ZMY11_HUMAN
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 03-AUG-2022, entry version 193.
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 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 [26]
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 [27] {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). Interacts (via MYND-type zinc
CC finger) with NCOR1 (PubMed:10734313). Interacts (via MYND-type zinc
CC finger) with MGA protein (via PXLXP motif) (PubMed:23372760). Interacts
CC (via MYND-type zinc finger) with EZH2 (PubMed:16565076). Interacts with
CC EMSY and E2F6 (PubMed:15947784, PubMed:16565076). Interacts with PIAS1
CC and UBE2I (PubMed:19766626). {ECO:0000269|PubMed:10734313,
CC ECO:0000269|PubMed:15947784, ECO:0000269|PubMed:16565076,
CC ECO:0000269|PubMed:19766626, ECO:0000269|PubMed:23372760,
CC ECO:0000269|PubMed:24675531, 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; Q96PC5: MIA2; NbExp=2; IntAct=EBI-2623509, EBI-1050253;
CC Q15326; Q5TI25: NBPF14; NbExp=2; IntAct=EBI-2623509, EBI-2692300;
CC Q15326; A0A087WUL8: NBPF19; NbExp=14; IntAct=EBI-2623509, EBI-30824005;
CC Q15326; P0DPF2: NBPF20; NbExp=22; IntAct=EBI-2623509, EBI-30824513;
CC Q15326; P0DPF3: NBPF9; NbExp=2; IntAct=EBI-2623509, EBI-30824775;
CC Q15326; Q9Y6X0: SETBP1; NbExp=2; IntAct=EBI-2623509, EBI-2548259;
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}. Chromosome
CC {ECO:0000269|PubMed:16565076}. Note=Associates with chromatin and
CC mitotic chromosomes. {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 (MRD30) [MIM:616083]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD30
CC patients manifest mild intellectual disability and subtle facial
CC dysmorphisms, including hypertelorism, ptosis, and a wide mouth.
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};
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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 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; 77.
DR ELM; Q15326; -.
DR IntAct; Q15326; 109.
DR MINT; Q15326; -.
DR STRING; 9606.ENSP00000381053; -.
DR ChEMBL; CHEMBL4739854; -.
DR iPTMnet; Q15326; -.
DR PhosphoSitePlus; Q15326; -.
DR BioMuta; ZMYND11; -.
DR DMDM; 425906058; -.
DR EPD; Q15326; -.
DR jPOST; Q15326; -.
DR MassIVE; Q15326; -.
DR MaxQB; Q15326; -.
DR PaxDb; Q15326; -.
DR PeptideAtlas; Q15326; -.
DR PRIDE; Q15326; -.
DR ProteomicsDB; 28024; -.
DR ProteomicsDB; 60529; -. [Q15326-1]
DR ProteomicsDB; 61337; -.
DR ProteomicsDB; 6423; -.
DR Antibodypedia; 9245; 259 antibodies from 30 providers.
DR DNASU; 10771; -.
DR Ensembl; ENST00000381591.5; ENSP00000371003.1; ENSG00000015171.20. [Q15326-1]
DR Ensembl; ENST00000381604.9; ENSP00000371017.6; ENSG00000015171.20. [Q15326-1]
DR Ensembl; ENST00000381607.8; ENSP00000371020.5; ENSG00000015171.20. [Q15326-2]
DR Ensembl; ENST00000397959.7; ENSP00000381050.3; ENSG00000015171.20. [Q15326-5]
DR Ensembl; ENST00000397962.8; ENSP00000381053.3; ENSG00000015171.20. [Q15326-1]
DR Ensembl; ENST00000509513.6; ENSP00000424205.2; ENSG00000015171.20. [Q15326-6]
DR Ensembl; ENST00000558098.4; ENSP00000452959.1; ENSG00000015171.20. [Q15326-3]
DR Ensembl; ENST00000602682.6; ENSP00000473321.1; ENSG00000015171.20. [Q15326-5]
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 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; MTRVHGM; -.
DR OrthoDB; 369818at2759; -.
DR PhylomeDB; Q15326; -.
DR TreeFam; TF106407; -.
DR PathwayCommons; Q15326; -.
DR SignaLink; Q15326; -.
DR SIGNOR; Q15326; -.
DR BioGRID-ORCS; 10771; 15 hits in 1096 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 212 other tissues.
DR ExpressionAtlas; Q15326; baseline and differential.
DR Genevisible; Q15326; HS.
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:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR CDD; cd05841; BS69_related; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR035505; ZMYND8/11_PWWP.
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 Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 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.
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 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 EBNA2-
FT 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 EBNA2-
FT mediated transcriptional activation; when associated with
FT 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
