; G5E8P1; -.
DR jPOST; G5E8P1; -.
DR MaxQB; G5E8P1; -.
DR PeptideAtlas; G5E8P1; -.
DR PRIDE; G5E8P1; -.
DR ProteomicsDB; 343018; -. [G5E8P1-1]
DR ProteomicsDB; 355447; -.
DR Antibodypedia; 251; 178 antibodies from 24 providers.
DR Ensembl; ENSMUST00000109380; ENSMUSP00000105006; ENSMUSG00000022387. [G5E8P1-1]
DR Ensembl; ENSMUST00000109381; ENSMUSP00000105007; ENSMUSG00000022387. [G5E8P1-2]
DR GeneID; 223770; -.
DR KEGG; mmu:223770; -.
DR CTD; 23774; -.
DR MGI; MGI:1924161; Brd1.
DR VEuPathDB; HostDB:ENSMUSG00000022387; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157236; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR OMA; RHASSPC; -.
DR OrthoDB; 566217at2759; -.
DR TreeFam; TF316118; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 223770; 14 hits in 62 CRISPR screens.
DR ChiTaRS; Brd1; mouse.
DR PRO; PR:G5E8P1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000022387; Expressed in animal zygote and 251 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR CDD; cd05839; BR140_related; 1.
DR CDD; cd15702; ePHD_BRPF2; 1.
DR CDD; cd15677; PHD_BRPF2; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR035502; BR140-rel_PWWD.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR042004; BRPF2_ePHD.
DR InterPro; IPR042009; BRPF2_PHD.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW Chromosome; Erythrocyte maturation; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1058
FT /note="Bromodomain-containing protein 1"
FT /id="PRO_0000449610"
FT DOMAIN 579..649
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 929..1012
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 214..264
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 268..301
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 325..389
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..80
FT /note="Interaction with KAT7/HBO1 and histones"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 516
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 903
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 1052
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95696"
FT VAR_SEQ 786
FT /note="E -> EGANSPPKLEPSDALPLPSNSETNSEPPTLNPVELHPEQSKLFKRVT
FT FDNESHSTCTQSALVSGHPPEPTLASSGDVPAAAASAVAEPSSDVNRRTSVLFCKSKSV
FT SPPKSAKNTETQPTSPQLGTKTFLSV (in isoform 2)"
FT /id="VSP_060568"
SQ SEQUENCE 1058 AA; 119714 MW; 4E44EA93A80325B0 CRC64;
MRRKGRCHRG SAARHPSSPC SIKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEVLPSTHGT PASASALPEP
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIIN EKRKGDCVSA
VSQNMFEFLM DRFEKESYCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL
YMKMEPVKEL TGGSATFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV
RSTSKVRKKA KKAKKTLAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW
LLKRLSRNGA PLLRRLQSSL QSQRNTQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE
LLRKREKLKR EQVKVEQMAM ELRLTPLTVL LRSVLEQLQE KDPAKIFAQP VSLKEVPDYL
DHIKHPMDFA TMRKRLEAQG YKNLHAFEED FNLIVDNCMK YNAKDTVFYR AAVRLRDQGG
VVLRQARREV ESIGLEEASG MHLPERPIAA PRRPFSWEEV DRLLDPANRA HMSLEEQLRE
LLDKLDLTCS MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QAPPTGAGTG GFEDEAAPLA
PDTAEEVLPR LETLLQPRKR SRSTCGDSEV EEESPGKRLD TGLTNGFGGA RSEQEPGGGP
GRKAAPRRRC ASESSICSSN SPLCDSSFST PKCGRGKPAL VRRHTLEDRS ELISCIENGN
YAKAARIAAE VGQSNMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP KMPRVPGHHN
GVTIPAPPLD VLKIGEHMQT KSEEKLFLVL FFDNKRSWQW LPKSKMVPLG VDETIDKLKM
MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP ASDLSDID
