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P42124

- EZ_DROME

UniProt

P42124 - EZ_DROME

Protein

Histone-lysine N-methyltransferase E(z)

Gene

E(z)

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (28 Mar 2003)
      Previous versions | rss
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    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

    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

    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. 1 Publication
    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 137 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