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Q921E6

- EED_MOUSE

UniProt

Q921E6 - EED_MOUSE

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Protein

Polycomb protein EED

Gene

Eed

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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. cytoplasm Source: Ensembl
  2. ESC/E(Z) complex Source: UniProtKB
  3. nucleus Source: MGI
  4. pronucleus Source: MGI
  5. sex chromatin Source: MGI
Complete GO annotation...

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 – 897Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi132 – 1398Combined sources
Beta strandi147 – 1548Combined sources
Turni156 – 1583Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi172 – 1765Combined sources
Turni177 – 1804Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi205 – 2106Combined sources
Beta strandi215 – 2195Combined sources
Turni220 – 2234Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi239 – 2446Combined sources
Beta strandi248 – 2558Combined sources
Beta strandi260 – 2678Combined sources
Helixi268 – 27912Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi318 – 3225Combined sources
Beta strandi324 – 33512Combined sources
Turni340 – 3423Combined sources
Beta strandi350 – 3578Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi376 – 3805Combined sources
Beta strandi386 – 3905Combined sources
Beta strandi393 – 3953Combined sources
Helixi396 – 3983Combined sources
Beta strandi401 – 4044Combined sources
Beta strandi413 – 4186Combined sources
Beta strandi422 – 4298Combined sources
Beta strandi432 – 4387Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT
60 70 80 90 100
ERPDTPTNTP NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ
110 120 130 140 150
FNWHSKEGDP LVFATVGSNR VTLYECHSQG EIRLLQSYVD ADADENFYTC
160 170 180 190 200
AWTYDSNTSH PLLAVAGSRG IIRIINPITM QCIKHYVGHG NAINELKFHP
210 220 230 240 250
RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL SADYDLLGEK
260 270 280 290 300
IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS
310 320 330 340 350
TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV
360 370 380 390 400
TILGRFDYSQ CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK
410 420 430 440
CTTLTHHKCG AAIRQTSFSR DSSILIAVCD DASIWRWDRL R
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:
     1-14: Missing.

Show »
Length:427
Mass (Da):48,765
Checksum:i794AABBF7BB46B99
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1414Missing in isoform 3. CuratedVSP_034693Add
BLAST
Alternative sequencei1 – 11M → MAGSHARPPRRLGAICDSGG SGGGGGAGSFAAGSGRACLT AVWRRPRPRRQEPGGRRRNM in isoform 2. 3 PublicationsVSP_034694

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

ChiTaRSi Eed. mouse.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 118 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