BRD2_HUMAN
ID BRD2_HUMAN Reviewed; 801 AA.
AC P25440; A2AAU0; B0S7P0; B1AZT1; O00699; O00700; Q15310; Q5STC9; Q63HQ9;
AC Q658Y7; Q6P3U2; Q969U4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Bromodomain-containing protein 2;
DE AltName: Full=O27.1.1;
DE AltName: Full=Really interesting new gene 3 protein;
GN Name=BRD2; Synonyms=KIAA9001, RING3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=1352711; DOI=10.3109/10425179209020804;
RA Beck S., Hanson I., Kelly A., Pappin D.J.C., Trowsdale J.;
RT "A homologue of the Drosophila female sterile homeotic (fsh) gene in the
RT class II region of the human MHC.";
RL DNA Seq. 2:203-210(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=8781126; DOI=10.1007/bf02602785;
RA Thorpe K.L., Abdulla S., Kaufman J., Trowsdale J., Beck S.;
RT "Phylogeny and structure of the RING3 gene.";
RL Immunogenetics 44:391-396(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki T., Ishikawa K., Tabata S.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Bone marrow, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-238.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [8]
RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION).
RX PubMed=16227282; DOI=10.1128/jvi.79.21.13618-13629.2005;
RA Viejo-Borbolla A., Ottinger M., Bruening E., Buerger A., Koenig R.,
RA Kati E., Sheldon J.A., Schulz T.F.;
RT "Brd2/RING3 interacts with a chromatin-binding domain in the Kaposi's
RT Sarcoma-associated herpesvirus latency-associated nuclear antigen 1 (LANA-
RT 1) that is required for multiple functions of LANA-1.";
RL J. Virol. 79:13618-13629(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH ACETYLATED CHROMATIN.
RX PubMed=18406326; DOI=10.1016/j.molcel.2008.01.018;
RA LeRoy G., Rickards B., Flint S.J.;
RT "The double bromodomain proteins Brd2 and Brd3 couple histone acetylation
RT to transcription.";
RL Mol. Cell 30:51-60(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301; SER-305 AND
RP SER-633, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-298 AND SER-301, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-6; SER-298 AND SER-301, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-633, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301 AND SER-305, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 73-194, HOMODIMERIZATION,
RP INTERACTION WITH E2F1 AND HISTONE H4, AND MUTAGENESIS OF GLN-78;
RP 142-MET-GLN-143; TYR-153; ILE-154; GLU-170; LEU-174; VAL-177 AND GLN-182.
RX PubMed=17148447; DOI=10.1074/jbc.m605971200;
RA Nakamura Y., Umehara T., Nakano K., Jang M.K., Shirouzu M., Morita S.,
RA Uda-Tochio H., Hamana H., Terada T., Adachi N., Matsumoto T., Tanaka A.,
RA Horikoshi M., Ozato K., Padmanabhan B., Yokoyama S.;
RT "Crystal structure of the human BRD2 bromodomain: insights into
RT dimerization and recognition of acetylated histone h4.";
RL J. Biol. Chem. 282:4193-4201(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 344-452.
RX PubMed=20871596; DOI=10.1038/nature09504;
RA Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O.,
RA Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M., Munro S.,
RA McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J., Schwartz B.,
RA Heightman T.D., La Thangue N., French C.A., Wiest O., Kung A.L., Knapp S.,
RA Bradner J.E.;
RT "Selective inhibition of BET bromodomains.";
RL Nature 468:1067-1073(2010).
RN [20]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-30; GLY-49; SER-49; PRO-212; PHE-238;
RP GLN-260; VAL-474; GLY-558; THR-569; PRO-599 AND LEU-714.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: May play a role in spermatogenesis or folliculogenesis (By
CC similarity). 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. {ECO:0000250, ECO:0000269|PubMed:18406326}.
CC -!- SUBUNIT: Homodimer. Interacts with E2F1 and with histone H4 acetylated
CC at 'Lys-13'. {ECO:0000269|PubMed:17148447,
CC ECO:0000269|PubMed:18406326}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein
CC LANA1. {ECO:0000269|PubMed:16227282}.
CC -!- INTERACTION:
CC P25440; P62805: H4C9; NbExp=5; IntAct=EBI-2874802, EBI-302023;
CC P25440; Q13761: RUNX3; NbExp=8; IntAct=EBI-2874802, EBI-925990;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Detected on chromatin
CC and nucleosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P25440-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25440-2; Sequence=VSP_022600;
CC Name=3;
CC IsoId=P25440-3; Sequence=VSP_055029;
CC Name=4;
CC IsoId=P25440-4; Sequence=VSP_055028;
CC -!- DOMAIN: One bromodomain is sufficient for a partial interaction with
CC histone H4 acetylated at 'Lys-13'.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68890.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X62083; CAA43996.1; -; mRNA.
DR EMBL; M80613; AAA68890.1; ALT_INIT; mRNA.
DR EMBL; X96670; CAA65450.1; -; Genomic_DNA.
DR EMBL; Z96104; CAC69989.1; -; Genomic_DNA.
DR EMBL; D42040; BAA07641.1; -; mRNA.
DR EMBL; BX647233; CAH56179.1; -; mRNA.
DR EMBL; BX648109; CAH56171.1; -; mRNA.
DR EMBL; AL832722; CAH56208.1; -; mRNA.
DR EMBL; AL645941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX908719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03662.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03663.1; -; Genomic_DNA.
DR EMBL; BC063840; AAH63840.1; -; mRNA.
DR CCDS; CCDS4762.1; -. [P25440-1]
DR CCDS; CCDS56420.1; -. [P25440-2]
DR CCDS; CCDS56421.1; -. [P25440-3]
DR PIR; A56619; A56619.
DR RefSeq; NP_001106653.1; NM_001113182.2. [P25440-1]
DR RefSeq; NP_001186384.1; NM_001199455.1. [P25440-2]
DR RefSeq; NP_001186385.1; NM_001199456.1. [P25440-3]
DR RefSeq; NP_001278915.1; NM_001291986.1. [P25440-4]
DR RefSeq; NP_005095.1; NM_005104.3. [P25440-1]
DR PDB; 1X0J; X-ray; 1.80 A; A/B/C=73-194.
DR PDB; 2DVQ; X-ray; 2.04 A; A/B/C=73-194.
DR PDB; 2DVR; X-ray; 2.30 A; A/B/C=73-194.
DR PDB; 2DVS; X-ray; 2.04 A; A/B/C=73-194.
DR PDB; 2DVV; X-ray; 1.80 A; A=348-455.
DR PDB; 2E3K; X-ray; 2.30 A; A/B/C/D=348-455.
DR PDB; 2G4A; NMR; -; A=348-455.
DR PDB; 2YDW; X-ray; 1.90 A; A/B/C=67-200.
DR PDB; 2YEK; X-ray; 1.98 A; A/B/C=67-200.
DR PDB; 3AQA; X-ray; 2.30 A; A/B/C=73-194.
DR PDB; 3ONI; X-ray; 1.61 A; A=344-455.
DR PDB; 4A9E; X-ray; 1.91 A; A/B/C=67-200.
DR PDB; 4A9F; X-ray; 1.73 A; A/B/C=67-200.
DR PDB; 4A9H; X-ray; 2.05 A; A/B/C=67-200.
DR PDB; 4A9I; X-ray; 2.25 A; A/B/C=67-200.
DR PDB; 4A9J; X-ray; 1.90 A; A/B/C=67-200.
DR PDB; 4A9M; X-ray; 2.06 A; A/B/C=67-200.
DR PDB; 4A9N; X-ray; 1.85 A; A/B/C=67-200.
DR PDB; 4A9O; X-ray; 1.78 A; A/B/C=67-200.
DR PDB; 4AKN; X-ray; 1.82 A; A/B/C=67-200.
DR PDB; 4ALG; X-ray; 1.60 A; A=67-200.
DR PDB; 4ALH; X-ray; 1.78 A; A/B/C=67-200.
DR PDB; 4J1P; X-ray; 1.08 A; A=344-455.
DR PDB; 4MR5; X-ray; 1.63 A; A=344-455.
DR PDB; 4MR6; X-ray; 1.67 A; A=344-455.
DR PDB; 4QEU; X-ray; 1.50 A; A=344-455.
DR PDB; 4QEV; X-ray; 1.80 A; A=344-455.
DR PDB; 4QEW; X-ray; 1.70 A; A=344-455.
DR PDB; 4UYF; X-ray; 1.60 A; A/B/C=67-200.
DR PDB; 4UYG; X-ray; 2.50 A; A/B/C/D/E/F=338-473.
DR PDB; 4UYH; X-ray; 1.73 A; A/B/C=67-200.
DR PDB; 5BT5; X-ray; 1.40 A; A=344-455.
DR PDB; 5DFB; X-ray; 1.40 A; A=344-455.
DR PDB; 5DFC; X-ray; 1.50 A; A=344-455.
DR PDB; 5DFD; X-ray; 1.50 A; A=344-455.
DR PDB; 5DW1; X-ray; 1.55 A; A/B/C/D=345-455.
DR PDB; 5EK9; X-ray; 2.08 A; A/B=344-455.
DR PDB; 5HEL; X-ray; 1.45 A; A=71-194.
DR PDB; 5HEM; X-ray; 1.65 A; A/B=71-194.
DR PDB; 5HEN; X-ray; 1.79 A; A/B/C=71-194.
DR PDB; 5HFQ; X-ray; 1.40 A; A=344-455.
DR PDB; 5IBN; X-ray; 0.94 A; A=348-455.
DR PDB; 5IG6; X-ray; 0.91 A; A=348-454.
DR PDB; 5N2L; X-ray; 1.89 A; A/B/C/D=344-455.
DR PDB; 5O38; X-ray; 1.20 A; A=344-455.
DR PDB; 5O39; X-ray; 1.74 A; A=344-455.
DR PDB; 5O3A; X-ray; 2.40 A; A=344-455.
DR PDB; 5O3B; X-ray; 1.95 A; A/B/C/D=344-455.
DR PDB; 5O3C; X-ray; 1.60 A; A=344-455.
DR PDB; 5O3D; X-ray; 1.60 A; A=345-455.
DR PDB; 5O3E; X-ray; 1.40 A; A=344-455.
DR PDB; 5O3F; X-ray; 1.75 A; A=344-455.
DR PDB; 5O3G; X-ray; 1.85 A; A/B=344-455.
DR PDB; 5O3H; X-ray; 1.40 A; A=344-455.
DR PDB; 5O3I; X-ray; 1.20 A; A=344-455.
DR PDB; 5U5S; NMR; -; A=344-455.
DR PDB; 5U6V; X-ray; 1.77 A; A=347-455.
DR PDB; 5UEW; X-ray; 1.83 A; A/B=347-454.
DR PDB; 5XHE; X-ray; 1.40 A; A=348-455.
DR PDB; 5XHK; X-ray; 1.28 A; A=348-455.
DR PDB; 6CUI; NMR; -; A=621-750.
DR PDB; 6DB0; X-ray; 1.70 A; A/B/C=67-200.
DR PDB; 6DBC; X-ray; 1.05 A; A=348-455.
DR PDB; 6DDI; X-ray; 1.50 A; A/B/C=67-200.
DR PDB; 6DDJ; X-ray; 1.05 A; A=348-455.
DR PDB; 6E6J; X-ray; 2.44 A; A/B/C/D/E/F=348-455.
DR PDB; 6FFE; X-ray; 1.76 A; A=344-455.
DR PDB; 6FFF; X-ray; 1.67 A; A=344-455.
DR PDB; 6FFG; X-ray; 1.59 A; A=344-455.
DR PDB; 6I80; X-ray; 1.14 A; A/B=348-455.
DR PDB; 6I81; X-ray; 1.74 A; A=348-455.
DR PDB; 6JKE; X-ray; 1.50 A; A/B/C=73-194.
DR PDB; 6K04; X-ray; 1.25 A; A=344-455.
DR PDB; 6K05; X-ray; 1.94 A; A/B/C=73-194.
DR PDB; 6MO7; X-ray; 1.85 A; A/B/C=71-194.
DR PDB; 6MO8; X-ray; 1.80 A; A/B/C=71-194.
DR PDB; 6MO9; X-ray; 1.80 A; A/B/C=71-194.
DR PDB; 6MOA; X-ray; 1.27 A; A=346-455.
DR PDB; 6ONY; X-ray; 1.98 A; A/B=73-194.
DR PDB; 6SWO; X-ray; 1.60 A; AAA=344-455.
DR PDB; 6SWP; X-ray; 1.60 A; AAA=344-455.
DR PDB; 6TQ1; X-ray; 1.90 A; AAA/BBB/CCC=67-200.
DR PDB; 6TQ2; X-ray; 2.26 A; AAA/BBB/CCC=67-200.
DR PDB; 6U61; X-ray; 2.29 A; A/B=65-194.
DR PDB; 6U71; X-ray; 1.47 A; A=347-455.
DR PDB; 6U8H; X-ray; 2.07 A; A=65-194.
DR PDB; 6ULQ; X-ray; 2.70 A; A/B/C=65-194.
DR PDB; 6ULT; X-ray; 2.80 A; A/B/C/D/E/F/G/H=347-454.
DR PDB; 6VIY; X-ray; 1.90 A; A/B=348-455.
DR PDB; 6WWB; X-ray; 1.31 A; A=348-455.
DR PDB; 6YTM; X-ray; 1.56 A; A/B=345-455.
DR PDB; 6Z7F; X-ray; 1.60 A; AAA=344-455.
DR PDB; 6Z8P; X-ray; 1.55 A; AAA=344-455.
DR PDB; 6ZB0; X-ray; 1.61 A; AAA=344-455.
DR PDB; 6ZB1; X-ray; 1.60 A; AAA=344-455.
DR PDB; 6ZB2; X-ray; 2.28 A; AAA=344-455.
DR PDB; 7DPN; X-ray; 1.80 A; A/B/C=73-194.
DR PDB; 7DPO; X-ray; 2.30 A; A=348-455.
DR PDB; 7ENV; X-ray; 2.45 A; A/B/C=73-194.
DR PDB; 7ENZ; X-ray; 1.70 A; A=348-455.
DR PDB; 7EO5; X-ray; 2.00 A; A=348-455.
DR PDB; 7JX7; X-ray; 1.75 A; A=347-455.
DR PDB; 7L6D; X-ray; 1.55 A; A=344-455.
DR PDB; 7L9G; X-ray; 1.36 A; A=344-455.
DR PDB; 7L9J; X-ray; 1.85 A; A=344-455.
DR PDB; 7L9K; X-ray; 1.95 A; A/B=344-455.
DR PDB; 7LAK; X-ray; 1.83 A; A=73-194.
DR PDB; 7NPY; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7NPZ; X-ray; 1.28 A; AAA=344-455.
DR PDB; 7NQ0; X-ray; 1.30 A; AAA=344-455.
DR PDB; 7NQ1; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7NQ2; X-ray; 1.74 A; AAA=344-455.
DR PDB; 7NQ3; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7NQ5; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7NQ7; X-ray; 1.70 A; AAA=344-455.
DR PDB; 7NQ8; X-ray; 1.60 A; A=344-455.
DR PDB; 7NQ9; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7NQI; X-ray; 1.60 A; A=344-455.
DR PDB; 7NQJ; X-ray; 1.73 A; A=344-455.
DR PDB; 7OE4; X-ray; 1.65 A; AAA=344-455.
DR PDB; 7OE5; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7OE6; X-ray; 1.76 A; AAA=344-455.
DR PDB; 7OE8; X-ray; 1.30 A; A=344-455.
DR PDB; 7OE9; X-ray; 1.60 A; A=344-455.
DR PDB; 7OEP; X-ray; 1.80 A; AAA=344-455.
DR PDB; 7OER; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7OES; X-ray; 1.60 A; AAA=344-455.
DR PDB; 7OET; X-ray; 1.41 A; AAA=344-455.
DR PDB; 7OGY; X-ray; 1.60 A; AAA=344-455.
DR PDBsum; 1X0J; -.
DR PDBsum; 2DVQ; -.
DR PDBsum; 2DVR; -.
DR PDBsum; 2DVS; -.
DR PDBsum; 2DVV; -.
DR PDBsum; 2E3K; -.
DR PDBsum; 2G4A; -.
DR PDBsum; 2YDW; -.
DR PDBsum; 2YEK; -.
DR PDBsum; 3AQA; -.
DR PDBsum; 3ONI; -.
DR PDBsum; 4A9E; -.
DR PDBsum; 4A9F; -.
DR PDBsum; 4A9H; -.
DR PDBsum; 4A9I; -.
DR PDBsum; 4A9J; -.
DR PDBsum; 4A9M; -.
DR PDBsum; 4A9N; -.
DR PDBsum; 4A9O; -.
DR PDBsum; 4AKN; -.
DR PDBsum; 4ALG; -.
DR PDBsum; 4ALH; -.
DR PDBsum; 4J1P; -.
DR PDBsum; 4MR5; -.
DR PDBsum; 4MR6; -.
DR PDBsum; 4QEU; -.
DR PDBsum; 4QEV; -.
DR PDBsum; 4QEW; -.
DR PDBsum; 4UYF; -.
DR PDBsum; 4UYG; -.
DR PDBsum; 4UYH; -.
DR PDBsum; 5BT5; -.
DR PDBsum; 5DFB; -.
DR PDBsum; 5DFC; -.
DR PDBsum; 5DFD; -.
DR PDBsum; 5DW1; -.
DR PDBsum; 5EK9; -.
DR PDBsum; 5HEL; -.
DR PDBsum; 5HEM; -.
DR PDBsum; 5HEN; -.
DR PDBsum; 5HFQ; -.
DR PDBsum; 5IBN; -.
DR PDBsum; 5IG6; -.
DR PDBsum; 5N2L; -.
DR PDBsum; 5O38; -.
DR PDBsum; 5O39; -.
DR PDBsum; 5O3A; -.
DR PDBsum; 5O3B; -.
DR PDBsum; 5O3C; -.
DR PDBsum; 5O3D; -.
DR PDBsum; 5O3E; -.
DR PDBsum; 5O3F; -.
DR PDBsum; 5O3G; -.
DR PDBsum; 5O3H; -.
DR PDBsum; 5O3I; -.
DR PDBsum; 5U5S; -.
DR PDBsum; 5U6V; -.
DR PDBsum; 5UEW; -.
DR PDBsum; 5XHE; -.
DR PDBsum; 5XHK; -.
DR PDBsum; 6CUI; -.
DR PDBsum; 6DB0; -.
DR PDBsum; 6DBC; -.
DR PDBsum; 6DDI; -.
DR PDBsum; 6DDJ; -.
DR PDBsum; 6E6J; -.
DR PDBsum; 6FFE; -.
DR PDBsum; 6FFF; -.
DR PDBsum; 6FFG; -.
DR PDBsum; 6I80; -.
DR PDBsum; 6I81; -.
DR PDBsum; 6JKE; -.
DR PDBsum; 6K04; -.
DR PDBsum; 6K05; -.
DR PDBsum; 6MO7; -.
DR PDBsum; 6MO8; -.
DR PDBsum; 6MO9; -.
DR PDBsum; 6MOA; -.
DR PDBsum; 6ONY; -.
DR PDBsum; 6SWO; -.
DR PDBsum; 6SWP; -.
DR PDBsum; 6TQ1; -.
DR PDBsum; 6TQ2; -.
DR PDBsum; 6U61; -.
DR PDBsum; 6U71; -.
DR PDBsum; 6U8H; -.
DR PDBsum; 6ULQ; -.
DR PDBsum; 6ULT; -.
DR PDBsum; 6VIY; -.
DR PDBsum; 6WWB; -.
DR PDBsum; 6YTM; -.
DR PDBsum; 6Z7F; -.
DR PDBsum; 6Z8P; -.
DR PDBsum; 6ZB0; -.
DR PDBsum; 6ZB1; -.
DR PDBsum; 6ZB2; -.
DR PDBsum; 7DPN; -.
DR PDBsum; 7DPO; -.
DR PDBsum; 7ENV; -.
DR PDBsum; 7ENZ; -.
DR PDBsum; 7EO5; -.
DR PDBsum; 7JX7; -.
DR PDBsum; 7L6D; -.
DR PDBsum; 7L9G; -.
DR PDBsum; 7L9J; -.
DR PDBsum; 7L9K; -.
DR PDBsum; 7LAK; -.
DR PDBsum; 7NPY; -.
DR PDBsum; 7NPZ; -.
DR PDBsum; 7NQ0; -.
DR PDBsum; 7NQ1; -.
DR PDBsum; 7NQ2; -.
DR PDBsum; 7NQ3; -.
DR PDBsum; 7NQ5; -.
DR PDBsum; 7NQ7; -.
DR PDBsum; 7NQ8; -.
DR PDBsum; 7NQ9; -.
DR PDBsum; 7NQI; -.
DR PDBsum; 7NQJ; -.
DR PDBsum; 7OE4; -.
DR PDBsum; 7OE5; -.
DR PDBsum; 7OE6; -.
DR PDBsum; 7OE8; -.
DR PDBsum; 7OE9; -.
DR PDBsum; 7OEP; -.
DR PDBsum; 7OER; -.
DR PDBsum; 7OES; -.
DR PDBsum; 7OET; -.
DR PDBsum; 7OGY; -.
DR AlphaFoldDB; P25440; -.
DR SASBDB; P25440; -.
DR SMR; P25440; -.
DR BioGRID; 111973; 378.
DR DIP; DIP-60835N; -.
DR IntAct; P25440; 45.
DR MINT; P25440; -.
DR STRING; 9606.ENSP00000378704; -.
DR BindingDB; P25440; -.
DR ChEMBL; CHEMBL1293289; -.
DR GuidetoPHARMACOLOGY; 1944; -.
DR GlyGen; P25440; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; P25440; -.
DR PhosphoSitePlus; P25440; -.
DR BioMuta; BRD2; -.
DR DMDM; 12230989; -.
DR CPTAC; CPTAC-1598; -.
DR EPD; P25440; -.
DR jPOST; P25440; -.
DR MassIVE; P25440; -.
DR MaxQB; P25440; -.
DR PaxDb; P25440; -.
DR PeptideAtlas; P25440; -.
DR PRIDE; P25440; -.
DR ProteomicsDB; 54271; -. [P25440-1]
DR ProteomicsDB; 54272; -. [P25440-2]
DR ProteomicsDB; 65931; -.
DR ABCD; P25440; 1 sequenced antibody.
DR Antibodypedia; 28816; 390 antibodies from 39 providers.
DR DNASU; 6046; -.
DR Ensembl; ENST00000374825.9; ENSP00000363958.4; ENSG00000204256.14. [P25440-1]
DR Ensembl; ENST00000374831.8; ENSP00000363964.4; ENSG00000204256.14. [P25440-1]
DR Ensembl; ENST00000383108.6; ENSP00000372588.2; ENSG00000234507.9. [P25440-1]
DR Ensembl; ENST00000395287.5; ENSP00000378702.1; ENSG00000204256.14. [P25440-2]
DR Ensembl; ENST00000399527.5; ENSP00000382443.1; ENSG00000215077.10. [P25440-2]
DR Ensembl; ENST00000399528.5; ENSP00000382444.1; ENSG00000215077.10. [P25440-1]
DR Ensembl; ENST00000399529.7; ENSP00000382445.3; ENSG00000215077.10. [P25440-1]
DR Ensembl; ENST00000414731.6; ENSP00000391246.2; ENSG00000234704.9.
DR Ensembl; ENST00000436979.5; ENSP00000405634.1; ENSG00000235307.12. [P25440-3]
DR Ensembl; ENST00000438194.6; ENSP00000401791.2; ENSG00000234507.9. [P25440-1]
DR Ensembl; ENST00000442863.5; ENSP00000410994.1; ENSG00000234507.9. [P25440-2]
DR Ensembl; ENST00000448067.5; ENSP00000412885.1; ENSG00000235307.12. [P25440-2]
DR Ensembl; ENST00000449085.4; ENSP00000409145.3; ENSG00000204256.14. [P25440-1]
DR Ensembl; ENST00000449118.5; ENSP00000399009.1; ENSG00000234704.9.
DR Ensembl; ENST00000549126.4; ENSP00000449380.2; ENSG00000235307.12. [P25440-1]
DR Ensembl; ENST00000552587.4; ENSP00000449609.1; ENSG00000235307.12. [P25440-1]
DR Ensembl; ENST00000678250.1; ENSP00000502900.1; ENSG00000204256.14. [P25440-1]
DR GeneID; 6046; -.
DR KEGG; hsa:6046; -.
DR MANE-Select; ENST00000374825.9; ENSP00000363958.4; NM_005104.4; NP_005095.1.
DR UCSC; uc003ocn.4; human. [P25440-1]
DR CTD; 6046; -.
DR DisGeNET; 6046; -.
DR GeneCards; BRD2; -.
DR HGNC; HGNC:1103; BRD2.
DR HPA; ENSG00000204256; Low tissue specificity.
DR MIM; 601540; gene.
DR neXtProt; NX_P25440; -.
DR OpenTargets; ENSG00000204256; -.
DR PharmGKB; PA25414; -.
DR VEuPathDB; HostDB:ENSG00000204256; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR HOGENOM; CLU_001499_0_4_1; -.
DR InParanoid; P25440; -.
DR OMA; MNIPHYP; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; P25440; -.
DR TreeFam; TF317345; -.
DR PathwayCommons; P25440; -.
DR Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
DR SignaLink; P25440; -.
DR SIGNOR; P25440; -.
DR BioGRID-ORCS; 6046; 284 hits in 1124 CRISPR screens.
DR ChiTaRS; BRD2; human.
DR EvolutionaryTrace; P25440; -.
DR GeneWiki; BRD2; -.
DR GenomeRNAi; 6046; -.
DR Pharos; P25440; Tchem.
DR PRO; PR:P25440; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P25440; protein.
DR Bgee; ENSG00000204256; Expressed in ventricular zone and 96 other tissues.
DR ExpressionAtlas; P25440; baseline and differential.
DR Genevisible; P25440; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
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 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; Host-virus interaction; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..801
FT /note="Bromodomain-containing protein 2"
FT /id="PRO_0000211180"
FT DOMAIN 91..163
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 364..436
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 632..714
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 555..559
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 312..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..511
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..563
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_055028"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_055029"
FT VAR_SEQ 615
FT /note="L -> LQAGVQWRDLGLLQPPLLGFKRFSCLSLPSSQDYRL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022600"
FT VARIANT 30
FT /note="G -> E (in a glioblastoma multiforme sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041904"
FT VARIANT 49
FT /note="A -> G (in dbSNP:rs3918144)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041905"
FT VARIANT 49
FT /note="A -> S (in dbSNP:rs55669504)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041906"
FT VARIANT 212
FT /note="A -> P (in dbSNP:rs35952031)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041907"
FT VARIANT 238
FT /note="L -> F (in dbSNP:rs176250)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_022132"
FT VARIANT 260
FT /note="P -> Q (in dbSNP:rs35294809)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041908"
FT VARIANT 474
FT /note="A -> V (in dbSNP:rs3918143)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_029300"
FT VARIANT 547
FT /note="R -> K (in dbSNP:rs1049369)"
FT /id="VAR_029301"
FT VARIANT 558
FT /note="R -> G (in a gastric adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041909"
FT VARIANT 569
FT /note="A -> T (in dbSNP:rs34530779)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041910"
FT VARIANT 599
FT /note="A -> P (in dbSNP:rs55952113)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041911"
FT VARIANT 714
FT /note="P -> L (in a glioblastoma multiforme sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041912"
FT MUTAGEN 78
FT /note="Q->A: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 142..143
FT /note="MQ->AA: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 153
FT /note="Y->K: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 154
FT /note="I->A: Partial loss of homodimerization; when
FT associated with A-182."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 170
FT /note="E->A: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 174
FT /note="L->E: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 177
FT /note="V->E: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:17148447"
FT MUTAGEN 182
FT /note="Q->A: Partial loss of homodimerization; when
FT associated with A-154."
FT /evidence="ECO:0000269|PubMed:17148447"
FT CONFLICT 490
FT /note="S -> F (in Ref. 4; CAH56179)"
FT /evidence="ECO:0000305"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:5HEL"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:5HEL"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6ULQ"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:5IG6"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:5IG6"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:5IG6"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:5IG6"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:5IG6"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:5IG6"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:5IG6"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:2G4A"
FT HELIX 411..428
FT /evidence="ECO:0007829|PDB:5IG6"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:5U5S"
FT HELIX 434..450
FT /evidence="ECO:0007829|PDB:5IG6"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:6CUI"
FT TURN 634..638
FT /evidence="ECO:0007829|PDB:6CUI"
FT HELIX 644..654
FT /evidence="ECO:0007829|PDB:6CUI"
FT HELIX 659..670
FT /evidence="ECO:0007829|PDB:6CUI"
FT TURN 674..678
FT /evidence="ECO:0007829|PDB:6CUI"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:6CUI"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:6CUI"
FT HELIX 693..707
FT /evidence="ECO:0007829|PDB:6CUI"
FT HELIX 725..743
FT /evidence="ECO:0007829|PDB:6CUI"
SQ 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
