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Q921E6 (EED_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:Eed
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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. Ref.3 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Subunit structure

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. Ref.6 Ref.19 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28

Subcellular location

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. Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.17 Ref.21 Ref.22

Tissue specificity

Expressed in brain, heart, kidney, liver, lung, muscle, ovary, spleen and testis. Expressed throughout the brain. Ref.1 Ref.3 Ref.22

Developmental stage

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. Ref.1 Ref.10 Ref.18

Induction

Induced in embryonic stem cells (ES cells) by STAT3 and POU5F1. Ref.24

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 By similarity.

Post-translational modification

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

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.

Sequence similarities

Belongs to the WD repeat ESC family.

Contains 7 WD repeats.

Caution

Was originally thought (Ref.3) to interact with HNRNPK. This apparent interaction may be mediated by the translated product of the 5'-UTR sequence of the 2-hybrid clone.

Sequence caution

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.

Binary interactions

Alternative products

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

Note: Additional isoforms may be produced by alternative initiation from other non-canonical start codons but their precise positions have not been unambiguously determined.
Isoform 1 (identifier: Q921E6-1)

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.
Isoform 2 (identifier: Q921E6-2)

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).
Isoform 3 (identifier: Q921E6-3)

Also known as: EED-4;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 441440Polycomb protein EED
PRO_0000343726

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

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue551Phosphothreonine By similarity
Modified residue661N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue661N6,N6-dimethyllysine; alternate By similarity
Modified residue661N6-methyllysine; alternate By similarity
Modified residue1971N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue1971N6,N6-dimethyllysine; alternate By similarity
Modified residue1971N6-methyllysine; alternate By similarity
Modified residue2681N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue2681N6,N6-dimethyllysine; alternate By similarity
Modified residue2681N6-methyllysine; alternate By similarity
Modified residue2841N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue2841N6,N6-dimethyllysine; alternate By similarity
Modified residue2841N6-methyllysine; alternate By similarity

Natural variations

Alternative sequence11M → MAGSHARPPRRLGAICDSGG SGGGGGAGSFAAGSGRACLT AVWRRPRPRRQEPGGRRRNM in isoform 2.
VSP_034694
Alternative sequence2 – 1413Missing in isoform 3.
VSP_034693

Experimental info

Mutagenesis1931I → N: Hypomorphic allele. Abrogates interaction with EZH2 and impairs transcriptional repression. Ref.3 Ref.6
Mutagenesis1961L → P: Null allele. Abrogates interaction with EZH2 and impairs transcriptional repression. Ref.3 Ref.6 Ref.22
Mutagenesis2461L → E: Abrogates interaction with EZH2. Ref.29
Mutagenesis3151L → E: Impairs interaction with EZH2. Ref.29
Mutagenesis3161G → A: Impairs interaction with EZH2. Ref.29

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (EED-3) [UniParc].

Last modified December 1, 2001. Version 1.
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 (EED-1) [UniParc].

Checksum: EC7081363459B105
Show »

FASTA50056,194
Isoform 3 (EED-4) [UniParc].

Checksum: 345AB4E1E93629EF
Show »

FASTA42848,896

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_068676.1. NM_021876.3.
UniGeneMm.380914.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QXVX-ray1.82A81-441[»]
ProteinModelPortalQ921E6.
SMRQ921E6. Positions 80-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199384. 16 interactions.
DIPDIP-29523N.
IntActQ921E6. 42 interactions.
MINTMINT-1539279.

PTM databases

PhosphoSiteQ921E6.

Proteomic databases

PaxDbQ921E6.
PRIDEQ921E6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000107234; ENSMUSP00000102853; ENSMUSG00000030619. [Q921E6-1]
GeneID13626.
KEGGmmu:13626.
UCSCuc009igk.2. mouse. [Q921E6-1]

Organism-specific databases

CTD8726.
MGIMGI:95286. Eed.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00510000047334.
HOGENOMHOG000005759.
HOVERGENHBG052708.
InParanoidQ921E6.
KOK11462.
OMACTTLTHP.
OrthoDBEOG7WQ7S8.
PhylomeDBQ921E6.
TreeFamTF314451.

Gene expression databases

BgeeQ921E6.
GenevestigatorQ921E6.

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

EvolutionaryTraceQ921E6.
NextBio284300.
PROQ921E6.
SOURCESearch...

Entry information

Entry nameEED_MOUSE
AccessionPrimary (citable) accession number: Q921E6
Secondary accession number(s): P97462
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot