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Q15326

- ZMY11_HUMAN

UniProt

Q15326 - ZMY11_HUMAN

Protein

Zinc finger MYND domain-containing protein 11

Gene

ZMYND11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (28 Nov 2012)
      Previous versions | rss
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    Functioni

    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.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi258 – 2581ZincBy similarity
    Metal bindingi261 – 2611ZincBy similarity
    Metal bindingi277 – 2771ZincBy similarity
    Metal bindingi281 – 2811Zinc; via tele nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri100 – 14849PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri563 – 59836MYND-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. methylated histone binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. transcription corepressor activity Source: UniProtKB
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell proliferation Source: ProtInc
    3. chromatin modification Source: UniProtKB-KW
    4. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    5. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    6. negative regulation of JNK cascade Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    8. regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW
    10. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Cell cycle, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ZMYND11
    Synonyms:BRAM1, BS69
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:16966. ZMYND11.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Associates with chromatin and mitotic chromosomes.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi562 – 5621W → Y: Reduced interaction with PXLXP ligand MGA without affecting interaction with viral human adenovirus early E1A protein. 1 Publication
    Mutagenesisi563 – 5631C → S: Abrogates binding to EZH2. 1 Publication
    Mutagenesisi567 – 5682EE → KK: Reduced interaction with PXLXP ligand proteins.
    Mutagenesisi599 – 6024RRKR → GGGG: Abolished interaction with PXLXP ligand proteins.

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA128394578.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 602602Zinc finger MYND domain-containing protein 11PRO_0000211218Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei421 – 4211Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated following its interaction with PIAS1 and UBE2I.1 Publication
    Ubiquitinated, leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15326.
    PaxDbiQ15326.
    PRIDEiQ15326.

    PTM databases

    PhosphoSiteiQ15326.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    Down-regulated in breast cancer patients with poor prognosis.1 Publication

    Gene expression databases

    ArrayExpressiQ15326.
    BgeeiQ15326.
    CleanExiHS_ZMYND11.
    GenevestigatoriQ15326.

    Organism-specific databases

    HPAiHPA015816.
    HPA030553.

    Interactioni

    Subunit structurei

    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 LMP1.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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

    Protein-protein interaction databases

    BioGridi115989. 33 interactions.
    IntActiQ15326. 19 interactions.
    MINTiMINT-156360.
    STRINGi9606.ENSP00000309992.

    Structurei

    Secondary structure

    1
    602
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi157 – 16913
    Helixi198 – 2069
    Helixi213 – 23119
    Helixi236 – 25722
    Helixi259 – 2679
    Helixi272 – 2743
    Beta strandi283 – 2875
    Beta strandi293 – 30210
    Beta strandi305 – 3106
    Beta strandi317 – 3215
    Helixi322 – 3243
    Beta strandi325 – 3273
    Helixi332 – 3343
    Helixi341 – 35919

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NS5X-ray1.90A154-371[»]
    ProteinModelPortaliQ15326.
    SMRiQ15326. Positions 99-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 23871BromoPROSITE-ProRule annotationAdd
    BLAST
    Domaini280 – 33152PWWPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni452 – 572121Interaction with human adenovirus E1AAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi394 – 4007Nuclear localization signalSequence Analysis

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PWWP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri100 – 14849PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri563 – 59836MYND-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG265768.
    HOGENOMiHOG000038026.
    HOVERGENiHBG054949.
    InParanoidiQ15326.
    OMAiTSDGVCQ.
    OrthoDBiEOG700875.
    PhylomeDBiQ15326.
    TreeFamiTF106407.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR001487. 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]
    PfamiPF00439. Bromodomain. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view]
    SMARTiSM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00293. PWWP. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS50014. 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]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15326-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK    50
    ETTRQLSLAV KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD 100
    WYCFECHLPG EVLICDLCFR VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK 150
    KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG KDNKHPMYRR LVHSAVDVPT 200
    IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI ARMLYKDTCH 250
    ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ 300
    KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL 350
    ELHQRFLREG RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR 400
    NQSVEPKKEE PEPETEAVSS SQEIPTMPQP IEKVSVSTQT KKLSASSPRM 450
    LHRSTQTTND GVCQSMCHDK YTKIFNDFKD RMKSDHKRET ERVVREALEK 500
    LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV EEIKKLATQH 550
    KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR 600
    KR 602
    Length:602
    Mass (Da):70,963
    Last modified:November 28, 2012 - v2
    Checksum:i3AD525B90574BDE8
    GO
    Isoform 2 (identifier: Q15326-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-146: Missing.

    Show »
    Length:548
    Mass (Da):64,426
    Checksum:i5EDF3D170E2EDD11
    GO
    Isoform 3 (identifier: Q15326-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

    Show »
    Length:568
    Mass (Da):66,590
    Checksum:i597E186F867E225B
    GO
    Isoform 4 (identifier: Q15326-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-146: Missing.
         563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

    Show »
    Length:514
    Mass (Da):60,053
    Checksum:iC20F5B606BAB0E2E
    GO
    Isoform 5 (identifier: Q15326-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-146: Missing.
         173-203: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:517
    Mass (Da):60,869
    Checksum:iE8EA00DD12FA4FF8
    GO
    Isoform 6 (identifier: Q15326-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         233-233: Missing.
         563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

    Note: No experimental confirmation available.

    Show »
    Length:567
    Mass (Da):66,519
    Checksum:i86FC85955F1022E5
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei93 – 14654Missing in isoform 2, isoform 4 and isoform 5. 2 PublicationsVSP_044482Add
    BLAST
    Alternative sequencei173 – 20331Missing in isoform 5. 1 PublicationVSP_046246Add
    BLAST
    Alternative sequencei233 – 2331Missing in isoform 6. 1 PublicationVSP_047209
    Alternative sequencei563 – 60240CYNCE…CRRKR → VNTSLF in isoform 3, isoform 4 and isoform 6. 2 PublicationsVSP_044483Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS55696.1. [Q15326-3]
    CCDS55697.1. [Q15326-5]
    CCDS7052.2. [Q15326-1]
    CCDS7053.2. [Q15326-6]
    PIRiS56145.
    RefSeqiNP_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]
    UniGeneiHs.292265.
    Hs.740145.

    Genome annotation databases

    EnsembliENST00000309776; 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]
    ENST00000602682; ENSP00000473321; ENSG00000015171. [Q15326-5]
    GeneIDi10771.
    KEGGihsa:10771.
    UCSCiuc001ifk.3. human.
    uc001ifm.3. human. [Q15326-2]
    uc001ifn.3. human. [Q15326-4]
    uc010pzu.2. human. [Q15326-1]
    uc010pzw.2. human.
    uc010pzx.2. human. [Q15326-3]

    Polymorphism databases

    DMDMi425906058.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS55696.1. [Q15326-3 ]
    CCDS55697.1. [Q15326-5 ]
    CCDS7052.2. [Q15326-1 ]
    CCDS7053.2. [Q15326-6 ]
    PIRi S56145.
    RefSeqi NP_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 ]
    UniGenei Hs.292265.
    Hs.740145.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NS5 X-ray 1.90 A 154-371 [» ]
    ProteinModelPortali Q15326.
    SMRi Q15326. Positions 99-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115989. 33 interactions.
    IntActi Q15326. 19 interactions.
    MINTi MINT-156360.
    STRINGi 9606.ENSP00000309992.

    PTM databases

    PhosphoSitei Q15326.

    Polymorphism databases

    DMDMi 425906058.

    Proteomic databases

    MaxQBi Q15326.
    PaxDbi Q15326.
    PRIDEi Q15326.

    Protocols and materials databases

    DNASUi 10771.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309776 ; 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 ]
    ENST00000602682 ; ENSP00000473321 ; ENSG00000015171 . [Q15326-5 ]
    GeneIDi 10771.
    KEGGi hsa:10771.
    UCSCi uc001ifk.3. human.
    uc001ifm.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

    CTDi 10771.
    GeneCardsi GC10P000170.
    H-InvDB HIX0025946.
    HGNCi HGNC:16966. ZMYND11.
    HPAi HPA015816.
    HPA030553.
    MIMi 608668. gene.
    neXtProti NX_Q15326.
    PharmGKBi PA128394578.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265768.
    HOGENOMi HOG000038026.
    HOVERGENi HBG054949.
    InParanoidi Q15326.
    OMAi TSDGVCQ.
    OrthoDBi EOG700875.
    PhylomeDBi Q15326.
    TreeFami TF106407.

    Miscellaneous databases

    ChiTaRSi ZMYND11. human.
    GeneWikii ZMYND11.
    GenomeRNAii 10771.
    NextBioi 40897.
    PROi Q15326.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15326.
    Bgeei Q15326.
    CleanExi HS_ZMYND11.
    Genevestigatori Q15326.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR001487. 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 ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view ]
    SMARTi SM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00293. PWWP. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS50014. 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. 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. 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.

    Entry informationi

    Entry nameiZMY11_HUMAN
    AccessioniPrimary (citable) accession number: Q15326
    Secondary accession number(s): B2R6G8
    , B7Z293, F6UH50, Q2LD45, Q2LD46, Q2LD47, Q2LD48, Q5VUI1, Q8N4B3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3