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Q921E6

- EED_MOUSE

UniProt

Q921E6 - EED_MOUSE

Protein

Polycomb protein EED

Gene

Eed

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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 By similarity. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems By similarity. Genes repressed by the PRC2/EED-EZH2 complex include HOXA7, HOXB6 and HOXC8. Plays a role in X chromosome inactivation (XCI), in which one of the two X chromosomes in female mammals is transcriptionally silenced to equalize X-linked gene dosage with XY males. Required for stable maintenance of XCI in both embryonic and extraembryonic tissues. May prevent transcriptional activation of facultative heterochromatin during differentiation. Required for development of secondary trophoblast giant cells during placental development. May regulate hippocampal synaptic plasticity in the developing brain.By similarity14 Publications

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
    REACT_222475. PRC2 methylates histones and DNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polycomb protein EED
    Gene namesi
    Name:Eed
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:95286. Eed.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Localizes to the inactive X chromosome in cells of the early embryo and in stem cells of the extraembryonic trophectoderm lineage. Recruitment to the inactive X-chromosome requires XIST.

    GO - Cellular componenti

    1. ESC/E(Z) complex Source: UniProtKB
    2. nucleus Source: MGI
    3. pronucleus Source: MGI
    4. sex chromatin Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi193 – 1931I → N: Hypomorphic allele. Abrogates interaction with EZH2 and impairs transcriptional repression. 2 Publications
    Mutagenesisi196 – 1961L → P: Null allele. Abrogates interaction with EZH2 and impairs transcriptional repression. 3 Publications
    Mutagenesisi246 – 2461L → E: Abrogates interaction with EZH2. 1 Publication
    Mutagenesisi315 – 3151L → E: Impairs interaction with EZH2. 1 Publication
    Mutagenesisi316 – 3161G → A: Impairs interaction with EZH2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 441440Polycomb protein EEDPRO_0000343726Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei55 – 551PhosphothreonineBy similarity
    Modified residuei66 – 661N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei66 – 661N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei66 – 661N6-methyllysine; alternateBy similarity
    Modified residuei197 – 1971N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei197 – 1971N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei197 – 1971N6-methyllysine; alternateBy similarity
    Modified residuei268 – 2681N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei268 – 2681N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei268 – 2681N6-methyllysine; alternateBy similarity
    Modified residuei284 – 2841N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei284 – 2841N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei284 – 2841N6-methyllysine; alternateBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ921E6.
    PaxDbiQ921E6.
    PRIDEiQ921E6.

    PTM databases

    PhosphoSiteiQ921E6.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, kidney, liver, lung, muscle, ovary, spleen and testis. Expressed throughout the brain.3 Publications

    Developmental stagei

    Maternally expressed. Expressed from E5.5, and expression remains high throughout development. Expression decreases during differentiation of embryonic stem cells (ES cells). Expression increases in prostate during prostate tumor development.3 Publications

    Inductioni

    Induced in embryonic stem cells (ES cells) by STAT3 and POU5F1.1 Publication

    Gene expression databases

    BgeeiQ921E6.
    GenevestigatoriQ921E6.

    Interactioni

    Subunit structurei

    Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 By similarity. The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12 By similarity. 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 By similarity. Interacts with HDAC, HDAC2, histone H1 and YY1 By similarity. May interact with ITGA4, ITGAE and ITGB7 By similarity. Interacts with CDYL By similarity. Interacts with EZH2. Interacts with KMT2A/MLL1 in adult brain. Interacts with ARNTL/BMAL1.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ezh2Q611889EBI-904301,EBI-904311
    Jarid2Q6231510EBI-904301,EBI-493592
    Mtf2Q023953EBI-904301,EBI-2531578

    Protein-protein interaction databases

    BioGridi199384. 1177 interactions.
    DIPiDIP-29523N.
    IntActiQ921E6. 42 interactions.
    MINTiMINT-1539279.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi83 – 897
    Beta strandi98 – 1014
    Beta strandi112 – 1176
    Beta strandi120 – 1267
    Beta strandi132 – 1398
    Beta strandi147 – 1548
    Turni156 – 1583
    Beta strandi161 – 1677
    Beta strandi172 – 1765
    Turni177 – 1804
    Beta strandi181 – 1866
    Beta strandi193 – 1986
    Beta strandi205 – 2106
    Beta strandi215 – 2195
    Turni220 – 2234
    Beta strandi224 – 2296
    Beta strandi239 – 2446
    Beta strandi248 – 2558
    Beta strandi260 – 2678
    Helixi268 – 27912
    Beta strandi292 – 2943
    Beta strandi298 – 3014
    Beta strandi311 – 3155
    Beta strandi318 – 3225
    Beta strandi324 – 33512
    Turni340 – 3423
    Beta strandi350 – 3578
    Beta strandi368 – 3703
    Beta strandi376 – 3805
    Beta strandi386 – 3905
    Beta strandi393 – 3953
    Helixi396 – 3983
    Beta strandi401 – 4044
    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
    2QXVX-ray1.82A81-441[»]
    ProteinModelPortaliQ921E6.
    SMRiQ921E6. Positions 80-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ921E6.

    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 EZH2Add
    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 By similarity.By similarity

    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.
    GeneTreeiENSGT00510000047334.
    HOGENOMiHOG000005759.
    HOVERGENiHBG052708.
    InParanoidiQ921E6.
    KOiK11462.
    OMAiCTTLTHP.
    OrthoDBiEOG7WQ7S8.
    PhylomeDBiQ921E6.
    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 initiation. Align

    Note: Additional isoforms may be produced by alternative initiation from other non-canonical start codons but their precise positions have not been unambiguously determined.2 Publications

    Isoform 1 (identifier: Q921E6-1) [UniParc]FASTAAdd to Basket

    Also known as: EED-3

    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:December 1, 2001 - v1
    Checksum:iD2E0A5BA27C0499A
    GO
    Isoform 2 (identifier: Q921E6-2) [UniParc]FASTAAdd to Basket

    Also known as: EED-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAGSHARPPRRLGAICDSGGSGGGGGAGSFAAGSGRACLTAVWRRPRPRRQEPGGRRRNM

    Note: Translation initiates from a non-canonical start codon (GUG).

    Show »
    Length:500
    Mass (Da):56,194
    Checksum:iEC7081363459B105
    GO
    Isoform 3 (identifier: Q921E6-3) [UniParc]FASTAAdd to Basket

    Also known as: EED-4

    The sequence of this isoform differs from the canonical sequence as follows:
         2-14: Missing.

    Show »
    Length:428
    Mass (Da):48,896
    Checksum:i345AB4E1E93629EF
    GO

    Sequence cautioni

    The sequence AAB38319.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAC53302.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH12966.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAGSHARPPRRLGAICDSGG SGGGGGAGSFAAGSGRACLT AVWRRPRPRRQEPGGRRRNM in isoform 2. 3 PublicationsVSP_034694
    Alternative sequencei2 – 1413Missing in isoform 3. CuratedVSP_034693Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78103 mRNA. Translation: AAB38319.1. Different initiation.
    U97675 mRNA. Translation: AAC53302.1. Different initiation.
    AK077664 mRNA. Translation: BAC36938.1.
    AK131976 mRNA. Translation: BAE20916.1.
    AK133890 mRNA. Translation: BAE21915.1.
    BC012966 mRNA. Translation: AAH12966.1. Different initiation.
    CCDSiCCDS40016.1. [Q921E6-1]
    RefSeqiNP_068676.1. NM_021876.3. [Q921E6-1]
    UniGeneiMm.380914.

    Genome annotation databases

    EnsembliENSMUST00000107234; ENSMUSP00000102853; ENSMUSG00000030619. [Q921E6-1]
    GeneIDi13626.
    KEGGimmu:13626.
    UCSCiuc009igk.2. mouse. [Q921E6-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78103 mRNA. Translation: AAB38319.1 . Different initiation.
    U97675 mRNA. Translation: AAC53302.1 . Different initiation.
    AK077664 mRNA. Translation: BAC36938.1 .
    AK131976 mRNA. Translation: BAE20916.1 .
    AK133890 mRNA. Translation: BAE21915.1 .
    BC012966 mRNA. Translation: AAH12966.1 . Different initiation.
    CCDSi CCDS40016.1. [Q921E6-1 ]
    RefSeqi NP_068676.1. NM_021876.3. [Q921E6-1 ]
    UniGenei Mm.380914.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QXV X-ray 1.82 A 81-441 [» ]
    ProteinModelPortali Q921E6.
    SMRi Q921E6. Positions 80-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199384. 1177 interactions.
    DIPi DIP-29523N.
    IntActi Q921E6. 42 interactions.
    MINTi MINT-1539279.

    PTM databases

    PhosphoSitei Q921E6.

    Proteomic databases

    MaxQBi Q921E6.
    PaxDbi Q921E6.
    PRIDEi Q921E6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000107234 ; ENSMUSP00000102853 ; ENSMUSG00000030619 . [Q921E6-1 ]
    GeneIDi 13626.
    KEGGi mmu:13626.
    UCSCi uc009igk.2. mouse. [Q921E6-1 ]

    Organism-specific databases

    CTDi 8726.
    MGIi MGI:95286. Eed.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00510000047334.
    HOGENOMi HOG000005759.
    HOVERGENi HBG052708.
    InParanoidi Q921E6.
    KOi K11462.
    OMAi CTTLTHP.
    OrthoDBi EOG7WQ7S8.
    PhylomeDBi Q921E6.
    TreeFami TF314451.

    Enzyme and pathway databases

    Reactomei REACT_188970. Oxidative Stress Induced Senescence.
    REACT_222475. PRC2 methylates histones and DNA.

    Miscellaneous databases

    EvolutionaryTracei Q921E6.
    NextBioi 284300.
    PROi Q921E6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q921E6.
    Genevestigatori Q921E6.

    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. "Positional cloning of a global regulator of anterior-posterior patterning in mice."
      Shumacher A., Faust C., Magnuson T.
      Nature 383:250-253(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION OF MUTANTS ASN-193 AND PRO-196, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Swiss Webster.
    2. Erratum
      Schumacher A., Faust C., Magnuson T.
      Nature 384:648-648(1996) [PubMed] [Europe PMC] [Abstract]
    3. "The product of the murine homolog of the Drosophila extra sex combs gene displays transcriptional repressor activity."
      Denisenko O.N., Bomsztyk K.
      Mol. Cell. Biol. 17:4707-4717(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE INITIATION, TISSUE SPECIFICITY, MUTAGENESIS OF ILE-193 AND LEU-196.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Embryo.
    5. "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).
      Strain: Czech II.
      Tissue: Mammary tumor.
    6. "Point mutations in the WD40 domain of Eed block its interaction with Ezh2."
      Denisenko O.N., Shnyreva M., Suzuki H., Bomsztyk K.
      Mol. Cell. Biol. 18:5634-5642(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZH2, MUTAGENESIS OF ILE-193 AND LEU-196.
    7. "Imprinted X inactivation maintained by a mouse Polycomb group gene."
      Wang J., Mager J., Chen Y., Schneider E., Cross J.C., Nagy A., Magnuson T.
      Nat. Genet. 28:371-375(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF MUTANTS ASN-193 AND PRO-196.
    8. "Mitotically stable association of polycomb group proteins Eed and Enx1 with the inactive X chromosome in trophoblast stem cells."
      Mak W., Baxter J., Silva J., Newall A.E., Otte A.P., Brockdorff N.
      Curr. Biol. 12:1016-1020(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "The mouse PcG gene Eed is required for Hox gene repression and extraembryonic development."
      Wang J., Mager J., Schnedier E., Magnuson T.
      Mamm. Genome 13:493-503(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF MUTANT ASN-193.
    10. "Establishment of histone H3 methylation on the inactive X chromosome requires transient recruitment of Eed-Enx1 polycomb group complexes."
      Silva J., Mak W., Zvetkova I., Appanah R., Nesterova T.B., Webster Z., Peters A.H.F.M., Jenuwein T., Otte A.P., Brockdorff N.
      Dev. Cell 4:481-495(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    11. "Genome imprinting regulated by the mouse Polycomb group protein Eed."
      Mager J., Montgomery N.D., de Villena F.P.-M., Magnuson T.
      Nat. Genet. 33:502-507(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Imprinting along the Kcnq1 domain on mouse chromosome 7 involves repressive histone methylation and recruitment of Polycomb group complexes."
      Umlauf D., Goto Y., Cao R., Cerqueira F., Wagschal A., Zhang Y., Feil R.
      Nat. Genet. 36:1296-1300(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Epigenetic dynamics of imprinted X inactivation during early mouse development."
      Okamoto I., Otte A.P., Allis C.D., Reinberg D., Heard E.
      Science 303:644-649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Reactivation of the paternal X chromosome in early mouse embryos."
      Mak W., Nesterova T.B., de Napoles M., Appanah R., Yamanaka S., Otte A.P., Brockdorff N.
      Science 303:666-669(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "The murine polycomb group protein Eed is required for global histone H3 lysine-27 methylation."
      Montgomery N.D., Yee D., Chen A., Kalantry S., Chamberlain S.J., Otte A.P., Magnuson T.
      Curr. Biol. 15:942-947(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Initiation of epigenetic reprogramming of the X chromosome in somatic nuclei transplanted to a mouse oocyte."
      Bao S., Miyoshi N., Okamoto I., Jenuwein T., Heard E., Azim Surani M.
      EMBO Rep. 6:748-754(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "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: DEVELOPMENTAL STAGE.
    19. "Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3."
      Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B., Otte A.P., Hung M.-C.
      Science 310:306-310(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EZH2.
    20. "Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions."
      Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.
      Genes Dev. 20:1123-1136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "The Polycomb group protein Eed protects the inactive X-chromosome from differentiation-induced reactivation."
      Kalantry S., Mills K.C., Yee D., Otte A.P., Panning B., Magnuson T.
      Nat. Cell Biol. 8:195-202(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    22. "Developmental regulation of Eed complex composition governs a switch in global histone modification in brain."
      Kim S.Y., Levenson J.M., Korsmeyer S., Sweatt J.D., Schumacher A.
      J. Biol. Chem. 282:9962-9972(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZH2 AND KMT2A/MLL1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LEU-196.
    23. "Molecular and functional mapping of EED motifs required for PRC2-dependent histone methylation."
      Montgomery N.D., Yee D., Montgomery S.A., Magnuson T.
      J. Mol. Biol. 374:1145-1157(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE INITIATION, INTERACTION WITH EZH2.
    24. "STAT3 and Oct-3/4 control histone modification through induction of Eed in embryonic stem cells."
      Ura H., Usuda M., Kinoshita K., Sun C., Mori K., Akagi T., Matsuda T., Koide H., Yokota T.
      J. Biol. Chem. 283:9713-9723(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    25. "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency."
      Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C., Orkin S.H.
      Mol. Cell 32:491-502(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
    26. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation."
      Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.
      Cell Stem Cell 6:153-166(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC2 COMPLEX.
    28. "Circadian gene Bmal1 regulates diurnal oscillations of Ly6C(hi) inflammatory monocytes."
      Nguyen K.D., Fentress S.J., Qiu Y., Yun K., Cox J.S., Chawla A.
      Science 341:1483-1488(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARNTL/BMAL1.
    29. "Structural basis of EZH2 recognition by EED."
      Han Z., Xing X., Hu M., Zhang Y., Liu P., Chai J.
      Structure 15:1306-1315(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 81-441 IN COMPLEX WITH EZH2, MUTAGENESIS OF LEU-246; LEU-315 AND GLY-316.

    Entry informationi

    Entry nameiEED_MOUSE
    AccessioniPrimary (citable) accession number: Q921E6
    Secondary accession number(s): P97462
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mice homozygous for a null allele of this protein (Pro-196) exhibit disrupted anterior posterior patterning of the primitive streak during gastrulation and reduced numbers of trophoblast giant cells. Mice homozygous for a hypomorphic allele of this protein (Asn-193) exhibit posterior transformations along the axial skeleton and altered patterns of Hox gene expression.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3