Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q24338 (ESC_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycomb protein esc
Alternative name(s):
Protein extra sex combs
Gene names
Name:esc
ORF Names:CG14941
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1

Subunit structure

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. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Nucleus Ref.1 Ref.11.

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. Ref.1 Ref.11

Sequence similarities

Belongs to the WD repeat ESC family.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionChromatin regulator
Developmental protein
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing

Inferred from physical interaction Ref.7. Source: FlyBase

chromatin-mediated maintenance of transcription

Non-traceable author statement Ref.1. Source: UniProtKB

dendrite morphogenesis

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

gene silencing

Inferred from mutant phenotype PubMed 11333237. Source: FlyBase

histone H3-K27 methylation

Inferred from mutant phenotype PubMed 18276122. Source: FlyBase

histone H3-K9 methylation

Inferred by curator Ref.9. Source: GOC

histone methylation

Inferred from direct assay Ref.9Ref.10. Source: FlyBase

muscle organ development

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

neuron development

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

positive regulation of catalytic activity

Inferred from direct assay PubMed 15776017. Source: GOC

positive regulation of histone methylation

Inferred from direct assay PubMed 15776017. Source: FlyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay Ref.9Ref.10PubMed 18276122PubMed 22354997. Source: FlyBase

histone methyltransferase complex

Inferred from direct assay PubMed 16055700. Source: FlyBase

nuclear chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

polytene chromosome

Inferred from direct assay PubMed 23139817. Source: FlyBase

   Molecular_functionenzyme activator activity

Inferred from direct assay PubMed 15776017. Source: FlyBase

identical protein binding

Inferred from physical interaction Ref.7Ref.10. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Polycomb protein esc
PRO_0000050972

Regions

Repeat71 – 11444WD 1
Repeat126 – 16540WD 2
Repeat168 – 20841WD 3
Repeat214 – 25340WD 4
Repeat284 – 32138WD 5
Repeat340 – 37940WD 6
Repeat388 – 42437WD 7

Amino acid modifications

Modified residue151Phosphoserine Ref.14

Experimental info

Mutagenesis641Y → F in esc1; induces homeotic transformation; when associated with R-240.
Mutagenesis210 – 2112GG → AA: Strongly reduces phosphorylation and the interaction with E(z).
Mutagenesis216 – 2183RDE → AAA: Strongly reduces phosphorylation and the interaction with E(z). Ref.6
Mutagenesis2401L → R in esc1; induces homeotic transformation; when associated with F-64.

Sequences

Sequence LengthMass (Da)Tools
Q24338 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 511C305E5DE86727

FASTA42547,988
        10         20         30         40         50         60 
MSSDKVKNGN EPEESEESCG DESASYTTNS TTSRSKSPSS STRSKRRGRR STKSKPKSRA 

        70         80         90        100        110        120 
AYKYDTHVKE NHGANIFGVA FNTLLGKDEP QVFATAGSNR VTVYECPRQG GMQLLHCYAD 

       130        140        150        160        170        180 
PDPDEVFYTC AWSYDLKTSS PLLAAAGYRG VIRVIDVEQN EAVGNYIGHG QAINELKFHP 

       190        200        210        220        230        240 
HKLQLLLSGS KDHAIRLWNI QSHVCIAILG GVEGHRDEVL SIDFNMRGDR IVSSGMDHSL 

       250        260        270        280        290        300 
KLWCLNTPEF HHKIELSNTF SQEKSTLPFP TVTKHFPDFS TRDIHRNYVD CVQWFGNFVL 

       310        320        330        340        350        360 
SKSCENAIVC WKPGQLHQSF EQVKPSDSSC TIIAEFEYDE CEIWFVRFGF NPWQKVIALG 

       370        380        390        400        410        420 
NQQGKVYVWE LDPSDPEGAH MTTLHNSRSV ATVRQIAFSR DASVLVYVCD DATVWRWNRR 


QTTSI 

« Hide

References

« Hide 'large scale' references
[1]"The Polycomb-group gene, extra sex combs, encodes a nuclear member of the WD-40 repeat family."
Gutjahr T., Frei E., Spicer C., Baumgartner S., White R.A.H., Noll M.
EMBO J. 14:4296-4306(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTANT ESC1.
Tissue: Embryo.
[2]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"The Drosophila esc and E(z) proteins are direct partners in polycomb group-mediated repression."
Jones C.A., Ng J., Peterson A.J., Morgan K., Simon J.A., Jones R.S.
Mol. Cell. Biol. 18:2825-2834(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E(Z).
[6]"A Drosophila ESC-E(Z) protein complex is distinct from other polycomb group complexes and contains covalently modified ESC."
Ng J., Hart C.M., Morgan K., Simon J.A.
Mol. Cell. Biol. 20:3069-3078(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, MUTAGENESIS OF 210-GLY-GLY-211 AND 216-ARG--GLU-218.
[7]"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."
Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.
Development 128:275-286(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RPD3; E(Z) AND CAF1.
[8]"Establishment of Polycomb silencing requires a transient interaction between PC and ESC."
Poux S., Melfi R., Pirrotta V.
Genes Dev. 15:2509-2514(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RPD3; PHO AND E(Z), TRANSIENT INTERACTION WITH THE PRC1 COMPLEX.
[9]"Drosophila Enhancer of zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites."
Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.
Cell 111:185-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; E(Z); RPD3 AND SU(Z)12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
[10]"Histone methyltransferase activity of a Drosophila Polycomb group repressor complex."
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.
Cell 111:197-208(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH E(Z); CAF1 AND SU(Z)12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
[11]"Polycomb group proteins ESC and E(Z) are present in multiple distinct complexes that undergo dynamic changes during development."
Furuyama T., Tie F., Harte P.J.
Genesis 35:114-124(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; E(Z) AND RPD3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[12]"A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike and RPD3."
Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.
Mol. Cell. Biol. 23:3352-3362(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; E(Z); PCL; RPD3 AND SU(Z)12.
[13]"The Drosophila Corto protein interacts with Polycomb-group proteins and the GAGA factor."
Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.
Nucleic Acids Res. 31:2873-2882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CORTO.
[14]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41867 Genomic DNA. Translation: AAA86427.1.
AE014134 Genomic DNA. Translation: AAF53124.1.
AY069796 mRNA. Translation: AAL39941.1.
PIRS58672.
RefSeqNP_477431.1. NM_058083.4.
UniGeneDm.1948.

3D structure databases

ProteinModelPortalQ24338.
SMRQ24338. Positions 61-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60648. 21 interactions.
DIPDIP-20069N.
IntActQ24338. 9 interactions.
MINTMINT-266724.
STRING7227.FBpp0079907.

Proteomic databases

PaxDbQ24338.
PRIDEQ24338.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080325; FBpp0079907; FBgn0000588.
GeneID34595.
KEGGdme:Dmel_CG14941.

Organism-specific databases

CTD34595.
FlyBaseFBgn0000588. esc.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00510000047334.
InParanoidQ24338.
KOK11462.
OMADECEIWF.
OrthoDBEOG7WQ7S8.
PhylomeDBQ24338.

Enzyme and pathway databases

SignaLinkQ24338.

Gene expression databases

BgeeQ24338.

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. 5 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

GenomeRNAi34595.
NextBio789223.

Entry information

Entry nameESC_DROME
AccessionPrimary (citable) accession number: Q24338
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase