ID BRD4_HUMAN Reviewed; 1362 AA. AC O60885; O60433; Q4G0X8; Q86YS8; Q96PD3; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 212. DE RecName: Full=Bromodomain-containing protein 4; DE AltName: Full=Protein HUNK1; GN Name=BRD4; Synonyms=HUNK1; 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 A), DISEASE, AND CHROMOSOMAL RP TRANSLOCATION WITH NUT. RX PubMed=11733348; DOI=10.1016/s0002-9440(10)63049-0; RA French C.A., Miyoshi I., Aster J.C., Kubonishi I., Kroll T.G., Dal Cin P., RA Vargas S.O., Perez-Atayde A.R., Fletcher J.A.; RT "BRD4 bromodomain gene rearrangement in aggressive carcinoma with RT translocation t(15;19)."; RL Am. J. Pathol. 159:1987-1992(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). RC TISSUE=Placenta; RA Weber B.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-719, DISEASE, CHROMOSOMAL TRANSLOCATION RP WITH NUT, AND TISSUE SPECIFICITY. RC TISSUE=Carcinoma; RX PubMed=12543779; RA French C.A., Miyoshi I., Kubonishi I., Grier H.E., Perez-Atayde A.R., RA Fletcher J.A.; RT "BRD4-NUT fusion oncogene: a novel mechanism in aggressive carcinoma."; RL Cancer Res. 63:304-307(2003). RN [7] RP FUNCTION, INTERACTION WITH CDK9 AND CCNT1, IDENTIFICATION IN THE P-TEFB RP COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=16109376; DOI=10.1016/j.molcel.2005.06.027; RA Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.; RT "The bromodomain protein Brd4 is a positive regulatory component of P-TEFb RT and stimulates RNA polymerase II-dependent transcription."; RL Mol. Cell 19:523-534(2005). RN [8] RP FUNCTION, INTERACTION WITH CDK9 AND CCNT1, AND IDENTIFICATION IN THE P-TEFB RP COMPLEX. RX PubMed=16109377; DOI=10.1016/j.molcel.2005.06.029; RA Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.; RT "Recruitment of P-TEFb for stimulation of transcriptional elongation by the RT bromodomain protein Brd4."; RL Mol. Cell 19:535-545(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP INTERACTION WITH KSHV PROTEIN LANA (MICROBIAL INFECTION). RX PubMed=16940503; DOI=10.1128/jvi.00502-06; RA You J., Srinivasan V., Denis G.V., Harrington W.J. Jr., Ballestas M.E., RA Kaye K.M., Howley P.M.; RT "Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen RT interacts with bromodomain protein Brd4 on host mitotic chromosomes."; RL J. Virol. 80:8909-8919(2006). RN [11] RP INTERACTION WITH BOVINE PAPILLOMAVIRUS TYPE 1 REGULATORY PROTEIN E2. RX PubMed=17189189; DOI=10.1016/j.molcel.2006.11.005; RA Parish J.L., Bean A.M., Park R.B., Androphy E.J.; RT "ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes RT and viral genome maintenance."; RL Mol. Cell 24:867-876(2006). RN [12] RP INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN EBNA1. RX PubMed=18922874; DOI=10.1128/jvi.01680-08; RA Lin A., Wang S., Nguyen T., Shire K., Frappier L.; RT "The EBNA1 protein of Epstein-Barr virus functionally interacts with RT Brd4."; RL J. Virol. 82:12009-12019(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY RP 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 [14] RP IDENTIFICATION BY MASS 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 [15] RP FUNCTION. RX PubMed=19596240; DOI=10.1016/j.cell.2009.05.047; RA Hargreaves D.C., Horng T., Medzhitov R.; RT "Control of inducible gene expression by signal-dependent transcriptional RT elongation."; RL Cell 138:129-145(2009). RN [16] RP FUNCTION, AND INTERACTION WITH RELA. RX PubMed=19103749; DOI=10.1128/mcb.01365-08; RA Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.; RT "Brd4 coactivates transcriptional activation of NF-kappaB via specific RT binding to acetylated RelA."; RL Mol. Cell. Biol. 29:1375-1387(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-1117, AND RP IDENTIFICATION BY MASS 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 [19] 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 [20] RP INTERACTION WITH NSD3; JMJD6; CHD4; BICRA AND ATAD5. RX PubMed=21555454; DOI=10.1128/mcb.01341-10; RA Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., RA Howley P.M.; RT "The Brd4 extraterminal domain confers transcription activation independent RT of pTEFb by recruiting multiple proteins, including NSD3."; RL Mol. Cell. Biol. 31:2641-2652(2011). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=21890894; DOI=10.1093/nar/gkr698; RA Ai N., Hu X., Ding F., Yu B., Wang H., Lu X., Zhang K., Li Y., Han A., RA Lin W., Liu R., Chen R.; RT "Signal-induced Brd4 release from chromatin is essential for its role RT transition from chromatin targeting to transcriptional regulation."; RL Nucleic Acids Res. 39:9592-9604(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-1117, AND RP IDENTIFICATION BY 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 [23] RP FUNCTION. RX PubMed=22334664; DOI=10.1074/jbc.m111.323493; RA Wang R., Li Q., Helfer C.M., Jiao J., You J.; RT "Bromodomain protein Brd4 associated with acetylated chromatin is important RT for maintenance of higher-order chromatin structure."; RL J. Biol. Chem. 287:10738-10752(2012). RN [24] RP FUNCTION. RX PubMed=23086925; DOI=10.1074/jbc.m112.413047; RA Zhang W., Prakash C., Sum C., Gong Y., Li Y., Kwok J.J., Thiessen N., RA Pettersson S., Jones S.J., Knapp S., Yang H., Chin K.C.; RT "Bromodomain-containing protein 4 (BRD4) regulates RNA polymerase II serine RT 2 phosphorylation in human CD4+ T cells."; RL J. Biol. Chem. 287:43137-43155(2012). RN [25] RP FUNCTION. RX PubMed=22509028; DOI=10.1073/pnas.1120422109; RA Devaiah B.N., Lewis B.A., Cherman N., Hewitt M.C., Albrecht B.K., RA Robey P.G., Ozato K., Sims R.J. III, Singer D.S.; RT "BRD4 is an atypical kinase that phosphorylates serine2 of the RNA RT polymerase II carboxy-terminal domain."; RL Proc. Natl. Acad. Sci. U.S.A. 109:6927-6932(2012). RN [26] RP FUNCTION, AND INTERACTION WITH JMJD6; CDK9 AND CCNT1. RX PubMed=24360279; DOI=10.1016/j.cell.2013.10.056; RA Liu W., Ma Q., Wong K., Li W., Ohgi K., Zhang J., Aggarwal A., RA Rosenfeld M.G.; RT "Brd4 and JMJD6-associated anti-pause enhancers in regulation of RT transcriptional pause release."; RL Cell 155:1581-1595(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-1126; SER-1201 AND RP SER-1204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [28] RP FUNCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT SER-484; SER-488; RP SER-492; SER-494; SER-498; SER-499 AND SER-503, AND MUTAGENESIS OF RP 492-SER--SER-494; 498-SER--THR-500 AND SER-503. RX PubMed=23317504; DOI=10.1016/j.molcel.2012.12.006; RA Wu S.Y., Lee A.Y., Lai H.T., Zhang H., Chiang C.M.; RT "Phospho switch triggers Brd4 chromatin binding and activator recruitment RT for gene-specific targeting."; RL Mol. Cell 49:843-857(2013). RN [29] RP FUNCTION. RX PubMed=23589332; DOI=10.1128/mcb.01180-12; RA Patel M.C., Debrosse M., Smith M., Dey A., Huynh W., Sarai N., RA Heightman T.D., Tamura T., Ozato K.; RT "BRD4 coordinates recruitment of pause release factor P-TEFb and the RT pausing complex NELF/DSIF to regulate transcription elongation of RT interferon-stimulated genes."; RL Mol. Cell. Biol. 33:2497-2507(2013). RN [30] RP FUNCTION (ISOFORM B), SUBCELLULAR LOCATION (ISOFORM B), INTERACTION WITH RP NCAPD3 AND SMC2, AND MUTAGENESIS OF ASN-140. RX PubMed=23728299; DOI=10.1038/nature12147; RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., Cannell I.G., RA Bryson B.D., Rameseder J., Lee M.J., Blake E.J., Fydrych A., Ho R., RA Greenberger B.A., Chen G.C., Maffa A., Del Rosario A.M., Root D.E., RA Carpenter A.E., Hahn W.C., Sabatini D.M., Chen C.C., White F.M., RA Bradner J.E., Yaffe M.B.; RT "The bromodomain protein Brd4 insulates chromatin from DNA damage RT signalling."; RL Nature 498:246-250(2013). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND SER-1117, 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 [32] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-694 AND LYS-1111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [33] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [34] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [35] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [37] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-585; LYS-645; LYS-694; RP LYS-1050; LYS-1111 AND LYS-1197, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [38] RP INTERACTION WITH BICRA. RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065; RA Alpsoy A., Dykhuizen E.C.; RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes."; RL J. Biol. Chem. 293:3892-3903(2018). RN [39] RP ACTIVITY REGULATION. RX PubMed=31969702; DOI=10.1038/s41586-020-1930-8; RA Faivre E.J., McDaniel K.F., Albert D.H., Mantena S.R., Plotnik J.P., RA Wilcox D., Zhang L., Bui M.H., Sheppard G.S., Wang L., Sehgal V., Lin X., RA Huang X., Lu X., Uziel T., Hessler P., Lam L.T., Bellin R.J., Mehta G., RA Fidanze S., Pratt J.K., Liu D., Hasvold L.A., Sun C., Panchal S.C., RA Nicolette J.J., Fossey S.L., Park C.H., Longenecker K., Bigelow L., RA Torrent M., Rosenberg S.H., Kati W.M., Shen Y.; RT "Selective inhibition of the BD2 bromodomain of BET proteins in prostate RT cancer."; RL Nature 578:306-310(2020). RN [40] RP VARIANTS [LARGE SCALE ANALYSIS] SER-37; GLY-371; ASN-563; SER-598 AND RP HIS-669. 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). RN [41] RP STRUCTURE BY NMR OF 352-457. RX PubMed=18500820; DOI=10.1021/bi8001659; RA Liu Y., Wang X., Zhang J., Huang H., Ding B., Wu J., Shi Y.; RT "Structural basis and binding properties of the second bromodomain of Brd4 RT with acetylated histone tails."; RL Biochemistry 47:6403-6417(2008). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 RP INHIBITOR, FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. 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 [43] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH I-BET RP INHIBITOR. RX PubMed=21068722; DOI=10.1038/nature09589; RA Nicodeme E., Jeffrey K.L., Schaefer U., Beinke S., Dewell S., Chung C.W., RA Chandwani R., Marazzi I., Wilson P., Coste H., White J., Kirilovsky J., RA Rice C.M., Lora J.M., Prinjha R.K., Lee K., Tarakhovsky A.; RT "Suppression of inflammation by a synthetic histone mimic."; RL Nature 468:1119-1123(2010). RN [44] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 44-168, AND X-RAY CRYSTALLOGRAPHY RP (2.3 ANGSTROMS) OF 333-460. RX PubMed=21568322; DOI=10.1021/jm200108t; RA Chung C.W., Coste H., White J.H., Mirguet O., Wilde J., Gosmini R.L., RA Delves C., Magny S.M., Woodward R., Hughes S.A., Boursier E.V., Flynn H., RA Bouillot A.M., Bamborough P., Brusq J.M., Gellibert F.J., Jones E.J., RA Riou A.M., Homes P., Martin S.L., Uings I.J., Toum J., Clement C.A., RA Boullay A.B., Grimley R.L., Blandel F.M., Prinjha R.K., Lee K., RA Kirilovsky J., Nicodeme E.; RT "Discovery and characterization of small molecule inhibitors of the BET RT family bromodomains."; RL J. Med. Chem. 54:3827-3838(2011). RN [45] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 RP INHIBITOR. RX PubMed=21964340; DOI=10.1038/nature10509; RA Dawson M.A., Prinjha R.K., Dittmann A., Giotopoulos G., Bantscheff M., RA Chan W.I., Robson S.C., Chung C.W., Hopf C., Savitski M.M., Huthmacher C., RA Gudgin E., Lugo D., Beinke S., Chapman T.D., Roberts E.J., Soden P.E., RA Auger K.R., Mirguet O., Doehner K., Delwel R., Burnett A.K., Jeffrey P., RA Drewes G., Lee K., Huntly B.J., Kouzarides T.; RT "Inhibition of BET recruitment to chromatin as an effective treatment for RT MLL-fusion leukaemia."; RL Nature 478:529-533(2011). RN [46] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH RP BENZODIAZEPINES AND BENZOTRIAZEPINES INHIBITORS. RX PubMed=22137933; DOI=10.1016/j.bmc.2011.10.080; RA Filippakopoulos P., Picaud S., Fedorov O., Keller M., Wrobel M., RA Morgenstern O., Bracher F., Knapp S.; RT "Benzodiazepines and benzotriazepines as protein interaction inhibitors RT targeting bromodomains of the BET family."; RL Bioorg. Med. Chem. 20:1878-1886(2012). RN [47] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 44-168, AND STRUCTURE BY NMR OF RP 333-460. RX PubMed=22645123; DOI=10.1074/jbc.m112.359505; RA Zhang G., Liu R., Zhong Y., Plotnikov A.N., Zhang W., Zeng L., Rusinova E., RA Gerona-Nevarro G., Moshkina N., Joshua J., Chuang P.Y., Ohlmeyer M., RA He J.C., Zhou M.M.; RT "Down-regulation of NF-kappaB transcriptional activity in HIV-associated RT kidney disease by BRD4 inhibition."; RL J. Biol. Chem. 287:28840-28851(2012). RN [48] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH RP BENZODIAZEPINES INHIBITORS. RX PubMed=22136404; DOI=10.1021/jm201320w; RA Chung C.W., Dean A.W., Woolven J.M., Bamborough P.; RT "Fragment-based discovery of bromodomain inhibitors part 1: inhibitor RT binding modes and implications for lead discovery."; RL J. Med. Chem. 55:576-586(2012). RN [49] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 44-168. RX PubMed=23095041; DOI=10.1021/jm3010515; RA Fish P.V., Filippakopoulos P., Bish G., Brennan P.E., Bunnage M.E., RA Cook A.S., Federov O., Gerstenberger B.S., Jones H., Knapp S., Marsden B., RA Nocka K., Owen D.R., Philpott M., Picaud S., Primiano M.J., Ralph M.J., RA Sciammetta N., Trzupek J.D.; RT "Identification of a chemical probe for bromo and extra C-terminal RT bromodomain inhibition through optimization of a fragment-derived hit."; RL J. Med. Chem. 55:9831-9837(2012). RN [50] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 44-168; 333-460 AND 1343-1362 IN RP COMPLEX WITH ACETYLATED HISTONE, AND MUTAGENESIS OF ASN-140 AND ASN-433. RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013; RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., RA Gingras A.C., Arrowsmith C.H., Knapp S.; RT "Histone recognition and large-scale structural analysis of the human RT bromodomain family."; RL Cell 149:214-231(2012). RN [51] RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 44-168 IN COMPLEX WITH RP 3,5-DIMETHYLISOXAZOLE INHIBITOR. RX PubMed=23517011; DOI=10.1021/jm301588r; RA Hewings D.S., Fedorov O., Filippakopoulos P., Martin S., Picaud S., RA Tumber A., Wells C., Olcina M.M., Freeman K., Gill A., Ritchie A.J., RA Sheppard D.W., Russell A.J., Hammond E.M., Knapp S., Brennan P.E., RA Conway S.J.; RT "Optimization of 3,5-dimethylisoxazole derivatives as potent bromodomain RT ligands."; RL J. Med. Chem. 56:3217-3227(2013). RN [52] RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 44-167 IN COMPLEX WITH RP 2-THIAZOLIDINONE INHIBITOR. RX PubMed=23530754; DOI=10.1021/jm301793a; RA Zhao L., Cao D., Chen T., Wang Y., Miao Z., Xu Y., Chen W., Wang X., Li Y., RA Du Z., Xiong B., Li J., Xu C., Zhang N., He J., Shen J.; RT "Fragment-based drug discovery of 2-thiazolidinones as inhibitors of the RT histone reader BRD4 bromodomain."; RL J. Med. Chem. 56:3833-3851(2013). RN [53] {ECO:0007744|PDB:6BNH} RP STRUCTURE BY NMR OF 601-683 IN COMPLEX WITH JMJD6, FUNCTION, INTERACTION RP WITH JMJD6 AND NSD3, AND MUTAGENESIS OF 651-GLU--GLU-653. RX PubMed=29176719; DOI=10.1038/s41598-017-16588-8; RA Konuma T., Yu D., Zhao C., Ju Y., Sharma R., Ren C., Zhang Q., Zhou M.M., RA Zeng L.; RT "Structural Mechanism of the Oxygenase JMJD6 Recognition by the RT Extraterminal (ET) Domain of BRD4."; RL Sci. Rep. 7:16272-16272(2017). RN [54] {ECO:0007744|PDB:6SWN, ECO:0007744|PDB:6SWQ} RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 44-168 IN COMPLEX WITH GSK778 AND RP GSK046. RX PubMed=32193360; DOI=10.1126/science.aaz8455; RA Gilan O., Rioja I., Knezevic K., Bell M.J., Yeung M.M., Harker N.R., RA Lam E.Y.N., Chung C.W., Bamborough P., Petretich M., Urh M., Atkinson S.J., RA Bassil A.K., Roberts E.J., Vassiliadis D., Burr M.L., Preston A.G.S., RA Wellaway C., Werner T., Gray J.R., Michon A.M., Gobbetti T., Kumar V., RA Soden P.E., Haynes A., Vappiani J., Tough D.F., Taylor S., Dawson S.J., RA Bantscheff M., Lindon M., Drewes G., Demont E.H., Daniels D.L., Grandi P., RA Prinjha R.K., Dawson M.A.; RT "Selective targeting of BD1 and BD2 of the BET proteins in cancer and RT immunoinflammation."; RL Science 368:387-394(2020). CC -!- FUNCTION: Chromatin reader protein that recognizes and binds acetylated CC histones and plays a key role in transmission of epigenetic memory CC across cell divisions and transcription regulation (PubMed:23086925, CC PubMed:23317504, PubMed:20871596, PubMed:29176719). Remains associated CC with acetylated chromatin throughout the entire cell cycle and provides CC epigenetic memory for postmitotic G1 gene transcription by preserving CC acetylated chromatin status and maintaining high-order chromatin CC structure (PubMed:23589332, PubMed:23317504, PubMed:22334664). During CC interphase, plays a key role in regulating the transcription of signal- CC inducible genes by associating with the P-TEFb complex and recruiting CC it to promoters (PubMed:23589332, PubMed:19596240, PubMed:16109377, CC PubMed:16109376, PubMed:24360279). Also recruits P-TEFb complex to CC distal enhancers, so called anti-pause enhancers in collaboration with CC JMJD6 (PubMed:23589332, PubMed:19596240, PubMed:16109377, CC PubMed:16109376, PubMed:24360279). BRD4 and JMJD6 are required to form CC the transcriptionally active P-TEFb complex by displacing negative CC regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby CC transforming it into an active form that can then phosphorylate the C- CC terminal domain (CTD) of RNA polymerase II (PubMed:23589332, CC PubMed:19596240, PubMed:16109377, PubMed:16109376, PubMed:24360279). CC Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by CC promoting recruitment of P-TEFb to promoters (By similarity). Promotes CC phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA CC polymerase II (PubMed:23086925). According to a report, directly acts CC as an atypical protein kinase and mediates phosphorylation of 'Ser-2' CC of the C-terminal domain (CTD) of RNA polymerase II; these data however CC need additional evidences in vivo (PubMed:22509028). In addition to CC acetylated histones, also recognizes and binds acetylated RELA, leading CC to further recruitment of the P-TEFb complex and subsequent activation CC of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53- CC mediated transcription: following phosphorylation by CK2, recruited to CC p53/TP53 specific target promoters (PubMed:23317504). CC {ECO:0000250|UniProtKB:Q9ESU6, ECO:0000269|PubMed:16109376, CC ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:19103749, CC ECO:0000269|PubMed:19596240, ECO:0000269|PubMed:22334664, CC ECO:0000269|PubMed:22509028, ECO:0000269|PubMed:23086925, CC ECO:0000269|PubMed:23317504, ECO:0000269|PubMed:23589332, CC ECO:0000269|PubMed:24360279, ECO:0000269|PubMed:29176719}. CC -!- FUNCTION: [Isoform B]: Acts as a chromatin insulator in the DNA damage CC response pathway. Inhibits DNA damage response signaling by recruiting CC the condensin-2 complex to acetylated histones, leading to chromatin CC structure remodeling, insulating the region from DNA damage response by CC limiting spreading of histone H2AX/H2A.x phosphorylation. CC {ECO:0000269|PubMed:23728299}. CC -!- ACTIVITY REGULATION: Inhibited by JQ1, a thieno-triazolo-1,4-diazepine CC derivative, which specifically inhibits members of the BET family CC (BRD2, BRD3 and BRD4) (PubMed:20871596). The first bromo domain is CC inhibited by GSK778 (iBET-BD1), which specifically inhibits the first CC bromo domain of members of the BET family (BRD2, BRD3 and BRD4) CC (PubMed:32193360). The second bromo domain is inhibited by ABBV-744, CC which specifically inhibits the second bromo domain of members of the CC BET family (BRD2, BRD3 and BRD4) (PubMed:31969702). The second bromo CC domain is inhibited by GSK046 (iBET-BD2), which specifically inhibits CC the second bromo domain of members of the BET family (BRD2, BRD3 and CC BRD4) (PubMed:32193360). {ECO:0000269|PubMed:20871596, CC ECO:0000269|PubMed:31969702, ECO:0000269|PubMed:32193360}. CC -!- SUBUNIT: Interacts with p53/TP53; the interaction is direct CC (PubMed:23317504). Interacts (via CTD region) with CDK9 and CCNT1, CC acting as an associated component of P-TEFb complex (PubMed:16109376, CC PubMed:16109377, PubMed:23317504, PubMed:24360279). Interacts with RELA CC (when acetylated at 'Lys-310')(PubMed:19103749). Interacts (via NET CC domain) with NSD3, CHD4, BICRA and ATAD5 (PubMed:21555454, CC PubMed:29176719). The interaction with BICRA bridges BRD4 to the GBAF CC complex (PubMed:29374058, PubMed:16109376, PubMed:16109377, CC PubMed:19103749, PubMed:21555454, PubMed:23317504). Interacts (via NET CC domain) with JMJD6 (via JmjC and N-terminal domains); the interaction CC is stronger in presence of ssRNA and recruits JMJD6 on distal enhancers CC (PubMed:24360279, PubMed:21555454, PubMed:29176719). Interacts with CC NSD3 (PubMed:29176719). {ECO:0000269|PubMed:16109376, CC ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:19103749, CC ECO:0000269|PubMed:21555454, ECO:0000269|PubMed:23317504, CC ECO:0000269|PubMed:24360279, ECO:0000269|PubMed:29374058}. CC -!- SUBUNIT: [Isoform B]: Interacts with SMC2 (PubMed:23728299). Interacts CC with NCAPD3 (PubMed:23728299). {ECO:0000269|PubMed:23728299}. CC -!- SUBUNIT: (Microbial infection) Interacts with bovine papillomavirus CC type 1 regulatory protein E2. This interactions may serve for the CC tethering of viral genomes to host mitotic chromosomes allowing CC successful partitioning of the viral genome during cell division. CC {ECO:0000269|PubMed:17189189}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus (EBV) CC protein EBNA1; this interaction facilitates transcriptional activation CC by EBNA1. {ECO:0000269|PubMed:18922874}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus-8 CC (HHV-8) protein LANA. {ECO:0000269|PubMed:16940503}. CC -!- INTERACTION: CC O60885; Q86YD7: FAM90A1; NbExp=5; IntAct=EBI-723869, EBI-6658203; CC O60885; P62993: GRB2; NbExp=2; IntAct=EBI-723869, EBI-401755; CC O60885; Q6NYC1: JMJD6; NbExp=10; IntAct=EBI-723869, EBI-8464037; CC O60885; P16333: NCK1; NbExp=2; IntAct=EBI-723869, EBI-389883; CC O60885; Q04206: RELA; NbExp=8; IntAct=EBI-723869, EBI-73886; CC O60885; A6NLX3: SPDYE4; NbExp=4; IntAct=EBI-723869, EBI-12047907; CC O60885; Q15672: TWIST1; NbExp=7; IntAct=EBI-723869, EBI-1797287; CC O60885; P03120: E2; Xeno; NbExp=4; IntAct=EBI-723869, EBI-1779322; CC O60885; P04015: E2; Xeno; NbExp=3; IntAct=EBI-723869, EBI-7010556; CC O60885; P06790: E2; Xeno; NbExp=2; IntAct=EBI-723869, EBI-7010629; CC O60885; P17383: E2; Xeno; NbExp=2; IntAct=EBI-723869, EBI-7010529; CC O60885-1; P10275: AR; NbExp=6; IntAct=EBI-9345088, EBI-608057; CC O60885-1; O60563: CCNT1; NbExp=6; IntAct=EBI-9345088, EBI-2479671; CC O60885-1; P50750: CDK9; NbExp=9; IntAct=EBI-9345088, EBI-1383449; CC O60885-1; P62805: H4C9; NbExp=10; IntAct=EBI-9345088, EBI-302023; CC O60885-1; Q15672: TWIST1; NbExp=9; IntAct=EBI-9345088, EBI-1797287; CC O60885-1; P03120: E2; Xeno; NbExp=2; IntAct=EBI-9345088, EBI-1779322; CC O60885-1; P03122: E2; Xeno; NbExp=2; IntAct=EBI-9345088, EBI-7028618; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16109376, CC ECO:0000269|PubMed:25593309}. Chromosome {ECO:0000269|PubMed:16109376, CC ECO:0000269|PubMed:21890894}. Note=Associates with acetylated chromatin CC (PubMed:21890894, PubMed:16109376). Released from chromatin upon CC deacetylation of histones that can be triggered by different signals CC such as activation of the JNK pathway or nocodazole treatment CC (PubMed:21890894, PubMed:16109376). Preferentially localizes to mitotic CC chromosomes, while it does not localize to meiotic chromosomes CC (PubMed:21890894, PubMed:16109376). {ECO:0000269|PubMed:16109376, CC ECO:0000269|PubMed:21890894}. CC -!- SUBCELLULAR LOCATION: [Isoform B]: Chromosome CC {ECO:0000269|PubMed:23728299}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=Brd4L, Long; CC IsoId=O60885-1; Sequence=Displayed; CC Name=C; Synonyms=Brd4S, Short; CC IsoId=O60885-2; Sequence=VSP_010902, VSP_010903; CC Name=B; CC IsoId=O60885-3; Sequence=VSP_047671; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:12543779}. CC -!- DOMAIN: The NET domain mediates interaction with a number of chromatin CC proteins involved in transcription regulation (NSD3, JMJD6, CHD4, CC GLTSCR1 and ATAD5). {ECO:0000269|PubMed:21555454}. CC -!- DOMAIN: The C-terminal (CTD) region mediates interaction and CC recruitment of CDK9 and CCNT1 subunits of the P-TEFb complex CC (PubMed:16109376, PubMed:16109377). It is also required for maintenance CC of higher-order chromatin structure (PubMed:22334664). CC {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, CC ECO:0000269|PubMed:22334664}. CC -!- DOMAIN: The 2 bromo domains mediate specific binding to acetylated CC histones via Asn-140 and Asn-433, respectively (PubMed:20871596). The CC exact combination of modified histone tails required to recruit BRD4 to CC target genes is still unclear. The first bromo domain has high affinity CC for acetylated histone H4 tail, whereas the second bromo domain CC recognizes multiply acetylated marks in histone H3 (PubMed:22464331). A CC number of specific inhibitors bind competitively to acetyl-lysine- CC binding residues Asn-140 and Asn-433, promoting removal from acetylated CC histones. Many of these inhibitors are benzodiazepine derivatives CC (PubMed:22137933, PubMed:22136404, PubMed:23517011, PubMed:23530754). CC {ECO:0000269|PubMed:20871596, ECO:0000269|PubMed:22136404, CC ECO:0000269|PubMed:22137933, ECO:0000269|PubMed:22464331, CC ECO:0000269|PubMed:23517011, ECO:0000269|PubMed:23530754}. CC -!- DOMAIN: [Isoform B]: Does not contain the C-terminal (CTD) region CC required to recruit the P-TEFb complex. {ECO:0000305|PubMed:23728299}. CC -!- PTM: Phosphorylation by CK2 disrupt the intramolecular binding between CC the bromo domain 2 and the NPS region and promotes binding between the CC NPS and the BID regions, leading to activate the protein and promote CC binding to acetylated histones. In absence of phosphorylation, BRD4 CC does not localize to p53/TP53 target gene promoters, phosphorylation CC promoting recruitment to p53/TP53 target promoters. CC {ECO:0000269|PubMed:23317504}. CC -!- DISEASE: Note=A chromosomal aberration involving BRD4 is found in a CC rare, aggressive, and lethal carcinoma arising in midline organs of CC young people. Translocation t(15;19)(q14;p13) with NUTM1 which produces CC a BRD4-NUTM1 fusion protein. {ECO:0000269|PubMed:11733348, CC ECO:0000269|PubMed:12543779}. CC -!- MISCELLANEOUS: Some specific inhibitors of BRD4 that prevent binding to CC acetylated histones by binding Asn-140 and Asn-433 are promising CC therapeutic molecules for the treatment of leukemias. JQ1, a thieno- CC triazolo-1,4-diazepine derivative, and I-BET, a benzodiazepine CC derivative, have been tested on tumors with success (PubMed:20871596, CC PubMed:21068722, PubMed:21964340) (Probable). Treatment with CC GSK1210151A (I-BET151, a I-BET derivative) has strong effets on mixed CC lineage leukemia and promotes myeloid differentiation and leukemia CC stem-cell depletion (PubMed:21964340) (Probable). The second bromo CC domain is inhibited by GSK046 (iBET-BD2), which specifically inhibits CC the second bromo domain of members of the BET family (BRD2, BRD3 and CC BRD4) (PubMed:32193360). {ECO:0000269|PubMed:32193360, CC ECO:0000305|PubMed:20871596, ECO:0000305|PubMed:21068722, CC ECO:0000305|PubMed:21964340}. CC -!- SIMILARITY: Belongs to the BET family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC27978.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/837/brd4"; 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; AF386649; AAL26987.1; -; mRNA. DR EMBL; Y12059; CAA72780.1; -; mRNA. DR EMBL; AC004798; AAC27978.1; ALT_INIT; Genomic_DNA. DR EMBL; AC003111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005776; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84470.1; -; Genomic_DNA. DR EMBL; BC035266; AAH35266.1; -; mRNA. DR EMBL; AY166680; AAO22237.1; ALT_TERM; mRNA. DR CCDS; CCDS12328.1; -. [O60885-1] DR CCDS; CCDS46004.1; -. [O60885-2] DR CCDS; CCDS82307.1; -. [O60885-3] DR RefSeq; NP_001317313.1; NM_001330384.1. [O60885-3] DR RefSeq; NP_055114.1; NM_014299.2. [O60885-2] DR RefSeq; NP_490597.1; NM_058243.2. [O60885-1] DR RefSeq; XP_011526156.1; XM_011527854.1. DR RefSeq; XP_011526158.1; XM_011527856.2. DR PDB; 2I8N; NMR; -; A=352-457. DR PDB; 2LSP; NMR; -; B=333-460. DR PDB; 2MJV; NMR; -; B=333-460. DR PDB; 2N3K; NMR; -; A=600-678. DR PDB; 2NCZ; NMR; -; A=601-683. DR PDB; 2ND0; NMR; -; A=601-683. DR PDB; 2ND1; NMR; -; A=601-683. DR PDB; 2NNU; X-ray; 1.59 A; B=1343-1362. DR PDB; 2OSS; X-ray; 1.35 A; A=44-168. DR PDB; 2OUO; X-ray; 1.89 A; A=333-460. DR PDB; 2YEL; X-ray; 1.65 A; A=44-168. DR PDB; 2YEM; X-ray; 2.30 A; A/B=333-460. DR PDB; 3MXF; X-ray; 1.60 A; A=42-168. DR PDB; 3P5O; X-ray; 1.60 A; A=44-168. DR PDB; 3SVF; X-ray; 1.98 A; A=44-168. DR PDB; 3SVG; X-ray; 1.68 A; A=44-168. DR PDB; 3U5J; X-ray; 1.60 A; A=44-168. DR PDB; 3U5K; X-ray; 1.80 A; A/B/C/D=44-168. DR PDB; 3U5L; X-ray; 1.39 A; A=44-168. DR PDB; 3UVW; X-ray; 1.37 A; A=44-168. DR PDB; 3UVX; X-ray; 1.91 A; A=44-168. DR PDB; 3UVY; X-ray; 2.02 A; A=44-168. DR PDB; 3UW9; X-ray; 2.30 A; A/B/C/D=44-168. DR PDB; 3ZYU; X-ray; 1.50 A; A/B=44-168. DR PDB; 4A9L; X-ray; 1.60 A; A=44-168. DR PDB; 4BJX; X-ray; 1.59 A; A=44-168. DR PDB; 4BW1; X-ray; 1.40 A; A=44-168. DR PDB; 4BW2; X-ray; 1.92 A; A=44-168. DR PDB; 4BW3; X-ray; 1.50 A; A=44-168. DR PDB; 4BW4; X-ray; 1.67 A; A=44-168. DR PDB; 4C66; X-ray; 1.87 A; A=44-167. DR PDB; 4C67; X-ray; 1.55 A; A=44-168. DR PDB; 4CFK; X-ray; 1.55 A; A=44-168. DR PDB; 4CFL; X-ray; 1.32 A; A=44-168. DR PDB; 4CL9; X-ray; 1.40 A; A=44-168. DR PDB; 4CLB; X-ray; 1.60 A; A=44-168. DR PDB; 4DON; X-ray; 1.52 A; A=44-166. DR PDB; 4E96; X-ray; 1.92 A; A=44-168. DR PDB; 4F3I; X-ray; 1.40 A; A=44-168. DR PDB; 4GPJ; X-ray; 1.60 A; A=44-168. DR PDB; 4HBV; X-ray; 1.63 A; A=42-168. DR PDB; 4HBW; X-ray; 1.69 A; A=42-168. DR PDB; 4HBX; X-ray; 1.62 A; A=42-168. DR PDB; 4HBY; X-ray; 1.59 A; A=44-168. DR PDB; 4HXK; X-ray; 1.61 A; A=44-167. DR PDB; 4HXL; X-ray; 1.52 A; A=44-167. DR PDB; 4HXM; X-ray; 1.50 A; A=44-166. DR PDB; 4HXN; X-ray; 1.49 A; A=44-167. DR PDB; 4HXO; X-ray; 1.76 A; A=44-167. DR PDB; 4HXP; X-ray; 1.73 A; A=44-166. DR PDB; 4HXR; X-ray; 1.53 A; A=44-167. DR PDB; 4HXS; X-ray; 1.43 A; A=44-166. DR PDB; 4IOO; X-ray; 1.25 A; A=44-168. DR PDB; 4IOQ; X-ray; 1.50 A; A=44-168. DR PDB; 4IOR; X-ray; 1.40 A; A=44-168. DR PDB; 4J0R; X-ray; 1.72 A; A=44-168. DR PDB; 4J0S; X-ray; 1.84 A; A=44-168. DR PDB; 4J3I; X-ray; 1.24 A; A=44-168. DR PDB; 4KV1; X-ray; 1.50 A; A/B=41-168. DR PDB; 4KV4; X-ray; 2.00 A; A=351-459. DR PDB; 4LR6; X-ray; 1.29 A; A=42-168. DR PDB; 4LRG; X-ray; 2.21 A; A=42-168. DR PDB; 4LYI; X-ray; 1.30 A; A=44-168. DR PDB; 4LYS; X-ray; 1.83 A; A=44-168. DR PDB; 4LYW; X-ray; 1.95 A; A=44-168. DR PDB; 4LZR; X-ray; 1.85 A; A=44-168. DR PDB; 4LZS; X-ray; 2.20 A; A=44-168. DR PDB; 4MEN; X-ray; 1.81 A; A=44-168. DR PDB; 4MEO; X-ray; 1.72 A; A=44-168. DR PDB; 4MEP; X-ray; 1.85 A; A=44-168. DR PDB; 4MEQ; X-ray; 1.77 A; A=44-168. DR PDB; 4MR3; X-ray; 1.68 A; A=44-168. DR PDB; 4MR4; X-ray; 1.66 A; A=44-168. DR PDB; 4NQM; X-ray; 1.58 A; A=44-168. DR PDB; 4NR8; X-ray; 1.64 A; A=44-168. DR PDB; 4NUC; X-ray; 1.40 A; A=44-168. DR PDB; 4NUD; X-ray; 1.20 A; A=44-168. DR PDB; 4NUE; X-ray; 1.30 A; A=44-168. DR PDB; 4O70; X-ray; 1.55 A; A/B=44-168. DR PDB; 4O71; X-ray; 1.36 A; A/B=44-168. DR PDB; 4O72; X-ray; 1.40 A; A=44-168. DR PDB; 4O74; X-ray; 1.45 A; A/B=44-168. DR PDB; 4O75; X-ray; 1.55 A; A=44-168. DR PDB; 4O76; X-ray; 1.70 A; A/B/C/D=44-168. DR PDB; 4O77; X-ray; 2.00 A; A/B=44-168. DR PDB; 4O78; X-ray; 1.34 A; A=44-168. DR PDB; 4O7A; X-ray; 1.34 A; A=44-168. DR PDB; 4O7B; X-ray; 1.50 A; A=44-168. DR PDB; 4O7C; X-ray; 1.55 A; A=44-168. DR PDB; 4O7E; X-ray; 1.85 A; A/B=44-168. DR PDB; 4O7F; X-ray; 1.80 A; A/B=44-168. DR PDB; 4OGI; X-ray; 1.73 A; A/B=44-168. DR PDB; 4OGJ; X-ray; 1.65 A; A/B=44-168. DR PDB; 4PCE; X-ray; 1.29 A; A=44-168. DR PDB; 4PCI; X-ray; 1.25 A; A=44-168. DR PDB; 4PS5; X-ray; 1.40 A; A/B=44-168. DR PDB; 4QB3; X-ray; 0.94 A; A=44-168. DR PDB; 4QR3; X-ray; 1.37 A; A=44-166. DR PDB; 4QR4; X-ray; 1.28 A; A=44-166. DR PDB; 4QR5; X-ray; 1.41 A; A=44-166. DR PDB; 4QZS; X-ray; 1.45 A; A=44-168. DR PDB; 4UIX; X-ray; 1.58 A; A/B/C=44-168. DR PDB; 4UIY; X-ray; 1.30 A; A=44-168. DR PDB; 4UIZ; X-ray; 1.19 A; A=44-168. DR PDB; 4UYD; X-ray; 1.37 A; A=44-183. DR PDB; 4WHW; X-ray; 1.34 A; A=44-168. DR PDB; 4WIV; X-ray; 1.56 A; A=44-168. DR PDB; 4X2I; X-ray; 1.20 A; A=42-166. DR PDB; 4XY9; X-ray; 1.83 A; A=42-168. DR PDB; 4XYA; X-ray; 2.05 A; A=42-168. DR PDB; 4YH3; X-ray; 1.60 A; A=44-170. DR PDB; 4YH4; X-ray; 1.33 A; A=44-170. DR PDB; 4Z1Q; X-ray; 1.40 A; A/B=42-167. DR PDB; 4Z1S; X-ray; 1.06 A; A/B=42-166. DR PDB; 4Z93; X-ray; 1.27 A; A=349-460. DR PDB; 4ZC9; X-ray; 0.99 A; A=44-168. DR PDB; 4ZW1; X-ray; 1.75 A; A=44-168. DR PDB; 5A5S; X-ray; 1.36 A; A=44-168. DR PDB; 5A85; X-ray; 1.72 A; A=44-168. DR PDB; 5ACY; X-ray; 2.01 A; A/B=44-168. DR PDB; 5AD2; X-ray; 2.01 A; A/B=44-168. DR PDB; 5AD3; X-ray; 1.49 A; A/B=44-168. DR PDB; 5BT4; X-ray; 1.50 A; A/B/C=44-168. DR PDB; 5CFW; X-ray; 1.15 A; A=44-168. DR PDB; 5COI; X-ray; 1.62 A; A=44-168. DR PDB; 5CP5; X-ray; 1.79 A; A=44-168. DR PDB; 5CPE; X-ray; 1.62 A; A=44-168. DR PDB; 5CQT; X-ray; 1.60 A; A=44-168. DR PDB; 5CRM; X-ray; 1.99 A; A=44-168. DR PDB; 5CRZ; X-ray; 2.12 A; A=44-168. DR PDB; 5CS8; X-ray; 1.62 A; A=44-168. DR PDB; 5CTL; X-ray; 2.51 A; A=44-168. DR PDB; 5CY9; X-ray; 1.55 A; A=44-168. DR PDB; 5D0C; X-ray; 1.49 A; A=44-168. DR PDB; 5D24; X-ray; 1.65 A; A=43-168. DR PDB; 5D25; X-ray; 1.70 A; A=43-168. DR PDB; 5D26; X-ray; 1.82 A; A=42-168. DR PDB; 5D3H; X-ray; 1.70 A; A=44-168. DR PDB; 5D3J; X-ray; 1.70 A; A=43-168. DR PDB; 5D3L; X-ray; 1.50 A; A=42-168. DR PDB; 5D3N; X-ray; 2.15 A; A=43-168. DR PDB; 5D3P; X-ray; 1.95 A; A=42-168. DR PDB; 5D3R; X-ray; 2.20 A; A=42-168. DR PDB; 5D3S; X-ray; 1.75 A; A=44-168. DR PDB; 5D3T; X-ray; 1.93 A; A=42-168. DR PDB; 5DLX; X-ray; 1.90 A; A=44-168. DR PDB; 5DLZ; X-ray; 1.70 A; A=44-168. DR PDB; 5DW2; X-ray; 1.12 A; A=44-170. DR PDB; 5DX4; X-ray; 2.30 A; A=44-168. DR PDB; 5E0R; X-ray; 1.35 A; A=44-168. DR PDB; 5EGU; X-ray; 2.21 A; A/B/C/D=44-168. DR PDB; 5EI4; X-ray; 1.05 A; A=44-168. DR PDB; 5EIS; X-ray; 1.60 A; A=44-168. DR PDB; 5F5Z; X-ray; 1.76 A; A=44-168. DR PDB; 5F60; X-ray; 1.35 A; A=44-168. DR PDB; 5F61; X-ray; 1.45 A; A/B=44-168. DR PDB; 5F62; X-ray; 1.35 A; A=44-168. DR PDB; 5F63; X-ray; 1.45 A; A=44-168. DR PDB; 5FBX; X-ray; 1.85 A; A=44-168. DR PDB; 5H21; X-ray; 1.59 A; A=44-167. DR PDB; 5HCL; X-ray; 1.50 A; A=44-168. DR PDB; 5HLS; X-ray; 2.18 A; A=42-168. DR PDB; 5HM0; X-ray; 1.40 A; A=42-168. DR PDB; 5HQ5; X-ray; 1.60 A; A=44-168. DR PDB; 5HQ6; X-ray; 1.95 A; A=44-166. DR PDB; 5HQ7; X-ray; 1.90 A; A=44-167. DR PDB; 5I80; X-ray; 1.45 A; A=42-167. DR PDB; 5I88; X-ray; 1.40 A; A=42-167. DR PDB; 5IGK; X-ray; 1.70 A; A=44-168. DR PDB; 5JWM; X-ray; 1.71 A; A/B=333-460. DR PDB; 5KDH; X-ray; 1.50 A; A=44-168. DR PDB; 5KHM; X-ray; 1.48 A; A/B=44-168. DR PDB; 5KJ0; X-ray; 1.51 A; A=44-168. DR PDB; 5KU3; X-ray; 1.14 A; A=42-167. DR PDB; 5LJ1; X-ray; 1.90 A; A=42-168. DR PDB; 5LJ2; X-ray; 1.19 A; A=42-168. DR PDB; 5LRQ; X-ray; 1.70 A; A=42-163. DR PDB; 5LUU; X-ray; 1.61 A; A=44-168. DR PDB; 5M39; X-ray; 1.38 A; A/B=42-168. DR PDB; 5M3A; X-ray; 1.65 A; A=44-168. DR PDB; 5MKZ; X-ray; 1.62 A; A=44-168. DR PDB; 5MLI; X-ray; 1.63 A; A=42-168. DR PDB; 5N2M; X-ray; 1.54 A; A=44-168. DR PDB; 5NNC; X-ray; 2.22 A; A/B=44-168. DR PDB; 5NND; X-ray; 1.82 A; A/B=44-168. DR PDB; 5NNE; X-ray; 1.15 A; A=44-168. DR PDB; 5NNF; X-ray; 1.15 A; A=44-168. DR PDB; 5NNG; X-ray; 1.20 A; A=44-168. DR PDB; 5O97; X-ray; 1.30 A; A=44-168. DR PDB; 5OVB; X-ray; 1.95 A; A/B=44-168. DR PDB; 5OWM; X-ray; 1.50 A; A=44-168. DR PDB; 5OWW; X-ray; 1.50 A; A/B/C/D=44-168. DR PDB; 5S9P; X-ray; 2.10 A; A/B/D/E=44-168. DR PDB; 5S9Q; X-ray; 1.85 A; A/B/D/E=44-168. DR PDB; 5S9R; X-ray; 1.85 A; A=44-168. DR PDB; 5T35; X-ray; 2.70 A; A/E=333-460. DR PDB; 5TI2; X-ray; 1.65 A; A=44-168. DR PDB; 5TI3; X-ray; 1.70 A; A=44-168. DR PDB; 5TI4; X-ray; 1.62 A; A=44-168. DR PDB; 5TI5; X-ray; 1.83 A; A=44-168. DR PDB; 5TI6; X-ray; 1.70 A; A=44-168. DR PDB; 5TI7; X-ray; 1.65 A; A=44-168. DR PDB; 5U28; X-ray; 1.80 A; A=44-180. DR PDB; 5U2C; X-ray; 3.30 A; A/B=342-460. DR PDB; 5U2E; X-ray; 1.99 A; A/B=42-180. DR PDB; 5U2F; X-ray; 2.52 A; A/B=42-180. DR PDB; 5UEO; X-ray; 1.85 A; A/B=352-457. DR PDB; 5UEP; X-ray; 1.77 A; A=352-457. DR PDB; 5UEQ; X-ray; 1.70 A; A=352-457. DR PDB; 5UER; X-ray; 1.87 A; A=352-457. DR PDB; 5UES; X-ray; 1.62 A; A=352-457. DR PDB; 5UET; X-ray; 2.29 A; A=352-457. DR PDB; 5UEU; X-ray; 2.26 A; A/B=352-457. DR PDB; 5UEV; X-ray; 1.94 A; A=352-457. DR PDB; 5UEX; X-ray; 2.29 A; A=352-457. DR PDB; 5UEY; X-ray; 2.41 A; A=352-457. DR PDB; 5UEZ; X-ray; 1.51 A; A=352-457. DR PDB; 5UF0; X-ray; 1.35 A; A=352-457. DR PDB; 5ULA; X-ray; 1.50 A; A/B=44-168. DR PDB; 5UOO; X-ray; 1.69 A; A=333-460. DR PDB; 5UVS; X-ray; 2.15 A; A=352-457. DR PDB; 5UVT; X-ray; 1.67 A; A=352-457. DR PDB; 5UVU; X-ray; 1.66 A; A=352-457. DR PDB; 5UVV; X-ray; 1.99 A; A/B=352-457. DR PDB; 5UVW; X-ray; 2.14 A; A/B/C=57-165. DR PDB; 5UVX; X-ray; 1.53 A; A/B=352-457. DR PDB; 5UVY; X-ray; 2.25 A; A=352-457. DR PDB; 5UVZ; X-ray; 1.63 A; A=352-457. DR PDB; 5V67; X-ray; 1.78 A; A=44-168. DR PDB; 5VBO; X-ray; 1.30 A; A=44-168. DR PDB; 5VBP; X-ray; 1.83 A; A/B=44-168. DR PDB; 5VOM; X-ray; 1.67 A; A/B=44-168. DR PDB; 5VZS; X-ray; 1.71 A; A/B=42-168. DR PDB; 5W55; X-ray; 1.35 A; A=42-168. DR PDB; 5WA5; X-ray; 1.17 A; A=42-168. DR PDB; 5WMA; X-ray; 1.40 A; A=44-168. DR PDB; 5WMD; X-ray; 1.27 A; A=44-168. DR PDB; 5WMG; X-ray; 1.19 A; A=44-168. DR PDB; 5WUU; X-ray; 1.72 A; A=44-167. DR PDB; 5XHY; X-ray; 1.98 A; A=44-166. DR PDB; 5XI2; X-ray; 1.91 A; A=44-166. DR PDB; 5XI3; X-ray; 1.67 A; A=44-166. DR PDB; 5XI4; X-ray; 1.49 A; A=44-166. DR PDB; 5Y1Y; X-ray; 1.91 A; A=44-167. DR PDB; 5Y8C; X-ray; 1.42 A; A=44-166. DR PDB; 5Y8W; X-ray; 1.76 A; A=44-168. DR PDB; 5Y8Y; X-ray; 1.87 A; A=44-168. DR PDB; 5Y8Z; X-ray; 1.84 A; A=44-168. DR PDB; 5Y93; X-ray; 1.62 A; A=44-168. DR PDB; 5Y94; X-ray; 2.00 A; A=44-168. DR PDB; 5YOU; X-ray; 1.50 A; A=42-168. DR PDB; 5YOV; X-ray; 1.45 A; A=42-168. DR PDB; 5YQX; X-ray; 1.82 A; A=44-167. DR PDB; 5Z1R; X-ray; 1.62 A; A=44-168. DR PDB; 5Z1S; X-ray; 1.42 A; A=44-168. DR PDB; 5Z1T; X-ray; 1.42 A; A=44-168. DR PDB; 5Z5T; X-ray; 1.99 A; A=44-167. DR PDB; 5Z5U; X-ray; 1.63 A; A=44-167. DR PDB; 5Z5V; X-ray; 1.66 A; A=44-167. DR PDB; 5Z8G; X-ray; 1.70 A; A=44-168. DR PDB; 5Z8R; X-ray; 2.00 A; A=44-168. DR PDB; 5Z8Z; X-ray; 1.80 A; A=44-168. DR PDB; 5Z90; X-ray; 1.80 A; A=44-168. DR PDB; 5Z9C; NMR; -; A=53-168. DR PDB; 5Z9K; X-ray; 1.89 A; A=44-168. DR PDB; 6AFR; X-ray; 2.00 A; A=44-168. DR PDB; 6AJV; X-ray; 1.45 A; A=42-168. DR PDB; 6AJW; X-ray; 1.40 A; A=42-168. DR PDB; 6AJX; X-ray; 1.89 A; A=42-168. DR PDB; 6AJY; X-ray; 1.60 A; A=42-168. DR PDB; 6AJZ; Other; 1.30 A; A=42-168. DR PDB; 6BN7; X-ray; 3.50 A; C=42-168. DR PDB; 6BN8; X-ray; 3.99 A; C=42-168. DR PDB; 6BN9; X-ray; 4.38 A; C=42-168. DR PDB; 6BNB; X-ray; 6.34 A; C=42-168. DR PDB; 6BNH; NMR; -; A=601-683. DR PDB; 6BOY; X-ray; 3.33 A; C=42-168. DR PDB; 6C7Q; X-ray; 1.51 A; A=333-460. DR PDB; 6C7R; X-ray; 1.50 A; A=44-165. DR PDB; 6CD4; X-ray; 1.23 A; A=42-168. DR PDB; 6CD5; X-ray; 1.58 A; A=44-168. DR PDB; 6CIS; X-ray; 1.51 A; A=44-166. DR PDB; 6CIY; X-ray; 1.68 A; A=44-168. DR PDB; 6CJ1; X-ray; 1.53 A; A=44-166. DR PDB; 6CJ2; X-ray; 1.47 A; A=42-166. DR PDB; 6CKR; X-ray; 1.62 A; A/B=44-168. DR PDB; 6CKS; X-ray; 1.72 A; A=44-168. DR PDB; 6CZU; X-ray; 1.47 A; A=42-170. DR PDB; 6CZV; X-ray; 1.88 A; A=42-170. DR PDB; 6DJC; X-ray; 1.46 A; A/B=44-173. DR PDB; 6DL2; X-ray; 1.47 A; A=44-168. DR PDB; 6DMJ; X-ray; 1.15 A; A=44-168. DR PDB; 6DML; X-ray; 1.50 A; A=44-168. DR PDB; 6DNE; X-ray; 2.96 A; A/B=44-477. DR PDB; 6DUV; X-ray; 1.80 A; A/B=347-458. DR PDB; 6E4A; X-ray; 1.26 A; A/B=44-170. DR PDB; 6FFD; X-ray; 1.83 A; A=347-463. DR PDB; 6FNX; X-ray; 1.19 A; A=44-168. DR PDB; 6FO5; X-ray; 0.95 A; A=44-168. DR PDB; 6FSY; X-ray; 1.34 A; A=42-168. DR PDB; 6FT3; X-ray; 1.28 A; A=42-168. DR PDB; 6FT4; X-ray; 1.34 A; A=42-168. DR PDB; 6G0D; X-ray; 1.31 A; A=42-168. DR PDB; 6G0E; X-ray; 1.61 A; A=42-168. DR PDB; 6G0F; X-ray; 1.62 A; A=42-168. DR PDB; 6G0G; X-ray; 1.48 A; A=42-168. DR PDB; 6G0H; X-ray; 1.91 A; A=42-168. DR PDB; 6G0O; X-ray; 1.40 A; A=42-168. DR PDB; 6G0P; X-ray; 1.30 A; A=42-168. DR PDB; 6G0Q; X-ray; 1.40 A; A=42-168. DR PDB; 6G0R; X-ray; 1.25 A; A=42-168. DR PDB; 6G0S; X-ray; 1.48 A; A/B=42-168. DR PDB; 6HDQ; X-ray; 1.70 A; A=44-168. DR PDB; 6HOV; X-ray; 1.85 A; A=44-168. DR PDB; 6I7X; X-ray; 1.20 A; A=44-168. DR PDB; 6I7Y; X-ray; 1.00 A; A=44-168. DR PDB; 6IN1; X-ray; 1.50 A; A=42-168. DR PDB; 6JI3; X-ray; 2.20 A; A=44-166. DR PDB; 6JI4; X-ray; 1.60 A; A=44-166. DR PDB; 6JI5; X-ray; 2.00 A; A=44-166. DR PDB; 6JJ3; X-ray; 1.72 A; A=44-167. DR PDB; 6JJ5; X-ray; 1.20 A; A=44-167. DR PDB; 6JJ6; X-ray; 1.40 A; A=44-167. DR PDB; 6JJB; X-ray; 1.51 A; A=44-167. DR PDB; 6KEC; X-ray; 1.35 A; A=44-168. DR PDB; 6KED; X-ray; 2.55 A; A=44-168. DR PDB; 6KEE; X-ray; 2.12 A; A=44-168. DR PDB; 6KEF; X-ray; 2.44 A; A=44-168. DR PDB; 6KEG; X-ray; 2.23 A; A=44-168. DR PDB; 6KEH; X-ray; 1.55 A; A=44-168. DR PDB; 6KEI; X-ray; 1.45 A; A=44-168. DR PDB; 6KEJ; X-ray; 1.85 A; A=44-168. DR PDB; 6KEK; X-ray; 1.55 A; A=44-168. DR PDB; 6KO2; X-ray; 1.50 A; A=351-457. DR PDB; 6LG4; X-ray; 1.85 A; A=44-167. DR PDB; 6LG5; X-ray; 1.83 A; A=44-167. DR PDB; 6LG6; X-ray; 1.98 A; A=44-167. DR PDB; 6LG7; X-ray; 1.83 A; A=44-167. DR PDB; 6LG8; X-ray; 1.58 A; A=44-167. DR PDB; 6LG9; X-ray; 1.81 A; A=44-167. DR PDB; 6LIH; X-ray; 1.62 A; A=44-166. DR PDB; 6LIM; X-ray; 1.76 A; A=44-166. DR PDB; 6MAU; X-ray; 2.11 A; A=44-170. DR PDB; 6MH1; X-ray; 1.60 A; A/B=44-168. DR PDB; 6MH7; X-ray; 1.74 A; A/B=44-168. DR PDB; 6MNL; NMR; -; B=333-460. DR PDB; 6P05; X-ray; 1.54 A; A=44-168. DR PDB; 6PRT; X-ray; 1.30 A; A=43-168. DR PDB; 6PS9; X-ray; 1.21 A; A=44-168. DR PDB; 6PSB; X-ray; 1.59 A; A=44-168. DR PDB; 6Q3Y; X-ray; 1.20 A; A/B=42-168. DR PDB; 6Q3Z; X-ray; 2.00 A; A/B=44-168. DR PDB; 6RWJ; X-ray; 1.40 A; A=44-168. DR PDB; 6S25; X-ray; 1.10 A; A=44-168. DR PDB; 6S4B; X-ray; 1.60 A; A=44-168. DR PDB; 6S6K; X-ray; 1.40 A; A=44-168. DR PDB; 6SA2; X-ray; 1.50 A; A=44-168. DR PDB; 6SA3; X-ray; 1.80 A; A=44-168. DR PDB; 6SAH; X-ray; 1.50 A; A=44-168. DR PDB; 6SAJ; X-ray; 1.50 A; A=44-168. DR PDB; 6SB8; X-ray; 1.50 A; A=44-168. DR PDB; 6SE4; X-ray; 1.38 A; A=44-168. DR PDB; 6SIS; X-ray; 3.50 A; A/E=333-460. DR PDB; 6SWN; X-ray; 1.28 A; AAA=44-168. DR PDB; 6SWQ; X-ray; 1.60 A; AAA=44-168. DR PDB; 6TPX; X-ray; 1.48 A; AAA=44-168. DR PDB; 6TPY; X-ray; 1.80 A; AAA=44-168. DR PDB; 6TPZ; X-ray; 1.30 A; AAA=44-168. DR PDB; 6U0D; X-ray; 1.43 A; A=44-168. DR PDB; 6U6K; X-ray; 1.70 A; A=42-168. DR PDB; 6U6L; X-ray; 2.60 A; A=347-464. DR PDB; 6U72; X-ray; 2.30 A; A/B=42-168. DR PDB; 6U74; X-ray; 1.85 A; A/B/C/D=42-168. DR PDB; 6U8G; X-ray; 2.60 A; A/B/C/D=42-168. DR PDB; 6U8I; X-ray; 2.50 A; A=347-464. DR PDB; 6U8M; X-ray; 1.95 A; A/B=42-168. DR PDB; 6ULS; X-ray; 1.50 A; A=42-168. DR PDB; 6ULV; X-ray; 2.20 A; A/B/C/D=42-168. DR PDB; 6UVJ; X-ray; 1.38 A; A=44-168. DR PDB; 6UVM; X-ray; 1.51 A; A=44-168. DR PDB; 6UWU; X-ray; 2.00 A; A=44-168. DR PDB; 6UWX; X-ray; 1.31 A; A=44-168. DR PDB; 6V0U; X-ray; 1.40 A; A=44-168. DR PDB; 6V1K; X-ray; 1.75 A; A=44-168. DR PDB; 6V1L; X-ray; 2.10 A; A=44-168. DR PDB; 6V1U; X-ray; 1.73 A; A=44-168. DR PDB; 6VIW; X-ray; 2.43 A; A/B/C=57-168. DR PDB; 6VIX; X-ray; 2.12 A; A/B/C/D=352-457. DR PDB; 6VIZ; X-ray; 2.39 A; A/B/C=57-168. DR PDB; 6VUB; X-ray; 1.50 A; A=44-168. DR PDB; 6VUC; X-ray; 1.55 A; A=44-168. DR PDB; 6VUF; X-ray; 1.59 A; A/B=44-168. DR PDB; 6VUJ; X-ray; 1.48 A; A=44-168. DR PDB; 6WGX; X-ray; 1.53 A; A/B=44-168. DR PDB; 6WVX; X-ray; 1.55 A; A/B=44-168. DR PDB; 6WW8; X-ray; 2.30 A; A=43-180. DR PDB; 6X7B; X-ray; 1.95 A; A/B=44-176. DR PDB; 6X7C; X-ray; 2.70 A; A=44-176. DR PDB; 6X7D; X-ray; 2.50 A; A/B=44-176. DR PDB; 6XUZ; X-ray; 1.07 A; A=44-168. DR PDB; 6XV3; X-ray; 1.47 A; A/B/C/D=44-168. DR PDB; 6XV7; X-ray; 1.67 A; A=44-168. DR PDB; 6XVC; X-ray; 1.10 A; B=44-168. DR PDB; 6YIN; X-ray; 1.53 A; A=44-168. DR PDB; 6YQN; X-ray; 1.05 A; A=44-168. DR PDB; 6YQO; X-ray; 1.07 A; A=44-168. DR PDB; 6YQP; X-ray; 1.25 A; A=44-168. DR PDB; 6YQZ; X-ray; 1.39 A; A=44-168. DR PDB; 6Z7G; X-ray; 1.59 A; AAA=44-168. DR PDB; 6Z7L; X-ray; 1.62 A; AAA=44-168. DR PDB; 6Z7M; X-ray; 1.26 A; AAA=44-168. DR PDB; 6ZB3; X-ray; 1.42 A; AAA=44-168. DR PDB; 6ZCI; X-ray; 1.98 A; A=44-168. DR PDB; 6ZED; X-ray; 1.08 A; AAA=44-168. DR PDB; 6ZEL; X-ray; 1.12 A; AAA=44-168. DR PDB; 6ZF9; X-ray; 1.20 A; AAA=44-168. DR PDB; 7A9U; X-ray; 1.44 A; AAA=44-168. DR PDB; 7AJN; X-ray; 1.48 A; A=44-168. DR PDB; 7AQT; NMR; -; A=351-459. DR PDB; 7AXR; X-ray; 1.50 A; A=44-168. DR PDB; 7B1T; X-ray; 1.92 A; A=44-168. DR PDB; 7C2Z; X-ray; 1.30 A; A=44-168. DR PDB; 7C6P; X-ray; 1.73 A; A=352-457. DR PDB; 7DHS; X-ray; 1.76 A; A/B=44-168. DR PDB; 7EHW; X-ray; 1.65 A; A=44-167. DR PDB; 7EHY; X-ray; 1.51 A; A=44-167. DR PDB; 7EIG; X-ray; 1.30 A; A=44-167. DR PDB; 7EIK; X-ray; 1.70 A; A=44-167. DR PDB; 7EIL; X-ray; 1.70 A; A=44-167. DR PDB; 7FH2; X-ray; 2.49 A; A/B/C/D=42-168. DR PDB; 7JKW; X-ray; 1.20 A; A=44-168. DR PDB; 7JKX; X-ray; 1.20 A; A=44-168. DR PDB; 7JKY; X-ray; 1.16 A; A=44-168. DR PDB; 7JKZ; X-ray; 2.49 A; A=333-460. DR PDB; 7K6G; X-ray; 1.70 A; A/B=44-168. DR PDB; 7K6H; X-ray; 1.50 A; A=44-168. DR PDB; 7KHH; X-ray; 2.28 A; D=44-168. DR PDB; 7KHL; X-ray; 1.29 A; A/B=44-168. DR PDB; 7KO0; X-ray; 1.90 A; A=349-460. DR PDB; 7L9M; X-ray; 1.45 A; A/B=44-168. DR PDB; 7LA9; X-ray; 2.20 A; A/B/C/D/E/F=44-168. DR PDB; 7LH8; X-ray; 1.75 A; A=44-168. DR PDB; 7M16; X-ray; 1.42 A; A=44-168. DR PDB; 7MCE; X-ray; 1.76 A; A=44-168. DR PDB; 7MCF; X-ray; 2.19 A; A/B=44-168. DR PDB; 7MLQ; X-ray; 1.32 A; A=44-168. DR PDB; 7MLR; X-ray; 1.20 A; A=44-168. DR PDB; 7MLS; X-ray; 1.26 A; A=44-168. DR PDB; 7MR5; X-ray; 1.82 A; A/B=44-168. DR PDB; 7MR6; X-ray; 1.85 A; A/B=44-168. DR PDB; 7MR7; X-ray; 1.40 A; A/B=44-168. DR PDB; 7MR8; X-ray; 1.20 A; A=44-168. DR PDB; 7MR9; X-ray; 1.19 A; A=44-168. DR PDB; 7MRA; X-ray; 1.16 A; A=44-168. DR PDB; 7MRB; X-ray; 1.20 A; A=44-168. DR PDB; 7O18; X-ray; 1.70 A; AAA=44-168. DR PDB; 7OEO; X-ray; 1.51 A; AAA=347-463. DR PDB; 7P6V; X-ray; 1.17 A; AAA=44-168. DR PDB; 7P6W; X-ray; 1.31 A; AAA=44-168. DR PDB; 7P6Y; X-ray; 1.88 A; AAA/BBB=44-168. DR PDB; 7Q3F; X-ray; 1.21 A; A=44-168. DR PDB; 7QDL; X-ray; 1.67 A; AAA=44-168. DR PDB; 7R5B; X-ray; 1.77 A; A=44-168. DR PDB; 7R9C; X-ray; 1.50 A; A=44-168. DR PDB; 7REK; X-ray; 1.20 A; A/B=44-168. DR PDB; 7REL; X-ray; 1.55 A; A=44-168. DR PDB; 7REM; X-ray; 1.80 A; A=44-168. DR PDB; 7RJO; X-ray; 1.38 A; A=44-168. DR PDB; 7RJP; X-ray; 1.25 A; A=44-168. DR PDB; 7RJQ; X-ray; 1.72 A; A=44-168. DR PDB; 7RJR; X-ray; 1.45 A; A=44-168. DR PDB; 7RMD; X-ray; 1.18 A; A=44-168. DR PDB; 7RN2; X-ray; 1.05 A; A=44-168. DR PDB; 7RUH; X-ray; 1.70 A; A=333-460. DR PDB; 7RUI; X-ray; 1.35 A; A=44-168. DR PDB; 7RXR; X-ray; 1.41 A; A/B=44-168. DR PDB; 7RXS; X-ray; 1.43 A; A=44-168. DR PDB; 7RXT; X-ray; 1.68 A; A=44-168. DR PDB; 7T3F; X-ray; 1.28 A; A=44-167. DR PDB; 7TUQ; X-ray; 2.68 A; A/B=42-180. DR PDB; 7TV0; X-ray; 2.60 A; A/B/C/D=42-180. DR PDB; 7UGF; X-ray; 1.45 A; A=44-168. DR PDB; 7USJ; X-ray; 2.08 A; A/B=352-457. DR PDB; 7USK; X-ray; 1.22 A; A=352-457. DR PDB; 7UTY; X-ray; 1.55 A; A=44-168. DR PDB; 7UZN; X-ray; 1.69 A; A=44-168. DR PDB; 7V1U; X-ray; 1.82 A; A=44-168. DR PDB; 7V2J; X-ray; 2.24 A; A=44-168. DR PDB; 7W3D; X-ray; 1.98 A; A=44-168. DR PDB; 7WJS; X-ray; 2.73 A; A/B/C=44-168. DR PDB; 7WKY; X-ray; 2.83 A; A/B/C=44-168. DR PDB; 7WL4; X-ray; 1.82 A; A/B/C/D=44-168. DR PDB; 7WWZ; X-ray; 1.16 A; A=43-168. DR PDB; 7X6T; X-ray; 1.44 A; A=42-165. DR PDB; 7YL2; X-ray; 1.62 A; A=44-168. DR PDB; 7YMG; X-ray; 1.40 A; A/B=44-168. DR PDB; 7YQ9; X-ray; 1.50 A; A/B=44-168. DR PDB; 7ZAQ; X-ray; 1.11 A; A=44-168. DR PDB; 7ZE6; X-ray; 1.04 A; A=44-168. DR PDB; 7ZE7; X-ray; 1.23 A; AAA=44-168. DR PDB; 7ZEF; X-ray; 1.12 A; A=44-168. DR PDB; 7ZFN; X-ray; 1.12 A; AAA=44-168. DR PDB; 7ZFS; X-ray; 1.25 A; AAA=44-168. DR PDB; 7ZFT; X-ray; 1.28 A; AAA=44-168. DR PDB; 7ZFU; X-ray; 1.29 A; AAA=44-168. DR PDB; 7ZFV; X-ray; 1.37 A; A=44-168. DR PDB; 7ZFY; X-ray; 1.15 A; AAA=44-168. DR PDB; 7ZFZ; X-ray; 1.08 A; AAA=44-168. DR PDB; 7ZG1; X-ray; 1.16 A; AAA=44-168. DR PDB; 7ZG2; X-ray; 1.18 A; AAA=44-168. DR PDB; 7ZNT; X-ray; 3.00 A; G/H=333-460. DR PDB; 8B5B; X-ray; 1.92 A; A/B/C=44-168. DR PDB; 8B5C; X-ray; 1.58 A; A=44-168. DR PDB; 8BDS; X-ray; 1.72 A; D=44-168. DR PDB; 8BDT; X-ray; 2.70 A; A/E=333-460. DR PDB; 8BDX; X-ray; 2.93 A; A/E=333-460. DR PDB; 8BEB; X-ray; 3.18 A; D=44-168. DR PDB; 8CKF; X-ray; 1.88 A; A=44-168. DR PDB; 8DYR; X-ray; 1.47 A; B=44-168. DR PDB; 8E17; X-ray; 1.47 A; B=44-168. DR PDB; 8E3W; X-ray; 1.47 A; B=44-168. DR PDB; 8EAD; X-ray; 1.65 A; A=44-168. DR PDB; 8EWV; X-ray; 3.40 A; D/H/L/P/T/X=44-168. DR PDB; 8G46; EM; 2.20 A; C=333-460. DR PDB; 8GPZ; X-ray; 1.53 A; A=44-166. DR PDB; 8GQ0; X-ray; 1.44 A; A=44-166. DR PDB; 8IBQ; X-ray; 1.45 A; A=44-165. DR PDB; 8IDH; X-ray; 1.57 A; A=349-460. DR PDB; 8OV6; EM; 3.77 A; C=42-459. DR PDB; 8P9F; X-ray; 1.30 A; A=44-168. DR PDB; 8P9G; X-ray; 1.10 A; A=44-168. DR PDB; 8P9H; X-ray; 1.19 A; A=44-168. DR PDB; 8P9I; X-ray; 1.23 A; A/B=44-168. DR PDB; 8P9J; X-ray; 1.42 A; A=44-168. DR PDB; 8P9K; X-ray; 1.25 A; A=44-168. DR PDB; 8P9L; X-ray; 1.29 A; A=44-168. DR PDB; 8PIQ; X-ray; 1.12 A; A=44-168. DR PDB; 8PXA; X-ray; 1.30 A; AAA=44-168. DR PDB; 8PXM; X-ray; 2.38 A; A/B=44-168. DR PDB; 8PXN; X-ray; 1.95 A; A/B/C/D=44-168. DR PDBsum; 2I8N; -. DR PDBsum; 2LSP; -. DR PDBsum; 2MJV; -. DR PDBsum; 2N3K; -. DR PDBsum; 2NCZ; -. DR PDBsum; 2ND0; -. DR PDBsum; 2ND1; -. DR PDBsum; 2NNU; -. DR PDBsum; 2OSS; -. DR PDBsum; 2OUO; -. DR PDBsum; 2YEL; -. DR PDBsum; 2YEM; -. DR PDBsum; 3MXF; -. DR PDBsum; 3P5O; -. DR PDBsum; 3SVF; -. DR PDBsum; 3SVG; -. DR PDBsum; 3U5J; -. DR PDBsum; 3U5K; -. DR PDBsum; 3U5L; -. DR PDBsum; 3UVW; -. DR PDBsum; 3UVX; -. DR PDBsum; 3UVY; -. DR PDBsum; 3UW9; -. DR PDBsum; 3ZYU; -. DR PDBsum; 4A9L; -. DR PDBsum; 4BJX; -. DR PDBsum; 4BW1; -. DR PDBsum; 4BW2; -. DR PDBsum; 4BW3; -. DR PDBsum; 4BW4; -. DR PDBsum; 4C66; -. DR PDBsum; 4C67; -. DR PDBsum; 4CFK; -. DR PDBsum; 4CFL; -. DR PDBsum; 4CL9; -. DR PDBsum; 4CLB; -. DR PDBsum; 4DON; -. DR PDBsum; 4E96; -. DR PDBsum; 4F3I; -. DR PDBsum; 4GPJ; -. DR PDBsum; 4HBV; -. DR PDBsum; 4HBW; -. DR PDBsum; 4HBX; -. DR PDBsum; 4HBY; -. DR PDBsum; 4HXK; -. DR PDBsum; 4HXL; -. DR PDBsum; 4HXM; -. DR PDBsum; 4HXN; -. DR PDBsum; 4HXO; -. DR PDBsum; 4HXP; -. DR PDBsum; 4HXR; -. DR PDBsum; 4HXS; -. DR PDBsum; 4IOO; -. DR PDBsum; 4IOQ; -. DR PDBsum; 4IOR; -. DR PDBsum; 4J0R; -. DR PDBsum; 4J0S; -. DR PDBsum; 4J3I; -. DR PDBsum; 4KV1; -. DR PDBsum; 4KV4; -. DR PDBsum; 4LR6; -. DR PDBsum; 4LRG; -. DR PDBsum; 4LYI; -. DR PDBsum; 4LYS; -. DR PDBsum; 4LYW; -. DR PDBsum; 4LZR; -. DR PDBsum; 4LZS; -. DR PDBsum; 4MEN; -. DR PDBsum; 4MEO; -. DR PDBsum; 4MEP; -. DR PDBsum; 4MEQ; -. DR PDBsum; 4MR3; -. DR PDBsum; 4MR4; -. DR PDBsum; 4NQM; -. DR PDBsum; 4NR8; -. DR PDBsum; 4NUC; -. DR PDBsum; 4NUD; -. DR PDBsum; 4NUE; -. DR PDBsum; 4O70; -. DR PDBsum; 4O71; -. DR PDBsum; 4O72; -. DR PDBsum; 4O74; -. DR PDBsum; 4O75; -. DR PDBsum; 4O76; -. DR PDBsum; 4O77; -. DR PDBsum; 4O78; -. DR PDBsum; 4O7A; -. DR PDBsum; 4O7B; -. DR PDBsum; 4O7C; -. DR PDBsum; 4O7E; -. DR PDBsum; 4O7F; -. DR PDBsum; 4OGI; -. DR PDBsum; 4OGJ; -. DR PDBsum; 4PCE; -. DR PDBsum; 4PCI; -. DR PDBsum; 4PS5; -. DR PDBsum; 4QB3; -. DR PDBsum; 4QR3; -. DR PDBsum; 4QR4; -. DR PDBsum; 4QR5; -. DR PDBsum; 4QZS; -. DR PDBsum; 4UIX; -. DR PDBsum; 4UIY; -. DR PDBsum; 4UIZ; -. DR PDBsum; 4UYD; -. DR PDBsum; 4WHW; -. DR PDBsum; 4WIV; -. DR PDBsum; 4X2I; -. DR PDBsum; 4XY9; -. DR PDBsum; 4XYA; -. DR PDBsum; 4YH3; -. DR PDBsum; 4YH4; -. DR PDBsum; 4Z1Q; -. DR PDBsum; 4Z1S; -. DR PDBsum; 4Z93; -. DR PDBsum; 4ZC9; -. DR PDBsum; 4ZW1; -. DR PDBsum; 5A5S; -. DR PDBsum; 5A85; -. DR PDBsum; 5ACY; -. DR PDBsum; 5AD2; -. DR PDBsum; 5AD3; -. DR PDBsum; 5BT4; -. DR PDBsum; 5CFW; -. DR PDBsum; 5COI; -. DR PDBsum; 5CP5; -. DR PDBsum; 5CPE; -. DR PDBsum; 5CQT; -. DR PDBsum; 5CRM; -. DR PDBsum; 5CRZ; -. DR PDBsum; 5CS8; -. DR PDBsum; 5CTL; -. DR PDBsum; 5CY9; -. DR PDBsum; 5D0C; -. DR PDBsum; 5D24; -. DR PDBsum; 5D25; -. DR PDBsum; 5D26; -. DR PDBsum; 5D3H; -. DR PDBsum; 5D3J; -. DR PDBsum; 5D3L; -. DR PDBsum; 5D3N; -. DR PDBsum; 5D3P; -. DR PDBsum; 5D3R; -. DR PDBsum; 5D3S; -. DR PDBsum; 5D3T; -. DR PDBsum; 5DLX; -. DR PDBsum; 5DLZ; -. DR PDBsum; 5DW2; -. DR PDBsum; 5DX4; -. DR PDBsum; 5E0R; -. DR PDBsum; 5EGU; -. DR PDBsum; 5EI4; -. DR PDBsum; 5EIS; -. DR PDBsum; 5F5Z; -. DR PDBsum; 5F60; -. DR PDBsum; 5F61; -. DR PDBsum; 5F62; -. DR PDBsum; 5F63; -. DR PDBsum; 5FBX; -. DR PDBsum; 5H21; -. DR PDBsum; 5HCL; -. DR PDBsum; 5HLS; -. DR PDBsum; 5HM0; -. DR PDBsum; 5HQ5; -. DR PDBsum; 5HQ6; -. DR PDBsum; 5HQ7; -. DR PDBsum; 5I80; -. DR PDBsum; 5I88; -. DR PDBsum; 5IGK; -. DR PDBsum; 5JWM; -. DR PDBsum; 5KDH; -. DR PDBsum; 5KHM; -. DR PDBsum; 5KJ0; -. DR PDBsum; 5KU3; -. DR PDBsum; 5LJ1; -. DR PDBsum; 5LJ2; -. DR PDBsum; 5LRQ; -. DR PDBsum; 5LUU; -. DR PDBsum; 5M39; -. DR PDBsum; 5M3A; -. DR PDBsum; 5MKZ; -. DR PDBsum; 5MLI; -. DR PDBsum; 5N2M; -. DR PDBsum; 5NNC; -. DR PDBsum; 5NND; -. DR PDBsum; 5NNE; -. DR PDBsum; 5NNF; -. DR PDBsum; 5NNG; -. DR PDBsum; 5O97; -. DR PDBsum; 5OVB; -. DR PDBsum; 5OWM; -. DR PDBsum; 5OWW; -. DR PDBsum; 5S9P; -. DR PDBsum; 5S9Q; -. DR PDBsum; 5S9R; -. DR PDBsum; 5T35; -. DR PDBsum; 5TI2; -. DR PDBsum; 5TI3; -. DR PDBsum; 5TI4; -. DR PDBsum; 5TI5; -. DR PDBsum; 5TI6; -. DR PDBsum; 5TI7; -. DR PDBsum; 5U28; -. DR PDBsum; 5U2C; -. DR PDBsum; 5U2E; -. DR PDBsum; 5U2F; -. DR PDBsum; 5UEO; -. DR PDBsum; 5UEP; -. DR PDBsum; 5UEQ; -. DR PDBsum; 5UER; -. DR PDBsum; 5UES; -. DR PDBsum; 5UET; -. DR PDBsum; 5UEU; -. DR PDBsum; 5UEV; -. DR PDBsum; 5UEX; -. DR PDBsum; 5UEY; -. DR PDBsum; 5UEZ; -. DR PDBsum; 5UF0; -. DR PDBsum; 5ULA; -. DR PDBsum; 5UOO; -. DR PDBsum; 5UVS; -. DR PDBsum; 5UVT; -. DR PDBsum; 5UVU; -. DR PDBsum; 5UVV; -. DR PDBsum; 5UVW; -. DR PDBsum; 5UVX; -. DR PDBsum; 5UVY; -. DR PDBsum; 5UVZ; -. DR PDBsum; 5V67; -. DR PDBsum; 5VBO; -. DR PDBsum; 5VBP; -. DR PDBsum; 5VOM; -. DR PDBsum; 5VZS; -. DR PDBsum; 5W55; -. DR PDBsum; 5WA5; -. DR PDBsum; 5WMA; -. DR PDBsum; 5WMD; -. DR PDBsum; 5WMG; -. DR PDBsum; 5WUU; -. DR PDBsum; 5XHY; -. DR PDBsum; 5XI2; -. DR PDBsum; 5XI3; -. DR PDBsum; 5XI4; -. DR PDBsum; 5Y1Y; -. DR PDBsum; 5Y8C; -. DR PDBsum; 5Y8W; -. DR PDBsum; 5Y8Y; -. DR PDBsum; 5Y8Z; -. DR PDBsum; 5Y93; -. DR PDBsum; 5Y94; -. DR PDBsum; 5YOU; -. DR PDBsum; 5YOV; -. DR PDBsum; 5YQX; -. DR PDBsum; 5Z1R; -. DR PDBsum; 5Z1S; -. DR PDBsum; 5Z1T; -. DR PDBsum; 5Z5T; -. DR PDBsum; 5Z5U; -. DR PDBsum; 5Z5V; -. DR PDBsum; 5Z8G; -. DR PDBsum; 5Z8R; -. DR PDBsum; 5Z8Z; -. DR PDBsum; 5Z90; -. DR PDBsum; 5Z9C; -. DR PDBsum; 5Z9K; -. DR PDBsum; 6AFR; -. DR PDBsum; 6AJV; -. DR PDBsum; 6AJW; -. DR PDBsum; 6AJX; -. DR PDBsum; 6AJY; -. DR PDBsum; 6AJZ; -. DR PDBsum; 6BN7; -. DR PDBsum; 6BN8; -. DR PDBsum; 6BN9; -. DR PDBsum; 6BNB; -. DR PDBsum; 6BNH; -. DR PDBsum; 6BOY; -. DR PDBsum; 6C7Q; -. DR PDBsum; 6C7R; -. DR PDBsum; 6CD4; -. DR PDBsum; 6CD5; -. DR PDBsum; 6CIS; -. DR PDBsum; 6CIY; -. DR PDBsum; 6CJ1; -. DR PDBsum; 6CJ2; -. DR PDBsum; 6CKR; -. DR PDBsum; 6CKS; -. DR PDBsum; 6CZU; -. DR PDBsum; 6CZV; -. DR PDBsum; 6DJC; -. DR PDBsum; 6DL2; -. DR PDBsum; 6DMJ; -. DR PDBsum; 6DML; -. DR PDBsum; 6DNE; -. DR PDBsum; 6DUV; -. DR PDBsum; 6E4A; -. DR PDBsum; 6FFD; -. DR PDBsum; 6FNX; -. DR PDBsum; 6FO5; -. DR PDBsum; 6FSY; -. DR PDBsum; 6FT3; -. DR PDBsum; 6FT4; -. DR PDBsum; 6G0D; -. DR PDBsum; 6G0E; -. DR PDBsum; 6G0F; -. DR PDBsum; 6G0G; -. DR PDBsum; 6G0H; -. DR PDBsum; 6G0O; -. DR PDBsum; 6G0P; -. DR PDBsum; 6G0Q; -. DR PDBsum; 6G0R; -. DR PDBsum; 6G0S; -. DR PDBsum; 6HDQ; -. DR PDBsum; 6HOV; -. DR PDBsum; 6I7X; -. DR PDBsum; 6I7Y; -. DR PDBsum; 6IN1; -. DR PDBsum; 6JI3; -. DR PDBsum; 6JI4; -. DR PDBsum; 6JI5; -. DR PDBsum; 6JJ3; -. DR PDBsum; 6JJ5; -. DR PDBsum; 6JJ6; -. DR PDBsum; 6JJB; -. DR PDBsum; 6KEC; -. DR PDBsum; 6KED; -. DR PDBsum; 6KEE; -. DR PDBsum; 6KEF; -. DR PDBsum; 6KEG; -. DR PDBsum; 6KEH; -. DR PDBsum; 6KEI; -. DR PDBsum; 6KEJ; -. DR PDBsum; 6KEK; -. DR PDBsum; 6KO2; -. DR PDBsum; 6LG4; -. DR PDBsum; 6LG5; -. DR PDBsum; 6LG6; -. DR PDBsum; 6LG7; -. DR PDBsum; 6LG8; -. DR PDBsum; 6LG9; -. DR PDBsum; 6LIH; -. DR PDBsum; 6LIM; -. DR PDBsum; 6MAU; -. DR PDBsum; 6MH1; -. DR PDBsum; 6MH7; -. DR PDBsum; 6MNL; -. DR PDBsum; 6P05; -. DR PDBsum; 6PRT; -. DR PDBsum; 6PS9; -. DR PDBsum; 6PSB; -. DR PDBsum; 6Q3Y; -. DR PDBsum; 6Q3Z; -. DR PDBsum; 6RWJ; -. DR PDBsum; 6S25; -. DR PDBsum; 6S4B; -. DR PDBsum; 6S6K; -. DR PDBsum; 6SA2; -. DR PDBsum; 6SA3; -. DR PDBsum; 6SAH; -. DR PDBsum; 6SAJ; -. DR PDBsum; 6SB8; -. DR PDBsum; 6SE4; -. DR PDBsum; 6SIS; -. DR PDBsum; 6SWN; -. DR PDBsum; 6SWQ; -. DR PDBsum; 6TPX; -. DR PDBsum; 6TPY; -. DR PDBsum; 6TPZ; -. DR PDBsum; 6U0D; -. DR PDBsum; 6U6K; -. DR PDBsum; 6U6L; -. DR PDBsum; 6U72; -. DR PDBsum; 6U74; -. DR PDBsum; 6U8G; -. DR PDBsum; 6U8I; -. DR PDBsum; 6U8M; -. DR PDBsum; 6ULS; -. DR PDBsum; 6ULV; -. DR PDBsum; 6UVJ; -. DR PDBsum; 6UVM; -. DR PDBsum; 6UWU; -. DR PDBsum; 6UWX; -. DR PDBsum; 6V0U; -. DR PDBsum; 6V1K; -. DR PDBsum; 6V1L; -. DR PDBsum; 6V1U; -. DR PDBsum; 6VIW; -. DR PDBsum; 6VIX; -. DR PDBsum; 6VIZ; -. DR PDBsum; 6VUB; -. DR PDBsum; 6VUC; -. DR PDBsum; 6VUF; -. DR PDBsum; 6VUJ; -. DR PDBsum; 6WGX; -. DR PDBsum; 6WVX; -. DR PDBsum; 6WW8; -. DR PDBsum; 6X7B; -. DR PDBsum; 6X7C; -. DR PDBsum; 6X7D; -. DR PDBsum; 6XUZ; -. DR PDBsum; 6XV3; -. DR PDBsum; 6XV7; -. DR PDBsum; 6XVC; -. DR PDBsum; 6YIN; -. DR PDBsum; 6YQN; -. DR PDBsum; 6YQO; -. DR PDBsum; 6YQP; -. DR PDBsum; 6YQZ; -. DR PDBsum; 6Z7G; -. DR PDBsum; 6Z7L; -. DR PDBsum; 6Z7M; -. DR PDBsum; 6ZB3; -. DR PDBsum; 6ZCI; -. DR PDBsum; 6ZED; -. DR PDBsum; 6ZEL; -. DR PDBsum; 6ZF9; -. DR PDBsum; 7A9U; -. DR PDBsum; 7AJN; -. DR PDBsum; 7AQT; -. DR PDBsum; 7AXR; -. DR PDBsum; 7B1T; -. DR PDBsum; 7C2Z; -. DR PDBsum; 7C6P; -. DR PDBsum; 7DHS; -. DR PDBsum; 7EHW; -. DR PDBsum; 7EHY; -. DR PDBsum; 7EIG; -. DR PDBsum; 7EIK; -. DR PDBsum; 7EIL; -. DR PDBsum; 7FH2; -. DR PDBsum; 7JKW; -. DR PDBsum; 7JKX; -. DR PDBsum; 7JKY; -. DR PDBsum; 7JKZ; -. DR PDBsum; 7K6G; -. DR PDBsum; 7K6H; -. DR PDBsum; 7KHH; -. DR PDBsum; 7KHL; -. DR PDBsum; 7KO0; -. DR PDBsum; 7L9M; -. DR PDBsum; 7LA9; -. DR PDBsum; 7LH8; -. DR PDBsum; 7M16; -. DR PDBsum; 7MCE; -. DR PDBsum; 7MCF; -. DR PDBsum; 7MLQ; -. DR PDBsum; 7MLR; -. DR PDBsum; 7MLS; -. DR PDBsum; 7MR5; -. DR PDBsum; 7MR6; -. DR PDBsum; 7MR7; -. DR PDBsum; 7MR8; -. DR PDBsum; 7MR9; -. DR PDBsum; 7MRA; -. DR PDBsum; 7MRB; -. DR PDBsum; 7O18; -. DR PDBsum; 7OEO; -. DR PDBsum; 7P6V; -. DR PDBsum; 7P6W; -. DR PDBsum; 7P6Y; -. DR PDBsum; 7Q3F; -. DR PDBsum; 7QDL; -. DR PDBsum; 7R5B; -. DR PDBsum; 7R9C; -. DR PDBsum; 7REK; -. DR PDBsum; 7REL; -. DR PDBsum; 7REM; -. DR PDBsum; 7RJO; -. DR PDBsum; 7RJP; -. DR PDBsum; 7RJQ; -. DR PDBsum; 7RJR; -. DR PDBsum; 7RMD; -. DR PDBsum; 7RN2; -. DR PDBsum; 7RUH; -. DR PDBsum; 7RUI; -. DR PDBsum; 7RXR; -. DR PDBsum; 7RXS; -. DR PDBsum; 7RXT; -. DR PDBsum; 7T3F; -. DR PDBsum; 7TUQ; -. DR PDBsum; 7TV0; -. DR PDBsum; 7UGF; -. DR PDBsum; 7USJ; -. DR PDBsum; 7USK; -. DR PDBsum; 7UTY; -. DR PDBsum; 7UZN; -. DR PDBsum; 7V1U; -. DR PDBsum; 7V2J; -. DR PDBsum; 7W3D; -. DR PDBsum; 7WJS; -. DR PDBsum; 7WKY; -. DR PDBsum; 7WL4; -. DR PDBsum; 7WWZ; -. DR PDBsum; 7X6T; -. DR PDBsum; 7YL2; -. DR PDBsum; 7YMG; -. DR PDBsum; 7YQ9; -. DR PDBsum; 7ZAQ; -. DR PDBsum; 7ZE6; -. DR PDBsum; 7ZE7; -. DR PDBsum; 7ZEF; -. DR PDBsum; 7ZFN; -. DR PDBsum; 7ZFS; -. DR PDBsum; 7ZFT; -. DR PDBsum; 7ZFU; -. DR PDBsum; 7ZFV; -. DR PDBsum; 7ZFY; -. DR PDBsum; 7ZFZ; -. DR PDBsum; 7ZG1; -. DR PDBsum; 7ZG2; -. DR PDBsum; 7ZNT; -. DR PDBsum; 8B5B; -. DR PDBsum; 8B5C; -. DR PDBsum; 8BDS; -. DR PDBsum; 8BDT; -. DR PDBsum; 8BDX; -. DR PDBsum; 8BEB; -. DR PDBsum; 8CKF; -. DR PDBsum; 8DYR; -. DR PDBsum; 8E17; -. DR PDBsum; 8E3W; -. DR PDBsum; 8EAD; -. DR PDBsum; 8EWV; -. DR PDBsum; 8G46; -. DR PDBsum; 8GPZ; -. DR PDBsum; 8GQ0; -. DR PDBsum; 8IBQ; -. DR PDBsum; 8IDH; -. DR PDBsum; 8OV6; -. DR PDBsum; 8P9F; -. DR PDBsum; 8P9G; -. DR PDBsum; 8P9H; -. DR PDBsum; 8P9I; -. DR PDBsum; 8P9J; -. DR PDBsum; 8P9K; -. DR PDBsum; 8P9L; -. DR PDBsum; 8PIQ; -. DR PDBsum; 8PXA; -. DR PDBsum; 8PXM; -. DR PDBsum; 8PXN; -. DR AlphaFoldDB; O60885; -. DR BMRB; O60885; -. DR EMDB; EMD-17172; -. DR EMDB; EMD-29714; -. DR SASBDB; O60885; -. DR SMR; O60885; -. DR BioGRID; 117036; 1612. DR CORUM; O60885; -. DR DIP; DIP-39776N; -. DR IntAct; O60885; 65. DR MINT; O60885; -. DR STRING; 9606.ENSP00000263377; -. DR BindingDB; O60885; -. DR ChEMBL; CHEMBL1163125; -. DR DrugCentral; O60885; -. DR GuidetoPHARMACOLOGY; 1945; -. DR GlyCosmos; O60885; 8 sites, 2 glycans. DR GlyGen; O60885; 11 sites, 2 O-linked glycans (11 sites). DR iPTMnet; O60885; -. DR MetOSite; O60885; -. DR PhosphoSitePlus; O60885; -. DR SwissPalm; O60885; -. DR BioMuta; BRD4; -. DR EPD; O60885; -. DR jPOST; O60885; -. DR MassIVE; O60885; -. DR MaxQB; O60885; -. DR PaxDb; 9606-ENSP00000263377; -. DR PeptideAtlas; O60885; -. DR ProteomicsDB; 49651; -. [O60885-1] DR ProteomicsDB; 49652; -. [O60885-2] DR ProteomicsDB; 62139; -. DR Pumba; O60885; -. DR ABCD; O60885; 4 sequenced antibodies. DR Antibodypedia; 13956; 521 antibodies from 38 providers. DR DNASU; 23476; -. DR Ensembl; ENST00000263377.6; ENSP00000263377.1; ENSG00000141867.19. [O60885-1] DR Ensembl; ENST00000360016.9; ENSP00000353112.4; ENSG00000141867.19. [O60885-3] DR Ensembl; ENST00000371835.8; ENSP00000360901.3; ENSG00000141867.19. [O60885-2] DR Ensembl; ENST00000679869.1; ENSP00000506350.1; ENSG00000141867.19. [O60885-1] DR GeneID; 23476; -. DR KEGG; hsa:23476; -. DR MANE-Select; ENST00000679869.1; ENSP00000506350.1; NM_001379291.1; NP_001366220.1. DR UCSC; uc002nar.4; human. [O60885-1] DR AGR; HGNC:13575; -. DR CTD; 23476; -. DR DisGeNET; 23476; -. DR GeneCards; BRD4; -. DR GeneReviews; BRD4; -. DR HGNC; HGNC:13575; BRD4. DR HPA; ENSG00000141867; Low tissue specificity. DR MalaCards; BRD4; -. DR MIM; 608749; gene. DR neXtProt; NX_O60885; -. DR OpenTargets; ENSG00000141867; -. DR Orphanet; 199; Cornelia de Lange syndrome. DR Orphanet; 443167; NUT midline carcinoma. DR PharmGKB; PA25416; -. DR VEuPathDB; HostDB:ENSG00000141867; -. DR eggNOG; KOG1474; Eukaryota. DR GeneTree; ENSGT00940000154549; -. DR HOGENOM; CLU_001499_0_3_1; -. DR InParanoid; O60885; -. DR OMA; LLMPSTH; -. DR OrthoDB; 152619at2759; -. DR PhylomeDB; O60885; -. DR TreeFam; TF317345; -. DR PathwayCommons; O60885; -. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR SignaLink; O60885; -. DR SIGNOR; O60885; -. DR BioGRID-ORCS; 23476; 721 hits in 1217 CRISPR screens. DR ChiTaRS; BRD4; human. DR EvolutionaryTrace; O60885; -. DR GeneWiki; BRD4; -. DR GenomeRNAi; 23476; -. DR Pharos; O60885; Tchem. DR PRO; PR:O60885; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; O60885; Protein. DR Bgee; ENSG00000141867; Expressed in buccal mucosa cell and 213 other cell types or tissues. DR ExpressionAtlas; O60885; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:UniProtKB. DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0140566; F:histone reader activity; IDA:GO_Central. DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB. DR GO; GO:0106140; F:P-TEFb complex binding; IDA:FlyBase. DR GO; GO:0002039; F:p53 binding; IDA:UniProtKB. DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IDA:MGI. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IMP:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:FlyBase. DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IMP:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI. DR GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI. 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; Bromodomain-like; 2. DR IDEAL; IID00111; -. DR InterPro; IPR031354; BRD4_CDT. 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 PANTHER; PTHR22880:SF143; BROMODOMAIN-CONTAINING PROTEIN 4; 1. DR PANTHER; PTHR22880; FALZ-RELATED BROMODOMAIN-CONTAINING PROTEINS; 1. DR Pfam; PF17035; BET; 1. DR Pfam; PF17105; BRD4_CDT; 1. DR Pfam; PF00439; Bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SUPFAM; SSF47370; Bromodomain; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 2. DR PROSITE; PS51525; NET; 1. DR Genevisible; O60885; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; KW Chromatin regulator; Chromosomal rearrangement; Chromosome; DNA damage; KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..1362 FT /note="Bromodomain-containing protein 4" FT /id="PRO_0000211183" FT DOMAIN 75..147 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 368..440 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 600..682 FT /note="NET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857" FT REGION 1..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 174..229 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 242..352 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 463..615 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 484..503 FT /note="NPS region" FT REGION 524..579 FT /note="BID region" FT REGION 674..1100 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1047..1362 FT /note="C-terminal (CTD) region" FT REGION 1116..1339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..207 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..224 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..274 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 316..340 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..496 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 503..517 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 549..573 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 597..615 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 694..708 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 729..745 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 751..788 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 830..847 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 926..941 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 947..999 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1012..1036 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1068..1094 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1176..1192 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1204..1224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1225..1287 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1288..1323 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1324..1339 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 140 FT /note="Acetylated histone binding" FT /evidence="ECO:0000269|PubMed:22464331" FT SITE 433 FT /note="Acetylated histone binding" FT /evidence="ECO:0000269|PubMed:22464331" FT SITE 719..720 FT /note="Breakpoint for translocation to form BDR4-NUTM1 FT fusion protein" FT MOD_RES 470 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 484 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 488 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 492 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 494 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 498 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 499 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 503 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:23317504" FT MOD_RES 601 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1111 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1126 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1201 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1204 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 99 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 585 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 645 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 694 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1050 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1111 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 1111 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 1197 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 720..1362 FT /note="EMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQ FT QQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHL FT PQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPA FT VSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSV FT KVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTH FT IQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPL FT MIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPF FT SPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEP FT KTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKA FT QAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAA FT AVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENL FT F -> AFCTSGDFVSPGPSPYHSHVQCGRFREMLRWFLVDVEQTAAGQPHRQSAAGPAI FT TWAPAIAYPSPECARCCVGCS (in isoform B)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_047671" FT VAR_SEQ 720..722 FT /note="EMA -> GPA (in isoform C)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_010902" FT VAR_SEQ 723..1362 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_010903" FT VARIANT 37 FT /note="P -> S (in dbSNP:rs35177876)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041919" FT VARIANT 371 FT /note="A -> G (in dbSNP:rs55805532)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041920" FT VARIANT 563 FT /note="S -> N (in dbSNP:rs55970906)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041921" FT VARIANT 598 FT /note="T -> S (in dbSNP:rs34362023)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041922" FT VARIANT 669 FT /note="R -> H (in dbSNP:rs35824241)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041923" FT VARIANT 1097 FT /note="R -> H (in dbSNP:rs35676845)" FT /id="VAR_048427" FT MUTAGEN 140 FT /note="N->A: Abolishes binding to acetylated histones." FT /evidence="ECO:0000269|PubMed:22464331, FT ECO:0000269|PubMed:23728299" FT MUTAGEN 433 FT /note="N->A: Abolishes binding to acetylated histones." FT /evidence="ECO:0000269|PubMed:22464331" FT MUTAGEN 492..494 FT /note="SSS->ASA: Impaired phosphorylation by CK2 and FT binding to acetylated histones." FT /evidence="ECO:0000269|PubMed:23317504" FT MUTAGEN 498..500 FT /note="SST->AAA: Impaired phosphorylation by CK2 and FT binding to acetylated histones." FT /evidence="ECO:0000269|PubMed:23317504" FT MUTAGEN 503 FT /note="S->A: Impaired phosphorylation by CK2 and binding to FT acetylated histones." FT /evidence="ECO:0000269|PubMed:23317504" FT MUTAGEN 651..653 FT /note="EIE->AIA: Decreases interaction with JMJD6 and FT NSD3.No effect on interaction with histone 4 acetylated." FT /evidence="ECO:0000269|PubMed:29176719" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:4WHW" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:6X7B" FT HELIX 61..68 FT /evidence="ECO:0007829|PDB:4QB3" FT HELIX 70..75 FT /evidence="ECO:0007829|PDB:4QB3" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:7TUQ" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:4QB3" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:5Z1S" FT TURN 89..93 FT /evidence="ECO:0007829|PDB:4QB3" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:4QB3" FT HELIX 107..115 FT /evidence="ECO:0007829|PDB:4QB3" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:6X7D" FT HELIX 122..139 FT /evidence="ECO:0007829|PDB:4QB3" FT HELIX 145..161 FT /evidence="ECO:0007829|PDB:4QB3" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:6X7B" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:2LSP" FT HELIX 352..364 FT /evidence="ECO:0007829|PDB:7USK" FT HELIX 367..369 FT /evidence="ECO:0007829|PDB:7USK" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:7USK" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:7USK" FT HELIX 382..385 FT /evidence="ECO:0007829|PDB:4Z93" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:7USK" FT HELIX 400..408 FT /evidence="ECO:0007829|PDB:7USK" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:2MJV" FT HELIX 415..432 FT /evidence="ECO:0007829|PDB:7USK" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:2I8N" FT HELIX 438..455 FT /evidence="ECO:0007829|PDB:7USK" FT HELIX 602..605 FT /evidence="ECO:0007829|PDB:2NCZ" FT HELIX 612..624 FT /evidence="ECO:0007829|PDB:2N3K" FT HELIX 627..640 FT /evidence="ECO:0007829|PDB:2N3K" FT HELIX 642..644 FT /evidence="ECO:0007829|PDB:2NCZ" FT STRAND 651..655 FT /evidence="ECO:0007829|PDB:2N3K" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:2N3K" FT HELIX 661..675 FT /evidence="ECO:0007829|PDB:2N3K" FT TURN 676..678 FT /evidence="ECO:0007829|PDB:6BNH" FT HELIX 1345..1354 FT /evidence="ECO:0007829|PDB:2NNU" FT TURN 1355..1357 FT /evidence="ECO:0007829|PDB:2NNU" SQ SEQUENCE 1362 AA; 152219 MW; D52EFE1CF9960907 CRC64; MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET SNPNKPKRQT NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI IKTPMDMGTI KKRLENNYYW NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK INELPTEETE IMIVQAKGRG RGRKETGTAK PGVSTVPNTT QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT VVPPQPLQTP PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV SEQLKCCSGI LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM STIKSKLEAR EYRDAQEFGA DVRLMFSNCY KYNPPDHEVV AMARKLQDVF EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV APPSSSDSSS DSSSDSDSST DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE KDKKEKKKEK HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD EIEIDFETLK PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS SESESSSESS SSDSEDSETE MAPKSKKKGH PGREQKKHHH HHHQQMQQAP APVPQQPPPP PQQPPPPPPP QQQQQPPPPP PPPSMPQQAA PAMKSSPPPF IATQVPVLEP QLPGSVFDPI GHFTQPILHL PQPELPPHLP QPPEHSTPPH LNQHAVVSPP ALHNALPQQP SRPSNRAAAL PPKPARPPAV SPALTQTPLL PQPPMAQPPQ VLLEDEEPPA PPLTSMQMQL YLQQLQKVQP PTPLLPSVKV QSQPPPPLPP PPHPSVQQQL QQQPPPPPPP QPQPPPQQQH QPPPRPVHLQ PMQFSTHIQQ PPPPQGQQPP HPPPGQQPPP PQPAKPQQVI QHHHSPRHHK SDPYSTGHLR EAPSPLMIHS PQMSQFQSLT HQSPPQQNVQ PKKQELRAAS VVQPQPLVVV KEEKIHSPII RSEPFSPSLR PEPPKHPESI KAPVHLPQRP EMKPVDVGRP VIRPPEQNAP PPGAPDKDKQ KQEPKTPVAP KKDLKIKNMG SWASLVQKHP TTPSSTAKSS SDSFEQFRRA AREKEEREKA LKAQAEHAEK EKERLRQERM RSREDEDALE QARRAHEEAR RRQEQQQQQR QEQQQQQQQQ AAAVAAAATP QAQSSQPQSM LDQQRELARK REQERRRREA MAATIDMNFQ SDLLSIFEEN LF //