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P42124 (EZ_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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:
Histone-lysine N-methyltransferase E(z)

EC=2.1.1.43
Alternative name(s):
Lysine N-methyltransferase 6
Protein enhancer of zeste
Gene names
Name:E(z)
Synonyms:KMT6
ORF Names:CG6502
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polycomb group (PcG) protein. Catalytic subunit of the Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. 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. 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.

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

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

Subcellular location

Nucleus Ref.5.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.

Contains 1 CXC domain.

Contains 1 SANT domain.

Contains 1 SET domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Developmental protein
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from mutant phenotype PubMed 16495309. Source: FlyBase

cuticle hydrocarbon biosynthetic process

Inferred from mutant phenotype PubMed 10663138. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

gene silencing

Non-traceable author statement Ref.9. Source: UniProtKB

histone H3-K27 methylation

Inferred from direct assay Ref.9. Source: FlyBase

histone H3-K9 methylation

Inferred from direct assay Ref.9. Source: FlyBase

histone methylation

Inferred from direct assay Ref.10. Source: FlyBase

muscle organ development

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11571280Ref.12. Source: UniProtKB

neurogenesis

Inferred from mutant phenotype PubMed 17287254. Source: FlyBase

syncytial blastoderm mitotic cell cycle

Inferred from mutant phenotype PubMed 16388795. 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

Non-traceable author statement Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7Ref.9. Source: FlyBase

   Molecular_functionDNA binding

Non-traceable author statement Ref.9. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: InterPro

histone methyltransferase activity

Inferred from direct assay PubMed 18693240. Source: FlyBase

histone methyltransferase activity (H3-K27 specific)

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

histone methyltransferase activity (H3-K9 specific)

Inferred from direct assay Ref.9. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 11571280Ref.12Ref.13. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11571280Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 760760Histone-lysine N-methyltransferase E(z)
PRO_0000213989

Regions

Domain443 – 49149SANT
Domain518 – 619102CXC
Domain626 – 741116SET
Motif505 – 5106Nuclear localization signal Potential
Compositional bias538 – 61982Cys-rich

Amino acid modifications

Modified residue4931Phosphoserine Ref.14
Modified residue5021Phosphothreonine Ref.14

Experimental info

Mutagenesis6991R → A or H: Strongly reduces methytransferase activity of the Esc/E(z) complex. Ref.9 Ref.10
Mutagenesis702 – 7032NH → AA: Abolishes methytransferase activity of the Esc/E(z) complex. Ref.9 Ref.10
Mutagenesis7031H → A or K: Strongly reduces methytransferase activity of the Esc/E(z) complex. Ref.9 Ref.10
Sequence conflict185 – 1873GTA → STS in AAC46462. Ref.1
Sequence conflict1941T → P in AAC46462. Ref.1
Sequence conflict2131G → C in AAC46462. Ref.1
Sequence conflict2231D → E in AAC46462. Ref.1
Sequence conflict2301E → D in AAC46462. Ref.1
Sequence conflict2401L → V in AAC46462. Ref.1
Sequence conflict2501D → A in AAC46462. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42124 [UniParc].

Last modified March 28, 2003. Version 2.
Checksum: 022360ED7772EB60

FASTA76086,935
        10         20         30         40         50         60 
MNSTKVPPEW KRRVKSEYIK IRQQKRYKRA DEIKEAWIRN WDEHNHNVQD LYCESKVWQA 

        70         80         90        100        110        120 
KPYDPPHVDC VKRAEVTSYN GIPSGPQKVP ICVINAVTPI PTMYTWAPTQ QNFMVEDETV 

       130        140        150        160        170        180 
LHNIPYMGDE VLDKDGKFIE ELIKNYDGKV HGDKDPSFMD DAIFVELVHA LMRSYSKELE 

       190        200        210        220        230        240 
EAAPGTATAI KTETLAKSKQ GEDDGVVDVD ADGESPMKLE KTDSKGDLTE VEKKETEEPL 

       250        260        270        280        290        300 
ETEDADVKPD VEEVKDKLPF PAPIIFQAIS ANFPDKGTAQ ELKEKYIELT EHQDPERPQE 

       310        320        330        340        350        360 
CTPNIDGIKA ESVSRERTMH SFHTLFCRRC FKYDCFLHRL QGHAGPNLQK RRYPELKPFA 

       370        380        390        400        410        420 
EPCSNSCYML IDGMKEKLAA DSKTPPIDSC NEASSEDSND SNSQFSNKDF NHENSKDNGL 

       430        440        450        460        470        480 
TVNSAAVAEI NSIMAGMMNI TSTQCVWTGA DQALYRVLHK VYLKNYCAIA HNMLTKTCRQ 

       490        500        510        520        530        540 
VYEFAQKEDA EFSFEDLRQD FTPPRKKKKK QRLWSLHCRK IQLKKDSSSN HVYNYTPCDH 

       550        560        570        580        590        600 
PGHPCDMNCS CIQTQNFCEK FCNCSSDCQN RFPGCRCKAQ CNTKQCPCYL AVRECDPDLC 

       610        620        630        640        650        660 
QACGADQFKL TKITCKNVCV QRGLHKHLLM APSDIAGWGI FLKEGAQKNE FISEYCGEII 

       670        680        690        700        710        720 
SQDEADRRGK VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF ANHSINPNCY AKVMMVTGDH 

       730        740        750        760 
RIGIFAKRAI QPGEELFFDY RYGPTEQLKF VGIEREMEIV 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila Polycomb-group gene Enhancer of zeste contains a region with sequence similarity to trithorax."
Jones R.S., Gelbart W.M.
Mol. Cell. Biol. 13:6357-6366(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Ovary.
[5]"The Drosophila Enhancer of zeste gene encodes a chromosomal protein: examination of wild-type and mutant protein distribution."
Carrington E.A., Jones R.S.
Development 122:4073-4083(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"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 ESC.
[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 AN ESC/E(Z) COMPLEX WITH CAF1; ESC AND RPD3.
[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 ESC, 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; ESC; RPD3 AND SU(Z)12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX, MUTAGENESIS OF 702-ASN-HIS-703.
[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 CAF1; ESC AND SU(Z)12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX, MUTAGENESIS OF ARG-699 AND HIS-703.
[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; ESC AND RPD3.
[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; ESC; 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-493 AND THR-502, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00180 mRNA. Translation: AAC46462.1.
AE014296 Genomic DNA. Translation: AAF50149.1.
AE014296 Genomic DNA. Translation: ACL83287.1.
AY051785 mRNA. Translation: AAK93209.1.
RefSeqNP_001137932.1. NM_001144460.3.
NP_524021.2. NM_079297.3.
UniGeneDm.2823.

3D structure databases

ProteinModelPortalP42124.
SMRP42124. Positions 537-742.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64582. 20 interactions.
DIPDIP-20386N.
IntActP42124. 15 interactions.
MINTMINT-266852.
STRING7227.FBpp0076008.

Chemistry

ChEMBLCHEMBL2169719.

Proteomic databases

PaxDbP42124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076279; FBpp0076008; FBgn0000629.
FBtr0273338; FBpp0271846; FBgn0000629.
GeneID39203.
KEGGdme:Dmel_CG6502.

Organism-specific databases

CTD39203.
FlyBaseFBgn0000629. E(z).

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00740000115009.
InParanoidP42124.
KOK11430.
OrthoDBEOG7VB2DR.
PhylomeDBP42124.

Enzyme and pathway databases

SignaLinkP42124.

Gene expression databases

BgeeP42124.

Family and domain databases

InterProIPR026489. CXC_dom.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view]
PfamPF00856. SET. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39203.
NextBio812462.
PROP42124.

Entry information

Entry nameEZ_DROME
AccessionPrimary (citable) accession number: P42124
Secondary accession number(s): B7Z0G2, Q9VTA3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 28, 2003
Last modified: July 9, 2014
This is version 136 of the entry and version 2 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