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Bromodomain-containing protein 2 (O27.1.1) (Really interesting new gene 3 protein)

 BRD2_HUMAN              Reviewed;         801 AA.
P25440; A2AAU0; B0S7P0; B1AZT1; O00699; O00700; Q15310; Q5STC9;
Q63HQ9; Q658Y7; Q6P3U2; Q969U4;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
23-MAY-2018, entry version 183.
RecName: Full=Bromodomain-containing protein 2;
AltName: Full=O27.1.1;
AltName: Full=Really interesting new gene 3 protein;
Name=BRD2; Synonyms=KIAA9001, RING3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=T-cell;
PubMed=1352711; DOI=10.3109/10425179209020804;
Beck S., Hanson I., Kelly A., Pappin D.J.C., Trowsdale J.;
"A homologue of the Drosophila female sterile homeotic (fsh) gene in
the class II region of the human MHC.";
DNA Seq. 2:203-210(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO
N-TERMINUS.
PubMed=8781126; DOI=10.1007/BF02602785;
Thorpe K.L., Abdulla S., Kaufman J., Trowsdale J., Beck S.;
"Phylogeny and structure of the RING3 gene.";
Immunogenetics 44:391-396(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki T., Ishikawa K., Tabata S.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Bone marrow, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-238.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND INTERACTION WITH ACETYLATED CHROMATIN.
PubMed=18406326; DOI=10.1016/j.molcel.2008.01.018;
LeRoy G., Rickards B., Flint S.J.;
"The double bromodomain proteins Brd2 and Brd3 couple histone
acetylation to transcription.";
Mol. Cell 30:51-60(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301; SER-305
AND SER-633, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-298 AND SER-301,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-6; SER-298 AND SER-301, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-633, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301 AND
SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 73-194, HOMODIMERIZATION,
INTERACTION WITH E2F1 AND HISTONE H4, AND MUTAGENESIS OF GLN-78;
142-MET-GLN-143; TYR-153; ILE-154; GLU-170; LEU-174; VAL-177 AND
GLN-182.
PubMed=17148447; DOI=10.1074/jbc.M605971200;
Nakamura Y., Umehara T., Nakano K., Jang M.K., Shirouzu M., Morita S.,
Uda-Tochio H., Hamana H., Terada T., Adachi N., Matsumoto T.,
Tanaka A., Horikoshi M., Ozato K., Padmanabhan B., Yokoyama S.;
"Crystal structure of the human BRD2 bromodomain: insights into
dimerization and recognition of acetylated histone h4.";
J. Biol. Chem. 282:4193-4201(2007).
[18]
X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 344-452.
PubMed=20871596; DOI=10.1038/nature09504;
Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O.,
Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M.,
Munro S., McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J.,
Schwartz B., Heightman T.D., La Thangue N., French C.A., Wiest O.,
Kung A.L., Knapp S., Bradner J.E.;
"Selective inhibition of BET bromodomains.";
Nature 468:1067-1073(2010).
[19]
VARIANTS [LARGE SCALE ANALYSIS] GLU-30; GLY-49; SER-49; PRO-212;
PHE-238; GLN-260; VAL-474; GLY-558; THR-569; PRO-599 AND LEU-714.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: May play a role in spermatogenesis or folliculogenesis
(By similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:18406326}.
-!- SUBUNIT: Homodimer. Interacts with E2F1 and with histone H4
acetylated at 'Lys-13'. {ECO:0000269|PubMed:17148447,
ECO:0000269|PubMed:18406326}.
-!- INTERACTION:
P62805:HIST2H4B; NbExp=5; IntAct=EBI-2874802, EBI-302023;
Q13761:RUNX3; NbExp=8; IntAct=EBI-2874802, EBI-925990;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Detected on
chromatin and nucleosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P25440-1; Sequence=Displayed;
Name=2;
IsoId=P25440-2; Sequence=VSP_022600;
Note=No experimental confirmation available.;
Name=3;
IsoId=P25440-3; Sequence=VSP_055029;
Name=4;
IsoId=P25440-4; Sequence=VSP_055028;
-!- DOMAIN: One bromodomain is sufficient for a partial interaction
with histone H4 acetylated at 'Lys-13'.
-!- SEQUENCE CAUTION:
Sequence=AAA68890.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X62083; CAA43996.1; -; mRNA.
EMBL; M80613; AAA68890.1; ALT_INIT; mRNA.
EMBL; X96670; CAA65450.1; -; Genomic_DNA.
EMBL; Z96104; CAC69989.1; -; Genomic_DNA.
EMBL; D42040; BAA07641.1; -; mRNA.
EMBL; BX647233; CAH56179.1; -; mRNA.
EMBL; BX648109; CAH56171.1; -; mRNA.
EMBL; AL832722; CAH56208.1; -; mRNA.
EMBL; AL645941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX005422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX908719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR936909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03662.1; -; Genomic_DNA.
EMBL; CH471081; EAX03663.1; -; Genomic_DNA.
EMBL; BC063840; AAH63840.1; -; mRNA.
CCDS; CCDS4762.1; -. [P25440-1]
CCDS; CCDS56420.1; -. [P25440-2]
CCDS; CCDS56421.1; -. [P25440-3]
PIR; A56619; A56619.
RefSeq; NP_001106653.1; NM_001113182.2. [P25440-1]
RefSeq; NP_001186384.1; NM_001199455.1. [P25440-2]
RefSeq; NP_001186385.1; NM_001199456.1. [P25440-3]
RefSeq; NP_001278915.1; NM_001291986.1. [P25440-4]
RefSeq; NP_005095.1; NM_005104.3. [P25440-1]
UniGene; Hs.734797; -.
UniGene; Hs.75243; -.
PDB; 1X0J; X-ray; 1.80 A; A/B/C=73-194.
PDB; 2DVQ; X-ray; 2.04 A; A/B/C=73-194.
PDB; 2DVR; X-ray; 2.30 A; A/B/C=73-194.
PDB; 2DVS; X-ray; 2.04 A; A/B/C=73-194.
PDB; 2DVV; X-ray; 1.80 A; A=348-455.
PDB; 2E3K; X-ray; 2.30 A; A/B/C/D=348-455.
PDB; 2G4A; NMR; -; A=348-455.
PDB; 2YDW; X-ray; 1.90 A; A/B/C=67-200.
PDB; 2YEK; X-ray; 1.98 A; A/B/C=67-200.
PDB; 3AQA; X-ray; 2.30 A; A/B/C=73-194.
PDB; 3ONI; X-ray; 1.61 A; A=344-455.
PDB; 4A9E; X-ray; 1.91 A; A/B/C=67-200.
PDB; 4A9F; X-ray; 1.73 A; A/B/C=67-200.
PDB; 4A9H; X-ray; 2.05 A; A/B/C=67-200.
PDB; 4A9I; X-ray; 2.25 A; A/B/C=67-200.
PDB; 4A9J; X-ray; 1.90 A; A/B/C=67-200.
PDB; 4A9M; X-ray; 2.06 A; A/B/C=67-200.
PDB; 4A9N; X-ray; 1.85 A; A/B/C=67-200.
PDB; 4A9O; X-ray; 1.78 A; A/B/C=67-200.
PDB; 4AKN; X-ray; 1.82 A; A/B/C=67-200.
PDB; 4ALG; X-ray; 1.60 A; A=67-200.
PDB; 4ALH; X-ray; 1.78 A; A/B/C=67-200.
PDB; 4J1P; X-ray; 1.08 A; A=344-455.
PDB; 4MR5; X-ray; 1.63 A; A=344-455.
PDB; 4MR6; X-ray; 1.67 A; A=344-455.
PDB; 4QEU; X-ray; 1.50 A; A=344-455.
PDB; 4QEV; X-ray; 1.80 A; A=344-455.
PDB; 4QEW; X-ray; 1.70 A; A=344-455.
PDB; 4UYF; X-ray; 1.60 A; A/B/C=67-200.
PDB; 4UYG; X-ray; 2.50 A; A/B/C/D/E/F=338-473.
PDB; 4UYH; X-ray; 1.73 A; A/B/C=67-200.
PDB; 5BT5; X-ray; 1.40 A; A=344-455.
PDB; 5DFB; X-ray; 1.40 A; A=344-455.
PDB; 5DFC; X-ray; 1.50 A; A=344-455.
PDB; 5DFD; X-ray; 1.50 A; A=344-455.
PDB; 5DW1; X-ray; 1.55 A; A/B/C/D=345-455.
PDB; 5EK9; X-ray; 2.08 A; A/B=344-455.
PDB; 5HEL; X-ray; 1.45 A; A=71-194.
PDB; 5HEM; X-ray; 1.65 A; A/B=71-194.
PDB; 5HEN; X-ray; 1.79 A; A/B/C=71-194.
PDB; 5HFQ; X-ray; 1.40 A; A=344-455.
PDB; 5IBN; X-ray; 0.94 A; A=348-455.
PDB; 5IG6; X-ray; 0.91 A; A=348-454.
PDB; 5N2L; X-ray; 1.89 A; A/B/C/D=344-455.
PDB; 5O38; X-ray; 1.20 A; A=344-455.
PDB; 5O39; X-ray; 1.74 A; A=344-455.
PDB; 5O3A; X-ray; 2.40 A; A=344-455.
PDB; 5O3B; X-ray; 1.95 A; A/B/C/D=344-455.
PDB; 5O3C; X-ray; 1.60 A; A=344-455.
PDB; 5O3D; X-ray; 1.60 A; A=345-455.
PDB; 5O3E; X-ray; 1.40 A; A=344-455.
PDB; 5O3F; X-ray; 1.75 A; A=344-455.
PDB; 5O3G; X-ray; 1.85 A; A/B=344-455.
PDB; 5O3H; X-ray; 1.40 A; A=344-455.
PDB; 5O3I; X-ray; 1.20 A; A=344-455.
PDB; 5U5S; NMR; -; A=344-455.
PDB; 5U6V; X-ray; 1.77 A; A=347-455.
PDB; 5UEW; X-ray; 1.83 A; A/B=347-454.
PDB; 5XHE; X-ray; 1.40 A; A=348-455.
PDB; 5XHK; X-ray; 1.28 A; A=348-455.
PDBsum; 1X0J; -.
PDBsum; 2DVQ; -.
PDBsum; 2DVR; -.
PDBsum; 2DVS; -.
PDBsum; 2DVV; -.
PDBsum; 2E3K; -.
PDBsum; 2G4A; -.
PDBsum; 2YDW; -.
PDBsum; 2YEK; -.
PDBsum; 3AQA; -.
PDBsum; 3ONI; -.
PDBsum; 4A9E; -.
PDBsum; 4A9F; -.
PDBsum; 4A9H; -.
PDBsum; 4A9I; -.
PDBsum; 4A9J; -.
PDBsum; 4A9M; -.
PDBsum; 4A9N; -.
PDBsum; 4A9O; -.
PDBsum; 4AKN; -.
PDBsum; 4ALG; -.
PDBsum; 4ALH; -.
PDBsum; 4J1P; -.
PDBsum; 4MR5; -.
PDBsum; 4MR6; -.
PDBsum; 4QEU; -.
PDBsum; 4QEV; -.
PDBsum; 4QEW; -.
PDBsum; 4UYF; -.
PDBsum; 4UYG; -.
PDBsum; 4UYH; -.
PDBsum; 5BT5; -.
PDBsum; 5DFB; -.
PDBsum; 5DFC; -.
PDBsum; 5DFD; -.
PDBsum; 5DW1; -.
PDBsum; 5EK9; -.
PDBsum; 5HEL; -.
PDBsum; 5HEM; -.
PDBsum; 5HEN; -.
PDBsum; 5HFQ; -.
PDBsum; 5IBN; -.
PDBsum; 5IG6; -.
PDBsum; 5N2L; -.
PDBsum; 5O38; -.
PDBsum; 5O39; -.
PDBsum; 5O3A; -.
PDBsum; 5O3B; -.
PDBsum; 5O3C; -.
PDBsum; 5O3D; -.
PDBsum; 5O3E; -.
PDBsum; 5O3F; -.
PDBsum; 5O3G; -.
PDBsum; 5O3H; -.
PDBsum; 5O3I; -.
PDBsum; 5U5S; -.
PDBsum; 5U6V; -.
PDBsum; 5UEW; -.
PDBsum; 5XHE; -.
PDBsum; 5XHK; -.
ProteinModelPortal; P25440; -.
SMR; P25440; -.
BioGrid; 111973; 41.
DIP; DIP-60835N; -.
IntAct; P25440; 23.
MINT; P25440; -.
STRING; 9606.ENSP00000378702; -.
BindingDB; P25440; -.
ChEMBL; CHEMBL1293289; -.
GuidetoPHARMACOLOGY; 1944; -.
iPTMnet; P25440; -.
PhosphoSitePlus; P25440; -.
BioMuta; BRD2; -.
DMDM; 12230989; -.
EPD; P25440; -.
MaxQB; P25440; -.
PaxDb; P25440; -.
PeptideAtlas; P25440; -.
PRIDE; P25440; -.
DNASU; 6046; -.
Ensembl; ENST00000374825; ENSP00000363958; ENSG00000204256. [P25440-1]
Ensembl; ENST00000374831; ENSP00000363964; ENSG00000204256. [P25440-1]
Ensembl; ENST00000383108; ENSP00000372588; ENSG00000234507. [P25440-1]
Ensembl; ENST00000395287; ENSP00000378702; ENSG00000204256. [P25440-2]
Ensembl; ENST00000399527; ENSP00000382443; ENSG00000215077. [P25440-2]
Ensembl; ENST00000399528; ENSP00000382444; ENSG00000215077. [P25440-1]
Ensembl; ENST00000399529; ENSP00000382445; ENSG00000215077. [P25440-1]
Ensembl; ENST00000414731; ENSP00000391246; ENSG00000234704.
Ensembl; ENST00000436979; ENSP00000405634; ENSG00000235307. [P25440-3]
Ensembl; ENST00000438194; ENSP00000401791; ENSG00000234507. [P25440-1]
Ensembl; ENST00000442863; ENSP00000410994; ENSG00000234507. [P25440-2]
Ensembl; ENST00000448067; ENSP00000412885; ENSG00000235307. [P25440-2]
Ensembl; ENST00000449085; ENSP00000409145; ENSG00000204256. [P25440-3]
Ensembl; ENST00000449118; ENSP00000399009; ENSG00000234704.
Ensembl; ENST00000549126; ENSP00000449380; ENSG00000235307. [P25440-1]
Ensembl; ENST00000552587; ENSP00000449609; ENSG00000235307. [P25440-1]
GeneID; 6046; -.
KEGG; hsa:6046; -.
UCSC; uc003ocn.4; human. [P25440-1]
CTD; 6046; -.
DisGeNET; 6046; -.
EuPathDB; HostDB:ENSG00000204256.12; -.
GeneCards; BRD2; -.
HGNC; HGNC:1103; BRD2.
HPA; HPA042816; -.
MIM; 601540; gene.
neXtProt; NX_P25440; -.
OpenTargets; ENSG00000204256; -.
PharmGKB; PA25414; -.
eggNOG; KOG1474; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119206; -.
HOGENOM; HOG000231200; -.
HOVERGEN; HBG004896; -.
InParanoid; P25440; -.
KO; K08871; -.
OMA; PTGYDSE; -.
OrthoDB; EOG091G01QC; -.
PhylomeDB; P25440; -.
TreeFam; TF317345; -.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SIGNOR; P25440; -.
ChiTaRS; BRD2; human.
EvolutionaryTrace; P25440; -.
GeneWiki; BRD2; -.
GenomeRNAi; 6046; -.
PRO; PR:P25440; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204256; -.
CleanEx; HS_BRD2; -.
ExpressionAtlas; P25440; baseline and differential.
Genevisible; P25440; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
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;
3D-structure; Acetylation; Alternative splicing; Bromodomain;
Chromatin regulator; Complete proteome; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 801 Bromodomain-containing protein 2.
/FTId=PRO_0000211180.
DOMAIN 91 163 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 364 436 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 632 714 NET. {ECO:0000255|PROSITE-
ProRule:PRU00857}.
MOTIF 555 559 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 61 64 Poly-Pro.
COMPBIAS 476 515 Glu/Ser-rich.
COMPBIAS 492 506 Poly-Glu.
COMPBIAS 544 566 Arg/Lys-rich (highly basic).
COMPBIAS 551 559 Poly-Lys.
COMPBIAS 634 638 Poly-Glu.
COMPBIAS 775 801 Ser-rich.
COMPBIAS 775 793 Poly-Ser.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231}.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 120 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_055028.
VAR_SEQ 1 47 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_055029.
VAR_SEQ 615 615 L -> LQAGVQWRDLGLLQPPLLGFKRFSCLSLPSSQDYRL
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022600.
VARIANT 30 30 G -> E (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041904.
VARIANT 49 49 A -> G (in dbSNP:rs3918144).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041905.
VARIANT 49 49 A -> S (in dbSNP:rs55669504).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041906.
VARIANT 212 212 A -> P (in dbSNP:rs35952031).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041907.
VARIANT 238 238 L -> F (in dbSNP:rs176250).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_022132.
VARIANT 260 260 P -> Q (in dbSNP:rs35294809).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041908.
VARIANT 474 474 A -> V (in dbSNP:rs3918143).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_029300.
VARIANT 547 547 R -> K (in dbSNP:rs1049369).
/FTId=VAR_029301.
VARIANT 558 558 R -> G (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041909.
VARIANT 569 569 A -> T (in dbSNP:rs34530779).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041910.
VARIANT 599 599 A -> P (in dbSNP:rs55952113).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041911.
VARIANT 714 714 P -> L (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041912.
MUTAGEN 78 78 Q->A: Loss of homodimerization.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 142 143 MQ->AA: Loss of homodimerization.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 153 153 Y->K: Loss of homodimerization.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 154 154 I->A: Partial loss of homodimerization;
when associated with A-182.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 170 170 E->A: Loss of homodimerization.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 174 174 L->E: Loss of homodimerization.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 177 177 V->E: Loss of homodimerization.
{ECO:0000269|PubMed:17148447}.
MUTAGEN 182 182 Q->A: Partial loss of homodimerization;
when associated with A-154.
{ECO:0000269|PubMed:17148447}.
CONFLICT 490 490 S -> F (in Ref. 4; CAH56179).
{ECO:0000305}.
HELIX 77 84 {ECO:0000244|PDB:5HEL}.
HELIX 86 91 {ECO:0000244|PDB:5HEL}.
HELIX 97 99 {ECO:0000244|PDB:5HEL}.
HELIX 105 108 {ECO:0000244|PDB:5HEL}.
HELIX 113 116 {ECO:0000244|PDB:5HEL}.
HELIX 123 131 {ECO:0000244|PDB:5HEL}.
HELIX 138 155 {ECO:0000244|PDB:5HEL}.
HELIX 161 177 {ECO:0000244|PDB:5HEL}.
HELIX 348 360 {ECO:0000244|PDB:5IG6}.
HELIX 363 365 {ECO:0000244|PDB:5IG6}.
HELIX 366 369 {ECO:0000244|PDB:5IG6}.
HELIX 370 372 {ECO:0000244|PDB:5IG6}.
HELIX 378 381 {ECO:0000244|PDB:5IG6}.
HELIX 386 389 {ECO:0000244|PDB:5IG6}.
HELIX 396 404 {ECO:0000244|PDB:5IG6}.
TURN 406 408 {ECO:0000244|PDB:2G4A}.
HELIX 411 428 {ECO:0000244|PDB:5IG6}.
STRAND 431 433 {ECO:0000244|PDB:5U5S}.
HELIX 434 450 {ECO:0000244|PDB:5IG6}.
SEQUENCE 801 AA; 88061 MW; 9A075EEB13507D8E CRC64;
MLQNVTPHNK LPGEGNAGLL GLGPEAAAPG KRIRKPSLLY EGFESPTMAS VPALQLTPAN
PPPPEVSNPK KPGRVTNQLQ YLHKVVMKAL WKHQFAWPFR QPVDAVKLGL PDYHKIIKQP
MDMGTIKRRL ENNYYWAASE CMQDFNTMFT NCYIYNKPTD DIVLMAQTLE KIFLQKVASM
PQEEQELVVT IPKNSHKKGA KLAALQGSVT SAHQVPAVSS VSHTALYTPP PEIPTTVLNI
PHPSVISSPL LKSLHSAGPP LLAVTAAPPA QPLAKKKGVK RKADTTTPTP TAILAPGSPA
SPPGSLEPKA ARLPPMRRES GRPIKPPRKD LPDSQQQHQS SKKGKLSEQL KHCNGILKEL
LSKKHAAYAW PFYKPVDASA LGLHDYHDII KHPMDLSTVK RKMENRDYRD AQEFAADVRL
MFSNCYKYNP PDHDVVAMAR KLQDVFEFRY AKMPDEPLEP GPLPVSTAMP PGLAKSSSES
SSEESSSESS SEEEEEEDEE DEEEEESESS DSEEERAHRL AELQEQLRAV HEQLAALSQG
PISKPKRKRE KKEKKKKRKA EKHRGRAGAD EDDKGPRAPR PPQPKKSKKA SGSGGGSAAL
GPSGFGPSGG SGTKLPKKAT KTAPPALPTG YDSEEEEESR PMSYDEKRQL SLDINKLPGE
KLGRVVHIIQ AREPSLRDSN PEEIEIDFET LKPSTLRELE RYVLSCLRKK PRKPYTIKKP
VGKTKEELAL EKKRELEKRL QDVSGQLNST KKPPKKANEK TESSSAQQVA VSRLSASSSS
SDSSSSSSSS SSSDTSDSDS G


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