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P42124

- EZ_DROME

UniProt

P42124 - EZ_DROME

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Protein

Histone-lysine N-methyltransferase E(z)

Gene
E(z), KMT6, CG6502
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

  1. chromatin binding Source: InterPro
  2. DNA binding Source: UniProtKB
  3. histone methyltransferase activity Source: FlyBase
  4. histone methyltransferase activity (H3-K27 specific) Source: FlyBase
  5. histone methyltransferase activity (H3-K9 specific) Source: FlyBase
  6. protein binding Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: FlyBase
  2. cuticle hydrocarbon biosynthetic process Source: FlyBase
  3. dendrite morphogenesis Source: FlyBase
  4. gene silencing Source: UniProtKB
  5. histone H3-K27 methylation Source: FlyBase
  6. histone H3-K9 methylation Source: FlyBase
  7. histone methylation Source: FlyBase
  8. muscle organ development Source: FlyBase
  9. negative regulation of transcription, DNA-templated Source: UniProtKB
  10. neurogenesis Source: FlyBase
  11. syncytial blastoderm mitotic cell cycle Source: FlyBase
  12. 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

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: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000629. E(z).

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. ESC/E(Z) complex Source: FlyBase
  2. histone methyltransferase complex Source: FlyBase
  3. nuclear chromatin Source: UniProtKB
  4. 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. 2 Publications
Mutagenesisi702 – 7032NH → AA: Abolishes methytransferase activity of the Esc/E(z) complex. 2 Publications
Mutagenesisi703 – 7031H → A or K: Strongly reduces methytransferase activity of the Esc/E(z) complex. 2 Publications

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.

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. 15 interactions.
MINTiMINT-266852.
STRINGi7227.FBpp0076008.

Structurei

3D structure databases

ProteinModelPortaliP42124.
SMRiP42124. Positions 537-742.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini443 – 49149SANTAdd
BLAST
Domaini518 – 619102CXCAdd
BLAST
Domaini626 – 741116SETAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi505 – 5106Nuclear localization signal Reviewed prediction

Compositional bias

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

Sequence similaritiesi

Contains 1 CXC domain.
Contains 1 SANT domain.
Contains 1 SET domain.

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00740000115009.
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

MNSTKVPPEW KRRVKSEYIK IRQQKRYKRA DEIKEAWIRN WDEHNHNVQD    50
LYCESKVWQA KPYDPPHVDC VKRAEVTSYN GIPSGPQKVP ICVINAVTPI 100
PTMYTWAPTQ QNFMVEDETV LHNIPYMGDE VLDKDGKFIE ELIKNYDGKV 150
HGDKDPSFMD DAIFVELVHA LMRSYSKELE EAAPGTATAI KTETLAKSKQ 200
GEDDGVVDVD ADGESPMKLE KTDSKGDLTE VEKKETEEPL ETEDADVKPD 250
VEEVKDKLPF PAPIIFQAIS ANFPDKGTAQ ELKEKYIELT EHQDPERPQE 300
CTPNIDGIKA ESVSRERTMH SFHTLFCRRC FKYDCFLHRL QGHAGPNLQK 350
RRYPELKPFA EPCSNSCYML IDGMKEKLAA DSKTPPIDSC NEASSEDSND 400
SNSQFSNKDF NHENSKDNGL TVNSAAVAEI NSIMAGMMNI TSTQCVWTGA 450
DQALYRVLHK VYLKNYCAIA HNMLTKTCRQ VYEFAQKEDA EFSFEDLRQD 500
FTPPRKKKKK QRLWSLHCRK IQLKKDSSSN HVYNYTPCDH PGHPCDMNCS 550
CIQTQNFCEK FCNCSSDCQN RFPGCRCKAQ CNTKQCPCYL AVRECDPDLC 600
QACGADQFKL TKITCKNVCV QRGLHKHLLM APSDIAGWGI FLKEGAQKNE 650
FISEYCGEII SQDEADRRGK VYDKYMCSFL FNLNNDFVVD ATRKGNKIRF 700
ANHSINPNCY AKVMMVTGDH RIGIFAKRAI QPGEELFFDY RYGPTEQLKF 750
VGIEREMEIV 760
Length:760
Mass (Da):86,935
Last modified:March 28, 2003 - v2
Checksum:i022360ED7772EB60
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1873GTA → STS in AAC46462. 1 Publication
Sequence conflicti194 – 1941T → P in AAC46462. 1 Publication
Sequence conflicti213 – 2131G → C in AAC46462. 1 Publication
Sequence conflicti223 – 2231D → E in AAC46462. 1 Publication
Sequence conflicti230 – 2301E → D in AAC46462. 1 Publication
Sequence conflicti240 – 2401L → V in AAC46462. 1 Publication
Sequence conflicti250 – 2501D → A in AAC46462. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U00180 mRNA. Translation: AAC46462.1 .
AE014296 Genomic DNA. Translation: AAF50149.1 .
AE014296 Genomic DNA. Translation: ACL83287.1 .
AY051785 mRNA. Translation: AAK93209.1 .
RefSeqi NP_001137932.1. NM_001144460.3.
NP_524021.2. NM_079297.3.
UniGenei Dm.2823.

3D structure databases

ProteinModelPortali P42124.
SMRi P42124. Positions 537-742.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 64582. 20 interactions.
DIPi DIP-20386N.
IntActi P42124. 15 interactions.
MINTi MINT-266852.
STRINGi 7227.FBpp0076008.

Chemistry

ChEMBLi CHEMBL2169719.

Proteomic databases

PaxDbi P42124.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0076279 ; FBpp0076008 ; FBgn0000629 .
FBtr0273338 ; FBpp0271846 ; FBgn0000629 .
GeneIDi 39203.
KEGGi dme:Dmel_CG6502.

Organism-specific databases

CTDi 39203.
FlyBasei FBgn0000629. E(z).

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00740000115009.
InParanoidi P42124.
KOi K11430.
OrthoDBi EOG7VB2DR.
PhylomeDBi P42124.

Enzyme and pathway databases

SignaLinki P42124.

Miscellaneous databases

GenomeRNAii 39203.
NextBioi 812462.
PROi P42124.

Gene expression databases

Bgeei P42124.

Family and domain databases

InterProi IPR026489. CXC_dom.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 136 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

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