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Q15326 (ZMY11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger MYND domain-containing protein 11
Alternative name(s):
Adenovirus 5 E1A-binding protein
Bone morphogenetic protein receptor-associated molecule 1
Protein BS69
Gene names
Name:ZMYND11
Synonyms:BRAM1, BS69
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth. Ref.2 Ref.7

Subunit structure

Homooligomer; forms homooligomers via its C-terminus. Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3). Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND-type zinc finger) with MGA protein (via PXLXP motif). Interacts (via MYND-type zinc finger) with EZH2. Interacts with C11orf30/EMSY and E2F6. Interacts with PIAS1 and UBE2I. Interacts (via MYND-type zinc finger) with human adenovirus early E1A protein (via PXLXP motif); this interaction inhibits E1A mediated transactivation. Interacts (via MYND-type zinc finger) with Epstein-Barr virus EBNA2 protein (via PXLXP motif). Interacts with Epstein-Barr virus-derived protein LMP1; leading to negatively regulate NF-kappa-B activation by Epstein-Barr virus-derived protein LMP1. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.19

Subcellular location

Nucleus. Chromosome. Note: Associates with chromatin and mitotic chromosomes. Ref.2 Ref.15

Tissue specificity

Ubiquitous. Ref.2

Induction

Down-regulated in breast cancer patients with poor prognosis. Ref.20

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 By similarity.

Post-translational modification

Sumoylated following its interaction with PIAS1 and UBE2I. Ref.15

Ubiquitinated, leading to proteasomal degradation. Ref.2

Involvement in disease

A chromosomal aberration involving ZMYND11 is a cause of acute poorly differentiated myeloid leukemia. Translocation (10;17)(p15;q21) with MBTD1.

Sequence similarities

Contains 1 bromo domain.

Contains 1 MYND-type zinc finger.

Contains 1 PHD-type zinc finger.

Contains 1 PWWP domain.

Sequence caution

The sequence AAH34784.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG35465.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA60052.1 differs from that shown. Reason: Frameshift at positions 11 and 39.

Ontologies

Keywords
   Biological processCell cycle
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseTumor suppressor
   DomainBromodomain
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 20732415. Source: UniProtKB

negative regulation of JNK cascade

Inferred from mutant phenotype PubMed 20732415. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 20732415. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription elongation from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylated histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.8Ref.14Ref.16PubMed 20732415. Source: IntAct

transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P032553EBI-2623509,EBI-2603114From a different organism.
EBNA2P129782EBI-2623509,EBI-8052923From a different organism.
LMP1P032303EBI-2623509,EBI-6973030From a different organism.
LTBRP369415EBI-2623509,EBI-3509981
TRAF3Q131142EBI-2623509,EBI-357631

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15326-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15326-2)

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
Isoform 3 (identifier: Q15326-3)

The sequence of this isoform differs from the canonical sequence as follows:
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF
Isoform 4 (identifier: Q15326-4)

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF
Isoform 5 (identifier: Q15326-5)

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     173-203: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q15326-6)

The sequence of this isoform differs from the canonical sequence as follows:
     233-233: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602Zinc finger MYND domain-containing protein 11
PRO_0000211218

Regions

Domain168 – 23871Bromo
Domain280 – 33152PWWP
Zinc finger100 – 14849PHD-type
Zinc finger563 – 59836MYND-type
Region452 – 572121Interaction with human adenovirus E1A
Motif394 – 4007Nuclear localization signal Potential

Sites

Metal binding2581Zinc By similarity
Metal binding2611Zinc By similarity
Metal binding2771Zinc By similarity
Metal binding2811Zinc; via tele nitrogen By similarity

Amino acid modifications

Modified residue4211Phosphoserine Ref.13

Natural variations

Alternative sequence93 – 14654Missing in isoform 2, isoform 4 and isoform 5.
VSP_044482
Alternative sequence173 – 20331Missing in isoform 5.
VSP_046246
Alternative sequence2331Missing in isoform 6.
VSP_047209
Alternative sequence563 – 60240CYNCE…CRRKR → VNTSLF in isoform 3, isoform 4 and isoform 6.
VSP_044483

Experimental info

Mutagenesis5621W → Y: Reduced interaction with PXLXP ligand MGA without affecting interaction with viral human adenovirus early E1A protein. Ref.19
Mutagenesis5631C → S: Abrogates binding to EZH2. Ref.2
Mutagenesis567 – 5682EE → KK: Reduced interaction with PXLXP ligand proteins.
Mutagenesis599 – 6024RRKR → GGGG: Abolished interaction with PXLXP ligand proteins. Ref.19

Secondary structure

........................... 602
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2012. Version 2.
Checksum: 3AD525B90574BDE8

FASTA60270,963
        10         20         30         40         50         60 
MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 

        70         80         90        100        110        120 
KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD WYCFECHLPG EVLICDLCFR 

       130        140        150        160        170        180 
VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG 

       190        200        210        220        230        240 
KDNKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI 

       250        260        270        280        290        300 
ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ 

       310        320        330        340        350        360 
KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL ELHQRFLREG 

       370        380        390        400        410        420 
RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS 

       430        440        450        460        470        480 
SQEIPTMPQP IEKVSVSTQT KKLSASSPRM LHRSTQTTND GVCQSMCHDK YTKIFNDFKD 

       490        500        510        520        530        540 
RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV 

       550        560        570        580        590        600 
EEIKKLATQH KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR 


KR 

« Hide

Isoform 2 [UniParc].

Checksum: 5EDF3D170E2EDD11
Show »

FASTA54864,426
Isoform 3 [UniParc].

Checksum: 597E186F867E225B
Show »

FASTA56866,590
Isoform 4 [UniParc].

Checksum: C20F5B606BAB0E2E
Show »

FASTA51460,053
Isoform 5 [UniParc].

Checksum: E8EA00DD12FA4FF8
Show »

FASTA51760,869
Isoform 6 [UniParc].

Checksum: 86FC85955F1022E5
Show »

FASTA56766,519

References

« Hide 'large scale' references
[1]"BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation."
Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M., Sonntag-Buck V., Stunnenberg H.G., Bernards R.
EMBO J. 14:3159-3169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon carcinoma.
[2]"New insights into BS69 functions."
Velasco G., Grkovic S., Ansieau S.
J. Biol. Chem. 281:16546-16550(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, UBIQUITINATION, INTERACTION WITH E2F6 AND EZH2, MUTAGENESIS OF CYS-563.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
Tissue: Amygdala and Brain.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
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. expand/collapse author list , 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.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Brain.
[7]"The adenovirus E1A binding protein BS69 is a corepressor of transcription through recruitment of N-CoR."
Masselink H., Bernards R.
Oncogene 19:1538-1546(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NCOR1.
[8]"The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif."
Ansieau S., Leutz A.
J. Biol. Chem. 277:4906-4910(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2 PROTEIN.
[9]"Negative regulation of Epstein-Barr virus latent membrane protein 1-mediated functions by the bone morphogenetic protein receptor IA-binding protein, BRAM1."
Chung P.J., Chang Y.S., Liang C.L., Meng C.L.
J. Biol. Chem. 277:39850-39857(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
[10]"Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69."
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.
EMBO Rep. 6:675-680(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C11ORF30.
[11]"BS69, a specific adaptor in the latent membrane protein 1-mediated c-Jun N-terminal kinase pathway."
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.
Mol. Cell. Biol. 26:448-456(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"BS69 negatively regulates the canonical NF-kappaB activation induced by Epstein-Barr virus-derived LMP1."
Ikeda O., Sekine Y., Mizushima A., Oritani K., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.
FEBS Lett. 583:1567-1574(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
[15]"BS69 undergoes SUMO modification and plays an inhibitory role in muscle and neuronal differentiation."
Yu B., Shao Y., Zhang C., Chen Y., Zhong Q., Zhang J., Yang H., Zhang W., Wan J.
Exp. Cell Res. 315:3543-3553(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUMOYLATION, INTERACTION WITH PIAS1 AND UBE2I.
[16]"BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-derived LMP1/CTAR1-induced NF-kappaB activation."
Ikeda O., Miyasaka Y., Yoshida R., Mizushima A., Oritani K., Sekine Y., Kuroda M., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.
FEBS Lett. 584:865-872(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Recurrent translocation (10;17)(p15;q21) in acute poorly differentiated myeloid leukemia likely results in ZMYND11-MBTD1 fusion."
De Braekeleer E., Auffret R., Douet-Guilbert N., Basinko A., Le Bris M.J., Morel F., De Braekeleer M.
Leuk. Lymphoma 55:1189-1190(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH MBTD1.
[19]"Structural and functional analysis of the DEAF-1 and BS69 MYND domains."
Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M., Franzmann T.M., Buchner J., Ansieau S., Sattler M.
PLoS ONE 8:E54715-E54715(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2 PROTEIN, INTERACTION WITH MGA, MUTAGENESIS OF TRP-562; 567-GLU-GLU-568 AND 599-ARG--ARG-602.
[20]"ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression."
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.
Nature 508:263-268(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86098 mRNA. Translation: CAA60052.1. Frameshift.
DQ335452 mRNA. Translation: ABC72408.1.
DQ335453 mRNA. Translation: ABC72409.1.
DQ335454 mRNA. Translation: ABC72410.1.
DQ335455 mRNA. Translation: ABC72411.1.
AK294469 mRNA. Translation: BAH11779.1.
AK312570 mRNA. Translation: BAG35465.1. Different initiation.
AL589988, AL603831 Genomic DNA. Translation: CAH69845.1.
AL603831, AL589988 Genomic DNA. Translation: CAI40899.1.
AL713922 Genomic DNA. No translation available.
AL731539 Genomic DNA. No translation available.
CH471072 Genomic DNA. Translation: EAW86539.1.
CH471072 Genomic DNA. Translation: EAW86540.1.
CH471072 Genomic DNA. Translation: EAW86541.1.
BC034784 mRNA. Translation: AAH34784.1. Different initiation.
CCDSCCDS55696.1. [Q15326-3]
CCDS55697.1. [Q15326-5]
CCDS7052.2. [Q15326-1]
CCDS7053.2. [Q15326-6]
PIRS56145.
RefSeqNP_001189393.1. NM_001202464.1. [Q15326-2]
NP_001189394.1. NM_001202465.1. [Q15326-5]
NP_001189396.1. NM_001202467.1. [Q15326-4]
NP_001189397.1. NM_001202468.1. [Q15326-3]
NP_006615.2. NM_006624.5. [Q15326-1]
NP_997644.2. NM_212479.3. [Q15326-6]
XP_005252416.1. XM_005252359.2. [Q15326-1]
XP_005252418.1. XM_005252361.1. [Q15326-2]
XP_005252419.1. XM_005252362.1. [Q15326-2]
XP_006717439.1. XM_006717376.1. [Q15326-2]
UniGeneHs.292265.
Hs.740145.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4NS5X-ray1.90A154-371[»]
ProteinModelPortalQ15326.
SMRQ15326. Positions 99-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115989. 33 interactions.
IntActQ15326. 19 interactions.
MINTMINT-156360.
STRING9606.ENSP00000309992.

PTM databases

PhosphoSiteQ15326.

Polymorphism databases

DMDM425906058.

Proteomic databases

MaxQBQ15326.
PaxDbQ15326.
PRIDEQ15326.

Protocols and materials databases

DNASU10771.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309776; ENSP00000309992; ENSG00000015171.
ENST00000381591; ENSP00000371003; ENSG00000015171. [Q15326-1]
ENST00000381604; ENSP00000371017; ENSG00000015171.
ENST00000397959; ENSP00000381050; ENSG00000015171. [Q15326-5]
ENST00000397962; ENSP00000381053; ENSG00000015171. [Q15326-1]
ENST00000509513; ENSP00000424205; ENSG00000015171. [Q15326-6]
ENST00000558098; ENSP00000452959; ENSG00000015171. [Q15326-3]
ENST00000563851; ENSP00000456634; ENSG00000260150. [Q15326-6]
ENST00000565311; ENSP00000457248; ENSG00000260150. [Q15326-1]
ENST00000602682; ENSP00000473321; ENSG00000015171. [Q15326-5]
GeneID10771.
KEGGhsa:10771.
UCSCuc001ifm.3. human. [Q15326-2]
uc001ifn.3. human. [Q15326-4]
uc010pzu.2. human. [Q15326-1]
uc010pzw.2. human.
uc010pzx.2. human. [Q15326-3]

Organism-specific databases

CTD10771.
GeneCardsGC10P000170.
H-InvDBHIX0025946.
HGNCHGNC:16966. ZMYND11.
HPAHPA015816.
HPA030553.
MIM608668. gene.
neXtProtNX_Q15326.
PharmGKBPA128394578.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265768.
HOGENOMHOG000038026.
HOVERGENHBG054949.
InParanoidQ15326.
OMATSDGVCQ.
OrthoDBEOG700875.
PhylomeDBQ15326.
TreeFamTF106407.

Gene expression databases

ArrayExpressQ15326.
BgeeQ15326.
CleanExHS_ZMYND11.
GenevestigatorQ15326.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR000313. PWWP_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR002893. Znf_MYND.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTSM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00293. PWWP. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS50014. BROMODOMAIN_2. 1 hit.
PS50812. PWWP. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZMYND11. human.
GeneWikiZMYND11.
GenomeRNAi10771.
NextBio40897.
PROQ15326.
SOURCESearch...

Entry information

Entry nameZMY11_HUMAN
AccessionPrimary (citable) accession number: Q15326
Secondary accession number(s): B2R6G8 expand/collapse secondary AC list , B7Z293, F6UH50, Q2LD45, Q2LD46, Q2LD47, Q2LD48, Q5VUI1, Q8N4B3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 28, 2012
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM