BRD3_MOUSE
ID BRD3_MOUSE Reviewed; 726 AA.
AC Q8K2F0; Q8C665; Q8CAX7; Q9JI25;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Bromodomain-containing protein 3;
DE AltName: Full=Bromodomain-containing FSH-like protein FSRG2;
GN Name=Brd3; Synonyms=Fsrg2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Shang E., Wolgemuth D.J.;
RT "Cloning and expression pattern of Fsrg2, a putative murine bromodomain-
RT containing homolog of the Drosophila gene female sterile homeotic.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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 [6]
RP INTERACTION WITH ACETYLATED GATA1 AND ACETYLATED HISTONE H4, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=21536911; DOI=10.1073/pnas.1102140108;
RA Lamonica J.M., Deng W., Kadauke S., Campbell A.E., Gamsjaeger R., Wang H.,
RA Cheng Y., Billin A.N., Hardison R.C., Mackay J.P., Blobel G.A.;
RT "Bromodomain protein Brd3 associates with acetylated GATA1 to promote its
RT chromatin occupancy at erythroid target genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E159-E168(2011).
RN [7]
RP STRUCTURE BY NMR OF 24-146 IN COMPLEX WITH ACETYLATED GATA1, INTERACTION
RP WITH ACETYLATED GATA1, AND FUNCTION.
RX PubMed=21555453; DOI=10.1128/mcb.05413-11;
RA Gamsjaeger R., Webb S.R., Lamonica J.M., Billin A., Blobel G.A.,
RA Mackay J.P.;
RT "Structural basis and specificity of acetylated transcription factor GATA1
RT recognition by BET family bromodomain protein Brd3.";
RL Mol. Cell. Biol. 31:2632-2640(2011).
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:21536911). Regulates transcription by promoting the binding of
CC the transcription factor GATA1 to its targets (PubMed:21536911).
CC {ECO:0000269|PubMed:21536911}.
CC -!- SUBUNIT: Interacts (via bromo domains) with acetylated lysine residues
CC on the N-terminus of histone H2A, H2B, H3 and H4 (in vitro)
CC (PubMed:21536911). Interacts (via bromo domain 1) with GATA1 acetylated
CC at 'Lys-312' and 'Lys-315' (PubMed:21555453). Interacts (via bromo
CC domain 1) with GATA2 acetylated on lysine residues (PubMed:21555453).
CC {ECO:0000269|PubMed:21536911, ECO:0000269|PubMed:21555453}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21536911}.
CC Note=Detected on chromatin. {ECO:0000269|PubMed:21536911}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2F0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2F0-2; Sequence=VSP_010249;
CC -!- DOMAIN: The Bromo domains specifically recognize and bind acetylated
CC histones. {ECO:0000250|UniProtKB:Q15059}.
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DR EMBL; AF269193; AAF78072.1; -; mRNA.
DR EMBL; BC031536; AAH31536.1; -; mRNA.
DR EMBL; AK037435; BAC29806.1; -; mRNA.
DR EMBL; AK076472; BAC36359.1; -; mRNA.
DR CCDS; CCDS15828.1; -. [Q8K2F0-1]
DR CCDS; CCDS50546.1; -. [Q8K2F0-2]
DR RefSeq; NP_001107045.1; NM_001113573.1. [Q8K2F0-1]
DR RefSeq; NP_001107046.1; NM_001113574.1. [Q8K2F0-2]
DR RefSeq; NP_075825.3; NM_023336.4. [Q8K2F0-1]
DR PDB; 2L5E; NMR; -; A=24-146.
DR PDBsum; 2L5E; -.
DR AlphaFoldDB; Q8K2F0; -.
DR SMR; Q8K2F0; -.
DR BioGRID; 212148; 3.
DR STRING; 10090.ENSMUSP00000028282; -.
DR iPTMnet; Q8K2F0; -.
DR PhosphoSitePlus; Q8K2F0; -.
DR EPD; Q8K2F0; -.
DR jPOST; Q8K2F0; -.
DR MaxQB; Q8K2F0; -.
DR PaxDb; Q8K2F0; -.
DR PRIDE; Q8K2F0; -.
DR ProteomicsDB; 273760; -. [Q8K2F0-1]
DR ProteomicsDB; 273761; -. [Q8K2F0-2]
DR Antibodypedia; 31966; 404 antibodies from 34 providers.
DR DNASU; 67382; -.
DR Ensembl; ENSMUST00000028282; ENSMUSP00000028282; ENSMUSG00000026918. [Q8K2F0-1]
DR Ensembl; ENSMUST00000077737; ENSMUSP00000076918; ENSMUSG00000026918. [Q8K2F0-1]
DR Ensembl; ENSMUST00000113941; ENSMUSP00000109574; ENSMUSG00000026918. [Q8K2F0-2]
DR Ensembl; ENSMUST00000164296; ENSMUSP00000128812; ENSMUSG00000026918. [Q8K2F0-1]
DR GeneID; 67382; -.
DR KEGG; mmu:67382; -.
DR UCSC; uc008ixm.2; mouse. [Q8K2F0-1]
DR CTD; 8019; -.
DR MGI; MGI:1914632; Brd3.
DR VEuPathDB; HostDB:ENSMUSG00000026918; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR InParanoid; Q8K2F0; -.
DR OMA; CYAFNPD; -.
DR TreeFam; TF317345; -.
DR BioGRID-ORCS; 67382; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Brd3; mouse.
DR EvolutionaryTrace; Q8K2F0; -.
DR PRO; PR:Q8K2F0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K2F0; protein.
DR Bgee; ENSMUSG00000026918; Expressed in undifferentiated genital tubercle and 250 other tissues.
DR ExpressionAtlas; Q8K2F0; baseline and differential.
DR Genevisible; Q8K2F0; MM.
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; ISO:MGI.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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 Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR IDEAL; IID50153; -.
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; Alternative splicing; Bromodomain; Chromatin regulator;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..726
FT /note="Bromodomain-containing protein 3"
FT /id="PRO_0000211182"
FT DOMAIN 50..122
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 325..397
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 563..645
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..79
FT /note="Acetylated histone H3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q15059"
FT REGION 147..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..482
FT /evidence="ECO:0000255"
FT COILED 646..689
FT /evidence="ECO:0000255"
FT COMPBIAS 13..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15059"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15059"
FT VAR_SEQ 468
FT /note="Q -> QTGCGAFQDQLLNVSSVQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010249"
FT CONFLICT 174
FT /note="S -> F (in Ref. 3; BAC36359)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="A -> T (in Ref. 2; AAH31536)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="A -> D (in Ref. 1; AAF78072)"
FT /evidence="ECO:0000305"
FT CONFLICT 659..660
FT /note="EE -> VV (in Ref. 1; AAF78072)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2L5E"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2L5E"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:2L5E"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:2L5E"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:2L5E"
SQ SEQUENCE 726 AA; 79762 MW; D5B2FC0ACA41D8ED CRC64;
MSTTAAAPTG IPAVPGPVNP PPPEVSNPSK PGRKTNQLQY MQNVVVKTLW KHQFAWPFYQ
PVDAIKLNLP DYHKIIKNPM DMGTIKKRLE NNYYWSASEC MQDFNTMFTN CYIYNKPTDD
IVLMAQALEK IFLQKVAQMP QEEVELLPPA PKGKGRKPAA GAQNAGSQQV AAVSSVSPAT
PFQNIPPTVS QTPVIAATPV PTITANVTSV PVPPPAAPPP PATPIVPVVP PTPPVVKKKG
VKRKADTTTP TTSAITASRS ESPPPLSEPK QAKVVARRES GGRPIKPPKK DLEDGEVPQH
AGKKGKLSEH LRHCDSILRE MLSKKHAAYA WPFYKPVDAE ALELHDYHDI IKHPMDLSTV
KRKMDSREYP DAQGFAADIR LMFSNCYKYN PPDHEVVAMA RKLQDVFEMR FAKMPDEPME
APALPAPTAP IVSKGAESSR SSEESSSDSG SSDSEEERAT RLAELQEQLK AVHEQLAALS
QAPVNKPKKK KEKKEKEKKK KDKDKDKEKE KHKAKSEEEK KAKAAPAAKQ AQQKKAPTKK
ANSTTTASRQ LKKGGKQASA SYDSEEEEEG LPMSYDEKRQ LSLDINRLPG EKLGRVVHII
QSREPSLRDS NPDEIEIDFE TLKPTTLREL ERYVKSCLQK KQRKPLSTSG KKQAAKSKEE
LAQEKKKELE KRLQDVSGQL NSKKPTKKEK SGSAPSGGPS RLSSSSSSES ASSSSSGSSS
DSSDSE
