EED_MOUSE
ID EED_MOUSE Reviewed; 441 AA.
AC Q921E6; P97462;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Polycomb protein EED;
GN Name=Eed;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION OF MUTANTS ASN-193
RP AND PRO-196, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster;
RX PubMed=8805699; DOI=10.1038/383250a0;
RA Shumacher A., Faust C., Magnuson T.;
RT "Positional cloning of a global regulator of anterior-posterior patterning
RT in mice.";
RL Nature 383:250-253(1996).
RN [2]
RP ERRATUM OF PUBMED:8805699.
RX PubMed=8984348; DOI=10.1038/384648a0;
RA Schumacher A., Faust C., Magnuson T.;
RL Nature 384:648-648(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE INITIATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF ILE-193 AND LEU-196.
RX PubMed=9234727; DOI=10.1128/mcb.17.8.4707;
RA Denisenko O.N., Bomsztyk K.;
RT "The product of the murine homolog of the Drosophila extra sex combs gene
RT displays transcriptional repressor activity.";
RL Mol. Cell. Biol. 17:4707-4717(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INTERACTION WITH EZH2, AND MUTAGENESIS OF ILE-193 AND LEU-196.
RX PubMed=9742080; DOI=10.1128/mcb.18.10.5634;
RA Denisenko O.N., Shnyreva M., Suzuki H., Bomsztyk K.;
RT "Point mutations in the WD40 domain of Eed block its interaction with
RT Ezh2.";
RL Mol. Cell. Biol. 18:5634-5642(1998).
RN [7]
RP FUNCTION, AND CHARACTERIZATION OF MUTANTS ASN-193 AND PRO-196.
RX PubMed=11479595; DOI=10.1038/ng574;
RA Wang J., Mager J., Chen Y., Schneider E., Cross J.C., Nagy A., Magnuson T.;
RT "Imprinted X inactivation maintained by a mouse Polycomb group gene.";
RL Nat. Genet. 28:371-375(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12123576; DOI=10.1016/s0960-9822(02)00892-8;
RA Mak W., Baxter J., Silva J., Newall A.E., Otte A.P., Brockdorff N.;
RT "Mitotically stable association of polycomb group proteins Eed and Enx1
RT with the inactive X chromosome in trophoblast stem cells.";
RL Curr. Biol. 12:1016-1020(2002).
RN [9]
RP FUNCTION, AND CHARACTERIZATION OF MUTANT ASN-193.
RX PubMed=12370779; DOI=10.1007/s00335-002-2182-7;
RA Wang J., Mager J., Schnedier E., Magnuson T.;
RT "The mouse PcG gene Eed is required for Hox gene repression and
RT extraembryonic development.";
RL Mamm. Genome 13:493-503(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12689588; DOI=10.1016/s1534-5807(03)00068-6;
RA Silva J., Mak W., Zvetkova I., Appanah R., Nesterova T.B., Webster Z.,
RA Peters A.H.F.M., Jenuwein T., Otte A.P., Brockdorff N.;
RT "Establishment of histone H3 methylation on the inactive X chromosome
RT requires transient recruitment of Eed-Enx1 polycomb group complexes.";
RL Dev. Cell 4:481-495(2003).
RN [11]
RP FUNCTION.
RX PubMed=12627233; DOI=10.1038/ng1125;
RA Mager J., Montgomery N.D., de Villena F.P.-M., Magnuson T.;
RT "Genome imprinting regulated by the mouse Polycomb group protein Eed.";
RL Nat. Genet. 33:502-507(2003).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12649488; DOI=10.1126/science.1084274;
RA Plath K., Fang J., Mlynarczyk-Evans S.K., Cao R., Worringer K.A., Wang H.,
RA de la Cruz C.C., Otte A.P., Panning B., Zhang Y.;
RT "Role of histone H3 lysine 27 methylation in X inactivation.";
RL Science 300:131-135(2003).
RN [13]
RP FUNCTION.
RX PubMed=15516932; DOI=10.1038/ng1467;
RA Umlauf D., Goto Y., Cao R., Cerqueira F., Wagschal A., Zhang Y., Feil R.;
RT "Imprinting along the Kcnq1 domain on mouse chromosome 7 involves
RT repressive histone methylation and recruitment of Polycomb group
RT complexes.";
RL Nat. Genet. 36:1296-1300(2004).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=14671313; DOI=10.1126/science.1092727;
RA Okamoto I., Otte A.P., Allis C.D., Reinberg D., Heard E.;
RT "Epigenetic dynamics of imprinted X inactivation during early mouse
RT development.";
RL Science 303:644-649(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=14752160; DOI=10.1126/science.1092674;
RA Mak W., Nesterova T.B., de Napoles M., Appanah R., Yamanaka S., Otte A.P.,
RA Brockdorff N.;
RT "Reactivation of the paternal X chromosome in early mouse embryos.";
RL Science 303:666-669(2004).
RN [16]
RP FUNCTION.
RX PubMed=15916951; DOI=10.1016/j.cub.2005.04.051;
RA Montgomery N.D., Yee D., Chen A., Kalantry S., Chamberlain S.J., Otte A.P.,
RA Magnuson T.;
RT "The murine polycomb group protein Eed is required for global histone H3
RT lysine-27 methylation.";
RL Curr. Biol. 15:942-947(2005).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=16007070; DOI=10.1038/sj.embor.7400461;
RA Bao S., Miyoshi N., Okamoto I., Jenuwein T., Heard E., Azim Surani M.;
RT "Initiation of epigenetic reprogramming of the X chromosome in somatic
RT nuclei transplanted to a mouse oocyte.";
RL EMBO Rep. 6:748-754(2005).
RN [18]
RP DEVELOPMENTAL STAGE.
RX PubMed=15684044; DOI=10.1073/pnas.0409875102;
RA Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M.,
RA Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J.,
RA Reinberg D.;
RT "Composition and histone substrates of polycomb repressive group complexes
RT change during cellular differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005).
RN [19]
RP INTERACTION WITH EZH2.
RX PubMed=16224021; DOI=10.1126/science.1118947;
RA Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B.,
RA Otte A.P., Hung M.-C.;
RT "Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27
RT in histone H3.";
RL Science 310:306-310(2005).
RN [20]
RP FUNCTION.
RX PubMed=16618801; DOI=10.1101/gad.381706;
RA Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.;
RT "Genome-wide mapping of Polycomb target genes unravels their roles in cell
RT fate transitions.";
RL Genes Dev. 20:1123-1136(2006).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16415857; DOI=10.1038/ncb1351;
RA Kalantry S., Mills K.C., Yee D., Otte A.P., Panning B., Magnuson T.;
RT "The Polycomb group protein Eed protects the inactive X-chromosome from
RT differentiation-induced reactivation.";
RL Nat. Cell Biol. 8:195-202(2006).
RN [22]
RP FUNCTION, INTERACTION WITH EZH2 AND KMT2A/MLL1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-196.
RX PubMed=17259173; DOI=10.1074/jbc.m608722200;
RA Kim S.Y., Levenson J.M., Korsmeyer S., Sweatt J.D., Schumacher A.;
RT "Developmental regulation of Eed complex composition governs a switch in
RT global histone modification in brain.";
RL J. Biol. Chem. 282:9962-9972(2007).
RN [23]
RP FUNCTION, ALTERNATIVE INITIATION, AND INTERACTION WITH EZH2.
RX PubMed=17997413; DOI=10.1016/j.jmb.2007.10.040;
RA Montgomery N.D., Yee D., Montgomery S.A., Magnuson T.;
RT "Molecular and functional mapping of EED motifs required for PRC2-dependent
RT histone methylation.";
RL J. Mol. Biol. 374:1145-1157(2007).
RN [24]
RP FUNCTION, AND INDUCTION.
RX PubMed=18201968; DOI=10.1074/jbc.m707275200;
RA Ura H., Usuda M., Kinoshita K., Sun C., Mori K., Akagi T., Matsuda T.,
RA Koide H., Yokota T.;
RT "STAT3 and Oct-3/4 control histone modification through induction of Eed in
RT embryonic stem cells.";
RL J. Biol. Chem. 283:9713-9723(2008).
RN [25]
RP IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
RX PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
RA Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
RA Orkin S.H.;
RT "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in
RT maintaining stem cell identity and executing pluripotency.";
RL Mol. Cell 32:491-502(2008).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [28]
RP IDENTIFICATION IN THE PRC2 COMPLEX.
RX PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J.,
RA Krogan N.J., Reiter J.F., Stanford W.L.;
RT "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT networks during mouse embryonic stem cell self-renewal and
RT differentiation.";
RL Cell Stem Cell 6:153-166(2010).
RN [29]
RP INTERACTION WITH ARNTL/BMAL1.
RX PubMed=23970558; DOI=10.1126/science.1240636;
RA Nguyen K.D., Fentress S.J., Qiu Y., Yun K., Cox J.S., Chawla A.;
RT "Circadian gene Bmal1 regulates diurnal oscillations of Ly6C(hi)
RT inflammatory monocytes.";
RL Science 341:1483-1488(2013).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 81-441 IN COMPLEX WITH EZH2, AND
RP MUTAGENESIS OF LEU-246; LEU-315 AND GLY-316.
RX PubMed=17937919; DOI=10.1016/j.str.2007.08.007;
RA Han Z., Xing X., Hu M., Zhang Y., Liu P., Chai J.;
RT "Structural basis of EZH2 recognition by EED.";
RL Structure 15:1306-1315(2007).
CC -!- FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2
CC complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading
CC to transcriptional repression of the affected target gene. Also
CC recognizes 'Lys-26' trimethylated histone H1 with the effect of
CC inhibiting PRC2 complex methyltransferase activity on nucleosomal
CC histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite
CC effect, enabling the propagation of this repressive mark (By
CC similarity). The PRC2/EED-EZH2 complex may also serve as a recruiting
CC platform for DNA methyltransferases, thereby linking two epigenetic
CC repression systems (By similarity). Genes repressed by the PRC2/EED-
CC EZH2 complex include HOXA7, HOXB6 and HOXC8. Plays a role in X
CC chromosome inactivation (XCI), in which one of the two X chromosomes in
CC female mammals is transcriptionally silenced to equalize X-linked gene
CC dosage with XY males. Required for stable maintenance of XCI in both
CC embryonic and extraembryonic tissues. May prevent transcriptional
CC activation of facultative heterochromatin during differentiation.
CC Required for development of secondary trophoblast giant cells during
CC placental development. May regulate hippocampal synaptic plasticity in
CC the developing brain. {ECO:0000250|UniProtKB:O75530,
CC ECO:0000269|PubMed:11479595, ECO:0000269|PubMed:12370779,
CC ECO:0000269|PubMed:12627233, ECO:0000269|PubMed:12649488,
CC ECO:0000269|PubMed:12689588, ECO:0000269|PubMed:15516932,
CC ECO:0000269|PubMed:15916951, ECO:0000269|PubMed:16415857,
CC ECO:0000269|PubMed:16618801, ECO:0000269|PubMed:17259173,
CC ECO:0000269|PubMed:17997413, ECO:0000269|PubMed:18201968,
CC ECO:0000269|PubMed:9234727, ECO:0000269|PubMed:9742080}.
CC -!- SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes EED,
CC EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 (By similarity). The
CC minimum components required for methyltransferase activity of the
CC PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12 (By similarity).
CC Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1,
CC SUZ12, RBBP4 and AEBP2. The PRC2 complex may also interact with DNMT1,
CC DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the
CC SUZ12 subunit (By similarity). Interacts with HDAC, HDAC2, histone H1
CC and YY1 (By similarity). May interact with ITGA4, ITGAE and ITGB7 (By
CC similarity). Interacts with CDYL (By similarity). Interacts with EZH2.
CC Interacts with KMT2A/MLL1 in adult brain. Interacts with ARNTL/BMAL1.
CC {ECO:0000250|UniProtKB:O75530, ECO:0000269|PubMed:16224021,
CC ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:17937919,
CC ECO:0000269|PubMed:17997413, ECO:0000269|PubMed:19026780,
CC ECO:0000269|PubMed:20144788, ECO:0000269|PubMed:23970558,
CC ECO:0000269|PubMed:9742080}.
CC -!- INTERACTION:
CC Q921E6; Q7TNS8: Epop; NbExp=2; IntAct=EBI-904301, EBI-16024836;
CC Q921E6; Q61188: Ezh2; NbExp=9; IntAct=EBI-904301, EBI-904311;
CC Q921E6; Q61188-1: Ezh2; NbExp=5; IntAct=EBI-904301, EBI-15665134;
CC Q921E6; Q62315: Jarid2; NbExp=11; IntAct=EBI-904301, EBI-493592;
CC Q921E6; Q02395: Mtf2; NbExp=3; IntAct=EBI-904301, EBI-2531578;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to the
CC inactive X chromosome in cells of the early embryo and in stem cells of
CC the extraembryonic trophectoderm lineage. Recruitment to the inactive
CC X-chromosome requires XIST.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Comment=Additional isoforms may be produced by alternative initiation
CC from other non-canonical start codons but their precise positions
CC have not been unambiguously determined. {ECO:0000269|PubMed:17997413,
CC ECO:0000269|PubMed:9234727};
CC Name=1; Synonyms=EED-3;
CC IsoId=Q921E6-1; Sequence=Displayed;
CC Name=2; Synonyms=EED-1;
CC IsoId=Q921E6-2; Sequence=VSP_034694;
CC Name=3; Synonyms=EED-4;
CC IsoId=Q921E6-3; Sequence=VSP_034693;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC muscle, ovary, spleen and testis. Expressed throughout the brain.
CC {ECO:0000269|PubMed:17259173, ECO:0000269|PubMed:8805699,
CC ECO:0000269|PubMed:9234727}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed. Expressed from 5.5 dpc, and
CC expression remains high throughout development. Expression decreases
CC during differentiation of embryonic stem cells (ES cells). Expression
CC increases in prostate during prostate tumor development.
CC {ECO:0000269|PubMed:12689588, ECO:0000269|PubMed:15684044,
CC ECO:0000269|PubMed:8805699}.
CC -!- INDUCTION: Induced in embryonic stem cells (ES cells) by STAT3 and
CC POU5F1. {ECO:0000269|PubMed:18201968}.
CC -!- DOMAIN: The WD repeat domain mediates recognition of trimethylated
CC histone peptides at the consensus sequence Ala-Arg-Lys-Ser. This is
CC achieved through an aromatic cage encircling the methyllysine, and
CC involving Phe-97, Tyr-148 and Tyr-365 (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-,
CC and trimethylation of internal lysines (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Mice homozygous for a null allele of this protein (Pro-
CC 196) exhibit disrupted anterior posterior patterning of the primitive
CC streak during gastrulation and reduced numbers of trophoblast giant
CC cells. Mice homozygous for a hypomorphic allele of this protein (Asn-
CC 193) exhibit posterior transformations along the axial skeleton and
CC altered patterns of Hox gene expression.
CC -!- MISCELLANEOUS: [Isoform 2]: Translation initiates from a non-canonical
CC start codon (GUG). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat ESC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought (PubMed:9234727) to interact with
CC HNRNPK. This apparent interaction may be mediated by the translated
CC product of the 5'-UTR sequence of the 2-hybrid clone.
CC {ECO:0000305|PubMed:9234727}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38319.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC53302.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH12966.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U78103; AAB38319.1; ALT_INIT; mRNA.
DR EMBL; U97675; AAC53302.1; ALT_INIT; mRNA.
DR EMBL; AK077664; BAC36938.1; -; mRNA.
DR EMBL; AK131976; BAE20916.1; -; mRNA.
DR EMBL; AK133890; BAE21915.1; -; mRNA.
DR EMBL; BC012966; AAH12966.1; ALT_INIT; mRNA.
DR CCDS; CCDS40016.1; -. [Q921E6-1]
DR RefSeq; NP_068676.1; NM_021876.3. [Q921E6-1]
DR PDB; 2QXV; X-ray; 1.82 A; A=81-441.
DR PDBsum; 2QXV; -.
DR AlphaFoldDB; Q921E6; -.
DR SMR; Q921E6; -.
DR BioGRID; 199384; 1180.
DR CORUM; Q921E6; -.
DR DIP; DIP-29523N; -.
DR IntAct; Q921E6; 46.
DR MINT; Q921E6; -.
DR STRING; 10090.ENSMUSP00000102853; -.
DR iPTMnet; Q921E6; -.
DR PhosphoSitePlus; Q921E6; -.
DR EPD; Q921E6; -.
DR MaxQB; Q921E6; -.
DR PaxDb; Q921E6; -.
DR PeptideAtlas; Q921E6; -.
DR PRIDE; Q921E6; -.
DR ProteomicsDB; 277716; -. [Q921E6-1]
DR ProteomicsDB; 277717; -. [Q921E6-2]
DR ProteomicsDB; 277718; -. [Q921E6-3]
DR Antibodypedia; 31435; 395 antibodies from 40 providers.
DR DNASU; 13626; -.
DR Ensembl; ENSMUST00000107234; ENSMUSP00000102853; ENSMUSG00000030619. [Q921E6-1]
DR Ensembl; ENSMUST00000238981; ENSMUSP00000159149; ENSMUSG00000030619. [Q921E6-1]
DR GeneID; 13626; -.
DR KEGG; mmu:13626; -.
DR UCSC; uc009igk.2; mouse. [Q921E6-1]
DR CTD; 8726; -.
DR MGI; MGI:95286; Eed.
DR VEuPathDB; HostDB:ENSMUSG00000030619; -.
DR eggNOG; KOG1034; Eukaryota.
DR GeneTree; ENSGT00510000047334; -.
DR HOGENOM; CLU_032683_1_0_1; -.
DR InParanoid; Q921E6; -.
DR OMA; WSYDSVT; -.
DR OrthoDB; 1191277at2759; -.
DR PhylomeDB; Q921E6; -.
DR TreeFam; TF314451; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 13626; 17 hits in 80 CRISPR screens.
DR ChiTaRS; Eed; mouse.
DR EvolutionaryTrace; Q921E6; -.
DR PRO; PR:Q921E6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q921E6; protein.
DR Bgee; ENSMUSG00000030619; Expressed in animal zygote and 271 other tissues.
DR ExpressionAtlas; Q921E6; baseline and differential.
DR Genevisible; Q921E6; MM.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0001739; C:sex chromatin; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0008047; F:enzyme activator activity; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0016571; P:histone methylation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:MGI.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IGI:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037352; Polycomb_EED.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10253:SF5; PTHR10253:SF5; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Chromatin regulator;
KW Chromosome; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT CHAIN 2..441
FT /note="Polycomb protein EED"
FT /id="PRO_0000343726"
FT REPEAT 91..134
FT /note="WD 1"
FT REPEAT 142..185
FT /note="WD 2"
FT REPEAT 188..228
FT /note="WD 3"
FT REPEAT 234..275
FT /note="WD 4"
FT REPEAT 304..341
FT /note="WD 5"
FT REPEAT 359..399
FT /note="WD 6"
FT REPEAT 408..441
FT /note="WD 7"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..441
FT /note="Interaction with EZH2"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 66
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 66
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 66
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 197
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 197
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 197
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 268
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 268
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 268
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 284
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 284
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 284
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034693"
FT VAR_SEQ 1
FT /note="M -> MAGSHARPPRRLGAICDSGGSGGGGGAGSFAAGSGRACLTAVWRRPR
FT PRRQEPGGRRRNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8805699, ECO:0000303|PubMed:9234727"
FT /id="VSP_034694"
FT MUTAGEN 193
FT /note="I->N: Hypomorphic allele. Abrogates interaction with
FT EZH2 and impairs transcriptional repression."
FT /evidence="ECO:0000269|PubMed:9234727,
FT ECO:0000269|PubMed:9742080"
FT MUTAGEN 196
FT /note="L->P: Null allele. Abrogates interaction with EZH2
FT and impairs transcriptional repression."
FT /evidence="ECO:0000269|PubMed:17259173,
FT ECO:0000269|PubMed:9234727, ECO:0000269|PubMed:9742080"
FT MUTAGEN 246
FT /note="L->E: Abrogates interaction with EZH2."
FT /evidence="ECO:0000269|PubMed:17937919"
FT MUTAGEN 315
FT /note="L->E: Impairs interaction with EZH2."
FT /evidence="ECO:0000269|PubMed:17937919"
FT MUTAGEN 316
FT /note="G->A: Impairs interaction with EZH2."
FT /evidence="ECO:0000269|PubMed:17937919"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2QXV"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2QXV"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2QXV"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:2QXV"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 324..335
FT /evidence="ECO:0007829|PDB:2QXV"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2QXV"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:2QXV"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:2QXV"
SQ SEQUENCE 441 AA; 50198 MW; D2E0A5BA27C0499A CRC64;
MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT ERPDTPTNTP
NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ FNWHSKEGDP LVFATVGSNR
VTLYECHSQG EIRLLQSYVD ADADENFYTC AWTYDSNTSH PLLAVAGSRG IIRIINPITM
QCIKHYVGHG NAINELKFHP RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL
SADYDLLGEK IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS
TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV TILGRFDYSQ
CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK CTTLTHHKCG AAIRQTSFSR
DSSILIAVCD DASIWRWDRL R
