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Q32KD2

- SETB1_DROME

UniProt

Q32KD2 - SETB1_DROME

Protein

Histone-lysine N-methyltransferase eggless

Gene

egg

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 82 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 in ovary. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting Su(var)205/HP1 to methylated histones. Plays a central role during oogenesis.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi948 – 9481Zinc 1By similarity
    Metal bindingi948 – 9481Zinc 2By similarity
    Metal bindingi950 – 9501Zinc 1By similarity
    Metal bindingi954 – 9541Zinc 1By similarity
    Metal bindingi954 – 9541Zinc 3By similarity
    Metal bindingi960 – 9601Zinc 1By similarity
    Metal bindingi962 – 9621Zinc 2By similarity
    Metal bindingi1000 – 10001Zinc 2By similarity
    Metal bindingi1000 – 10001Zinc 3By similarity
    Metal bindingi1004 – 10041Zinc 2By similarity
    Metal bindingi1006 – 10061Zinc 3By similarity
    Metal bindingi1010 – 10101Zinc 3By similarity
    Binding sitei1069 – 10691S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei1071 – 10711S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei1191 – 11911S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi1197 – 11971Zinc 4By similarity
    Metal bindingi1250 – 12501Zinc 4By similarity
    Metal bindingi1252 – 12521Zinc 4By similarity
    Metal bindingi1257 – 12571Zinc 4By similarity

    GO - Molecular functioni

    1. double-stranded methylated DNA binding Source: FlyBase
    2. histone-lysine N-methyltransferase activity Source: UniProtKB
    3. histone methyltransferase activity (H3-K9 specific) Source: FlyBase
    4. protein binding Source: FlyBase
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA hypermethylation Source: FlyBase
    2. female germ-line stem cell asymmetric division Source: FlyBase
    3. histone H3-K9 methylation Source: FlyBase
    4. instar larval or pupal development Source: FlyBase
    5. negative regulation of gene expression, epigenetic Source: FlyBase
    6. negative regulation of transcription, DNA-templated Source: FlyBase
    7. negative regulation of transcription during meiosis Source: UniProtKB
    8. oogenesis Source: UniProtKB
    9. regulation of gene expression, epigenetic Source: FlyBase
    10. regulation of gene silencing Source: FlyBase
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. wing disc development Source: FlyBase

    Keywords - Molecular functioni

    Chromatin regulator, Developmental protein, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Differentiation, Oogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase eggless (EC:2.1.1.43)
    Alternative name(s):
    SETDB1 homolog
    Gene namesi
    Name:egg
    ORF Names:CG12196
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0086908. egg.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. nucleus Source: UniProtKB
    3. polytene chromosome Source: FlyBase

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Oogenesis arrests at early stages. This arrest is accompanied by reduced proliferation of somatic cells required for egg chamber formation, and by apoptosis in both germ and somatic cell populations.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12621262Histone-lysine N-methyltransferase egglessPRO_0000281822Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei217 – 2171Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ32KD2.
    PRIDEiQ32KD2.

    Expressioni

    Tissue specificityi

    Expressed in ovary (at protein level).1 Publication

    Developmental stagei

    Present most strongly at early stages of oogenesis, in germ cells in the germarium. Present in germ stem cells and dividing germline cyst cells. Weakly or not expressed in somatic cells at the tip of the germarium, including the terminal filament, inner sheath cells, or cap cells, but it is present at low levels in somatic cells in regions 2 and 3 of the germarium, including the prefollicular cells and the follicle cells of stage 1 egg chambers. Soon after egg chambers budd off the germarium, levels increase in the follicle cells. By mid-oogenesis it decreases in the nurse cells, while levels continued to increase in the follicle cells (at protein level).1 Publication

    Gene expression databases

    BgeeiQ32KD2.

    Interactioni

    Protein-protein interaction databases

    BioGridi63532. 12 interactions.
    DIPiDIP-46503N.
    IntActiQ32KD2. 2 interactions.
    MINTiMINT-749161.

    Structurei

    3D structure databases

    ProteinModelPortaliQ32KD2.
    SMRiQ32KD2. Positions 498-680, 828-881, 896-1257.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini529 – 60274Tudor 1Add
    BLAST
    Domaini629 – 68658Tudor 2Add
    BLAST
    Domaini818 – 88467MBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini946 – 101873Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1021 – 1237217SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1246 – 126217Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1031 – 10333S-adenosyl-L-methionine bindingBy similarity
    Regioni1194 – 11952S-adenosyl-L-methionine bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili353 – 42068Sequence AnalysisAdd
    BLAST

    Domaini

    In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
    Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation
    Contains 2 Tudor domains.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00750000117355.
    KOiK11421.
    OMAiCKCKKNC.
    OrthoDBiEOG7ZD1TG.
    PhylomeDBiQ32KD2.

    Family and domain databases

    Gene3Di3.30.890.10. 1 hit.
    InterProiIPR016177. DNA-bd_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF01429. MBD. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF54171. SSF54171. 1 hit.
    PROSITEiPS50982. MBD. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q32KD2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA     50
    AKDVEIEELT HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT 100
    KAIASSPVLV AVDSDSSVEL IESPVKFSSA NESEKDPPKP DAVNEAAAKE 150
    AEEMTDSSIS SPTSESFPEK DEKTNKENEQ EPPGMEVDQD VEESISRPAE 200
    EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT APKAAEDEKL 250
    NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL 300
    CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK 350
    QPEKSDFSKN KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL 400
    ERQFALADVE LEKVQTTADK MHCALYNSCP VAHKHLPTLD IEPSDYVHEV 450
    PPPGEIVRPP IQLGETYYAV KNKAIASWVS IKVIEFTEST AINGNTMKSY 500
    KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF DGTTLSRGKD 550
    KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE 600
    KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI 650
    DIDCSLVLMQ FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP 700
    RRTEPFIRYT KEMESSSKVN QQMRAFARKS SASAQNNALA AASSAATPAG 750
    GRTNAGGVST SNSASAVRHL NNSTIYVDDE NRPKGHVVYF TAKRNLPPKM 800
    YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK TKKSVVYKGP 850
    CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD 900
    ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC 950
    EDDCSDKSKC ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC 1000
    NSRCKCKKNC LNRVVQFSLE MKLQVFKTSN RGWGLRCVND IPKGAFICIY 1050
    AGHLLTETMA NEGGQDAGDE YFADLDYIEV AEQLKEGYES EVDHSDPDAE 1100
    EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS SELDSQERAV 1150
    INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN 1200
    LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC 1250
    QCGAPNCRLR LL 1262
    Length:1,262
    Mass (Da):141,946
    Last modified:December 6, 2005 - v1
    Checksum:iA89DFF1CC6FCED1C
    GO

    Sequence cautioni

    The sequence AAK93223.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAN71064.2 differs from that shown. Reason: Erroneous initiation.
    The sequence ABC86335.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF47268.3.
    BT023947 mRNA. Translation: ABB36451.1.
    BT024273 mRNA. Translation: ABC86335.1. Different initiation.
    AY051799 mRNA. Translation: AAK93223.1. Different initiation.
    BT001309 mRNA. Translation: AAN71064.2. Different initiation.
    RefSeqiNP_611966.3. NM_138122.5.
    UniGeneiDm.14397.

    Genome annotation databases

    EnsemblMetazoaiFBtr0112777; FBpp0111689; FBgn0086908.
    GeneIDi37962.
    KEGGidme:Dmel_CG12196.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF47268.3 .
    BT023947 mRNA. Translation: ABB36451.1 .
    BT024273 mRNA. Translation: ABC86335.1 . Different initiation.
    AY051799 mRNA. Translation: AAK93223.1 . Different initiation.
    BT001309 mRNA. Translation: AAN71064.2 . Different initiation.
    RefSeqi NP_611966.3. NM_138122.5.
    UniGenei Dm.14397.

    3D structure databases

    ProteinModelPortali Q32KD2.
    SMRi Q32KD2. Positions 498-680, 828-881, 896-1257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63532. 12 interactions.
    DIPi DIP-46503N.
    IntActi Q32KD2. 2 interactions.
    MINTi MINT-749161.

    Proteomic databases

    PaxDbi Q32KD2.
    PRIDEi Q32KD2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0112777 ; FBpp0111689 ; FBgn0086908 .
    GeneIDi 37962.
    KEGGi dme:Dmel_CG12196.

    Organism-specific databases

    CTDi 37962.
    FlyBasei FBgn0086908. egg.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00750000117355.
    KOi K11421.
    OMAi CKCKKNC.
    OrthoDBi EOG7ZD1TG.
    PhylomeDBi Q32KD2.

    Miscellaneous databases

    GenomeRNAii 37962.
    NextBioi 806265.

    Gene expression databases

    Bgeei Q32KD2.

    Family and domain databases

    Gene3Di 3.30.890.10. 1 hit.
    InterProi IPR016177. DNA-bd_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF01429. MBD. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54171. SSF54171. 1 hit.
    PROSITEi PS50982. MBD. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 378-1262.
      Strain: Berkeley.
      Tissue: Embryo and Testis.
    5. "Histone methylation is required for oogenesis in Drosophila."
      Clough E., Moon W., Wang S., Smith K., Hazelrigg T.
      Development 134:157-165(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    6. "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-215 AND THR-217, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiSETB1_DROME
    AccessioniPrimary (citable) accession number: Q32KD2
    Secondary accession number(s): Q29QW7
    , Q8IHC9, Q8MMD1, Q960X1, Q9W110
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 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