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Bromodomain-containing protein 2 (Female sterile homeotic-related protein 1) (Fsrg-1) (Protein RING3)

 BRD2_MOUSE              Reviewed;         798 AA.
Q7JJ13; O54795; O88411; Q3UGI0; Q5DTS6; Q794H7; Q794H9; Q99PC5;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 114.
RecName: Full=Bromodomain-containing protein 2;
AltName: Full=Female sterile homeotic-related protein 1;
AltName: Full=Fsrg-1;
AltName: Full=Protein RING3;
Name=Brd2; Synonyms=Fsrg1, Kiaa4005, Ring3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
AND FUNCTION.
TISSUE=Testis;
PubMed=9811568;
Rhee K., Brunori M., Besset V., Trousdale R., Wolgemuth D.J.;
"Expression and potential role of Fsrg1, a murine bromodomain-
containing homologue of the Drosophila gene female sterile homeotic.";
J. Cell Sci. 111:3541-3550(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [GENOMIC DNA / MRNA] OF 1-549 (ISOFORM 2), TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
STRAIN=129/SvJ, and CD-1; TISSUE=Testis;
PubMed=9693039; DOI=10.1006/geno.1998.5262;
Taniguchi Y., Matsuzaka Y., Fujimoto H., Miyado K., Kohda A.,
Okumura K., Kimura M., Inoko H.;
"Nucleotide sequence of the ring3 gene in the class II region of the
mouse MHC and its abundant expression in testicular germ cells.";
Genomics 51:114-123(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9601950; DOI=10.1007/s002510050406;
Thorpe K.L., Beck S.;
"DNA sequence and structure of the mouse RING3 gene: identification of
variant RING3 transcripts.";
Immunogenetics 48:82-86(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129/SvJ;
Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L.,
Hall J., Lasky S., Hood L.;
"Sequence of the mouse major histocompatibility locus class II
region.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Amnion, and Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-503.
STRAIN=C57BL/6J;
Korf I.;
"Complete sequence of UL26B06.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-300, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-300 AND
SER-304, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Binds hyperacetylated chromatin and plays a role in the
regulation of transcription, probably by chromatin remodeling.
Regulates transcription of the CCND1 gene. Plays a role in
nucleosome assembly (By similarity). May play a role in
spermatogenesis or folliculogenesis. {ECO:0000250,
ECO:0000269|PubMed:9693039, ECO:0000269|PubMed:9811568}.
-!- SUBUNIT: Homodimer. Interacts with E2F1 and with histone H4
acetylated at 'Lys-13' (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9693039,
ECO:0000269|PubMed:9811568}. Note=Detected on chromatin and
nucleosomes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7JJ13-1; Sequence=Displayed;
Name=2;
IsoId=Q7JJ13-2; Sequence=VSP_022601;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in the testis,
followed by ovary, placenta, embryo and to a lower extent in
somatic tissues. {ECO:0000269|PubMed:9693039,
ECO:0000269|PubMed:9811568}.
-!- DOMAIN: One bromodomain is sufficient for a partial interaction
with histone H4 acetylated at 'Lys-13'. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BAD90273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF045462; AAC24810.1; -; mRNA.
EMBL; AB010246; BAA24377.1; -; mRNA.
EMBL; AB010247; BAA24378.1; -; mRNA.
EMBL; AB010248; BAA24379.1; -; mRNA.
EMBL; AB212273; BAD97682.1; -; mRNA.
EMBL; D89801; BAA25416.1; -; Genomic_DNA.
EMBL; AL009226; CAA15818.1; -; Genomic_DNA.
EMBL; AL009226; CAA15819.1; -; Genomic_DNA.
EMBL; AF100956; AAC69907.1; -; Genomic_DNA.
EMBL; AK147918; BAE28228.1; -; mRNA.
EMBL; AK158970; BAE34749.1; -; mRNA.
EMBL; AK168525; BAE40404.1; -; mRNA.
EMBL; AK220444; BAD90273.1; ALT_INIT; mRNA.
EMBL; AF318183; AAK07919.1; -; mRNA.
CCDS; CCDS28641.1; -. [Q7JJ13-1]
RefSeq; NP_001191902.1; NM_001204973.1. [Q7JJ13-1]
RefSeq; NP_034368.2; NM_010238.3. [Q7JJ13-1]
UniGene; Mm.3444; -.
ProteinModelPortal; Q7JJ13; -.
SMR; Q7JJ13; -.
BioGrid; 199750; 1.
IntAct; Q7JJ13; 1.
MINT; Q7JJ13; -.
STRING; 10090.ENSMUSP00000025193; -.
iPTMnet; Q7JJ13; -.
PhosphoSitePlus; Q7JJ13; -.
EPD; Q7JJ13; -.
PaxDb; Q7JJ13; -.
PeptideAtlas; Q7JJ13; -.
PRIDE; Q7JJ13; -.
Ensembl; ENSMUST00000025193; ENSMUSP00000025193; ENSMUSG00000024335. [Q7JJ13-1]
Ensembl; ENSMUST00000114242; ENSMUSP00000109880; ENSMUSG00000024335. [Q7JJ13-1]
GeneID; 14312; -.
KEGG; mmu:14312; -.
UCSC; uc008cbi.1; mouse. [Q7JJ13-1]
CTD; 6046; -.
MGI; MGI:99495; Brd2.
eggNOG; KOG1474; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00920000148952; -.
HOVERGEN; HBG004896; -.
InParanoid; Q7JJ13; -.
KO; K08871; -.
OMA; PTGYDSE; -.
OrthoDB; EOG091G01QC; -.
PhylomeDB; Q7JJ13; -.
TreeFam; TF317345; -.
Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
ChiTaRS; Brd2; mouse.
PRO; PR:Q7JJ13; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024335; Expressed in 328 organ(s), highest expression level in rostral migratory stream.
CleanEx; MM_BRD2; -.
ExpressionAtlas; Q7JJ13; baseline and differential.
Genevisible; Q7JJ13; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.220; -; 1.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR027353; NET_dom.
InterPro; IPR038336; NET_sf.
Pfam; PF17035; BET; 1.
Pfam; PF00439; Bromodomain; 2.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS00633; BROMODOMAIN_1; 2.
PROSITE; PS50014; BROMODOMAIN_2; 2.
PROSITE; PS51525; NET; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Transcription; Transcription regulation.
CHAIN 1 798 Bromodomain-containing protein 2.
/FTId=PRO_0000274005.
DOMAIN 90 162 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 363 435 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 630 712 NET. {ECO:0000255|PROSITE-
ProRule:PRU00857}.
MOTIF 553 557 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 60 63 Poly-Pro.
COMPBIAS 228 331 Pro-rich.
COMPBIAS 478 523 Glu-rich.
COMPBIAS 549 557 Poly-Lys.
COMPBIAS 589 592 Poly-Gly.
COMPBIAS 632 636 Poly-Glu.
COMPBIAS 761 797 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P25440}.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000250|UniProtKB:P25440}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:P25440}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000250|UniProtKB:P25440}.
VAR_SEQ 1 46 Missing (in isoform 2).
{ECO:0000303|PubMed:9693039}.
/FTId=VSP_022601.
CONFLICT 169 169 E -> K (in Ref. 5; BAE28228).
{ECO:0000305}.
CONFLICT 199 199 A -> G (in Ref. 1; AAC24810).
{ECO:0000305}.
CONFLICT 691 691 P -> L (in Ref. 6; BAD90273).
{ECO:0000305}.
CONFLICT 765 767 QVA -> LVP (in Ref. 1; AAC24810).
{ECO:0000305}.
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


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