Full text data of ZMYND11
ZMYND11
(BS69)
[Confidence: low (only semi-automatic identification from reviews)]
Zinc finger MYND domain-containing protein 11 (Adenovirus 5 E1A-binding protein; Protein BS69)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Zinc finger MYND domain-containing protein 11 (Adenovirus 5 E1A-binding protein; Protein BS69)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15326
ID ZMY11_HUMAN Reviewed; 602 AA.
AC Q15326; B2R6G8; B7Z293; F6UH50; Q2LD45; Q2LD46; Q2LD47; Q2LD48;
read moreAC Q5VUI1; Q8N4B3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Zinc finger MYND domain-containing protein 11;
DE AltName: Full=Adenovirus 5 E1A-binding protein;
DE AltName: Full=Protein BS69;
GN Name=ZMYND11; Synonyms=BS69;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RX PubMed=7621829;
RA Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M.,
RA Sonntag-Buck V., 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
RP SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION,
RP UBIQUITINATION, INTERACTION WITH E2F6 AND EZH2, AND MUTAGENESIS OF
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT transcription through recruitment of N-CoR.";
RL Oncogene 19:1538-1546(2000).
RN [8]
RP INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, AND INTERACTION
RP WITH 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
RT proteins through a common PXLXP motif.";
RL J. Biol. Chem. 277:4906-4910(2002).
RN [9]
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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP SPECTROMETRY.
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 [11]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Corepressor of transcription (Probable). May be involved
CC in chromatin remodeling through association with several
CC remodeling factors.
CC -!- SUBUNIT: Interacts (via MYND-type zinc finger) with NCOR1.
CC Interacts (via MYND-type zinc finger) with human adenovirus early
CC E1A protein (via PXLXP motif); this interaction inhibits E1A
CC mediated transactivation. Interacts (via MYND-type zinc finger)
CC with Epstein-Barr virus EBNA2 protein (via PXLXP motif). Interacts
CC (via MYND-type zinc finger) with EZH2. Interacts with E2F6.
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. Chromosome. Note=Associates with
CC chromatin and mitotic chromosomes.
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 Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q15326-6; Sequence=VSP_047209, VSP_044483;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC -!- SIMILARITY: Contains 1 bromo domain.
CC -!- SIMILARITY: Contains 1 MYND-type zinc finger.
CC -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC -!- SIMILARITY: Contains 1 PWWP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34784.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAG35465.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA60052.1; Type=Frameshift; Positions=11, 39;
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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; CAH69845.1; -; Genomic_DNA.
DR EMBL; AL603831; CAH69845.1; JOINED; Genomic_DNA.
DR EMBL; AL603831; CAI40899.1; -; Genomic_DNA.
DR EMBL; AL589988; CAI40899.1; JOINED; 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 PIR; S56145; S56145.
DR RefSeq; NP_001189393.1; NM_001202464.1.
DR RefSeq; NP_001189394.1; NM_001202465.1.
DR RefSeq; NP_001189396.1; NM_001202467.1.
DR RefSeq; NP_001189397.1; NM_001202468.1.
DR RefSeq; NP_006615.2; NM_006624.5.
DR RefSeq; NP_997644.2; NM_212479.3.
DR RefSeq; XP_005252416.1; XM_005252359.1.
DR RefSeq; XP_005252418.1; XM_005252361.1.
DR RefSeq; XP_005252419.1; XM_005252362.1.
DR UniGene; Hs.292265; -.
DR UniGene; Hs.740145; -.
DR ProteinModelPortal; Q15326; -.
DR SMR; Q15326; 95-239.
DR IntAct; Q15326; 19.
DR MINT; MINT-156360; -.
DR STRING; 9606.ENSP00000309992; -.
DR PhosphoSite; Q15326; -.
DR DMDM; 10719919; -.
DR PaxDb; Q15326; -.
DR PRIDE; Q15326; -.
DR DNASU; 10771; -.
DR Ensembl; ENST00000309776; ENSP00000309992; ENSG00000015171.
DR Ensembl; ENST00000381591; ENSP00000371003; ENSG00000015171.
DR Ensembl; ENST00000381604; ENSP00000371017; ENSG00000015171.
DR Ensembl; ENST00000397959; ENSP00000381050; ENSG00000015171.
DR Ensembl; ENST00000397962; ENSP00000381053; ENSG00000015171.
DR Ensembl; ENST00000509513; ENSP00000424205; ENSG00000015171.
DR Ensembl; ENST00000558098; ENSP00000452959; ENSG00000015171.
DR Ensembl; ENST00000563851; ENSP00000456634; ENSG00000260150.
DR Ensembl; ENST00000565311; ENSP00000457248; ENSG00000260150.
DR Ensembl; ENST00000602682; ENSP00000473321; ENSG00000015171.
DR GeneID; 10771; -.
DR KEGG; hsa:10771; -.
DR UCSC; uc010pzw.2; human.
DR CTD; 10771; -.
DR GeneCards; GC10P000170; -.
DR H-InvDB; HIX0025946; -.
DR HGNC; HGNC:16966; ZMYND11.
DR HPA; HPA015816; -.
DR HPA; HPA030553; -.
DR MIM; 608668; gene.
DR neXtProt; NX_Q15326; -.
DR PharmGKB; PA128394578; -.
DR eggNOG; NOG265768; -.
DR HOGENOM; HOG000038026; -.
DR HOVERGEN; HBG054949; -.
DR InParanoid; Q15326; -.
DR OMA; TSDGVCQ; -.
DR OrthoDB; EOG700875; -.
DR ChiTaRS; ZMYND11; human.
DR GeneWiki; ZMYND11; -.
DR GenomeRNAi; 10771; -.
DR NextBio; 40897; -.
DR PRO; PR:Q15326; -.
DR ArrayExpress; Q15326; -.
DR Bgee; Q15326; -.
DR CleanEx; HS_ZMYND11; -.
DR Genevestigator; Q15326; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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 cascade; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
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 SMART; SM00184; RING; 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 Alternative splicing; Bromodomain; Cell cycle; Chromatin regulator;
KW Chromosome; Complete proteome; DNA-binding; Host-virus interaction;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1 602 Zinc finger MYND domain-containing
FT protein 11.
FT /FTId=PRO_0000211218.
FT DOMAIN 168 238 Bromo.
FT DOMAIN 280 331 PWWP.
FT ZN_FING 100 148 PHD-type.
FT ZN_FING 563 598 MYND-type.
FT REGION 452 572 Interaction with human adenovirus E1A.
FT MOTIF 394 400 Nuclear localization signal (Potential).
FT MOD_RES 421 421 Phosphoserine.
FT VAR_SEQ 93 146 Missing (in isoform 2, isoform 4 and
FT isoform 5).
FT /FTId=VSP_044482.
FT VAR_SEQ 173 203 Missing (in isoform 5).
FT /FTId=VSP_046246.
FT VAR_SEQ 233 233 Missing (in isoform 6).
FT /FTId=VSP_047209.
FT VAR_SEQ 563 602 CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
FT -> VNTSLF (in isoform 3, isoform 4 and
FT isoform 6).
FT /FTId=VSP_044483.
FT MUTAGEN 563 563 C->S: Abrogates binding to EZH2.
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
//
ID ZMY11_HUMAN Reviewed; 602 AA.
AC Q15326; B2R6G8; B7Z293; F6UH50; Q2LD45; Q2LD46; Q2LD47; Q2LD48;
read moreAC Q5VUI1; Q8N4B3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Zinc finger MYND domain-containing protein 11;
DE AltName: Full=Adenovirus 5 E1A-binding protein;
DE AltName: Full=Protein BS69;
GN Name=ZMYND11; Synonyms=BS69;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RX PubMed=7621829;
RA Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M.,
RA Sonntag-Buck V., 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
RP SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION,
RP UBIQUITINATION, INTERACTION WITH E2F6 AND EZH2, AND MUTAGENESIS OF
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT transcription through recruitment of N-CoR.";
RL Oncogene 19:1538-1546(2000).
RN [8]
RP INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, AND INTERACTION
RP WITH 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
RT proteins through a common PXLXP motif.";
RL J. Biol. Chem. 277:4906-4910(2002).
RN [9]
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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP SPECTROMETRY.
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 [11]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Corepressor of transcription (Probable). May be involved
CC in chromatin remodeling through association with several
CC remodeling factors.
CC -!- SUBUNIT: Interacts (via MYND-type zinc finger) with NCOR1.
CC Interacts (via MYND-type zinc finger) with human adenovirus early
CC E1A protein (via PXLXP motif); this interaction inhibits E1A
CC mediated transactivation. Interacts (via MYND-type zinc finger)
CC with Epstein-Barr virus EBNA2 protein (via PXLXP motif). Interacts
CC (via MYND-type zinc finger) with EZH2. Interacts with E2F6.
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. Chromosome. Note=Associates with
CC chromatin and mitotic chromosomes.
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 Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q15326-6; Sequence=VSP_047209, VSP_044483;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC -!- SIMILARITY: Contains 1 bromo domain.
CC -!- SIMILARITY: Contains 1 MYND-type zinc finger.
CC -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC -!- SIMILARITY: Contains 1 PWWP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34784.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAG35465.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA60052.1; Type=Frameshift; Positions=11, 39;
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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; CAH69845.1; -; Genomic_DNA.
DR EMBL; AL603831; CAH69845.1; JOINED; Genomic_DNA.
DR EMBL; AL603831; CAI40899.1; -; Genomic_DNA.
DR EMBL; AL589988; CAI40899.1; JOINED; 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 PIR; S56145; S56145.
DR RefSeq; NP_001189393.1; NM_001202464.1.
DR RefSeq; NP_001189394.1; NM_001202465.1.
DR RefSeq; NP_001189396.1; NM_001202467.1.
DR RefSeq; NP_001189397.1; NM_001202468.1.
DR RefSeq; NP_006615.2; NM_006624.5.
DR RefSeq; NP_997644.2; NM_212479.3.
DR RefSeq; XP_005252416.1; XM_005252359.1.
DR RefSeq; XP_005252418.1; XM_005252361.1.
DR RefSeq; XP_005252419.1; XM_005252362.1.
DR UniGene; Hs.292265; -.
DR UniGene; Hs.740145; -.
DR ProteinModelPortal; Q15326; -.
DR SMR; Q15326; 95-239.
DR IntAct; Q15326; 19.
DR MINT; MINT-156360; -.
DR STRING; 9606.ENSP00000309992; -.
DR PhosphoSite; Q15326; -.
DR DMDM; 10719919; -.
DR PaxDb; Q15326; -.
DR PRIDE; Q15326; -.
DR DNASU; 10771; -.
DR Ensembl; ENST00000309776; ENSP00000309992; ENSG00000015171.
DR Ensembl; ENST00000381591; ENSP00000371003; ENSG00000015171.
DR Ensembl; ENST00000381604; ENSP00000371017; ENSG00000015171.
DR Ensembl; ENST00000397959; ENSP00000381050; ENSG00000015171.
DR Ensembl; ENST00000397962; ENSP00000381053; ENSG00000015171.
DR Ensembl; ENST00000509513; ENSP00000424205; ENSG00000015171.
DR Ensembl; ENST00000558098; ENSP00000452959; ENSG00000015171.
DR Ensembl; ENST00000563851; ENSP00000456634; ENSG00000260150.
DR Ensembl; ENST00000565311; ENSP00000457248; ENSG00000260150.
DR Ensembl; ENST00000602682; ENSP00000473321; ENSG00000015171.
DR GeneID; 10771; -.
DR KEGG; hsa:10771; -.
DR UCSC; uc010pzw.2; human.
DR CTD; 10771; -.
DR GeneCards; GC10P000170; -.
DR H-InvDB; HIX0025946; -.
DR HGNC; HGNC:16966; ZMYND11.
DR HPA; HPA015816; -.
DR HPA; HPA030553; -.
DR MIM; 608668; gene.
DR neXtProt; NX_Q15326; -.
DR PharmGKB; PA128394578; -.
DR eggNOG; NOG265768; -.
DR HOGENOM; HOG000038026; -.
DR HOVERGEN; HBG054949; -.
DR InParanoid; Q15326; -.
DR OMA; TSDGVCQ; -.
DR OrthoDB; EOG700875; -.
DR ChiTaRS; ZMYND11; human.
DR GeneWiki; ZMYND11; -.
DR GenomeRNAi; 10771; -.
DR NextBio; 40897; -.
DR PRO; PR:Q15326; -.
DR ArrayExpress; Q15326; -.
DR Bgee; Q15326; -.
DR CleanEx; HS_ZMYND11; -.
DR Genevestigator; Q15326; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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 cascade; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
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 SMART; SM00184; RING; 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 Alternative splicing; Bromodomain; Cell cycle; Chromatin regulator;
KW Chromosome; Complete proteome; DNA-binding; Host-virus interaction;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1 602 Zinc finger MYND domain-containing
FT protein 11.
FT /FTId=PRO_0000211218.
FT DOMAIN 168 238 Bromo.
FT DOMAIN 280 331 PWWP.
FT ZN_FING 100 148 PHD-type.
FT ZN_FING 563 598 MYND-type.
FT REGION 452 572 Interaction with human adenovirus E1A.
FT MOTIF 394 400 Nuclear localization signal (Potential).
FT MOD_RES 421 421 Phosphoserine.
FT VAR_SEQ 93 146 Missing (in isoform 2, isoform 4 and
FT isoform 5).
FT /FTId=VSP_044482.
FT VAR_SEQ 173 203 Missing (in isoform 5).
FT /FTId=VSP_046246.
FT VAR_SEQ 233 233 Missing (in isoform 6).
FT /FTId=VSP_047209.
FT VAR_SEQ 563 602 CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
FT -> VNTSLF (in isoform 3, isoform 4 and
FT isoform 6).
FT /FTId=VSP_044483.
FT MUTAGEN 563 563 C->S: Abrogates binding to EZH2.
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
//
MIM
608668
*RECORD*
*FIELD* NO
608668
*FIELD* TI
*608668 ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 11; ZMYND11
;;BS69
BONE MORPHOGENETIC PROTEIN RECEPTOR-ASSOCIATED MOLECULE 1, INCLUDED;
read moreBRAM1, INCLUDED
*FIELD* TX
CLONING
Using adenovirus E1A as bait in a yeast 2-hybrid screen of a 16-day
whole mouse embryo cDNA library, followed by screening a human colon
carcinoma cDNA library, Hateboer et al. (1995) cloned ZMYND11, which
they called BS69. The deduced 562-amino acid protein had an apparent
molecular mass of about 69 kD following in vitro transcription and
translation. BS69 contains 2 N-terminal zinc finger motifs, followed by
a nuclear localization signal and a C-terminal E1A-binding domain.
Northern blot analysis detected a 4.7-kb transcript in all mouse tissues
examined, with highest expression in kidney.
Using the transmembrane and cytoplasmic domains of mouse Bmpr1a (601299)
as bait in a yeast 2-hybrid screen of a human placenta cDNA library,
followed by screening a kidney cDNA library and 5-prime RACE, Kurozumi
et al. (1998) cloned a splice variant of BS69 that they designated
BRAM1. The deduced BRAM1 protein contains the C-terminal 186 amino acids
of BS69 preceded by 12 amino acids unique to BRAM1. Northern blot
analysis detected variable expression of 4.4-kb and 1.3-kb transcripts
in all tissues examined. Following transfection in mouse fibroblasts,
BRAM1 localized to the cytoplasm, whereas BS69 localized to the nucleus.
Masselink and Bernards (2000) noted that BS69 contains 3 motifs involved
in transcription regulation: a PHD finger and bromodomain in its
N-terminal half, and a MYND domain at its extreme C terminus. The MYND
domain, which is also present in the BRAM1 variant, is a 2-zinc finger
motif first identified in Drosophila Deaf1 (602635) and human MTG8
(133435).
GENE FUNCTION
By coimmunoprecipitation, Hateboer et al. (1995) confirmed direct
interaction between BS69 and the 289-amino acid isoform of E1A (289R)
following cotransfection in a human cell line; BS69 did not interact
with the shorter 243R E1A isoform. Endogenous BS69 complexed with E1A in
adenovirus-transformed human embryonic kidney cells. C-terminal deletion
mutants of BS69 failed to interact with E1A. BS69 inhibited
transactivation mediated by the 289R E1A protein, but not the 243R E1A
protein. BS69 also suppressed E1A-stimulated transcription of retinoic
acid receptor (see 180240) in COS cells.
Kurozumi et al. (1998) determined that BRAM1 interacts specifically with
the kinase domain of BMPR1A. BS69 did not interact with BMPR1A,
suggesting that the N terminus of BS69 interferes with this interaction.
Further investigation indicated that BRAM1 also interacts with TAB1
(602615). Kurozumi et al. (1998) hypothesized that a ternary complex of
MBPR1A, TAB1, and BRAM1 may be involved in BMP-TAB1-TAK1 (601426)
signaling.
Masselink and Bernards (2000) determined that full transcriptional
repression by BS69 requires the MYND domain. BS69 and BRAM1 interacted
with NCOR (600849) through the MYND domain, but BRAM1 was unable to
repress transcription, indicating that NCOR interaction is necessary but
not sufficient for BS69 repression. Expression of E1A inhibited
repression mediated by BS69.
Ansieau and Leutz (2002) showed that the MYND domain of BS69 interacts
with a conserved PxLxP motif in E1A, the Epstein-Barr virus oncoprotein
EBNA2, and a MYC (190080)-related cellular protein, MGA. The viral
proteins competed with MGA for BS69 binding in a PxLxP-dependent
fashion.
MAPPING
By FISH, Masselink and Bernards (2000) mapped the ZMYND11 gene to
chromosome 10p14.
*FIELD* RF
1. 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.
2. 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.
3. Kurozumi, K.; Nishita, M.; Yamaguchi, K.; Fujita, T.; Ueno, N.;
Shibuya, H.: BRAM1, a BMP receptor-associated molecule involved in
BMP signalling. Genes Cells 3: 257-264, 1998.
4. 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.
*FIELD* CD
Patricia A. Hartz: 5/19/2004
*FIELD* ED
carol: 05/19/2004
mgross: 5/19/2004
*RECORD*
*FIELD* NO
608668
*FIELD* TI
*608668 ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 11; ZMYND11
;;BS69
BONE MORPHOGENETIC PROTEIN RECEPTOR-ASSOCIATED MOLECULE 1, INCLUDED;
read moreBRAM1, INCLUDED
*FIELD* TX
CLONING
Using adenovirus E1A as bait in a yeast 2-hybrid screen of a 16-day
whole mouse embryo cDNA library, followed by screening a human colon
carcinoma cDNA library, Hateboer et al. (1995) cloned ZMYND11, which
they called BS69. The deduced 562-amino acid protein had an apparent
molecular mass of about 69 kD following in vitro transcription and
translation. BS69 contains 2 N-terminal zinc finger motifs, followed by
a nuclear localization signal and a C-terminal E1A-binding domain.
Northern blot analysis detected a 4.7-kb transcript in all mouse tissues
examined, with highest expression in kidney.
Using the transmembrane and cytoplasmic domains of mouse Bmpr1a (601299)
as bait in a yeast 2-hybrid screen of a human placenta cDNA library,
followed by screening a kidney cDNA library and 5-prime RACE, Kurozumi
et al. (1998) cloned a splice variant of BS69 that they designated
BRAM1. The deduced BRAM1 protein contains the C-terminal 186 amino acids
of BS69 preceded by 12 amino acids unique to BRAM1. Northern blot
analysis detected variable expression of 4.4-kb and 1.3-kb transcripts
in all tissues examined. Following transfection in mouse fibroblasts,
BRAM1 localized to the cytoplasm, whereas BS69 localized to the nucleus.
Masselink and Bernards (2000) noted that BS69 contains 3 motifs involved
in transcription regulation: a PHD finger and bromodomain in its
N-terminal half, and a MYND domain at its extreme C terminus. The MYND
domain, which is also present in the BRAM1 variant, is a 2-zinc finger
motif first identified in Drosophila Deaf1 (602635) and human MTG8
(133435).
GENE FUNCTION
By coimmunoprecipitation, Hateboer et al. (1995) confirmed direct
interaction between BS69 and the 289-amino acid isoform of E1A (289R)
following cotransfection in a human cell line; BS69 did not interact
with the shorter 243R E1A isoform. Endogenous BS69 complexed with E1A in
adenovirus-transformed human embryonic kidney cells. C-terminal deletion
mutants of BS69 failed to interact with E1A. BS69 inhibited
transactivation mediated by the 289R E1A protein, but not the 243R E1A
protein. BS69 also suppressed E1A-stimulated transcription of retinoic
acid receptor (see 180240) in COS cells.
Kurozumi et al. (1998) determined that BRAM1 interacts specifically with
the kinase domain of BMPR1A. BS69 did not interact with BMPR1A,
suggesting that the N terminus of BS69 interferes with this interaction.
Further investigation indicated that BRAM1 also interacts with TAB1
(602615). Kurozumi et al. (1998) hypothesized that a ternary complex of
MBPR1A, TAB1, and BRAM1 may be involved in BMP-TAB1-TAK1 (601426)
signaling.
Masselink and Bernards (2000) determined that full transcriptional
repression by BS69 requires the MYND domain. BS69 and BRAM1 interacted
with NCOR (600849) through the MYND domain, but BRAM1 was unable to
repress transcription, indicating that NCOR interaction is necessary but
not sufficient for BS69 repression. Expression of E1A inhibited
repression mediated by BS69.
Ansieau and Leutz (2002) showed that the MYND domain of BS69 interacts
with a conserved PxLxP motif in E1A, the Epstein-Barr virus oncoprotein
EBNA2, and a MYC (190080)-related cellular protein, MGA. The viral
proteins competed with MGA for BS69 binding in a PxLxP-dependent
fashion.
MAPPING
By FISH, Masselink and Bernards (2000) mapped the ZMYND11 gene to
chromosome 10p14.
*FIELD* RF
1. 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.
2. 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.
3. Kurozumi, K.; Nishita, M.; Yamaguchi, K.; Fujita, T.; Ueno, N.;
Shibuya, H.: BRAM1, a BMP receptor-associated molecule involved in
BMP signalling. Genes Cells 3: 257-264, 1998.
4. 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.
*FIELD* CD
Patricia A. Hartz: 5/19/2004
*FIELD* ED
carol: 05/19/2004
mgross: 5/19/2004