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Zinc finger MYND domain-containing protein 11 (Adenovirus 5 E1A-binding protein) (Bone morphogenetic protein receptor-associated molecule 1) (Protein BS69)

 ZMY11_HUMAN             Reviewed;         602 AA.
Q15326; B2R6G8; B7Z293; F6UH50; Q2LD45; Q2LD46; Q2LD47; Q2LD48;
Q5VUI1; Q8N4B3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
28-NOV-2012, sequence version 2.
25-OCT-2017, entry version 163.
RecName: Full=Zinc finger MYND domain-containing protein 11 {ECO:0000305};
AltName: Full=Adenovirus 5 E1A-binding protein;
AltName: Full=Bone morphogenetic protein receptor-associated molecule 1;
AltName: Full=Protein BS69;
Name=ZMYND11 {ECO:0000312|HGNC:HGNC:16966};
Synonyms=BRAM1, BS69 {ECO:0000303|PubMed:24675531};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon carcinoma;
PubMed=7621829;
Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M.,
Sonntag-Buck V., Stunnenberg H.G., Bernards R.;
"BS69, a novel adenovirus E1A-associated protein that inhibits E1A
transactivation.";
EMBO J. 14:3159-3169(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE
SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION,
UBIQUITINATION, INTERACTION WITH E2F6 AND EZH2, AND MUTAGENESIS OF
CYS-563.
PubMed=16565076; DOI=10.1074/jbc.M600573200;
Velasco G., Grkovic S., Ansieau S.;
"New insights into BS69 functions.";
J. Biol. Chem. 281:16546-16550(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
TISSUE=Amygdala, and Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND INTERACTION WITH NCOR1.
PubMed=10734313; DOI=10.1038/sj.onc.1203421;
Masselink H., Bernards R.;
"The adenovirus E1A binding protein BS69 is a corepressor of
transcription through recruitment of N-CoR.";
Oncogene 19:1538-1546(2000).
[8]
INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, AND INTERACTION
WITH EPSTEIN-BARR VIRUS EBNA2 PROTEIN.
PubMed=11733528; DOI=10.1074/jbc.M110078200;
Ansieau S., Leutz A.;
"The conserved Mynd domain of BS69 binds cellular and oncoviral
proteins through a common PXLXP motif.";
J. Biol. Chem. 277:4906-4910(2002).
[9]
INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
PubMed=12181323; DOI=10.1074/jbc.M206736200;
Chung P.J., Chang Y.S., Liang C.L., Meng C.L.;
"Negative regulation of Epstein-Barr virus latent membrane protein 1-
mediated functions by the bone morphogenetic protein receptor IA-
binding protein, BRAM1.";
J. Biol. Chem. 277:39850-39857(2002).
[10]
INTERACTION WITH EMSY.
PubMed=15947784; DOI=10.1038/sj.embor.7400415;
Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D.,
Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S.;
"Binding of EMSY to HP1beta: implications for recruitment of HP1beta
and BS69.";
EMBO Rep. 6:675-680(2005).
[11]
INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
PubMed=16382137; DOI=10.1128/MCB.26.2.448-456.2006;
Wan J., Zhang W., Wu L., Bai T., Zhang M., Lo K.W., Chui Y.L., Cui Y.,
Tao Q., Yamamoto M., Akira S., Wu Z.;
"BS69, a specific adaptor in the latent membrane protein 1-mediated c-
Jun N-terminal kinase pathway.";
Mol. Cell. Biol. 26:448-456(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
PubMed=19379743; DOI=10.1016/j.febslet.2009.04.022;
Ikeda O., Sekine Y., Mizushima A., Oritani K., Yasui T., Fujimuro M.,
Muromoto R., Nanbo A., Matsuda T.;
"BS69 negatively regulates the canonical NF-kappaB activation induced
by Epstein-Barr virus-derived LMP1.";
FEBS Lett. 583:1567-1574(2009).
[15]
SUBCELLULAR LOCATION, SUMOYLATION, AND INTERACTION WITH PIAS1 AND
UBE2I.
PubMed=19766626; DOI=10.1016/j.yexcr.2009.09.011;
Yu B., Shao Y., Zhang C., Chen Y., Zhong Q., Zhang J., Yang H.,
Zhang W., Wan J.;
"BS69 undergoes SUMO modification and plays an inhibitory role in
muscle and neuronal differentiation.";
Exp. Cell Res. 315:3543-3553(2009).
[16]
INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
PubMed=20138174; DOI=10.1016/j.febslet.2010.01.060;
Ikeda O., Miyasaka Y., Yoshida R., Mizushima A., Oritani K.,
Sekine Y., Kuroda M., Yasui T., Fujimuro M., Muromoto R., Nanbo A.,
Matsuda T.;
"BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-
derived LMP1/CTAR1-induced NF-kappaB activation.";
FEBS Lett. 584:865-872(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
CHROMOSOMAL TRANSLOCATION WITH MBTD1.
PubMed=23915195; DOI=10.3109/10428194.2013.820292;
De Braekeleer E., Auffret R., Douet-Guilbert N., Basinko A.,
Le Bris M.J., Morel F., De Braekeleer M.;
"Recurrent translocation (10;17)(p15;q21) in acute poorly
differentiated myeloid leukemia likely results in ZMYND11-MBTD1
fusion.";
Leuk. Lymphoma 55:1189-1190(2014).
[20]
INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH
EPSTEIN-BARR VIRUS EBNA2 PROTEIN, INTERACTION WITH MGA, AND
MUTAGENESIS OF TRP-562; 567-GLU-GLU-568 AND 599-ARG--ARG-602.
PubMed=23372760; DOI=10.1371/journal.pone.0054715;
Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R.,
Bottomley M., Franzmann T.M., Buchner J., Ansieau S., Sattler M.;
"Structural and functional analysis of the DEAF-1 and BS69 MYND
domains.";
PLoS ONE 8:E54715-E54715(2013).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
INDUCTION.
PubMed=24590075; DOI=10.1038/nature13045;
Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K.,
Ren Y., Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.;
"ZMYND11 links histone H3.3K36me3 to transcription elongation and
tumour suppression.";
Nature 508:263-268(2014).
[23]
INVOLVEMENT IN MRD30.
PubMed=25217958; DOI=10.1038/ng.3092;
Coe B.P., Witherspoon K., Rosenfeld J.A., van Bon B.W.,
Vulto-van Silfhout A.T., Bosco P., Friend K.L., Baker C., Buono S.,
Vissers L.E., Schuurs-Hoeijmakers J.H., Hoischen A., Pfundt R.,
Krumm N., Carvill G.L., Li D., Amaral D., Brown N., Lockhart P.J.,
Scheffer I.E., Alberti A., Shaw M., Pettinato R., Tervo R.,
de Leeuw N., Reijnders M.R., Torchia B.S., Peeters H., O'Roak B.J.,
Fichera M., Hehir-Kwa J.Y., Shendure J., Mefford H.C., Haan E.,
Gecz J., de Vries B.B., Romano C., Eichler E.E.;
"Refining analyses of copy number variation identifies specific genes
associated with developmental delay.";
Nat. Genet. 46:1063-1071(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-366; LYS-407 AND LYS-408,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 154-371 IN COMPLEX WITH
ZINC, INTERACTION WITH HISTONE 3, SUBCELLULAR LOCATION, DNA-BINDING,
DOMAIN, MUTAGENESIS OF 258-CYS--CYS-261; LYS-287; LYS-289; PHE-291;
TRP-294; PHE-310; ARG-334; 338-LYS-ARG-339 AND 344-LYS-LYS-345, AND
FUNCTION.
PubMed=24675531; DOI=10.1038/cr.2014.38;
Wang J., Qin S., Li F., Li S., Zhang W., Peng J., Zhang Z., Gong Q.,
Wu J., Shi Y.;
"Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in
H3K36me3 nucleosome binding.";
Cell Res. 24:890-893(2014).
[27] {ECO:0000244|PDB:5HDA}
X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 480-602 IN COMPLEX WITH ZINC
AND EPSTEIN-BARR VIRUS EBNA2 PEPTIDE, SUBUNIT, INTERACTION WITH
EPSTEIN-BARR VIRUS EBNA2 PROTEIN, FUNCTION (MICROBIAL INFECTION), AND
MUTAGENESIS OF TYR-572; GLN-586; TRP-590 AND ARG-600.
PubMed=26845565; DOI=10.1371/journal.ppat.1005414;
Harter M.R., Liu C.D., Shen C.L., Gonzalez-Hurtado E., Zhang Z.M.,
Xu M., Martinez E., Peng C.W., Song J.;
"BS69/ZMYND11 C-Terminal Domains Bind and Inhibit EBNA2.";
PLoS Pathog. 12:1005414-1005414(2016).
-!- FUNCTION: Chromatin reader that specifically recognizes and binds
histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates
RNA polymerase II elongation. Does not bind other histone H3
subtypes (H3.1 or H3.2) (By similarity). Colocalizes with highly
expressed genes and functions as a transcription corepressor by
modulating RNA polymerase II at the elongation stage. Binds non-
specifically to dsDNA (PubMed:24675531). Acts as a tumor-
suppressor by repressing a transcriptional program essential for
tumor cell growth. {ECO:0000250|UniProtKB:Q8R5C8,
ECO:0000269|PubMed:10734313, ECO:0000269|PubMed:16565076,
ECO:0000269|PubMed:24675531}.
-!- FUNCTION: (Microbial infection) Inhibits Epstein-Barr virus EBNA2-
mediated transcriptional activation and host cell proliferation,
through direct interaction. {ECO:0000269|PubMed:26845565}.
-!- SUBUNIT: Homooligomer; forms homooligomers via its C-terminus
(PubMed:26845565). Interacts with histone H3.3 trimethylated at
'Lys-36' (H3.3K36me3) (PubMed:24675531). Interacts (via MYND-type
zinc finger) with NCOR1 (PubMed:10734313). Interacts (via MYND-
type zinc finger) with MGA protein (via PXLXP motif)
(PubMed:23372760). Interacts (via MYND-type zinc finger) with EZH2
(PubMed:16565076). Interacts with EMSY and E2F6 (PubMed:15947784,
PubMed:16565076). Interacts with PIAS1 and UBE2I
(PubMed:19766626). {ECO:0000269|PubMed:10734313,
ECO:0000269|PubMed:15947784, ECO:0000269|PubMed:16565076,
ECO:0000269|PubMed:19766626, ECO:0000269|PubMed:23372760,
ECO:0000269|PubMed:24675531, ECO:0000269|PubMed:26845565}.
-!- SUBUNIT: (Microbial infection) Interacts (via MYND-type zinc
finger) with human adenovirus early E1A protein (via PXLXP motif);
this interaction inhibits E1A mediated transactivation
(PubMed:11733528, PubMed:23372760). Interacts (via MYND-type zinc
finger) with Epstein-Barr virus EBNA2 protein (via PXLXP motif)
(PubMed:11733528, PubMed:26845565). Interacts with Epstein-Barr
virus-derived protein LMP1; leading to negatively regulate NF-
kappa-B activation by Epstein-Barr virus-derived protein LMP1
(PubMed:12181323, PubMed:16382137, PubMed:19379743,
PubMed:20138174). {ECO:0000269|PubMed:11733528,
ECO:0000269|PubMed:12181323, ECO:0000269|PubMed:16382137,
ECO:0000269|PubMed:19379743, ECO:0000269|PubMed:20138174,
ECO:0000269|PubMed:23372760, ECO:0000269|PubMed:26845565}.
-!- INTERACTION:
P03255:- (xeno); NbExp=3; IntAct=EBI-2623509, EBI-2603114;
P12978:EBNA2 (xeno); NbExp=2; IntAct=EBI-2623509, EBI-8052923;
P03230:LMP1 (xeno); NbExp=3; IntAct=EBI-2623509, EBI-6973030;
P36941:LTBR; NbExp=5; IntAct=EBI-2623509, EBI-3509981;
Q13114:TRAF3; NbExp=2; IntAct=EBI-2623509, EBI-357631;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16565076,
ECO:0000269|PubMed:19766626, ECO:0000269|PubMed:24675531}.
Chromosome {ECO:0000269|PubMed:16565076}. Note=Associates with
chromatin and mitotic chromosomes. {ECO:0000269|PubMed:16565076}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q15326-1; Sequence=Displayed;
Name=2;
IsoId=Q15326-2; Sequence=VSP_044482;
Name=3;
IsoId=Q15326-3; Sequence=VSP_044483;
Name=4;
IsoId=Q15326-4; Sequence=VSP_044482, VSP_044483;
Name=5;
IsoId=Q15326-5; Sequence=VSP_044482, VSP_046246;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q15326-6; Sequence=VSP_047209, VSP_044483;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16565076}.
-!- INDUCTION: Down-regulated in breast cancer patients with poor
prognosis. {ECO:0000269|PubMed:24590075}.
-!- DOMAIN: The PWWP domain specifically recognizes and binds histone
H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-
bladed beta-barrel fold with an extended C-terminal alpha-helix,
with a conserved H3.3K36me3-binding aromatic cage formed by Phe-
291 and Trp-294 of the beta1-beta2 loop and Phe-310 of the beta3-
beta4 loop. Specific recognition of H3.3 histone is mediated by
the encapsulation of the H3.3-specific 'Ser 31' residue in a
composite pocket formed by the tandem bromo-PWWP domains.
{ECO:0000269|PubMed:24675531}.
-!- PTM: Sumoylated following its interaction with PIAS1 and UBE2I.
{ECO:0000269|PubMed:19766626}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation.
{ECO:0000269|PubMed:16565076}.
-!- DISEASE: Note=A chromosomal aberration involving ZMYND11 is a
cause of acute poorly differentiated myeloid leukemia.
Translocation (10;17)(p15;q21) with MBTD1.
{ECO:0000269|PubMed:23915195}.
-!- DISEASE: Mental retardation, autosomal dominant 30 (MRD30)
[MIM:616083]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. MRD30 patients manifest mild intellectual
disability and subtle facial dysmorphisms, including
hypertelorism, ptosis, and a wide mouth.
{ECO:0000269|PubMed:25217958}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH34784.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG35465.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA60052.1; Type=Frameshift; Positions=11, 39; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X86098; CAA60052.1; ALT_FRAME; mRNA.
EMBL; DQ335452; ABC72408.1; -; mRNA.
EMBL; DQ335453; ABC72409.1; -; mRNA.
EMBL; DQ335454; ABC72410.1; -; mRNA.
EMBL; DQ335455; ABC72411.1; -; mRNA.
EMBL; AK294469; BAH11779.1; -; mRNA.
EMBL; AK312570; BAG35465.1; ALT_INIT; mRNA.
EMBL; AL589988; CAH69845.1; -; Genomic_DNA.
EMBL; AL603831; CAH69845.1; JOINED; Genomic_DNA.
EMBL; AL603831; CAI40899.1; -; Genomic_DNA.
EMBL; AL589988; CAI40899.1; JOINED; Genomic_DNA.
EMBL; AL713922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL731539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471072; EAW86539.1; -; Genomic_DNA.
EMBL; CH471072; EAW86540.1; -; Genomic_DNA.
EMBL; CH471072; EAW86541.1; -; Genomic_DNA.
EMBL; BC034784; AAH34784.1; ALT_INIT; mRNA.
CCDS; CCDS55696.1; -. [Q15326-3]
CCDS; CCDS55697.1; -. [Q15326-5]
CCDS; CCDS7052.2; -. [Q15326-1]
CCDS; CCDS7053.2; -. [Q15326-6]
CCDS; CCDS73060.1; -. [Q15326-2]
PIR; S56145; S56145.
RefSeq; NP_001189393.1; NM_001202464.1. [Q15326-2]
RefSeq; NP_001189394.1; NM_001202465.1. [Q15326-5]
RefSeq; NP_001189396.1; NM_001202467.1. [Q15326-4]
RefSeq; NP_001189397.1; NM_001202468.1. [Q15326-3]
RefSeq; NP_006615.2; NM_006624.5. [Q15326-1]
RefSeq; NP_997644.2; NM_212479.3. [Q15326-6]
RefSeq; XP_005252416.1; XM_005252359.4. [Q15326-1]
RefSeq; XP_005252418.1; XM_005252361.3. [Q15326-2]
RefSeq; XP_005252419.1; XM_005252362.2. [Q15326-2]
RefSeq; XP_006717439.1; XM_006717376.2. [Q15326-2]
RefSeq; XP_016871076.1; XM_017015587.1. [Q15326-1]
RefSeq; XP_016871077.1; XM_017015588.1. [Q15326-1]
RefSeq; XP_016871078.1; XM_017015589.1. [Q15326-1]
RefSeq; XP_016871079.1; XM_017015590.1. [Q15326-1]
RefSeq; XP_016871081.1; XM_017015592.1. [Q15326-2]
RefSeq; XP_016871082.1; XM_017015593.1. [Q15326-2]
UniGene; Hs.292265; -.
UniGene; Hs.740145; -.
PDB; 4NS5; X-ray; 1.90 A; A=154-371.
PDB; 5HDA; X-ray; 2.39 A; A/C=480-602.
PDBsum; 4NS5; -.
PDBsum; 5HDA; -.
ProteinModelPortal; Q15326; -.
SMR; Q15326; -.
BioGrid; 115989; 57.
ELM; Q15326; -.
IntAct; Q15326; 24.
MINT; MINT-156360; -.
STRING; 9606.ENSP00000371003; -.
iPTMnet; Q15326; -.
PhosphoSitePlus; Q15326; -.
BioMuta; ZMYND11; -.
DMDM; 425906058; -.
EPD; Q15326; -.
PaxDb; Q15326; -.
PeptideAtlas; Q15326; -.
PRIDE; Q15326; -.
DNASU; 10771; -.
Ensembl; ENST00000381591; ENSP00000371003; ENSG00000015171. [Q15326-1]
Ensembl; ENST00000381607; ENSP00000371020; ENSG00000015171. [Q15326-2]
Ensembl; ENST00000397959; ENSP00000381050; ENSG00000015171. [Q15326-5]
Ensembl; ENST00000397962; ENSP00000381053; ENSG00000015171. [Q15326-1]
Ensembl; ENST00000509513; ENSP00000424205; ENSG00000015171. [Q15326-6]
Ensembl; ENST00000558098; ENSP00000452959; ENSG00000015171. [Q15326-3]
Ensembl; ENST00000602682; ENSP00000473321; ENSG00000015171. [Q15326-5]
GeneID; 10771; -.
KEGG; hsa:10771; -.
UCSC; uc001ifk.4; human. [Q15326-1]
CTD; 10771; -.
DisGeNET; 10771; -.
EuPathDB; HostDB:ENSG00000015171.18; -.
GeneCards; ZMYND11; -.
H-InvDB; HIX0025946; -.
HGNC; HGNC:16966; ZMYND11.
HPA; HPA015816; -.
MalaCards; ZMYND11; -.
MIM; 608668; gene.
MIM; 616083; phenotype.
neXtProt; NX_Q15326; -.
OpenTargets; ENSG00000015171; -.
PharmGKB; PA128394578; -.
eggNOG; KOG3612; Eukaryota.
eggNOG; ENOG410XTCC; LUCA.
GeneTree; ENSGT00530000063428; -.
HOGENOM; HOG000038026; -.
HOVERGEN; HBG054949; -.
InParanoid; Q15326; -.
OMA; KCLSDEY; -.
OrthoDB; EOG091G0B2W; -.
PhylomeDB; Q15326; -.
TreeFam; TF106407; -.
ChiTaRS; ZMYND11; human.
GeneWiki; ZMYND11; -.
GenomeRNAi; 10771; -.
PRO; PR:Q15326; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000015171; -.
CleanEx; HS_ZMYND11; -.
ExpressionAtlas; Q15326; baseline and differential.
Genevisible; Q15326; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003712; F:transcription cofactor activity; IBA:GO_Central.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd05841; BS69_related; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR035505; ZMYND8/11_PWWP.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR002893; Znf_MYND.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00855; PWWP; 1.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 1.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50812; PWWP; 1.
PROSITE; PS01360; ZF_MYND_1; 1.
PROSITE; PS50865; ZF_MYND_2; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Bromodomain; Cell cycle;
Chromatin regulator; Chromosomal rearrangement; Chromosome;
Complete proteome; DNA-binding; Host-virus interaction;
Isopeptide bond; Mental retardation; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 602 Zinc finger MYND domain-containing
protein 11.
/FTId=PRO_0000211218.
DOMAIN 168 238 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 280 331 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
ZN_FING 100 148 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 563 598 MYND-type. {ECO:0000255|PROSITE-
ProRule:PRU00134,
ECO:0000269|PubMed:26845565}.
REGION 452 572 Interaction with human adenovirus E1A.
MOTIF 394 400 Nuclear localization signal.
{ECO:0000255}.
METAL 258 258 Zinc. {ECO:0000244|PDB:4NS5,
ECO:0000269|PubMed:24675531}.
METAL 261 261 Zinc. {ECO:0000244|PDB:4NS5,
ECO:0000269|PubMed:24675531}.
METAL 277 277 Zinc. {ECO:0000244|PDB:4NS5,
ECO:0000269|PubMed:24675531}.
METAL 281 281 Zinc; via tele nitrogen.
{ECO:0000244|PDB:4NS5,
ECO:0000269|PubMed:24675531}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 407 407 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 408 408 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 93 146 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16565076}.
/FTId=VSP_044482.
VAR_SEQ 173 203 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046246.
VAR_SEQ 233 233 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047209.
VAR_SEQ 563 602 CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
-> VNTSLF (in isoform 3, isoform 4 and
isoform 6). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16565076}.
/FTId=VSP_044483.
MUTAGEN 258 261 CKNC->AKNA: No effect on nuclear
location. {ECO:0000269|PubMed:24675531}.
MUTAGEN 287 287 K->A: Abolishes binding to DNA. No effect
on nuclear location.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 289 289 K->A: Abolishes binding to DNA. No effect
on nuclear location.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 291 291 F->A: No effect on nuclear location.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 294 294 W->A: Abolishes interaction with Histone
3. Diffused distribution in the nucleus.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 310 310 F->A: Diffused distribution in the
nucleus. {ECO:0000269|PubMed:24675531}.
MUTAGEN 334 334 R->A: Decreases binding to DNA.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 338 339 KR->AA: No effect on interaction with
Histone 3. Abolishes binding to DNA.
Changes location from nuclear to
cytoplasmic.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 344 345 KK->AA: Abolishes binding to DNA. No
effect on nuclear location.
{ECO:0000269|PubMed:24675531}.
MUTAGEN 562 562 W->Y: Reduced interaction with PXLXP
ligand MGA without affecting interaction
with viral human adenovirus early E1A
protein. {ECO:0000269|PubMed:23372760}.
MUTAGEN 563 563 C->S: Abrogates binding to EZH2.
{ECO:0000269|PubMed:16565076}.
MUTAGEN 567 568 EE->KK: Reduced interaction with PXLXP
ligand proteins.
{ECO:0000269|PubMed:23372760}.
MUTAGEN 572 572 Y->A: Decreases interaction with Epstein-
Barr virus EBNA2 protein.
{ECO:0000269|PubMed:26845565}.
MUTAGEN 586 586 Q->A: Highly decreases interaction with
Epstein-Barr virus EBNA2 protein. No
effect on the inhibition of EBNA2-
mediated transcriptional activation.
Almost abolishes interaction with
Epstein-Barr virus EBNA2 protein and
inhibition of EBNA2-mediated
transcriptional activation; when
associated with A-590.
{ECO:0000269|PubMed:26845565}.
MUTAGEN 590 590 W->A: Highly decreases interaction with
Epstein-Barr virus EBNA2 protein. Almost
abolishes interaction with Epstein-Barr
virus EBNA2 protein and inhibition of
EBNA2-mediated transcriptional
activation; when associated with A-590.
{ECO:0000269|PubMed:26845565}.
MUTAGEN 599 602 RRKR->GGGG: Abolished interaction with
PXLXP ligand proteins.
{ECO:0000269|PubMed:23372760}.
MUTAGEN 600 600 R->A: Highly decreases interaction with
Epstein-Barr virus EBNA2 protein.
{ECO:0000269|PubMed:26845565}.
HELIX 157 169 {ECO:0000244|PDB:4NS5}.
HELIX 198 206 {ECO:0000244|PDB:4NS5}.
HELIX 213 231 {ECO:0000244|PDB:4NS5}.
HELIX 236 257 {ECO:0000244|PDB:4NS5}.
HELIX 259 267 {ECO:0000244|PDB:4NS5}.
HELIX 272 274 {ECO:0000244|PDB:4NS5}.
STRAND 283 287 {ECO:0000244|PDB:4NS5}.
STRAND 293 302 {ECO:0000244|PDB:4NS5}.
STRAND 305 310 {ECO:0000244|PDB:4NS5}.
STRAND 317 321 {ECO:0000244|PDB:4NS5}.
HELIX 322 324 {ECO:0000244|PDB:4NS5}.
STRAND 325 327 {ECO:0000244|PDB:4NS5}.
HELIX 332 334 {ECO:0000244|PDB:4NS5}.
HELIX 341 359 {ECO:0000244|PDB:4NS5}.
HELIX 482 558 {ECO:0000244|PDB:5HDA}.
STRAND 562 566 {ECO:0000244|PDB:5HDA}.
STRAND 572 575 {ECO:0000244|PDB:5HDA}.
STRAND 578 582 {ECO:0000244|PDB:5HDA}.
HELIX 583 592 {ECO:0000244|PDB:5HDA}.
HELIX 594 596 {ECO:0000244|PDB:5HDA}.
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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