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O75530 (EED_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

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

Names and origin

Protein namesRecommended name:
Polycomb protein EED

Short name=hEED
Alternative name(s):
WD protein associating with integrin cytoplasmic tails 1
Short name=WAIT-1
Gene names
Name:EED
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.9 Ref.14 Ref.16 Ref.17 Ref.19 Ref.22 Ref.27 Ref.32

Subunit structure

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. Ref.2 Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.30

Subcellular location

Nucleus. Chromosome. Note: Transiently colocalizes with XIST at inactive X chromosomes. Ref.2 Ref.3 Ref.12 Ref.15 Ref.17

Tissue specificity

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. Ref.1 Ref.2 Ref.3 Ref.8 Ref.20

Developmental stage

Expression peaks at the G1/S phase boundary. Ref.14

Induction

Expression is induced by E2F1, E2F2 and E2F3. Ref.14

Domain

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. Ref.32

Post-translational modification

Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines. Ref.24 Ref.32

Sequence similarities

Belongs to the WD repeat ESC family.

Contains 7 WD repeats.

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 (Ref.18 and Ref.20), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (Ref.21).

Sequence caution

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

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
   DomainRepeat
WD repeat
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of transcription, DNA-templated

Non-traceable author statement Ref.2. Source: UniProtKB

positive regulation of histone H3-K27 methylation

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression by genetic imprinting

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.2. Source: UniProtKB

pronucleus

Inferred from electronic annotation. Source: Ensembl

sex chromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase activity

Inferred from direct assay Ref.16. Source: MGI

identical protein binding

Inferred from physical interaction PubMed 11124122. Source: IntAct

protein binding

Inferred from physical interaction Ref.30. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

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)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75530-2)

The sequence of this isoform differs from the canonical sequence as follows:
     322-322: K → KSGRAILHSHQQCMRDPVSPNLRQHL
Isoform 3 (identifier: O75530-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.29
Chain2 – 441440Polycomb protein EED
PRO_0000343725

Regions

Repeat91 – 13444WD 1
Repeat142 – 18544WD 2
Repeat188 – 22841WD 3
Repeat234 – 27542WD 4
Repeat304 – 34138WD 5
Repeat359 – 39941WD 6
Repeat408 – 44134WD 7
Region81 – 441361Interaction with EZH2 By similarity
Region149 – 303155Required for interaction with the matrix protein MA of HIV-1
Region301 – 441141Required for interaction with the matrix protein MA of HIV-1

Amino acid modifications

Modified residue21N-acetylserine Ref.29
Modified residue551Phosphothreonine Ref.28
Modified residue661N6,N6,N6-trimethyllysine; alternate Ref.32
Modified residue661N6,N6-dimethyllysine; alternate Ref.32
Modified residue661N6-methyllysine; alternate Ref.32
Modified residue1971N6,N6,N6-trimethyllysine; alternate Ref.32
Modified residue1971N6,N6-dimethyllysine; alternate Ref.32
Modified residue1971N6-methyllysine; alternate Ref.32
Modified residue2681N6,N6,N6-trimethyllysine; alternate Ref.32
Modified residue2681N6,N6-dimethyllysine; alternate Ref.32
Modified residue2681N6-methyllysine; alternate Ref.32
Modified residue2841N6,N6,N6-trimethyllysine; alternate Ref.32
Modified residue2841N6,N6-dimethyllysine; alternate Ref.32
Modified residue2841N6-methyllysine; alternate Ref.32

Natural variations

Alternative sequence3221K → KSGRAILHSHQQCMRDPVSP NLRQHL in isoform 2.
VSP_034691
Alternative sequence401 – 44141Missing in isoform 3.
VSP_034692

Experimental info

Mutagenesis971F → A: Abolishes binding to H3K27me3. Ref.3 Ref.32
Mutagenesis1481Y → A: Abolishes binding to H3K27me3. Ref.3 Ref.32
Mutagenesis1931I → N: Impairs interaction with EZH2. Ref.2 Ref.3
Mutagenesis1961L → P: Impairs interaction with EZH2. Ref.2 Ref.3
Mutagenesis300 – 3012ST → AA: Impairs interaction with the matrix protein MA of HIV-1. Ref.3
Mutagenesis305 – 3084HRNY → AAAA: Impairs interaction with the matrix protein MA of HIV-1. Ref.3
Mutagenesis3641W → A: Abolishes binding to H3K27me3. Ref.3 Ref.32
Mutagenesis3641W → L: Abolishes binding to H3K27me3. Ref.3 Ref.32
Mutagenesis3651Y → A: Abolishes binding to H3K27me3. Ref.3 Ref.32
Sequence conflict321D → E in AAC68675. Ref.8
Sequence conflict741K → S in AAD08714. Ref.3
Sequence conflict741K → S in AAD08815. Ref.3
Sequence conflict3371E → K in AAD08714. Ref.3
Sequence conflict3371E → K in AAD08815. Ref.3
Sequence conflict4171S → G in BAF84809. Ref.4

Secondary structure

.......................................................................... 441
Helix Strand Turn

Details...

Sequences

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

Last modified July 22, 2008. Version 2.
Checksum: D2E0A5BA27C0499A

FASTA44150,198
        10         20         30         40         50         60 
MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT ERPDTPTNTP 

        70         80         90        100        110        120 
NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ FNWHSKEGDP LVFATVGSNR 

       130        140        150        160        170        180 
VTLYECHSQG EIRLLQSYVD ADADENFYTC AWTYDSNTSH PLLAVAGSRG IIRIINPITM 

       190        200        210        220        230        240 
QCIKHYVGHG NAINELKFHP RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL 

       250        260        270        280        290        300 
SADYDLLGEK IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS 

       310        320        330        340        350        360 
TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV TILGRFDYSQ 

       370        380        390        400        410        420 
CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK CTTLTHHKCG AAIRQTSFSR 

       430        440 
DSSILIAVCD DASIWRWDRL R 

« Hide

Isoform 2 [UniParc].

Checksum: 614B2E31B2A9D41F
Show »

FASTA46653,061
Isoform 3 [UniParc].

Checksum: 45DD879776FF83D5
Show »

FASTA40045,524

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Synovium.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Role of histone H3 lysine 27 methylation in X inactivation."
Plath K., Fang J., Mlynarczyk-Evans S.K., Cao R., Worringer K.A., Wang H., de la Cruz C.C., Otte A.P., Panning B., Zhang Y.
Science 300:131-135(2003) [PubMed] [Europe PMC] [Abstract]
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]"The Polycomb group protein EZH2 directly controls DNA methylation."
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.
Nature 439:871-874(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND DNMT3B.
[23]Erratum
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.
Nature 446:824-824(2007)
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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].
[30]"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.
[31]"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].
[32]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8273.1. [O75530-1]
CCDS8274.1. [O75530-3]
RefSeqNP_003788.2. NM_003797.3. [O75530-1]
NP_694536.1. NM_152991.2. [O75530-3]
UniGeneHs.503510.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO75530.
SMRO75530. Positions 80-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114265. 460 interactions.
DIPDIP-36673N.
IntActO75530. 35 interactions.
MINTMINT-6630924.
STRING9606.ENSP00000263360.

PTM databases

PhosphoSiteO75530.

Proteomic databases

MaxQBO75530.
PaxDbO75530.
PRIDEO75530.

Protocols and materials databases

DNASU8726.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263360; ENSP00000263360; ENSG00000074266. [O75530-1]
ENST00000327320; ENSP00000315587; ENSG00000074266. [O75530-3]
ENST00000351625; ENSP00000338186; ENSG00000074266. [O75530-2]
GeneID8726.
KEGGhsa:8726.
UCSCuc001pbp.3. human. [O75530-1]
uc001pbr.3. human. [O75530-2]

Organism-specific databases

CTD8726.
GeneCardsGC11P085955.
HGNCHGNC:3188. EED.
HPACAB012211.
HPA046731.
MIM605984. gene.
neXtProtNX_O75530.
PharmGKBPA27624.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG052708.
KOK11462.
OMACTTLTHP.
OrthoDBEOG7WQ7S8.
PhylomeDBO75530.
TreeFamTF314451.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_71. Gene Expression.
SignaLinkO75530.

Gene expression databases

ArrayExpressO75530.
BgeeO75530.
CleanExHS_EED.
GenevestigatorO75530.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 2 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEED. human.
EvolutionaryTraceO75530.
GeneWikiEED.
GenomeRNAi8726.
NextBio32733.
PROO75530.
SOURCESearch...

Entry information

Entry nameEED_HUMAN
AccessionPrimary (citable) accession number: O75530
Secondary accession number(s): A8K7V5 expand/collapse secondary AC list , O00149, Q6NTH2, Q7LDA5, Q7LDG8, Q86VV2, Q9UNY7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM