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Polycomb protein esc (Protein extra sex combs)

 ESC_DROME               Reviewed;         425 AA.
Q24338;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 170.
RecName: Full=Polycomb protein esc;
AltName: Full=Protein extra sex combs;
Name=esc; ORFNames=CG14941;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND MUTANT ESC1.
TISSUE=Embryo;
PubMed=7556071;
Gutjahr T., Frei E., Spicer C., Baumgartner S., White R.A.H., Noll M.;
"The Polycomb-group gene, extra sex combs, encodes a nuclear member of
the WD-40 repeat family.";
EMBO J. 14:4296-4306(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
INTERACTION WITH E(Z).
PubMed=9566901; DOI=10.1128/MCB.18.5.2825;
Jones C.A., Ng J., Peterson A.J., Morgan K., Simon J.A., Jones R.S.;
"The Drosophila esc and E(z) proteins are direct partners in polycomb
group-mediated repression.";
Mol. Cell. Biol. 18:2825-2834(1998).
[6]
PHOSPHORYLATION, AND MUTAGENESIS OF 210-GLY-GLY-211 AND
216-ARG--GLU-218.
PubMed=10757791; DOI=10.1128/MCB.20.9.3069-3078.2000;
Ng J., Hart C.M., Morgan K., Simon J.A.;
"A Drosophila ESC-E(Z) protein complex is distinct from other polycomb
group complexes and contains covalently modified ESC.";
Mol. Cell. Biol. 20:3069-3078(2000).
[7]
IDENTIFICATION IN A COMPLEX WITH RPD3; E(Z) AND CAF1.
PubMed=11124122;
Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.;
"The Drosophila polycomb group proteins ESC and E(Z) are present in a
complex containing the histone-binding protein p55 and the histone
deacetylase RPD3.";
Development 128:275-286(2001).
[8]
IDENTIFICATION IN A COMPLEX WITH RPD3; PHO AND E(Z), AND TRANSIENT
INTERACTION WITH THE PRC1 COMPLEX.
PubMed=11581156; DOI=10.1101/gad.208901;
Poux S., Melfi R., Pirrotta V.;
"Establishment of Polycomb silencing requires a transient interaction
between PC and ESC.";
Genes Dev. 15:2509-2514(2001).
[9]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; E(Z); RPD3 AND
SU(Z)12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
PubMed=12408863; DOI=10.1016/S0092-8674(02)00975-3;
Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
"Drosophila Enhancer of zeste/ESC complexes have a histone H3
methyltransferase activity that marks chromosomal Polycomb sites.";
Cell 111:185-196(2002).
[10]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH E(Z); CAF1 AND SU(Z)12, AND
METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
PubMed=12408864; DOI=10.1016/S0092-8674(02)00976-5;
Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A.,
Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
"Histone methyltransferase activity of a Drosophila Polycomb group
repressor complex.";
Cell 111:197-208(2002).
[11]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; E(Z) AND RPD3,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=12533794; DOI=10.1002/gene.10173;
Furuyama T., Tie F., Harte P.J.;
"Polycomb group proteins ESC and E(Z) are present in multiple distinct
complexes that undergo dynamic changes during development.";
Genesis 35:114-124(2003).
[12]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; E(Z); PCL; RPD3 AND
SU(Z)12.
PubMed=12697833; DOI=10.1128/MCB.23.9.3352-3362.2003;
Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
"A 1-megadalton ESC/E(Z) complex from Drosophila that contains
polycomblike and RPD3.";
Mol. Cell. Biol. 23:3352-3362(2003).
[13]
INTERACTION WITH CORTO.
PubMed=12771214; DOI=10.1093/nar/gkg381;
Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
"The Drosophila Corto protein interacts with Polycomb-group proteins
and the GAGA factor.";
Nucleic Acids Res. 31:2873-2882(2003).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Polycomb group (PcG) protein. While PcG proteins are
generally required to maintain the transcriptionally repressive
state of homeotic genes throughout development, this protein is
specifically required during the first 6 hours of embryogenesis to
establish the repressed state. Component of the Esc/E(z) complex,
which methylates 'Lys-9' and 'Lys-27' residues of histone H3,
leading to transcriptional repression of the affected target gene.
The Esc/E(z) complex is necessary but not sufficient for the
repression of homeotic target genes, suggesting that the
recruitment of the distinct PRC1 complex is also required.
{ECO:0000269|PubMed:7556071}.
-!- SUBUNIT: Component of the Esc/E(z) complex, composed of Caf1, esc,
E(z), Su(z)12, and possibly pho. The Esc/E(z) complex may also
associate with Pcl and Rpd3 during early embryogenesis. This
complex is distinct from the PRC1 complex, which contains many
other PcG proteins like Pc, Ph, Psc, Su(z)2. The two complexes
however cooperate and interact together during the first 3 hours
of development to establish PcG silencing. Interacts with corto in
vitro. {ECO:0000269|PubMed:11124122, ECO:0000269|PubMed:11581156,
ECO:0000269|PubMed:12408863, ECO:0000269|PubMed:12408864,
ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:12697833,
ECO:0000269|PubMed:12771214, ECO:0000269|PubMed:9566901}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-88911, EBI-88911;
Q24572:Caf1; NbExp=11; IntAct=EBI-88911, EBI-75924;
P41046:corto; NbExp=3; IntAct=EBI-88911, EBI-300379;
P42124:E(z); NbExp=22; IntAct=EBI-88911, EBI-112315;
Q94517:Rpd3; NbExp=11; IntAct=EBI-88911, EBI-302197;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12533794,
ECO:0000269|PubMed:7556071}.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Strongly expressed in the oocyte and in early embryos, then
decreases at the end of embryogenesis. Weakly expressed in third
instar larvae. Transiently required between 2 and 6 hours of
embryogenesis to establish PcG silencing and promote viable
adults. {ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:7556071}.
-!- SIMILARITY: Belongs to the WD repeat ESC family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L41867; AAA86427.1; -; Genomic_DNA.
EMBL; AE014134; AAF53124.1; -; Genomic_DNA.
EMBL; AY069796; AAL39941.1; -; mRNA.
PIR; S58672; S58672.
RefSeq; NP_477431.1; NM_058083.4.
UniGene; Dm.1948; -.
ProteinModelPortal; Q24338; -.
SMR; Q24338; -.
BioGrid; 60648; 28.
DIP; DIP-20069N; -.
IntAct; Q24338; 13.
MINT; Q24338; -.
STRING; 7227.FBpp0079907; -.
iPTMnet; Q24338; -.
PaxDb; Q24338; -.
PRIDE; Q24338; -.
EnsemblMetazoa; FBtr0080325; FBpp0079907; FBgn0000588.
GeneID; 34595; -.
KEGG; dme:Dmel_CG14941; -.
CTD; 34595; -.
FlyBase; FBgn0000588; esc.
eggNOG; KOG1034; Eukaryota.
eggNOG; ENOG410XRQI; LUCA.
GeneTree; ENSGT00510000047334; -.
InParanoid; Q24338; -.
KO; K11462; -.
OMA; HVCIAIF; -.
OrthoDB; EOG091G082Z; -.
PhylomeDB; Q24338; -.
Reactome; R-DME-212300; PRC2 methylates histones and DNA.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-3214841; PKMTs methylate histone lysines.
Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
SignaLink; Q24338; -.
GenomeRNAi; 34595; -.
PRO; PR:Q24338; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000588; -.
ExpressionAtlas; Q24338; baseline and differential.
Genevisible; Q24338; DM.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0008047; F:enzyme activator activity; IDA:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006342; P:chromatin silencing; IPI:FlyBase.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; NAS:UniProtKB.
GO; GO:0016458; P:gene silencing; IMP:FlyBase.
GO; GO:0070734; P:histone H3-K27 methylation; IMP:FlyBase.
GO; GO:0051567; P:histone H3-K9 methylation; IEA:GOC.
GO; GO:0016571; P:histone methylation; IDA:FlyBase.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0031062; P:positive regulation of histone methylation; IDA:FlyBase.
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; 5.
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;
Chromatin regulator; Complete proteome; Developmental protein;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; WD repeat.
CHAIN 1 425 Polycomb protein esc.
/FTId=PRO_0000050972.
REPEAT 71 114 WD 1.
REPEAT 126 165 WD 2.
REPEAT 168 208 WD 3.
REPEAT 214 253 WD 4.
REPEAT 284 321 WD 5.
REPEAT 340 379 WD 6.
REPEAT 388 424 WD 7.
MOD_RES 15 15 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 64 64 Y->F: In esc1; induces homeotic
transformation; when associated with R-
240.
MUTAGEN 210 211 GG->AA: Strongly reduces phosphorylation
and the interaction with E(z).
{ECO:0000269|PubMed:10757791}.
MUTAGEN 216 218 RDE->AAA: Strongly reduces
phosphorylation and the interaction with
E(z). {ECO:0000269|PubMed:10757791}.
MUTAGEN 240 240 L->R: In esc1; induces homeotic
transformation; when associated with F-
64.
SEQUENCE 425 AA; 47988 MW; 511C305E5DE86727 CRC64;
MSSDKVKNGN EPEESEESCG DESASYTTNS TTSRSKSPSS STRSKRRGRR STKSKPKSRA
AYKYDTHVKE NHGANIFGVA FNTLLGKDEP QVFATAGSNR VTVYECPRQG GMQLLHCYAD
PDPDEVFYTC AWSYDLKTSS PLLAAAGYRG VIRVIDVEQN EAVGNYIGHG QAINELKFHP
HKLQLLLSGS KDHAIRLWNI QSHVCIAILG GVEGHRDEVL SIDFNMRGDR IVSSGMDHSL
KLWCLNTPEF HHKIELSNTF SQEKSTLPFP TVTKHFPDFS TRDIHRNYVD CVQWFGNFVL
SKSCENAIVC WKPGQLHQSF EQVKPSDSSC TIIAEFEYDE CEIWFVRFGF NPWQKVIALG
NQQGKVYVWE LDPSDPEGAH MTTLHNSRSV ATVRQIAFSR DASVLVYVCD DATVWRWNRR
QTTSI


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