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O75530

- EED_HUMAN

UniProt

O75530 - EED_HUMAN

Protein

Polycomb protein EED

Gene

EED

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.9 Publications

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. histone methyltransferase activity Source: MGI
    3. identical protein binding Source: IntAct
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: UniProtKB
    2. positive regulation of histone H3-K27 methylation Source: Ensembl
    3. regulation of gene expression by genetic imprinting Source: Ensembl
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    REACT_200808. PRC2 methylates histones and DNA.
    SignaLinkiO75530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polycomb protein EED
    Short name:
    hEED
    Alternative name(s):
    WD protein associating with integrin cytoplasmic tails 1
    Short name:
    WAIT-1
    Gene namesi
    Name:EED
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3188. EED.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Transiently colocalizes with XIST at inactive X chromosomes.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. ESC/E(Z) complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. pronucleus Source: Ensembl
    6. sex chromatin Source: Ensembl

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi97 – 971F → A: Abolishes binding to H3K27me3. 2 Publications
    Mutagenesisi148 – 1481Y → A: Abolishes binding to H3K27me3. 2 Publications
    Mutagenesisi193 – 1931I → N: Impairs interaction with EZH2. 2 Publications
    Mutagenesisi196 – 1961L → P: Impairs interaction with EZH2. 2 Publications
    Mutagenesisi300 – 3012ST → AA: Impairs interaction with the matrix protein MA of HIV-1. 1 Publication
    Mutagenesisi305 – 3084HRNY → AAAA: Impairs interaction with the matrix protein MA of HIV-1. 1 Publication
    Mutagenesisi364 – 3641W → A: Abolishes binding to H3K27me3. 2 Publications
    Mutagenesisi364 – 3641W → L: Abolishes binding to H3K27me3. 2 Publications
    Mutagenesisi365 – 3651Y → A: Abolishes binding to H3K27me3. 2 Publications

    Organism-specific databases

    PharmGKBiPA27624.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 441440Polycomb protein EEDPRO_0000343725Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei55 – 551Phosphothreonine1 Publication
    Modified residuei66 – 661N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei66 – 661N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei66 – 661N6-methyllysine; alternate1 Publication
    Modified residuei197 – 1971N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei197 – 1971N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei197 – 1971N6-methyllysine; alternate1 Publication
    Modified residuei268 – 2681N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei268 – 2681N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei268 – 2681N6-methyllysine; alternate1 Publication
    Modified residuei284 – 2841N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei284 – 2841N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei284 – 2841N6-methyllysine; alternate1 Publication

    Post-translational modificationi

    Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75530.
    PaxDbiO75530.
    PRIDEiO75530.

    PTM databases

    PhosphoSiteiO75530.

    Expressioni

    Tissue specificityi

    Expressed in brain, colon, heart, kidney, liver, lung, muscle, ovary, peripheral blood leukocytes, pancreas, placenta, prostate, spleen, small intestine, testis, thymus and uterus. Appears to be overexpressed in breast and colon cancer.5 Publications

    Developmental stagei

    Expression peaks at the G1/S phase boundary.1 Publication

    Inductioni

    Expression is induced by E2F1, E2F2 and E2F3.1 Publication

    Gene expression databases

    ArrayExpressiO75530.
    BgeeiO75530.
    CleanExiHS_EED.
    GenevestigatoriO75530.

    Organism-specific databases

    HPAiCAB012211.
    HPA046731.

    Interactioni

    Subunit structurei

    Interacts with KMT2A/MLL1 By similarity. Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2. The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit. Interacts with HDAC, HDAC2, histone H1 and YY1. May interact with ITGA4, ITGAE and ITGB7. Interacts with CDYL. May interact with the MA protein of HIV-1. Interacts with ARNTL/BMAL1.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-923794,EBI-923794
    ASXL1Q8IXJ95EBI-923794,EBI-1646500
    DDB1Q165314EBI-923794,EBI-350322
    DNMT1P263583EBI-923794,EBI-719459
    DNMT3AQ9Y6K12EBI-923794,EBI-923653
    DNMT3BQ9UBC34EBI-923794,EBI-80125
    EZH2Q159107EBI-923794,EBI-530054
    PINK1Q9BXM76EBI-923794,EBI-2846068
    PML-RARQ151562EBI-923794,EBI-867256

    Protein-protein interaction databases

    BioGridi114265. 460 interactions.
    DIPiDIP-36673N.
    IntActiO75530. 35 interactions.
    MINTiMINT-6630924.
    STRINGi9606.ENSP00000263360.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi83 – 897
    Beta strandi96 – 1016
    Beta strandi111 – 1177
    Beta strandi120 – 1267
    Helixi128 – 1303
    Beta strandi132 – 1398
    Beta strandi147 – 1548
    Turni156 – 1583
    Beta strandi161 – 1677
    Beta strandi171 – 1755
    Turni177 – 1793
    Beta strandi182 – 1887
    Beta strandi193 – 1986
    Beta strandi205 – 2106
    Beta strandi215 – 2195
    Turni220 – 2234
    Beta strandi224 – 2296
    Beta strandi231 – 2344
    Beta strandi239 – 2446
    Beta strandi248 – 2558
    Beta strandi260 – 2656
    Helixi268 – 27811
    Helixi282 – 2843
    Beta strandi292 – 2943
    Beta strandi298 – 3014
    Beta strandi311 – 3155
    Beta strandi318 – 3225
    Beta strandi324 – 33512
    Helixi340 – 3423
    Beta strandi350 – 3578
    Beta strandi374 – 3807
    Beta strandi386 – 3905
    Beta strandi393 – 3953
    Helixi396 – 3983
    Beta strandi400 – 4045
    Beta strandi413 – 4186
    Beta strandi422 – 4298
    Beta strandi432 – 4387

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IIWX-ray1.80A77-441[»]
    3IIYX-ray2.65A77-441[»]
    3IJ0X-ray2.45A77-441[»]
    3IJ1X-ray2.10A77-441[»]
    3IJCX-ray1.95A77-441[»]
    3JPXX-ray2.05A40-441[»]
    3JZGX-ray2.10A40-441[»]
    3JZHX-ray2.05A40-441[»]
    3JZNX-ray2.60A76-441[»]
    3K26X-ray1.58A76-441[»]
    3K27X-ray1.76A76-441[»]
    ProteinModelPortaliO75530.
    SMRiO75530. Positions 80-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75530.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati91 – 13444WD 1Add
    BLAST
    Repeati142 – 18544WD 2Add
    BLAST
    Repeati188 – 22841WD 3Add
    BLAST
    Repeati234 – 27542WD 4Add
    BLAST
    Repeati304 – 34138WD 5Add
    BLAST
    Repeati359 – 39941WD 6Add
    BLAST
    Repeati408 – 44134WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni81 – 441361Interaction with EZH2By similarityAdd
    BLAST
    Regioni149 – 303155Required for interaction with the matrix protein MA of HIV-1Add
    BLAST
    Regioni301 – 441141Required for interaction with the matrix protein MA of HIV-1Add
    BLAST

    Domaini

    The WD repeat domain mediates recognition of trimethylated histone peptides at the consensus sequence Ala-Arg-Lys-Ser. This is achieved through an aromatic cage encircling the methyllysine, and involving Phe-97, Tyr-148 and Tyr-365.1 Publication

    Sequence similaritiesi

    Belongs to the WD repeat ESC family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOVERGENiHBG052708.
    KOiK11462.
    OMAiCTTLTHP.
    OrthoDBiEOG7WQ7S8.
    PhylomeDBiO75530.
    TreeFamiTF314451.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 2 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. Align

    Note: Additional isoforms may be produced by alternative initiation, both from non-canonical start codons upstream of the initiator methionine displayed and from other canonical start codons downstream of that displayed (PubMed:15099518 and PubMed:15684044). The precise sites of translation initiation have not been unambiguously identified.

    Isoform 1 (identifier: O75530-1) [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

    MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT    50
    ERPDTPTNTP NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ 100
    FNWHSKEGDP LVFATVGSNR VTLYECHSQG EIRLLQSYVD ADADENFYTC 150
    AWTYDSNTSH PLLAVAGSRG IIRIINPITM QCIKHYVGHG NAINELKFHP 200
    RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL SADYDLLGEK 250
    IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS 300
    TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV 350
    TILGRFDYSQ CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK 400
    CTTLTHHKCG AAIRQTSFSR DSSILIAVCD DASIWRWDRL R 441
    Length:441
    Mass (Da):50,198
    Last modified:July 22, 2008 - v2
    Checksum:iD2E0A5BA27C0499A
    GO
    Isoform 2 (identifier: O75530-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         322-322: K → KSGRAILHSHQQCMRDPVSPNLRQHL

    Show »
    Length:466
    Mass (Da):53,061
    Checksum:i614B2E31B2A9D41F
    GO
    Isoform 3 (identifier: O75530-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-441: Missing.

    Show »
    Length:400
    Mass (Da):45,524
    Checksum:i45DD879776FF83D5
    GO

    Sequence cautioni

    The sequence AAC23685.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAC68675.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321D → E in AAC68675. (PubMed:9765275)Curated
    Sequence conflicti74 – 741K → S in AAD08714. (PubMed:9880543)Curated
    Sequence conflicti74 – 741K → S in AAD08815. (PubMed:9880543)Curated
    Sequence conflicti337 – 3371E → K in AAD08714. (PubMed:9880543)Curated
    Sequence conflicti337 – 3371E → K in AAD08815. (PubMed:9880543)Curated
    Sequence conflicti417 – 4171S → G in BAF84809. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei322 – 3221K → KSGRAILHSHQQCMRDPVSP NLRQHL in isoform 2. 1 PublicationVSP_034691
    Alternative sequencei401 – 44141Missing in isoform 3. 1 PublicationVSP_034692Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF080227 mRNA. Translation: AAC95144.1.
    AF070418 mRNA. Translation: AAC23685.1. Different initiation.
    U90651 mRNA. Translation: AAD08714.1.
    AF099032 mRNA. Translation: AAD08815.1.
    AK292120 mRNA. Translation: BAF84809.1.
    AP003084 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW75129.1.
    CH471076 Genomic DNA. Translation: EAW75130.1.
    BC047672 mRNA. Translation: AAH47672.1.
    BC068995 mRNA. Translation: AAH68995.1.
    AF078933 mRNA. Translation: AAC68675.1. Different initiation.
    CCDSiCCDS8273.1. [O75530-1]
    CCDS8274.1. [O75530-3]
    RefSeqiNP_003788.2. NM_003797.3. [O75530-1]
    NP_694536.1. NM_152991.2. [O75530-3]
    UniGeneiHs.503510.

    Genome annotation databases

    EnsembliENST00000263360; ENSP00000263360; ENSG00000074266. [O75530-1]
    ENST00000327320; ENSP00000315587; ENSG00000074266. [O75530-3]
    ENST00000351625; ENSP00000338186; ENSG00000074266. [O75530-2]
    GeneIDi8726.
    KEGGihsa:8726.
    UCSCiuc001pbp.3. human. [O75530-1]
    uc001pbr.3. human. [O75530-2]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF080227 mRNA. Translation: AAC95144.1 .
    AF070418 mRNA. Translation: AAC23685.1 . Different initiation.
    U90651 mRNA. Translation: AAD08714.1 .
    AF099032 mRNA. Translation: AAD08815.1 .
    AK292120 mRNA. Translation: BAF84809.1 .
    AP003084 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW75129.1 .
    CH471076 Genomic DNA. Translation: EAW75130.1 .
    BC047672 mRNA. Translation: AAH47672.1 .
    BC068995 mRNA. Translation: AAH68995.1 .
    AF078933 mRNA. Translation: AAC68675.1 . Different initiation.
    CCDSi CCDS8273.1. [O75530-1 ]
    CCDS8274.1. [O75530-3 ]
    RefSeqi NP_003788.2. NM_003797.3. [O75530-1 ]
    NP_694536.1. NM_152991.2. [O75530-3 ]
    UniGenei Hs.503510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IIW X-ray 1.80 A 77-441 [» ]
    3IIY X-ray 2.65 A 77-441 [» ]
    3IJ0 X-ray 2.45 A 77-441 [» ]
    3IJ1 X-ray 2.10 A 77-441 [» ]
    3IJC X-ray 1.95 A 77-441 [» ]
    3JPX X-ray 2.05 A 40-441 [» ]
    3JZG X-ray 2.10 A 40-441 [» ]
    3JZH X-ray 2.05 A 40-441 [» ]
    3JZN X-ray 2.60 A 76-441 [» ]
    3K26 X-ray 1.58 A 76-441 [» ]
    3K27 X-ray 1.76 A 76-441 [» ]
    ProteinModelPortali O75530.
    SMRi O75530. Positions 80-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114265. 460 interactions.
    DIPi DIP-36673N.
    IntActi O75530. 35 interactions.
    MINTi MINT-6630924.
    STRINGi 9606.ENSP00000263360.

    PTM databases

    PhosphoSitei O75530.

    Proteomic databases

    MaxQBi O75530.
    PaxDbi O75530.
    PRIDEi O75530.

    Protocols and materials databases

    DNASUi 8726.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263360 ; ENSP00000263360 ; ENSG00000074266 . [O75530-1 ]
    ENST00000327320 ; ENSP00000315587 ; ENSG00000074266 . [O75530-3 ]
    ENST00000351625 ; ENSP00000338186 ; ENSG00000074266 . [O75530-2 ]
    GeneIDi 8726.
    KEGGi hsa:8726.
    UCSCi uc001pbp.3. human. [O75530-1 ]
    uc001pbr.3. human. [O75530-2 ]

    Organism-specific databases

    CTDi 8726.
    GeneCardsi GC11P085955.
    HGNCi HGNC:3188. EED.
    HPAi CAB012211.
    HPA046731.
    MIMi 605984. gene.
    neXtProti NX_O75530.
    PharmGKBi PA27624.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOVERGENi HBG052708.
    KOi K11462.
    OMAi CTTLTHP.
    OrthoDBi EOG7WQ7S8.
    PhylomeDBi O75530.
    TreeFami TF314451.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    REACT_200808. PRC2 methylates histones and DNA.
    SignaLinki O75530.

    Miscellaneous databases

    ChiTaRSi EED. human.
    EvolutionaryTracei O75530.
    GeneWikii EED.
    GenomeRNAii 8726.
    NextBioi 32733.
    PROi O75530.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75530.
    Bgeei O75530.
    CleanExi HS_EED.
    Genevestigatori O75530.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 2 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The murine Polycomb-group gene eed and its human orthologue: functional implications of evolutionary conservation."
      Schumacher A., Lichtarge O., Schwartz S., Magnuson T.
      Genomics 54:79-88(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes."
      Sewalt R.G.A.B., van der Vlag J., Gunster M.J., Hamer K.M., den Blaauwen J.L., Satijn D.P.E., Hendrix T., van Driel R., Otte A.P.
      Mol. Cell. Biol. 18:3586-3595(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EZH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ILE-193 AND LEU-196, PUTATIVE ALTERNATIVE INITIATION.
    3. "HEED, the product of the human homolog of the murine eed gene, binds to the matrix protein of HIV-1."
      Peytavi R., Hong S.S., Gay B., d'Angeac A.D., Selig L., Benichou S., Benarous R., Boulanger P.
      J. Biol. Chem. 274:1635-1645(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH THE HIV-1 MA PROTEIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 300-SER-THR-301 AND 305-HIS-TYR-308.
      Tissue: Spleen.
    4. "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] (ISOFORM 1).
      Tissue: Synovium.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-441 (ISOFORM 1).
      Tissue: Eye and Lung.
    8. "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins."
      Rietzler M., Bittner M., Kolanus W., Schuster A., Holzmann B.
      J. Biol. Chem. 273:27459-27466(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-441 (ISOFORM 1), INTERACTION WITH ITGA4; ITGAE AND ITGB7, TISSUE SPECIFICITY.
    9. "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation."
      van der Vlag J., Otte A.P.
      Nat. Genet. 23:474-478(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZH2; HDAC1 AND HDAC2.
    10. "The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos."
      Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.
      Mol. Cell. Biol. 21:1360-1369(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EZH2 AND YY1.
    11. "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
      Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
      Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    12. "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins."
      Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.
      Mol. Cell. Biol. 22:5539-5553(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
      Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
      Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    14. "EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer."
      Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.
      EMBO J. 22:5323-5335(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION.
    15. Cited for: SUBCELLULAR LOCATION.
    16. "Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity."
      Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.
      EMBO J. 23:4061-4071(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZH2, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    17. "Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27."
      Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D., Green R., Farnham P.J.
      Genes Dev. 18:1592-1605(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    18. "Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3."
      Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.
      Mol. Cell 14:183-193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND PRC3 COMPLEXES, PUTATIVE ALTERNATIVE INITIATION.
    19. "SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex."
      Cao R., Zhang Y.
      Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED; EZH2; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    20. "Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation."
      Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M., Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J., Reinberg D.
      Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4; RBBP7; SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4 COMPLEX, TISSUE SPECIFICITY.
    21. "Substrate preferences of the EZH2 histone methyltransferase complex."
      Martin C., Cao R., Zhang Y.
      J. Biol. Chem. 281:8365-8370(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, INTERACTION WITH HISTONE H1.
    22. Cited for: FUNCTION, INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND DNMT3B.
    23. "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."
      Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H.
      Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
    24. "Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms."
      Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L., Dynlacht B.D., Reinberg D.
      Mol. Cell 32:503-518(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
    25. "Role of hPHF1 in H3K27 methylation and Hox gene silencing."
      Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.
      Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION OF THE PRC2 COMPLEX WITH PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    26. "Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo."
      Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.
      Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZH2 AND SUZ12, INTERACTION OF THE PRC2 COMPLEX WITH PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    29. "Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27."
      Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.
      J. Biol. Chem. 286:42414-42425(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDYL.
    30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2)."
      Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones A.E., MacKenzie F., Pan P., Li S.S., Wang H., Min J.
      Proc. Natl. Acad. Sci. U.S.A. 107:19266-19271(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 40-441 ALONE AND IN COMPLEX WITH METHYLATED HISTONE PEPTIDES, FUNCTION, DOMAIN WD REPEATS, METHYLATION AT LYS-66; LYS-197; LYS-268 AND LYS-284, MUTAGENESIS OF PHE-97; TYR-148; TRP-364 AND TYR-365.

    Entry informationi

    Entry nameiEED_HUMAN
    AccessioniPrimary (citable) accession number: O75530
    Secondary accession number(s): A8K7V5
    , O00149, Q6NTH2, Q7LDA5, Q7LDG8, Q86VV2, Q9UNY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 117 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

    Caution

    Two variants of the PRC2 complex have been described, termed PRC3 and PRC4. Each of the three complexes may include a different complement of EED isoforms, although the precise sequences of the isoforms in each complex have not been determined. The PRC2 and PRC4 complexes may also methylate 'Lys-26' of histone H1 in addition to 'Lys-27' of histone H3 (PubMed:15099518 and PubMed:15684044), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (PubMed:16431907).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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