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Polycomb protein EED (hEED) (Embryonic ectoderm development protein) (WD protein associating with integrin cytoplasmic tails 1) (WAIT-1)

 EED_HUMAN               Reviewed;         441 AA.
O75530; A8K7V5; O00149; Q6NTH2; Q7LDA5; Q7LDG8; Q86VV2; Q9UNY7;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
18-JUL-2018, entry version 160.
RecName: Full=Polycomb protein EED {ECO:0000305};
Short=hEED;
AltName: Full=Embryonic ectoderm development protein {ECO:0000303|PubMed:28229514};
AltName: Full=WD protein associating with integrin cytoplasmic tails 1;
Short=WAIT-1;
Name=EED {ECO:0000312|HGNC:HGNC:3188};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9806832; DOI=10.1006/geno.1998.5509;
Schumacher A., Lichtarge O., Schwartz S., Magnuson T.;
"The murine Polycomb-group gene eed and its human orthologue:
functional implications of evolutionary conservation.";
Genomics 54:79-88(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
EZH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ILE-193
AND LEU-196, AND PUTATIVE ALTERNATIVE INITIATION.
PubMed=9584199; DOI=10.1128/MCB.18.6.3586;
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.;
"Characterization of interactions between the mammalian polycomb-group
proteins Enx1/EZH2 and EED suggests the existence of different
mammalian polycomb-group protein complexes.";
Mol. Cell. Biol. 18:3586-3595(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH THE
HIV-1 MA PROTEIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF 300-SER-THR-301 AND 305-HIS-TYR-308.
TISSUE=Spleen;
PubMed=9880543; DOI=10.1074/jbc.274.3.1635;
Peytavi R., Hong S.S., Gay B., d'Angeac A.D., Selig L., Benichou S.,
Benarous R., Boulanger P.;
"HEED, the product of the human homolog of the murine eed gene, binds
to the matrix protein of HIV-1.";
J. Biol. Chem. 274:1635-1645(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 15-441 (ISOFORM 1).
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-441 (ISOFORM 1), INTERACTION WITH
ITGA4; ITGAE AND ITGB7, AND TISSUE SPECIFICITY.
PubMed=9765275; DOI=10.1074/jbc.273.42.27459;
Rietzler M., Bittner M., Kolanus W., Schuster A., Holzmann B.;
"The human WD repeat protein WAIT-1 specifically interacts with the
cytoplasmic tails of beta7-integrins.";
J. Biol. Chem. 273:27459-27466(1998).
[9]
FUNCTION, AND INTERACTION WITH EZH2; HDAC1 AND HDAC2.
PubMed=10581039; DOI=10.1038/70602;
van der Vlag J., Otte A.P.;
"Transcriptional repression mediated by the human polycomb-group
protein EED involves histone deacetylation.";
Nat. Genet. 23:474-478(1999).
[10]
INTERACTION WITH EZH2 AND YY1.
PubMed=11158321; DOI=10.1128/MCB.21.4.1360-1369.2001;
Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.;
"The polycomb group protein EED interacts with YY1, and both proteins
induce neural tissue in Xenopus embryos.";
Mol. Cell. Biol. 21:1360-1369(2001).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX WITH EZH2; RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX.
PubMed=12435631; DOI=10.1101/gad.1035902;
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
Reinberg D.;
"Histone methyltransferase activity associated with a human
multiprotein complex containing the Enhancer of Zeste protein.";
Genes Dev. 16:2893-2905(2002).
[12]
SUBCELLULAR LOCATION.
PubMed=12101246; DOI=10.1128/MCB.22.15.5539-5553.2002;
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.;
"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.";
Mol. Cell. Biol. 22:5539-5553(2002).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX WITH EZH2; RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX.
PubMed=12351676; DOI=10.1126/science.1076997;
Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H3 lysine 27 methylation in Polycomb-group
silencing.";
Science 298:1039-1043(2002).
[14]
FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=14532106; DOI=10.1093/emboj/cdg542;
Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.;
"EZH2 is downstream of the pRB-E2F pathway, essential for
proliferation and amplified in cancer.";
EMBO J. 22:5323-5335(2003).
[15]
SUBCELLULAR LOCATION.
PubMed=12649488; DOI=10.1126/science.1084274;
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.;
"Role of histone H3 lysine 27 methylation in X inactivation.";
Science 300:131-135(2003).
[16]
FUNCTION, INTERACTION WITH EZH2, AND METHYLTRANSFERASE ACTIVITY OF THE
PRC2 COMPLEX.
PubMed=15385962; DOI=10.1038/sj.emboj.7600402;
Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.;
"Suz12 is essential for mouse development and for EZH2 histone
methyltransferase activity.";
EMBO J. 23:4061-4071(2004).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15231737; DOI=10.1101/gad.1200204;
Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D.,
Green R., Farnham P.J.;
"Silencing of human polycomb target genes is associated with
methylation of histone H3 Lys 27.";
Genes Dev. 18:1592-1605(2004).
[18]
CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2;
RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND
PRC3 COMPLEXES, AND PUTATIVE ALTERNATIVE INITIATION.
PubMed=15099518; DOI=10.1016/S1097-2765(04)00185-6;
Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.;
"Different EZH2-containing complexes target methylation of histone H1
or nucleosomal histone H3.";
Mol. Cell 14:183-193(2004).
[19]
FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED;
EZH2; RBBP4 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2
COMPLEX.
PubMed=15225548; DOI=10.1016/j.molcel.2004.06.020;
Cao R., Zhang Y.;
"SUZ12 is required for both the histone methyltransferase activity and
the silencing function of the EED-EZH2 complex.";
Mol. Cell 15:57-67(2004).
[20]
CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4;
RBBP7; SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4
COMPLEX, AND TISSUE SPECIFICITY.
PubMed=15684044; DOI=10.1073/pnas.0409875102;
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.;
"Composition and histone substrates of polycomb repressive group
complexes change during cellular differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005).
[21]
METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, AND INTERACTION WITH
HISTONE H1.
PubMed=16431907; DOI=10.1074/jbc.M513425200;
Martin C., Cao R., Zhang Y.;
"Substrate preferences of the EZH2 histone methyltransferase
complex.";
J. Biol. Chem. 281:8365-8370(2006).
[22]
FUNCTION, AND INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND
DNMT3B.
PubMed=16357870; DOI=10.1038/nature04431;
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.;
"The Polycomb group protein EZH2 directly controls DNA methylation.";
Nature 439:871-874(2006).
[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]
DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
PubMed=17200670; DOI=10.1038/ng1950;
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.;
"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes
for de novo methylation in cancer.";
Nat. Genet. 39:232-236(2007).
[25]
IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
PubMed=19026781; DOI=10.1016/j.molcel.2008.11.004;
Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L.,
Dynlacht B.D., Reinberg D.;
"Ezh1 and Ezh2 maintain repressive chromatin through different
mechanisms.";
Mol. Cell 32:503-518(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION OF THE PRC2 COMPLEX
WITH PHF1, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
PubMed=18086877; DOI=10.1128/MCB.01589-07;
Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.;
"Role of hPHF1 in H3K27 methylation and Hox gene silencing.";
Mol. Cell. Biol. 28:1862-1872(2008).
[27]
FUNCTION, INTERACTION WITH EZH2 AND SUZ12, INTERACTION OF THE PRC2
COMPLEX WITH PHF1, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
PubMed=18285464; DOI=10.1128/MCB.02017-07;
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.;
"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27
trimethylation in vivo.";
Mol. Cell. Biol. 28:2718-2731(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
INTERACTION WITH CDYL.
PubMed=22009739; DOI=10.1074/jbc.M111.271064;
Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.;
"Corepressor protein CDYL functions as a molecular bridge between
polycomb repressor complex 2 and repressive chromatin mark
trimethylated histone lysine 27.";
J. Biol. Chem. 286:42414-42425(2011).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
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, AND MUTAGENESIS
OF PHE-97; TYR-148; TRP-364 AND TYR-365.
PubMed=20974918; DOI=10.1073/pnas.1008937107;
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.;
"Binding of different histone marks differentially regulates the
activity and specificity of polycomb repressive complex 2 (PRC2).";
Proc. Natl. Acad. Sci. U.S.A. 107:19266-19271(2010).
[35]
INVOLVEMENT IN COGIS, AND VARIANT COGIS SER-302.
PubMed=25787343; DOI=10.1038/jhg.2015.26;
Cohen A.S., Tuysuz B., Shen Y., Bhalla S.K., Jones S.J., Gibson W.T.;
"A novel mutation in EED associated with overgrowth.";
J. Hum. Genet. 60:339-342(2015).
[36]
VARIANT COGIS TYR-258.
PubMed=27193220; DOI=10.1038/jhg.2016.51;
Cohen A.S., Gibson W.T.;
"EED-associated overgrowth in a second male patient.";
J. Hum. Genet. 61:831-834(2016).
[37]
VARIANTS COGIS SER-194 AND GLY-236.
PubMed=28475857; DOI=10.1016/j.ajhg.2017.03.010;
Childhood Overgrowth Collaboration;
Tatton-Brown K., Loveday C., Yost S., Clarke M., Ramsay E.,
Zachariou A., Elliott A., Wylie H., Ardissone A., Rittinger O.,
Stewart F., Temple I.K., Cole T., Mahamdallie S., Seal S., Ruark E.,
Rahman N.;
"Mutations in epigenetic regulation genes are a major cause of
overgrowth with intellectual disability.";
Am. J. Hum. Genet. 100:725-736(2017).
[38]
VARIANT COGIS GLY-302.
PubMed=27868325; DOI=10.1002/ajmg.a.38055;
Cooney E., Bi W., Schlesinger A.E., Vinson S., Potocki L.;
"Novel EED mutation in patient with Weaver syndrome.";
Am. J. Med. Genet. A 173:541-545(2017).
[39]
VARIANT COGIS THR-236, CHARACTERIZATION OF VARIANTS COGIS THR-236 AND
SER-302, AND FUNCTION.
PubMed=28229514; DOI=10.1002/humu.23200;
Imagawa E., Higashimoto K., Sakai Y., Numakura C., Okamoto N.,
Matsunaga S., Ryo A., Sato Y., Sanefuji M., Ihara K., Takada Y.,
Nishimura G., Saitsu H., Mizuguchi T., Miyatake S., Nakashima M.,
Miyake N., Soejima H., Matsumoto N.;
"Mutations in genes encoding polycomb repressive complex 2 subunits
cause Weaver syndrome.";
Hum. Mutat. 38:637-648(2017).
-!- 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.
{ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106,
ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737,
ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918,
ECO:0000269|PubMed:28229514, ECO:0000269|PubMed:9584199}.
-!- SUBUNIT: 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.
Interacts with ARNTL/BMAL1. Interacts with KMT2A/MLL1 (By
similarity). {ECO:0000250|UniProtKB:Q921E6,
ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:11158321,
ECO:0000269|PubMed:12351676, ECO:0000269|PubMed:12435631,
ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:16431907, ECO:0000269|PubMed:18086877,
ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:19026781,
ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:22009739,
ECO:0000269|PubMed:9584199, ECO:0000269|PubMed:9765275}.
-!- SUBUNIT: (Microbial infection) May interact with the MA protein of
HIV-1. {ECO:0000269|PubMed:9880543}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-923794, EBI-923794;
Q8IXJ9:ASXL1; NbExp=5; IntAct=EBI-923794, EBI-1646500;
Q16531:DDB1; NbExp=4; IntAct=EBI-923794, EBI-350322;
P26358:DNMT1; NbExp=3; IntAct=EBI-923794, EBI-719459;
Q9Y6K1:DNMT3A; NbExp=2; IntAct=EBI-923794, EBI-923653;
Q9UBC3:DNMT3B; NbExp=4; IntAct=EBI-923794, EBI-80125;
Q15910:EZH2; NbExp=11; IntAct=EBI-923794, EBI-530054;
Q92833-1:JARID2; NbExp=4; IntAct=EBI-923794, EBI-15825247;
Q15156:PML-RAR; NbExp=2; IntAct=EBI-923794, EBI-867256;
P63244:RACK1; NbExp=3; IntAct=EBI-923794, EBI-296739;
Q9NY59:SMPD3; NbExp=2; IntAct=EBI-923794, EBI-715400;
Q9JJY3:Smpd3 (xeno); NbExp=5; IntAct=EBI-923794, EBI-9817007;
Q15022:SUZ12; NbExp=8; IntAct=EBI-923794, EBI-1264675;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Transiently
colocalizes with XIST at inactive X chromosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Comment=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.;
Name=1;
IsoId=O75530-1; Sequence=Displayed;
Name=2;
IsoId=O75530-2; Sequence=VSP_034691;
Name=3;
IsoId=O75530-3; Sequence=VSP_034692;
-!- 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.
{ECO:0000269|PubMed:15684044, ECO:0000269|PubMed:9584199,
ECO:0000269|PubMed:9765275, ECO:0000269|PubMed:9806832,
ECO:0000269|PubMed:9880543}.
-!- DEVELOPMENTAL STAGE: Expression peaks at the G1/S phase boundary.
{ECO:0000269|PubMed:14532106}.
-!- INDUCTION: Expression is induced by E2F1, E2F2 and E2F3.
{ECO:0000269|PubMed:14532106}.
-!- 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.
{ECO:0000269|PubMed:20974918}.
-!- PTM: Methylated. Binding to histone H1 'Lys-26' promotes mono-,
di-, and trimethylation of internal lysines.
{ECO:0000269|PubMed:20974918}.
-!- DISEASE: Cohen-Gibson syndrome (COGIS) [MIM:617561]: An autosomal
dominant overgrowth disorder characterized by accelerated osseous
maturation, advanced bone age, skeletal abnormalities including
flaring of the metaphyses of the long bones, large hands with long
fingers and camptodactyly, scoliosis, cervical spine anomalies,
dysmorphic facial features, and variable intellectual disability.
{ECO:0000269|PubMed:25787343, ECO:0000269|PubMed:27193220,
ECO:0000269|PubMed:27868325, ECO:0000269|PubMed:28229514,
ECO:0000269|PubMed:28475857}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat ESC family. {ECO:0000305}.
-!- 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
(PubMed:15099518 and PubMed:15684044), although other studies have
demonstrated no methylation of 'Lys-26' of histone H1 by PRC2
(PubMed:16431907). {ECO:0000305|PubMed:16431907}.
-!- SEQUENCE CAUTION:
Sequence=AAC23685.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAC68675.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF080227; AAC95144.1; -; mRNA.
EMBL; AF070418; AAC23685.1; ALT_INIT; mRNA.
EMBL; U90651; AAD08714.1; -; mRNA.
EMBL; AF099032; AAD08815.1; -; mRNA.
EMBL; AK292120; BAF84809.1; -; mRNA.
EMBL; AP003084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW75129.1; -; Genomic_DNA.
EMBL; CH471076; EAW75130.1; -; Genomic_DNA.
EMBL; BC047672; AAH47672.1; -; mRNA.
EMBL; BC068995; AAH68995.1; -; mRNA.
EMBL; AF078933; AAC68675.1; ALT_INIT; mRNA.
CCDS; CCDS76463.1; -. [O75530-2]
CCDS; CCDS8273.1; -. [O75530-1]
RefSeq; NP_001294936.1; NM_001308007.1. [O75530-2]
RefSeq; NP_003788.2; NM_003797.4. [O75530-1]
UniGene; Hs.503510; -.
UniGene; Hs.528103; -.
PDB; 3IIW; X-ray; 1.80 A; A=77-441.
PDB; 3IIY; X-ray; 2.65 A; A=77-441.
PDB; 3IJ0; X-ray; 2.45 A; A=77-441.
PDB; 3IJ1; X-ray; 2.10 A; A=77-441.
PDB; 3IJC; X-ray; 1.95 A; A=77-441.
PDB; 3JPX; X-ray; 2.05 A; A=40-441.
PDB; 3JZG; X-ray; 2.10 A; A=40-441.
PDB; 3JZH; X-ray; 2.05 A; A=40-441.
PDB; 3JZN; X-ray; 2.60 A; A=76-441.
PDB; 3K26; X-ray; 1.58 A; A=76-441.
PDB; 3K27; X-ray; 1.76 A; A=76-441.
PDB; 4W2R; X-ray; 2.81 A; E/F=81-441.
PDB; 4X3E; X-ray; 2.30 A; A=77-441.
PDB; 5GSA; X-ray; 2.49 A; A/B=76-441.
PDB; 5H13; X-ray; 1.90 A; A=76-441.
PDB; 5H14; X-ray; 1.90 A; A/B=76-441.
PDB; 5H15; X-ray; 2.27 A; A/B=76-441.
PDB; 5H17; X-ray; 2.30 A; A=76-441.
PDB; 5H19; X-ray; 1.90 A; A=76-441.
PDB; 5H24; X-ray; 2.50 A; A/B=76-441.
PDB; 5H25; X-ray; 2.88 A; A/B=76-441.
PDB; 5HYN; X-ray; 2.95 A; B/G/L/R=77-441.
PDB; 5IJ7; X-ray; 2.62 A; E/F=81-441.
PDB; 5IJ8; X-ray; 2.99 A; E/F=81-441.
PDB; 5K0M; X-ray; 1.83 A; A=77-441.
PDB; 5LS6; X-ray; 3.47 A; B/E/H/K=77-441.
PDB; 5TTW; X-ray; 1.74 A; A/C=76-441.
PDB; 5U5H; X-ray; 1.80 A; A=76-441.
PDB; 5U5K; X-ray; 2.33 A; A=76-441.
PDB; 5U5T; X-ray; 1.60 A; A/B=76-441.
PDB; 5U62; X-ray; 1.90 A; A/B=76-441.
PDB; 5U69; X-ray; 1.28 A; A=77-441.
PDB; 5U6D; X-ray; 1.64 A; A=77-441.
PDB; 5U8A; X-ray; 1.45 A; A=77-441.
PDB; 5U8F; X-ray; 1.34 A; A=77-441.
PDB; 5WP3; X-ray; 2.55 A; A=75-441.
PDB; 5WUK; X-ray; 2.03 A; A=76-441.
PDB; 6B3W; X-ray; 3.05 A; E/F=81-441.
PDB; 6C23; EM; 3.90 A; L=1-441.
PDB; 6C24; EM; 3.50 A; L=1-441.
PDBsum; 3IIW; -.
PDBsum; 3IIY; -.
PDBsum; 3IJ0; -.
PDBsum; 3IJ1; -.
PDBsum; 3IJC; -.
PDBsum; 3JPX; -.
PDBsum; 3JZG; -.
PDBsum; 3JZH; -.
PDBsum; 3JZN; -.
PDBsum; 3K26; -.
PDBsum; 3K27; -.
PDBsum; 4W2R; -.
PDBsum; 4X3E; -.
PDBsum; 5GSA; -.
PDBsum; 5H13; -.
PDBsum; 5H14; -.
PDBsum; 5H15; -.
PDBsum; 5H17; -.
PDBsum; 5H19; -.
PDBsum; 5H24; -.
PDBsum; 5H25; -.
PDBsum; 5HYN; -.
PDBsum; 5IJ7; -.
PDBsum; 5IJ8; -.
PDBsum; 5K0M; -.
PDBsum; 5LS6; -.
PDBsum; 5TTW; -.
PDBsum; 5U5H; -.
PDBsum; 5U5K; -.
PDBsum; 5U5T; -.
PDBsum; 5U62; -.
PDBsum; 5U69; -.
PDBsum; 5U6D; -.
PDBsum; 5U8A; -.
PDBsum; 5U8F; -.
PDBsum; 5WP3; -.
PDBsum; 5WUK; -.
PDBsum; 6B3W; -.
PDBsum; 6C23; -.
PDBsum; 6C24; -.
ProteinModelPortal; O75530; -.
SMR; O75530; -.
BioGrid; 114265; 485.
CORUM; O75530; -.
DIP; DIP-36673N; -.
IntAct; O75530; 70.
MINT; O75530; -.
STRING; 9606.ENSP00000263360; -.
BindingDB; O75530; -.
ChEMBL; CHEMBL2189117; -.
GuidetoPHARMACOLOGY; 2487; -.
iPTMnet; O75530; -.
PhosphoSitePlus; O75530; -.
BioMuta; EED; -.
EPD; O75530; -.
MaxQB; O75530; -.
PaxDb; O75530; -.
PeptideAtlas; O75530; -.
PRIDE; O75530; -.
ProteomicsDB; 50068; -.
ProteomicsDB; 50069; -. [O75530-2]
ProteomicsDB; 50070; -. [O75530-3]
DNASU; 8726; -.
Ensembl; ENST00000263360; ENSP00000263360; ENSG00000074266. [O75530-1]
Ensembl; ENST00000327320; ENSP00000315587; ENSG00000074266. [O75530-3]
Ensembl; ENST00000351625; ENSP00000338186; ENSG00000074266. [O75530-2]
GeneID; 8726; -.
KEGG; hsa:8726; -.
UCSC; uc001pbp.4; human. [O75530-1]
CTD; 8726; -.
DisGeNET; 8726; -.
EuPathDB; HostDB:ENSG00000074266.17; -.
GeneCards; EED; -.
HGNC; HGNC:3188; EED.
HPA; CAB012211; -.
HPA; HPA060089; -.
HPA; HPA061140; -.
MalaCards; EED; -.
MIM; 605984; gene.
MIM; 617561; phenotype.
neXtProt; NX_O75530; -.
OpenTargets; ENSG00000074266; -.
PharmGKB; PA27624; -.
eggNOG; KOG1034; Eukaryota.
eggNOG; ENOG410XRQI; LUCA.
GeneTree; ENSGT00510000047334; -.
HOVERGEN; HBG052708; -.
InParanoid; O75530; -.
KO; K11462; -.
OMA; CTTLTHP; -.
OrthoDB; EOG091G082Z; -.
PhylomeDB; O75530; -.
TreeFam; TF314451; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; O75530; -.
SIGNOR; O75530; -.
ChiTaRS; EED; human.
EvolutionaryTrace; O75530; -.
GeneWiki; EED; -.
GenomeRNAi; 8726; -.
PRO; PR:O75530; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000074266; -.
CleanEx; HS_EED; -.
ExpressionAtlas; O75530; baseline and differential.
Genevisible; O75530; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0045120; C:pronucleus; IEA:Ensembl.
GO; GO:0001739; C:sex chromatin; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0070734; P:histone H3-K27 methylation; IEA:GOC.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IEA:Ensembl.
GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR037352; Polycomb_EED.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10253; PTHR10253; 1.
Pfam; PF00400; WD40; 2.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Chromatin regulator; Chromosome;
Complete proteome; Disease mutation; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 441 Polycomb protein EED.
/FTId=PRO_0000343725.
REPEAT 91 134 WD 1.
REPEAT 142 185 WD 2.
REPEAT 188 228 WD 3.
REPEAT 234 275 WD 4.
REPEAT 304 341 WD 5.
REPEAT 359 399 WD 6.
REPEAT 408 441 WD 7.
REGION 81 441 Interaction with EZH2. {ECO:0000250}.
REGION 149 303 Required for interaction with the matrix
protein MA of HIV-1.
REGION 301 441 Required for interaction with the matrix
protein MA of HIV-1.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:Q921E6}.
MOD_RES 55 55 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 66 66 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 66 66 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 66 66 N6-methyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 197 197 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 197 197 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 197 197 N6-methyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 268 268 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 268 268 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 268 268 N6-methyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 284 284 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 284 284 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
MOD_RES 284 284 N6-methyllysine; alternate.
{ECO:0000269|PubMed:20974918}.
VAR_SEQ 322 322 K -> KSGRAILHSHQQCMRDPVSPNLRQHL (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034691.
VAR_SEQ 401 441 Missing (in isoform 3).
{ECO:0000303|PubMed:9880543}.
/FTId=VSP_034692.
VARIANT 194 194 N -> S (in COGIS).
{ECO:0000269|PubMed:28475857}.
/FTId=VAR_079255.
VARIANT 236 236 R -> G (in COGIS).
{ECO:0000269|PubMed:28475857}.
/FTId=VAR_079256.
VARIANT 236 236 R -> T (in COGIS; decreased
trimethylation of 'Lys-27' of histone H3;
no effect on interaction with EZH2;
dbSNP:rs1131692176).
{ECO:0000269|PubMed:28229514}.
/FTId=VAR_078316.
VARIANT 258 258 H -> Y (in COGIS; dbSNP:rs1131692174).
{ECO:0000269|PubMed:27193220}.
/FTId=VAR_079257.
VARIANT 302 302 R -> G (in COGIS; dbSNP:rs1131692175).
{ECO:0000269|PubMed:27868325}.
/FTId=VAR_079258.
VARIANT 302 302 R -> S (in COGIS; decreased
trimethylation of 'Lys-27' of histone H3;
dbSNP:rs1131692173).
{ECO:0000269|PubMed:25787343,
ECO:0000269|PubMed:28229514}.
/FTId=VAR_078317.
MUTAGEN 97 97 F->A: Abolishes binding to H3K27me3.
{ECO:0000269|PubMed:20974918}.
MUTAGEN 148 148 Y->A: Abolishes binding to H3K27me3.
{ECO:0000269|PubMed:20974918}.
MUTAGEN 193 193 I->N: Impairs interaction with EZH2.
{ECO:0000269|PubMed:9584199}.
MUTAGEN 196 196 L->P: Impairs interaction with EZH2.
{ECO:0000269|PubMed:9584199}.
MUTAGEN 300 301 ST->AA: Impairs interaction with the
matrix protein MA of HIV-1.
{ECO:0000269|PubMed:9880543}.
MUTAGEN 305 308 HRNY->AAAA: Impairs interaction with the
matrix protein MA of HIV-1.
{ECO:0000269|PubMed:9880543}.
MUTAGEN 364 364 W->A: Abolishes binding to H3K27me3.
{ECO:0000269|PubMed:20974918}.
MUTAGEN 364 364 W->L: Abolishes binding to H3K27me3.
{ECO:0000269|PubMed:20974918}.
MUTAGEN 365 365 Y->A: Abolishes binding to H3K27me3.
{ECO:0000269|PubMed:20974918}.
CONFLICT 32 32 D -> E (in Ref. 8; AAC68675).
{ECO:0000305}.
CONFLICT 74 74 K -> S (in Ref. 3; AAD08714/AAD08815).
{ECO:0000305}.
CONFLICT 337 337 E -> K (in Ref. 3; AAD08714/AAD08815).
{ECO:0000305}.
CONFLICT 417 417 S -> G (in Ref. 4; BAF84809).
{ECO:0000305}.
STRAND 83 89 {ECO:0000244|PDB:5U69}.
STRAND 96 101 {ECO:0000244|PDB:5U69}.
STRAND 103 105 {ECO:0000244|PDB:5H17}.
STRAND 107 109 {ECO:0000244|PDB:5U5K}.
STRAND 111 117 {ECO:0000244|PDB:5U69}.
STRAND 120 126 {ECO:0000244|PDB:5U69}.
HELIX 128 130 {ECO:0000244|PDB:3K26}.
STRAND 132 139 {ECO:0000244|PDB:5U69}.
STRAND 147 154 {ECO:0000244|PDB:5U69}.
TURN 156 158 {ECO:0000244|PDB:5U69}.
STRAND 161 167 {ECO:0000244|PDB:5U69}.
TURN 168 170 {ECO:0000244|PDB:6C24}.
STRAND 171 175 {ECO:0000244|PDB:5U69}.
TURN 177 179 {ECO:0000244|PDB:5U69}.
STRAND 182 190 {ECO:0000244|PDB:5U69}.
STRAND 193 198 {ECO:0000244|PDB:5U69}.
STRAND 200 202 {ECO:0000244|PDB:6C24}.
STRAND 205 210 {ECO:0000244|PDB:5U69}.
STRAND 211 213 {ECO:0000244|PDB:6C24}.
STRAND 215 219 {ECO:0000244|PDB:5U69}.
TURN 220 223 {ECO:0000244|PDB:5U69}.
STRAND 224 229 {ECO:0000244|PDB:5U69}.
STRAND 231 234 {ECO:0000244|PDB:3JZN}.
STRAND 239 244 {ECO:0000244|PDB:5U69}.
STRAND 248 255 {ECO:0000244|PDB:5U69}.
STRAND 260 265 {ECO:0000244|PDB:5U69}.
HELIX 268 279 {ECO:0000244|PDB:5U69}.
HELIX 282 284 {ECO:0000244|PDB:5U69}.
STRAND 292 294 {ECO:0000244|PDB:5U69}.
STRAND 298 301 {ECO:0000244|PDB:5U69}.
STRAND 311 315 {ECO:0000244|PDB:5U69}.
STRAND 318 322 {ECO:0000244|PDB:5U69}.
STRAND 324 335 {ECO:0000244|PDB:5U69}.
HELIX 340 342 {ECO:0000244|PDB:5U69}.
STRAND 350 357 {ECO:0000244|PDB:5U69}.
STRAND 363 365 {ECO:0000244|PDB:5GSA}.
STRAND 368 370 {ECO:0000244|PDB:5U69}.
STRAND 372 374 {ECO:0000244|PDB:4W2R}.
STRAND 376 380 {ECO:0000244|PDB:5U69}.
STRAND 382 384 {ECO:0000244|PDB:4W2R}.
STRAND 386 390 {ECO:0000244|PDB:5U69}.
STRAND 393 395 {ECO:0000244|PDB:5U69}.
HELIX 396 398 {ECO:0000244|PDB:5U69}.
STRAND 400 404 {ECO:0000244|PDB:5U69}.
STRAND 413 418 {ECO:0000244|PDB:5U69}.
STRAND 422 429 {ECO:0000244|PDB:5U69}.
STRAND 432 438 {ECO:0000244|PDB:5U69}.
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


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