BRD2_MOUSE
ID BRD2_MOUSE Reviewed; 798 AA.
AC Q7JJ13; O54795; O88411; Q3UGI0; Q5DTS6; Q794H7; Q794H9; Q99PC5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Bromodomain-containing protein 2;
DE AltName: Full=Female sterile homeotic-related protein 1;
DE AltName: Full=Fsrg-1;
DE AltName: Full=Protein RING3;
GN Name=Brd2; Synonyms=Fsrg1, Kiaa4005, Ring3;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC TISSUE=Testis;
RX PubMed=9811568; DOI=10.1242/jcs.111.23.3541;
RA Rhee K., Brunori M., Besset V., Trousdale R., Wolgemuth D.J.;
RT "Expression and potential role of Fsrg1, a murine bromodomain-containing
RT homologue of the Drosophila gene female sterile homeotic.";
RL J. Cell Sci. 111:3541-3550(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA / MRNA] OF 1-549 (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RC STRAIN=129/SvJ, and CD-1; TISSUE=Testis;
RX PubMed=9693039; DOI=10.1006/geno.1998.5262;
RA Taniguchi Y., Matsuzaka Y., Fujimoto H., Miyado K., Kohda A., Okumura K.,
RA Kimura M., Inoko H.;
RT "Nucleotide sequence of the ring3 gene in the class II region of the mouse
RT MHC and its abundant expression in testicular germ cells.";
RL Genomics 51:114-123(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9601950; DOI=10.1007/s002510050406;
RA Thorpe K.L., Beck S.;
RT "DNA sequence and structure of the mouse RING3 gene: identification of
RT variant RING3 transcripts.";
RL Immunogenetics 48:82-86(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Visual cortex;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA 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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-503.
RC STRAIN=C57BL/6J;
RA Korf I.;
RT "Complete sequence of UL26B06.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-300, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-300 AND SER-304, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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).
CC -!- FUNCTION: Binds hyperacetylated chromatin and plays a role in the
CC regulation of transcription, probably by chromatin remodeling.
CC Regulates transcription of the CCND1 gene. Plays a role in nucleosome
CC assembly (By similarity). May play a role in spermatogenesis or
CC folliculogenesis. {ECO:0000250, ECO:0000269|PubMed:9693039,
CC ECO:0000269|PubMed:9811568}.
CC -!- SUBUNIT: Homodimer. Interacts with E2F1 and with histone H4 acetylated
CC at 'Lys-13' (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9693039,
CC ECO:0000269|PubMed:9811568}. Note=Detected on chromatin and
CC nucleosomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7JJ13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7JJ13-2; Sequence=VSP_022601;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the testis, followed by
CC ovary, placenta, embryo and to a lower extent in somatic tissues.
CC {ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}.
CC -!- DOMAIN: One bromodomain is sufficient for a partial interaction with
CC histone H4 acetylated at 'Lys-13'. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90273.1; 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; AF045462; AAC24810.1; -; mRNA.
DR EMBL; AB010246; BAA24377.1; -; mRNA.
DR EMBL; AB010247; BAA24378.1; -; mRNA.
DR EMBL; AB010248; BAA24379.1; -; mRNA.
DR EMBL; AB212273; BAD97682.1; -; mRNA.
DR EMBL; D89801; BAA25416.1; -; Genomic_DNA.
DR EMBL; AL009226; CAA15818.1; -; Genomic_DNA.
DR EMBL; AL009226; CAA15819.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69907.1; -; Genomic_DNA.
DR EMBL; AK147918; BAE28228.1; -; mRNA.
DR EMBL; AK158970; BAE34749.1; -; mRNA.
DR EMBL; AK168525; BAE40404.1; -; mRNA.
DR EMBL; AK220444; BAD90273.1; ALT_INIT; mRNA.
DR EMBL; AF318183; AAK07919.1; -; mRNA.
DR CCDS; CCDS28641.1; -. [Q7JJ13-1]
DR RefSeq; NP_001191902.1; NM_001204973.1. [Q7JJ13-1]
DR RefSeq; NP_034368.2; NM_010238.3. [Q7JJ13-1]
DR AlphaFoldDB; Q7JJ13; -.
DR SMR; Q7JJ13; -.
DR BioGRID; 199750; 7.
DR STRING; 10090.ENSMUSP00000109880; -.
DR iPTMnet; Q7JJ13; -.
DR PhosphoSitePlus; Q7JJ13; -.
DR EPD; Q7JJ13; -.
DR jPOST; Q7JJ13; -.
DR MaxQB; Q7JJ13; -.
DR PaxDb; Q7JJ13; -.
DR PeptideAtlas; Q7JJ13; -.
DR PRIDE; Q7JJ13; -.
DR ProteomicsDB; 265230; -. [Q7JJ13-1]
DR ProteomicsDB; 265231; -. [Q7JJ13-2]
DR Antibodypedia; 28816; 390 antibodies from 39 providers.
DR DNASU; 14312; -.
DR Ensembl; ENSMUST00000025193; ENSMUSP00000025193; ENSMUSG00000024335. [Q7JJ13-1]
DR Ensembl; ENSMUST00000095347; ENSMUSP00000092990; ENSMUSG00000024335. [Q7JJ13-2]
DR Ensembl; ENSMUST00000114242; ENSMUSP00000109880; ENSMUSG00000024335. [Q7JJ13-1]
DR GeneID; 14312; -.
DR KEGG; mmu:14312; -.
DR UCSC; uc008cbi.1; mouse. [Q7JJ13-1]
DR CTD; 6046; -.
DR MGI; MGI:99495; Brd2.
DR VEuPathDB; HostDB:ENSMUSG00000024335; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR HOGENOM; CLU_001499_0_4_1; -.
DR InParanoid; Q7JJ13; -.
DR OMA; MNIPHYP; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; Q7JJ13; -.
DR TreeFam; TF317345; -.
DR Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
DR BioGRID-ORCS; 14312; 21 hits in 76 CRISPR screens.
DR ChiTaRS; Brd2; mouse.
DR PRO; PR:Q7JJ13; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q7JJ13; protein.
DR Bgee; ENSMUSG00000024335; Expressed in embryonic post-anal tail and 294 other tissues.
DR ExpressionAtlas; Q7JJ13; baseline and differential.
DR Genevisible; Q7JJ13; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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 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 Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..798
FT /note="Bromodomain-containing protein 2"
FT /id="PRO_0000274005"
FT DOMAIN 90..162
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 363..435
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 630..712
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 553..557
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 311..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..561
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9693039"
FT /id="VSP_022601"
FT CONFLICT 169
FT /note="E -> K (in Ref. 5; BAE28228)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> G (in Ref. 1; AAC24810)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="P -> L (in Ref. 6; BAD90273)"
FT /evidence="ECO:0000305"
FT CONFLICT 765..767
FT /note="QVA -> LVP (in Ref. 1; AAC24810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 88067 MW; 08DD57FBF1385E96 CRC64;
MLQNVTPHKL PGEGNAGLLG LGPEAAAPGK RIRKPSLLYE GFESPTMASV PALQLAPANP
PPPEVSNPKK PGRVTNQLQY LHKVVMKALW KHQFAWPFRQ PVDAVKLGLP DYHKIIKQPM
DMGTIKRRLE NNYYWAASEC MQDFNTMFTN CYIYNKPTDD IVLMAQTLEK IFLQKVASMP
QEEQELVVTI PKNSHKKGAK LAALQGSITS AHQVPAVSSV SHTALYTPPP EIPTTVLNIP
HPSVISSPLL KSLHSAGPPL LAVSAAPPAQ PLAKKKGVKR KADTTTPTPT AILAPGSPAS
PPGSLEPKAA RLPPMRRESG RPIKPPRKDL PDSQQQHQSS KKGKLSEQLK HCNGILKELL
SKKHAAYAWP FYKPVDASAL GLHDYHDIIK HPMDLSTVKR KMENRDYRDA QEFAADVRLM
FSNCYKYNPP DHDVVAMARK LQDVFEFRYA KMPDEPLEPG PLPVSTALPP GLTKSSSESS
SEESSSESSS EEEEEEEEDE DEEESESSDS EEERAHRLAE LQEQLRAVHE QLAALSQGPI
SKPKRKREKK EKKKKRKAEK HRGRIGIDED DKGPRAPRPP QPKKSKKAGG GGSNATTLSH
PGFGTSGGSS NKLPKKSQKT APPVLPTGYD SEEEEESRPM SYDEKRQLSL DINKLPGEKL
GRVVHIIQAR EPSLRDSNPE EIEIDFETLK PSTLRELERY VLSCLRKKPR KPYTIRKPVG
KTKEELALEK KRELEKRLQD VSGQLNSTKK PPKKASEKTE SSAQQVAVSR LSASSSSSDS
SSSSSSSSSS DTSDSDSG
