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Protein

Histone-lysine N-methyltransferase E(z)

Gene

E(z)

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

GO - Molecular functioni

  • chromatin binding Source: InterPro
  • DNA binding Source: UniProtKB
  • histone methyltransferase activity Source: FlyBase
  • histone methyltransferase activity (H3-K27 specific) Source: FlyBase
  • histone methyltransferase activity (H3-K9 specific) Source: FlyBase
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  • axon guidance Source: FlyBase
  • cuticle hydrocarbon biosynthetic process Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • gene silencing Source: UniProtKB
  • histone H3-K27 methylation Source: FlyBase
  • histone H3-K9 methylation Source: FlyBase
  • histone methylation Source: FlyBase
  • muscle organ development Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • neurogenesis Source: FlyBase
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_285740. PKMTs methylate histone lysines.
REACT_288099. Oxidative Stress Induced Senescence.
REACT_344008. PRC2 methylates histones and DNA.
SignaLinkiP42124.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase E(z) (EC:2.1.1.43)
Alternative name(s):
Lysine N-methyltransferase 6
Protein enhancer of zeste
Gene namesi
Name:E(z)
Synonyms:KMT6
ORF Names:CG6502
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000629. E(z).

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • ESC/E(Z) complex Source: FlyBase
  • histone methyltransferase complex Source: FlyBase
  • nuclear chromatin Source: UniProtKB
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi699 – 6991R → A or H: Strongly reduces methytransferase activity of the Esc/E(z) complex. 1 Publication
Mutagenesisi702 – 7032NH → AA: Abolishes methytransferase activity of the Esc/E(z) complex. 1 Publication
Mutagenesisi703 – 7031H → A or K: Strongly reduces methytransferase activity of the Esc/E(z) complex. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 760760Histone-lysine N-methyltransferase E(z)PRO_0000213989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei493 – 4931Phosphoserine1 Publication
Modified residuei502 – 5021Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP42124.

Expressioni

Gene expression databases

BgeeiP42124.
ExpressionAtlasiP42124. differential.
GenevisibleiP42124. DM.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bin1Q9VEX97EBI-112315,EBI-129424
Caf1Q245727EBI-112315,EBI-75924
cortoP410462EBI-112315,EBI-300379
escQ2433821EBI-112315,EBI-88911
esclQ95SW62EBI-112315,EBI-1207935
PclQ2445914EBI-112315,EBI-430086
Rpd3Q945179EBI-112315,EBI-302197

Protein-protein interaction databases

BioGridi64582. 20 interactions.
DIPiDIP-20386N.
IntActiP42124. 23 interactions.
MINTiMINT-266852.
STRINGi7227.FBpp0306192.

Structurei

3D structure databases

ProteinModelPortaliP42124.
SMRiP42124. Positions 537-742.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini443 – 49149SANTAdd
BLAST
Domaini518 – 619102CXCPROSITE-ProRule annotationAdd
BLAST
Domaini626 – 741116SETPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi505 – 5106Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi538 – 61982Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.PROSITE-ProRule annotation
Contains 1 CXC domain.PROSITE-ProRule annotation
Contains 1 SANT domain.Curated
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
InParanoidiP42124.
KOiK11430.
OrthoDBiEOG7VB2DR.
PhylomeDBiP42124.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42124-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSTKVPPEW KRRVKSEYIK IRQQKRYKRA DEIKEAWIRN WDEHNHNVQD
60 70 80 90 100
LYCESKVWQA KPYDPPHVDC VKRAEVTSYN GIPSGPQKVP ICVINAVTPI
110 120 130 140 150
PTMYTWAPTQ QNFMVEDETV LHNIPYMGDE VLDKDGKFIE ELIKNYDGKV
160 170 180 190 200
HGDKDPSFMD DAIFVELVHA LMRSYSKELE EAAPGTATAI KTETLAKSKQ
210 220 230 240 250
GEDDGVVDVD ADGESPMKLE KTDSKGDLTE VEKKETEEPL ETEDADVKPD
260 270 280 290 300
VEEVKDKLPF PAPIIFQAIS ANFPDKGTAQ ELKEKYIELT EHQDPERPQE
310 320 330 340 350
CTPNIDGIKA ESVSRERTMH SFHTLFCRRC FKYDCFLHRL QGHAGPNLQK
360 370 380 390 400
RRYPELKPFA EPCSNSCYML IDGMKEKLAA DSKTPPIDSC NEASSEDSND
410 420 430 440 450
SNSQFSNKDF NHENSKDNGL TVNSAAVAEI NSIMAGMMNI TSTQCVWTGA
460 470 480 490 500
DQALYRVLHK VYLKNYCAIA HNMLTKTCRQ VYEFAQKEDA EFSFEDLRQD
510 520 530 540 550
FTPPRKKKKK QRLWSLHCRK IQLKKDSSSN HVYNYTPCDH PGHPCDMNCS
560 570 580 590 600
CIQTQNFCEK FCNCSSDCQN RFPGCRCKAQ CNTKQCPCYL AVRECDPDLC
610 620 630 640 650
QACGADQFKL TKITCKNVCV QRGLHKHLLM APSDIAGWGI FLKEGAQKNE
660 670 680 690 700
FISEYCGEII SQDEADRRGK VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF
710 720 730 740 750
ANHSINPNCY AKVMMVTGDH RIGIFAKRAI QPGEELFFDY RYGPTEQLKF
760
VGIEREMEIV
Length:760
Mass (Da):86,935
Last modified:March 28, 2003 - v2
Checksum:i022360ED7772EB60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1873GTA → STS in AAC46462 (PubMed:8413234).Curated
Sequence conflicti194 – 1941T → P in AAC46462 (PubMed:8413234).Curated
Sequence conflicti213 – 2131G → C in AAC46462 (PubMed:8413234).Curated
Sequence conflicti223 – 2231D → E in AAC46462 (PubMed:8413234).Curated
Sequence conflicti230 – 2301E → D in AAC46462 (PubMed:8413234).Curated
Sequence conflicti240 – 2401L → V in AAC46462 (PubMed:8413234).Curated
Sequence conflicti250 – 2501D → A in AAC46462 (PubMed:8413234).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00180 mRNA. Translation: AAC46462.1.
AE014296 Genomic DNA. Translation: AAF50149.1.
AE014296 Genomic DNA. Translation: ACL83287.1.
AY051785 mRNA. Translation: AAK93209.1.
RefSeqiNP_001137932.1. NM_001144460.3.
NP_524021.2. NM_079297.3.
UniGeneiDm.2823.

Genome annotation databases

EnsemblMetazoaiFBtr0076279; FBpp0076008; FBgn0000629.
FBtr0273338; FBpp0271846; FBgn0000629.
GeneIDi39203.
KEGGidme:Dmel_CG6502.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00180 mRNA. Translation: AAC46462.1.
AE014296 Genomic DNA. Translation: AAF50149.1.
AE014296 Genomic DNA. Translation: ACL83287.1.
AY051785 mRNA. Translation: AAK93209.1.
RefSeqiNP_001137932.1. NM_001144460.3.
NP_524021.2. NM_079297.3.
UniGeneiDm.2823.

3D structure databases

ProteinModelPortaliP42124.
SMRiP42124. Positions 537-742.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64582. 20 interactions.
DIPiDIP-20386N.
IntActiP42124. 23 interactions.
MINTiMINT-266852.
STRINGi7227.FBpp0306192.

Chemistry

BindingDBiP42124.
ChEMBLiCHEMBL2169719.

Proteomic databases

PaxDbiP42124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076279; FBpp0076008; FBgn0000629.
FBtr0273338; FBpp0271846; FBgn0000629.
GeneIDi39203.
KEGGidme:Dmel_CG6502.

Organism-specific databases

CTDi39203.
FlyBaseiFBgn0000629. E(z).

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
InParanoidiP42124.
KOiK11430.
OrthoDBiEOG7VB2DR.
PhylomeDBiP42124.

Enzyme and pathway databases

ReactomeiREACT_285740. PKMTs methylate histone lysines.
REACT_288099. Oxidative Stress Induced Senescence.
REACT_344008. PRC2 methylates histones and DNA.
SignaLinkiP42124.

Miscellaneous databases

GenomeRNAii39203.
NextBioi812462.
PROiP42124.

Gene expression databases

BgeeiP42124.
ExpressionAtlasiP42124. differential.
GenevisibleiP42124. DM.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiEZ_DROME
AccessioniPrimary (citable) accession number: P42124
Secondary accession number(s): B7Z0G2, Q9VTA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 28, 2003
Last modified: June 24, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.