ID ZMY11_HUMAN Reviewed; 602 AA. AC Q15326; B2R6G8; B7Z293; F6UH50; Q2LD45; Q2LD46; Q2LD47; Q2LD48; Q5VUI1; AC Q8N4B3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2012, sequence version 2. DT 27-MAR-2024, entry version 202. DE RecName: Full=Zinc finger MYND domain-containing protein 11 {ECO:0000305}; DE AltName: Full=Adenovirus 5 E1A-binding protein; DE AltName: Full=Bone morphogenetic protein receptor-associated molecule 1; DE AltName: Full=Protein BS69; GN Name=ZMYND11 {ECO:0000312|HGNC:HGNC:16966}; GN Synonyms=BRAM1, BS69 {ECO:0000303|PubMed:24675531}; 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=Colon carcinoma; RX PubMed=7621829; DOI=10.1002/j.1460-2075.1995.tb07318.x; RA Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M., Sonntag-Buck V., RA Stunnenberg H.G., Bernards R.; RT "BS69, a novel adenovirus E1A-associated protein that inhibits E1A RT transactivation."; RL EMBO J. 14:3159-3169(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, UBIQUITINATION, RP INTERACTION WITH E2F6 AND EZH2, AND MUTAGENESIS OF CYS-563. RX PubMed=16565076; DOI=10.1074/jbc.m600573200; RA Velasco G., Grkovic S., Ansieau S.; RT "New insights into BS69 functions."; RL J. Biol. Chem. 281:16546-16550(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5). RC TISSUE=Amygdala, and Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Brain; 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 [7] RP FUNCTION, AND INTERACTION WITH NCOR1. RX PubMed=10734313; DOI=10.1038/sj.onc.1203421; RA Masselink H., Bernards R.; RT "The adenovirus E1A binding protein BS69 is a corepressor of transcription RT through recruitment of N-CoR."; RL Oncogene 19:1538-1546(2000). RN [8] RP INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, AND INTERACTION WITH RP EPSTEIN-BARR VIRUS EBNA2 PROTEIN. RX PubMed=11733528; DOI=10.1074/jbc.m110078200; RA Ansieau S., Leutz A.; RT "The conserved Mynd domain of BS69 binds cellular and oncoviral proteins RT through a common PXLXP motif."; RL J. Biol. Chem. 277:4906-4910(2002). RN [9] RP INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1. RX PubMed=12181323; DOI=10.1074/jbc.m206736200; RA Chung P.J., Chang Y.S., Liang C.L., Meng C.L.; RT "Negative regulation of Epstein-Barr virus latent membrane protein 1- RT mediated functions by the bone morphogenetic protein receptor IA-binding RT protein, BRAM1."; RL J. Biol. Chem. 277:39850-39857(2002). RN [10] RP INTERACTION WITH EMSY. RX PubMed=15947784; DOI=10.1038/sj.embor.7400415; RA Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D., RA Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S.; RT "Binding of EMSY to HP1beta: implications for recruitment of HP1beta and RT BS69."; RL EMBO Rep. 6:675-680(2005). RN [11] RP INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1. RX PubMed=16382137; DOI=10.1128/mcb.26.2.448-456.2006; RA Wan J., Zhang W., Wu L., Bai T., Zhang M., Lo K.W., Chui Y.L., Cui Y., RA Tao Q., Yamamoto M., Akira S., Wu Z.; RT "BS69, a specific adaptor in the latent membrane protein 1-mediated c-Jun RT N-terminal kinase pathway."; RL Mol. Cell. Biol. 26:448-456(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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 INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1. RX PubMed=19379743; DOI=10.1016/j.febslet.2009.04.022; RA Ikeda O., Sekine Y., Mizushima A., Oritani K., Yasui T., Fujimuro M., RA Muromoto R., Nanbo A., Matsuda T.; RT "BS69 negatively regulates the canonical NF-kappaB activation induced by RT Epstein-Barr virus-derived LMP1."; RL FEBS Lett. 583:1567-1574(2009). RN [15] RP SUBCELLULAR LOCATION, SUMOYLATION, AND INTERACTION WITH PIAS1 AND UBE2I. RX PubMed=19766626; DOI=10.1016/j.yexcr.2009.09.011; RA Yu B., Shao Y., Zhang C., Chen Y., Zhong Q., Zhang J., Yang H., Zhang W., RA Wan J.; RT "BS69 undergoes SUMO modification and plays an inhibitory role in muscle RT and neuronal differentiation."; RL Exp. Cell Res. 315:3543-3553(2009). RN [16] RP INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1. RX PubMed=20138174; DOI=10.1016/j.febslet.2010.01.060; RA Ikeda O., Miyasaka Y., Yoshida R., Mizushima A., Oritani K., Sekine Y., RA Kuroda M., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.; RT "BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-derived RT LMP1/CTAR1-induced NF-kappaB activation."; RL FEBS Lett. 584:865-872(2010). RN [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY RP 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 [19] RP CHROMOSOMAL TRANSLOCATION WITH MBTD1. RX PubMed=23915195; DOI=10.3109/10428194.2013.820292; RA De Braekeleer E., Auffret R., Douet-Guilbert N., Basinko A., Le Bris M.J., RA Morel F., De Braekeleer M.; RT "Recurrent translocation (10;17)(p15;q21) in acute poorly differentiated RT myeloid leukemia likely results in ZMYND11-MBTD1 fusion."; RL Leuk. Lymphoma 55:1189-1190(2014). RN [20] RP INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH RP EPSTEIN-BARR VIRUS EBNA2 PROTEIN, INTERACTION WITH MGA, AND MUTAGENESIS OF RP TRP-562; 567-GLU-GLU-568 AND 599-ARG--ARG-602. RX PubMed=23372760; DOI=10.1371/journal.pone.0054715; RA Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M., RA Franzmann T.M., Buchner J., Ansieau S., Sattler M.; RT "Structural and functional analysis of the DEAF-1 and BS69 MYND domains."; RL PLoS ONE 8:E54715-E54715(2013). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY MASS RP 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 [22] RP INDUCTION. RX PubMed=24590075; DOI=10.1038/nature13045; RA Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K., Ren Y., RA Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.; RT "ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour RT suppression."; RL Nature 508:263-268(2014). RN [23] RP INVOLVEMENT IN MRD30. RX PubMed=25217958; DOI=10.1038/ng.3092; RA Coe B.P., Witherspoon K., Rosenfeld J.A., van Bon B.W., RA Vulto-van Silfhout A.T., Bosco P., Friend K.L., Baker C., Buono S., RA Vissers L.E., Schuurs-Hoeijmakers J.H., Hoischen A., Pfundt R., Krumm N., RA Carvill G.L., Li D., Amaral D., Brown N., Lockhart P.J., Scheffer I.E., RA Alberti A., Shaw M., Pettinato R., Tervo R., de Leeuw N., Reijnders M.R., RA Torchia B.S., Peeters H., O'Roak B.J., Fichera M., Hehir-Kwa J.Y., RA Shendure J., Mefford H.C., Haan E., Gecz J., de Vries B.B., Romano C., RA Eichler E.E.; RT "Refining analyses of copy number variation identifies specific genes RT associated with developmental delay."; RL Nat. Genet. 46:1063-1071(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-407, 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 [25] 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 [26] RP INTERACTION WITH HISTONE H3. RX PubMed=26655721; DOI=10.1074/jbc.m115.679985; RA Adhikary S., Sanyal S., Basu M., Sengupta I., Sen S., Srivastava D.K., RA Roy S., Das C.; RT "Selective Recognition of H3.1K36 Dimethylation/H4K16 Acetylation RT Facilitates the Regulation of All-trans-retinoic Acid (ATRA)-responsive RT Genes by Putative Chromatin Reader ZMYND8."; RL J. Biol. Chem. 291:2664-2681(2016). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-366; LYS-407 AND LYS-408, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [28] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 154-371 IN COMPLEX WITH ZINC, RP INTERACTION WITH HISTONE 3, SUBCELLULAR LOCATION, DNA-BINDING, DOMAIN, RP MUTAGENESIS OF 258-CYS--CYS-261; LYS-287; LYS-289; PHE-291; TRP-294; RP PHE-310; ARG-334; 338-LYS-ARG-339 AND 344-LYS-LYS-345, AND FUNCTION. RX PubMed=24675531; DOI=10.1038/cr.2014.38; RA Wang J., Qin S., Li F., Li S., Zhang W., Peng J., Zhang Z., Gong Q., Wu J., RA Shi Y.; RT "Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in RT H3K36me3 nucleosome binding."; RL Cell Res. 24:890-893(2014). RN [29] {ECO:0007744|PDB:5HDA} RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 480-602 IN COMPLEX WITH ZINC AND RP EPSTEIN-BARR VIRUS EBNA2 PEPTIDE, SUBUNIT, INTERACTION WITH EPSTEIN-BARR RP VIRUS EBNA2 PROTEIN, FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF RP TYR-572; GLN-586; TRP-590 AND ARG-600. RX PubMed=26845565; DOI=10.1371/journal.ppat.1005414; RA Harter M.R., Liu C.D., Shen C.L., Gonzalez-Hurtado E., Zhang Z.M., Xu M., RA Martinez E., Peng C.W., Song J.; RT "BS69/ZMYND11 C-Terminal Domains Bind and Inhibit EBNA2."; RL PLoS Pathog. 12:1005414-1005414(2016). CC -!- FUNCTION: Chromatin reader that specifically recognizes and binds CC histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA CC polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 CC or H3.2) (By similarity). Colocalizes with highly expressed genes and CC functions as a transcription corepressor by modulating RNA polymerase CC II at the elongation stage. Binds non-specifically to dsDNA CC (PubMed:24675531). Acts as a tumor-suppressor by repressing a CC transcriptional program essential for tumor cell growth. CC {ECO:0000250|UniProtKB:Q8R5C8, ECO:0000269|PubMed:10734313, CC ECO:0000269|PubMed:16565076, ECO:0000269|PubMed:24675531}. CC -!- FUNCTION: (Microbial infection) Inhibits Epstein-Barr virus EBNA2- CC mediated transcriptional activation and host cell proliferation, CC through direct interaction. {ECO:0000269|PubMed:26845565}. CC -!- SUBUNIT: Homooligomer; forms homooligomers via its C-terminus CC (PubMed:26845565). Interacts with histone H3.3 trimethylated at 'Lys- CC 36' (H3.3K36me3) (PubMed:24675531, PubMed:26655721). Interacts (via CC MYND-type zinc finger) with NCOR1 (PubMed:10734313). Interacts (via CC MYND-type zinc finger) with MGA protein (via PXLXP motif) CC (PubMed:23372760). Interacts (via MYND-type zinc finger) with EZH2 CC (PubMed:16565076). Interacts with EMSY and E2F6 (PubMed:15947784, CC PubMed:16565076). Interacts with PIAS1 and UBE2I (PubMed:19766626). CC {ECO:0000269|PubMed:10734313, ECO:0000269|PubMed:15947784, CC ECO:0000269|PubMed:16565076, ECO:0000269|PubMed:19766626, CC ECO:0000269|PubMed:23372760, ECO:0000269|PubMed:24675531, CC ECO:0000269|PubMed:26845565}. CC -!- SUBUNIT: (Microbial infection) Interacts (via MYND-type zinc finger) CC with human adenovirus early E1A protein (via PXLXP motif); this CC interaction inhibits E1A mediated transactivation. CC {ECO:0000269|PubMed:11733528, ECO:0000269|PubMed:23372760}. CC -!- SUBUNIT: (Microbial infection) Interacts (via MYND-type zinc finger) CC with Epstein-Barr virus EBNA2 protein (via PXLXP motif) CC (PubMed:11733528, PubMed:26845565). Interacts with Epstein-Barr virus- CC derived protein LMP1; leading to negatively regulate NF-kappa-B CC activation by Epstein-Barr virus-derived protein LMP1 (PubMed:12181323, CC PubMed:16382137, PubMed:19379743, PubMed:20138174). CC {ECO:0000269|PubMed:11733528, ECO:0000269|PubMed:12181323, CC ECO:0000269|PubMed:16382137, ECO:0000269|PubMed:19379743, CC ECO:0000269|PubMed:20138174, ECO:0000269|PubMed:26845565}. CC -!- INTERACTION: CC Q15326; P36941: LTBR; NbExp=5; IntAct=EBI-2623509, EBI-3509981; CC Q15326; Q13114: TRAF3; NbExp=2; IntAct=EBI-2623509, EBI-357631; CC Q15326; Q9UKY1: ZHX1; NbExp=2; IntAct=EBI-2623509, EBI-347767; CC Q15326; P12978: EBNA2; Xeno; NbExp=2; IntAct=EBI-2623509, EBI-8052923; CC Q15326; P03230: LMP1; Xeno; NbExp=3; IntAct=EBI-2623509, EBI-6973030; CC Q15326; P03255; Xeno; NbExp=3; IntAct=EBI-2623509, EBI-2603114; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16565076, CC ECO:0000269|PubMed:19766626, ECO:0000269|PubMed:24675531, CC ECO:0000269|PubMed:25593309}. Chromosome {ECO:0000269|PubMed:16565076}. CC Note=Associates with chromatin and mitotic chromosomes. CC {ECO:0000269|PubMed:16565076}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q15326-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15326-2; Sequence=VSP_044482; CC Name=3; CC IsoId=Q15326-3; Sequence=VSP_044483; CC Name=4; CC IsoId=Q15326-4; Sequence=VSP_044482, VSP_044483; CC Name=5; CC IsoId=Q15326-5; Sequence=VSP_044482, VSP_046246; CC Name=6; CC IsoId=Q15326-6; Sequence=VSP_047209, VSP_044483; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16565076}. CC -!- INDUCTION: Down-regulated in breast cancer patients with poor CC prognosis. {ECO:0000269|PubMed:24590075}. CC -!- DOMAIN: The PWWP domain specifically recognizes and binds histone H3.3 CC trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta- CC barrel fold with an extended C-terminal alpha-helix, with a conserved CC H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the CC beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific CC recognition of H3.3 histone is mediated by the encapsulation of the CC H3.3-specific 'Ser 31' residue in a composite pocket formed by the CC tandem bromo-PWWP domains. {ECO:0000269|PubMed:24675531}. CC -!- PTM: Sumoylated following its interaction with PIAS1 and UBE2I. CC {ECO:0000269|PubMed:19766626}. CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. CC {ECO:0000269|PubMed:16565076}. CC -!- DISEASE: Note=A chromosomal aberration involving ZMYND11 is a cause of CC acute poorly differentiated myeloid leukemia. Translocation CC (10;17)(p15;q21) with MBTD1. {ECO:0000269|PubMed:23915195}. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 30, CC with speech delay and behavioral abnormalities (MRD30) [MIM:616083]: A CC disorder characterized by significantly below average general CC intellectual functioning associated with impairments in adaptive CC behavior and manifested during the developmental period. MRD30 patients CC manifest intellectual disability, speech delay, and subtle facial CC dysmorphisms, including hypertelorism, ptosis, and a wide mouth. CC Behavioral abnormalities, including attention-deficit hyperactivity CC disorder, autistic features, and aggression are commonly observed. CC {ECO:0000269|PubMed:25217958}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH34784.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG35465.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA60052.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X86098; CAA60052.1; ALT_FRAME; mRNA. DR EMBL; DQ335452; ABC72408.1; -; mRNA. DR EMBL; DQ335453; ABC72409.1; -; mRNA. DR EMBL; DQ335454; ABC72410.1; -; mRNA. DR EMBL; DQ335455; ABC72411.1; -; mRNA. DR EMBL; AK294469; BAH11779.1; -; mRNA. DR EMBL; AK312570; BAG35465.1; ALT_INIT; mRNA. DR EMBL; AL589988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL603831; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL713922; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL731539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86539.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86540.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86541.1; -; Genomic_DNA. DR EMBL; BC034784; AAH34784.1; ALT_INIT; mRNA. DR CCDS; CCDS55696.1; -. [Q15326-3] DR CCDS; CCDS55697.1; -. [Q15326-5] DR CCDS; CCDS7052.2; -. [Q15326-1] DR CCDS; CCDS7053.2; -. [Q15326-6] DR CCDS; CCDS73060.1; -. [Q15326-2] DR CCDS; CCDS91197.1; -. [Q15326-4] DR PIR; S56145; S56145. DR RefSeq; NP_001189393.1; NM_001202464.1. [Q15326-2] DR RefSeq; NP_001189394.1; NM_001202465.1. [Q15326-5] DR RefSeq; NP_001189396.1; NM_001202467.1. [Q15326-4] DR RefSeq; NP_001189397.1; NM_001202468.1. [Q15326-3] DR RefSeq; NP_006615.2; NM_006624.5. [Q15326-1] DR RefSeq; NP_997644.2; NM_212479.3. [Q15326-6] DR RefSeq; XP_005252416.1; XM_005252359.4. DR RefSeq; XP_005252418.1; XM_005252361.3. DR RefSeq; XP_005252419.1; XM_005252362.2. DR RefSeq; XP_006717439.1; XM_006717376.2. DR RefSeq; XP_016871076.1; XM_017015587.1. DR RefSeq; XP_016871077.1; XM_017015588.1. DR RefSeq; XP_016871078.1; XM_017015589.1. DR RefSeq; XP_016871079.1; XM_017015590.1. DR RefSeq; XP_016871081.1; XM_017015592.1. DR RefSeq; XP_016871082.1; XM_017015593.1. DR PDB; 4NS5; X-ray; 1.90 A; A=154-371. DR PDB; 5HDA; X-ray; 2.39 A; A/C=480-602. DR PDBsum; 4NS5; -. DR PDBsum; 5HDA; -. DR AlphaFoldDB; Q15326; -. DR SASBDB; Q15326; -. DR SMR; Q15326; -. DR BioGRID; 115989; 97. DR ELM; Q15326; -. DR IntAct; Q15326; 48. DR MINT; Q15326; -. DR STRING; 9606.ENSP00000371003; -. DR ChEMBL; CHEMBL4739854; -. DR GlyGen; Q15326; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15326; -. DR PhosphoSitePlus; Q15326; -. DR SwissPalm; Q15326; -. DR BioMuta; ZMYND11; -. DR DMDM; 425906058; -. DR EPD; Q15326; -. DR jPOST; Q15326; -. DR MassIVE; Q15326; -. DR MaxQB; Q15326; -. DR PaxDb; 9606-ENSP00000381053; -. DR PeptideAtlas; Q15326; -. DR ProteomicsDB; 28024; -. DR ProteomicsDB; 60529; -. [Q15326-1] DR ProteomicsDB; 61337; -. DR ProteomicsDB; 6423; -. DR Pumba; Q15326; -. DR Antibodypedia; 9245; 288 antibodies from 30 providers. DR DNASU; 10771; -. DR Ensembl; ENST00000381591.5; ENSP00000371003.1; ENSG00000015171.21. [Q15326-1] DR Ensembl; ENST00000381604.9; ENSP00000371017.6; ENSG00000015171.21. [Q15326-1] DR Ensembl; ENST00000397962.8; ENSP00000381053.3; ENSG00000015171.21. [Q15326-1] DR Ensembl; ENST00000509513.6; ENSP00000424205.2; ENSG00000015171.21. [Q15326-6] DR Ensembl; ENST00000558098.4; ENSP00000452959.1; ENSG00000015171.21. [Q15326-3] DR Ensembl; ENST00000602682.6; ENSP00000473321.1; ENSG00000015171.21. [Q15326-5] DR Ensembl; ENST00000704295.1; ENSP00000515819.1; ENSG00000015171.21. [Q15326-2] DR Ensembl; ENST00000704301.1; ENSP00000515825.1; ENSG00000015171.21. [Q15326-1] DR Ensembl; ENST00000704303.1; ENSP00000515827.1; ENSG00000015171.21. [Q15326-2] DR Ensembl; ENST00000704335.1; ENSP00000515849.1; ENSG00000015171.21. [Q15326-4] DR GeneID; 10771; -. DR KEGG; hsa:10771; -. DR MANE-Select; ENST00000381604.9; ENSP00000371017.6; NM_001370100.5; NP_001357029.1. DR UCSC; uc001ifk.4; human. [Q15326-1] DR AGR; HGNC:16966; -. DR CTD; 10771; -. DR DisGeNET; 10771; -. DR GeneCards; ZMYND11; -. DR HGNC; HGNC:16966; ZMYND11. DR HPA; ENSG00000015171; Low tissue specificity. DR MalaCards; ZMYND11; -. DR MIM; 608668; gene. DR MIM; 616083; phenotype. DR neXtProt; NX_Q15326; -. DR OpenTargets; ENSG00000015171; -. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR PharmGKB; PA128394578; -. DR VEuPathDB; HostDB:ENSG00000015171; -. DR eggNOG; KOG3612; Eukaryota. DR GeneTree; ENSGT00940000156942; -. DR HOGENOM; CLU_031462_2_0_1; -. DR InParanoid; Q15326; -. DR OMA; HQLVYAK; -. DR OrthoDB; 764287at2759; -. DR PhylomeDB; Q15326; -. DR TreeFam; TF106407; -. DR PathwayCommons; Q15326; -. DR SignaLink; Q15326; -. DR SIGNOR; Q15326; -. DR BioGRID-ORCS; 10771; 17 hits in 1177 CRISPR screens. DR ChiTaRS; ZMYND11; human. DR GeneWiki; ZMYND11; -. DR GenomeRNAi; 10771; -. DR Pharos; Q15326; Tbio. DR PRO; PR:Q15326; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q15326; Protein. DR Bgee; ENSG00000015171; Expressed in cranial nerve II and 214 other cell types or tissues. DR ExpressionAtlas; Q15326; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; TAS:GO_Central. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central. DR GO; GO:0034243; P:regulation of transcription elongation by RNA polymerase II; ISS:UniProtKB. DR CDD; cd05492; Bromo_ZMYND11; 1. DR CDD; cd15537; PHD_BS69; 1. DR CDD; cd20159; PWWP_BS69; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 6.10.140.2220; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR047268; PWWP_BS69. DR InterPro; IPR000313; PWWP_dom. DR InterPro; IPR048589; SAMD1-like_WH. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR047269; ZMY11. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR002893; Znf_MYND. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46379; ZINC FINGER MYND DOMAIN-CONTAINING; 1. DR PANTHER; PTHR46379:SF1; ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 11; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00855; PWWP; 1. DR Pfam; PF21524; SAMD1_WH; 1. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00293; PWWP; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS50812; PWWP; 1. DR PROSITE; PS52014; SAMD1_WH; 1. DR PROSITE; PS01360; ZF_MYND_1; 1. DR PROSITE; PS50865; ZF_MYND_2; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q15326; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Bromodomain; Cell cycle; KW Chromatin regulator; Chromosomal rearrangement; Chromosome; DNA-binding; KW Host-virus interaction; Intellectual disability; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation; KW Zinc; Zinc-finger. FT CHAIN 1..602 FT /note="Zinc finger MYND domain-containing protein 11" FT /id="PRO_0000211218" FT DOMAIN 6..82 FT /note="SAMD1-like winged helix (WH)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01358" FT DOMAIN 168..238 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 280..331 FT /note="PWWP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162" FT ZN_FING 100..148 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 563..598 FT /note="MYND-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134, FT ECO:0000269|PubMed:26845565" FT REGION 366..459 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 452..572 FT /note="Interaction with human adenovirus E1A" FT MOTIF 394..400 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 390..415 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 417..459 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:24675531, FT ECO:0007744|PDB:4NS5" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:24675531, FT ECO:0007744|PDB:4NS5" FT BINDING 277 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:24675531, FT ECO:0007744|PDB:4NS5" FT BINDING 281 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:24675531, FT ECO:0007744|PDB:4NS5" FT BINDING 563 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 566 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 574 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 575 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 581 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 585 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 594 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 598 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 366 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 407 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 408 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 93..146 FT /note="Missing (in isoform 2, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:16565076" FT /id="VSP_044482" FT VAR_SEQ 173..203 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046246" FT VAR_SEQ 233 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_047209" FT VAR_SEQ 563..602 FT /note="CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR -> VNTSLF FT (in isoform 3, isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16565076" FT /id="VSP_044483" FT MUTAGEN 258..261 FT /note="CKNC->AKNA: No effect on nuclear location." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 287 FT /note="K->A: Abolishes binding to DNA. No effect on nuclear FT location." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 289 FT /note="K->A: Abolishes binding to DNA. No effect on nuclear FT location." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 291 FT /note="F->A: No effect on nuclear location." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 294 FT /note="W->A: Abolishes interaction with Histone 3. Diffused FT distribution in the nucleus." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 310 FT /note="F->A: Diffused distribution in the nucleus." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 334 FT /note="R->A: Decreases binding to DNA." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 338..339 FT /note="KR->AA: No effect on interaction with Histone 3. FT Abolishes binding to DNA. Changes location from nuclear to FT cytoplasmic." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 344..345 FT /note="KK->AA: Abolishes binding to DNA. No effect on FT nuclear location." FT /evidence="ECO:0000269|PubMed:24675531" FT MUTAGEN 562 FT /note="W->Y: Reduced interaction with PXLXP ligand MGA FT without affecting interaction with viral human adenovirus FT early E1A protein." FT /evidence="ECO:0000269|PubMed:23372760" FT MUTAGEN 563 FT /note="C->S: Abrogates binding to EZH2." FT /evidence="ECO:0000269|PubMed:16565076" FT MUTAGEN 567..568 FT /note="EE->KK: Reduced interaction with PXLXP ligand FT proteins." FT /evidence="ECO:0000269|PubMed:23372760" FT MUTAGEN 572 FT /note="Y->A: Decreases interaction with Epstein-Barr virus FT EBNA2 protein." FT /evidence="ECO:0000269|PubMed:26845565" FT MUTAGEN 586 FT /note="Q->A: Highly decreases interaction with Epstein-Barr FT virus EBNA2 protein. No effect on the inhibition of FT EBNA2-mediated transcriptional activation. Almost abolishes FT interaction with Epstein-Barr virus EBNA2 protein and FT inhibition of EBNA2-mediated transcriptional activation; FT when associated with A-590." FT /evidence="ECO:0000269|PubMed:26845565" FT MUTAGEN 590 FT /note="W->A: Highly decreases interaction with Epstein-Barr FT virus EBNA2 protein. Almost abolishes interaction with FT Epstein-Barr virus EBNA2 protein and inhibition of FT EBNA2-mediated transcriptional activation; when associated FT with A-590." FT /evidence="ECO:0000269|PubMed:26845565" FT MUTAGEN 599..602 FT /note="RRKR->GGGG: Abolished interaction with PXLXP ligand FT proteins." FT /evidence="ECO:0000269|PubMed:23372760" FT MUTAGEN 600 FT /note="R->A: Highly decreases interaction with Epstein-Barr FT virus EBNA2 protein." FT /evidence="ECO:0000269|PubMed:26845565" FT HELIX 157..169 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 198..206 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 213..231 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 236..257 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 259..267 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:4NS5" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:4NS5" FT STRAND 293..302 FT /evidence="ECO:0007829|PDB:4NS5" FT STRAND 305..310 FT /evidence="ECO:0007829|PDB:4NS5" FT STRAND 317..321 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:4NS5" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 341..359 FT /evidence="ECO:0007829|PDB:4NS5" FT HELIX 482..558 FT /evidence="ECO:0007829|PDB:5HDA" FT STRAND 562..566 FT /evidence="ECO:0007829|PDB:5HDA" FT STRAND 572..575 FT /evidence="ECO:0007829|PDB:5HDA" FT STRAND 578..582 FT /evidence="ECO:0007829|PDB:5HDA" FT HELIX 583..592 FT /evidence="ECO:0007829|PDB:5HDA" FT HELIX 594..596 FT /evidence="ECO:0007829|PDB:5HDA" SQ SEQUENCE 602 AA; 70963 MW; 3AD525B90574BDE8 CRC64; MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD WYCFECHLPG EVLICDLCFR VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG KDNKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL ELHQRFLREG RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS SQEIPTMPQP IEKVSVSTQT KKLSASSPRM LHRSTQTTND GVCQSMCHDK YTKIFNDFKD RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV EEIKKLATQH KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR KR //