(data stored in ACNUC27125 zone)

SWISSPROT: 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   11-DEC-2019, entry version 180.
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:0000244|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       P03255:- (xeno); NbExp=3; IntAct=EBI-2623509, EBI-2603114;
CC       P12978:EBNA2 (xeno); NbExp=2; IntAct=EBI-2623509, EBI-8052923;
CC       P03230:LMP1 (xeno); NbExp=3; IntAct=EBI-2623509, EBI-6973030;
CC       P36941:LTBR; NbExp=5; IntAct=EBI-2623509, EBI-3509981;
CC       Q13114:TRAF3; NbExp=2; IntAct=EBI-2623509, EBI-357631;
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: Mental retardation, autosomal dominant 30 (MRD30)
CC       [MIM:616083]: A disorder characterized by significantly below average
CC       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 mutations
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};
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   SMR; Q15326; -.
DR   BioGrid; 115989; 61.
DR   ELM; Q15326; -.
DR   IntAct; Q15326; 27.
DR   MINT; Q15326; -.
DR   STRING; 9606.ENSP00000381053; -.
DR   iPTMnet; Q15326; -.
DR   PhosphoSitePlus; Q15326; -.
DR   BioMuta; ZMYND11; -.
DR   DMDM; 425906058; -.
DR   EPD; Q15326; -.
DR   jPOST; Q15326; -.
DR   MassIVE; 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   DNASU; 10771; -.
DR   Ensembl; ENST00000381591; ENSP00000371003; ENSG00000015171. [Q15326-1]
DR   Ensembl; ENST00000381607; ENSP00000371020; ENSG00000015171. [Q15326-2]
DR   Ensembl; ENST00000397959; ENSP00000381050; ENSG00000015171. [Q15326-5]
DR   Ensembl; ENST00000397962; ENSP00000381053; ENSG00000015171. [Q15326-1]
DR   Ensembl; ENST00000509513; ENSP00000424205; ENSG00000015171. [Q15326-6]
DR   Ensembl; ENST00000558098; ENSP00000452959; ENSG00000015171. [Q15326-3]
DR   Ensembl; ENST00000602682; ENSP00000473321; ENSG00000015171. [Q15326-5]
DR   GeneID; 10771; -.
DR   KEGG; hsa:10771; -.
DR   UCSC; uc001ifk.4; human. [Q15326-1]
DR   CTD; 10771; -.
DR   DisGeNET; 10771; -.
DR   EuPathDB; HostDB:ENSG00000015171.18; -.
DR   GeneCards; ZMYND11; -.
DR   HGNC; HGNC:16966; ZMYND11.
DR   HPA; HPA015816; -.
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   eggNOG; KOG3612; Eukaryota.
DR   eggNOG; ENOG410XTCC; LUCA.
DR   GeneTree; ENSGT00940000156942; -.
DR   HOGENOM; HOG000038026; -.
DR   InParanoid; Q15326; -.
DR   KO; K23218; -.
DR   OMA; REHKRVC; -.
DR   OrthoDB; 369818at2759; -.
DR   PhylomeDB; Q15326; -.
DR   TreeFam; TF106407; -.
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 252 organ(s), highest expression level in cauda epididymis.
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:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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;
DR   PRODOM; Q8N4B3.
DR   SWISS-2DPAGE; Q8N4B3.
KW   3D-structure; Alternative splicing; Bromodomain; Cell cycle;
KW   Chromatin regulator; Chromosomal rearrangement; Chromosome; DNA-binding;
KW   Host-virus interaction; Isopeptide bond; Mental retardation; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc;
KW   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          452..572
FT                   /note="Interaction with human adenovirus E1A"
FT   MOTIF           394..400
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   METAL           258
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:4NS5,
FT                   ECO:0000269|PubMed:24675531"
FT   METAL           261
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:4NS5,
FT                   ECO:0000269|PubMed:24675531"
FT   METAL           277
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:4NS5,
FT                   ECO:0000269|PubMed:24675531"
FT   METAL           281
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:4NS5,
FT                   ECO:0000269|PubMed:24675531"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   CROSSLNK        366
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        407
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25772364, ECO:0000244|PubMed:28112733"
FT   CROSSLNK        408
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|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:0000244|PDB:4NS5"
FT   HELIX           198..206
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           213..231
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           236..257
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           259..267
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           272..274
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   STRAND          283..287
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   STRAND          293..302
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   STRAND          305..310
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   STRAND          317..321
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           322..324
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   STRAND          325..327
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           332..334
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           341..359
FT                   /evidence="ECO:0000244|PDB:4NS5"
FT   HELIX           482..558
FT                   /evidence="ECO:0000244|PDB:5HDA"
FT   STRAND          562..566
FT                   /evidence="ECO:0000244|PDB:5HDA"
FT   STRAND          572..575
FT                   /evidence="ECO:0000244|PDB:5HDA"
FT   STRAND          578..582
FT                   /evidence="ECO:0000244|PDB:5HDA"
FT   HELIX           583..592
FT                   /evidence="ECO:0000244|PDB:5HDA"
FT   HELIX           594..596
FT                   /evidence="ECO:0000244|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
//

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