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Q9VB08

- RING1_DROME

UniProt

Q9VB08 - RING1_DROME

Protein

E3 ubiquitin-protein ligase RING1

Gene

Sce

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 106 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-118' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-118' ubiquitination gives a specific tag for epigenetic transcriptional repression. Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. PcG complexes act via modification of histones, such as methylation, deacetylation, ubiquitination rendering chromatin heritably changed in its expressibility. May play a role in meiotic sister chromatid cohesion.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri46 – 8641RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin silencing Source: UniProtKB
    2. germarium-derived female germ-line cyst encapsulation Source: FlyBase
    3. histone H2A monoubiquitination Source: FlyBase
    4. meiotic nuclear division Source: UniProtKB-KW
    5. multicellular organismal development Source: UniProtKB
    6. neurogenesis Source: FlyBase
    7. ovarian follicle cell stalk formation Source: FlyBase
    8. sex comb development Source: UniProtKB
    9. sister chromatid cohesion Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Cell cycle, Meiosis, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RING1 (EC:6.3.2.-)
    Alternative name(s):
    Sex comb extra protein
    dRING protein
    dRING1
    Gene namesi
    Name:Sce
    ORF Names:CG5595
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003330. Sce.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Colocalizes with ubiquitinated histone H2A. Colocalizes with Pc, Pcl, Psc, ph at many sites on polytene chromosomes. Colocalizes with ORD on the chromatin of primary spermatocytes during G2 of meiosis.

    GO - Cellular componenti

    1. cohesin complex Source: UniProtKB
    2. nucleolus Source: FlyBase
    3. nucleus Source: FlyBase
    4. PRC1 complex Source: FlyBase

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651R → C in Sce33M2; induces extra sex combs due to derepression of Ubx homeotic gene and abolishes ability to ubiquitinate histone H2A. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435E3 ubiquitin-protein ligase RING1PRO_0000056113Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021Phosphoserine1 Publication
    Modified residuei266 – 2661Phosphoserine1 Publication
    Modified residuei267 – 2671Phosphothreonine1 Publication
    Modified residuei269 – 2691Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9VB08.
    PRIDEiQ9VB08.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in syncytial blastoderm embryos. Ubiquitously expressed until stage 11. Then, it is only expressed in the neuroectoderm. Later in embryonic development, it is only expressed in the CNS. In larvae, it is expressed in all imaginal disks. Expressed in the male and female gonads.2 Publications

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiQ9VB08.

    Interactioni

    Subunit structurei

    Interacts with ORD. Component of PRC1 complex, which contains many PcG proteins like Pc, ph, Scm, Psc, Sce and also chromatin remodeling proteins such as histone deacetylases. This complex is distinct from the Esc/E(z) complex, at least composed of esc, E(z), Su(z)12, Rpd3 and Caf1. The two complexes however cooperate and interact together during the first 3 hours of development to establish PcG silencing.4 Publications

    Protein-protein interaction databases

    BioGridi68209. 16 interactions.
    DIPiDIP-21764N.
    IntActiQ9VB08. 3 interactions.
    MINTiMINT-860974.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VB08.
    SMRiQ9VB08. Positions 10-109, 326-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi158 – 17114Gly-richAdd
    BLAST
    Compositional biasi222 – 29978Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri46 – 8641RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG324386.
    GeneTreeiENSGT00390000016977.
    InParanoidiQ9VB08.
    KOiK10695.
    OMAiSDCIITA.
    OrthoDBiEOG7NGQC3.
    PhylomeDBiQ9VB08.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VB08-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSLDPAPNK TWELSLYELQ RKPQEVITDS TEIAVSPRSL HSELMCPICL    50
    DMLKKTMTTK ECLHRFCSDC IVTALRSGNK ECPTCRKKLV SKRSLRADPN 100
    FDLLISKIYP SREEYEAIQE KVMAKFNQTQ SQQALVNSIN EGIKLQSQNR 150
    PQRFRTKGGG GGGGGGGNGN GAANVAAPPA PGAPTAVGRN ASNQMHVHDT 200
    ASNDSNSNTN SIDRENRDPG HSGTSAASAI TSASNAAPSS SANSGASTSA 250
    TRMQVDDASN PPSVRSTPSP VPSNSSSSKP KRAMSVLTSE RSEESESDSQ 300
    MDCRTEGDSN IDTEGEGNGE LGINDEIELV FKPHPTEMSA DNQLIRALKE 350
    NCVRYIKTTA NATVDHLSKY LAMRLTLDLG ADLPEACRVL NFCIYVAPQP 400
    QQLVILNGNQ TLHQVNDKFW KVNKPMEMYY SWKKT 435
    Length:435
    Mass (Da):47,256
    Last modified:May 1, 2000 - v1
    Checksum:i5DC5834BD3CC516C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761A → P in CAA04797. 1 PublicationCurated
    Sequence conflicti201 – 2011A → P in CAA04797. 1 PublicationCurated
    Sequence conflicti279 – 2791K → N in CAA04797. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001514 mRNA. Translation: CAA04797.1.
    AE014297 Genomic DNA. Translation: AAF56737.1.
    AY058535 mRNA. Translation: AAL13764.1.
    RefSeqiNP_477509.1. NM_058161.4.
    UniGeneiDm.4170.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085245; FBpp0084614; FBgn0003330.
    GeneIDi43327.
    KEGGidme:Dmel_CG5595.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001514 mRNA. Translation: CAA04797.1 .
    AE014297 Genomic DNA. Translation: AAF56737.1 .
    AY058535 mRNA. Translation: AAL13764.1 .
    RefSeqi NP_477509.1. NM_058161.4.
    UniGenei Dm.4170.

    3D structure databases

    ProteinModelPortali Q9VB08.
    SMRi Q9VB08. Positions 10-109, 326-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68209. 16 interactions.
    DIPi DIP-21764N.
    IntActi Q9VB08. 3 interactions.
    MINTi MINT-860974.

    Proteomic databases

    PaxDbi Q9VB08.
    PRIDEi Q9VB08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085245 ; FBpp0084614 ; FBgn0003330 .
    GeneIDi 43327.
    KEGGi dme:Dmel_CG5595.

    Organism-specific databases

    CTDi 43327.
    FlyBasei FBgn0003330. Sce.

    Phylogenomic databases

    eggNOGi NOG324386.
    GeneTreei ENSGT00390000016977.
    InParanoidi Q9VB08.
    KOi K10695.
    OMAi SDCIITA.
    OrthoDBi EOG7NGQC3.
    PhylomeDBi Q9VB08.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GenomeRNAii 43327.
    NextBioi 833362.
    PROi Q9VB08.

    Gene expression databases

    Bgeei Q9VB08.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Dyer M.J., Abdul-Rauf M., White R.A.H.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      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. "Reconstitution of a functional core polycomb repressive complex."
      Francis N.J., Saurin A.J., Shao Z., Kingston R.E.
      Mol. Cell 8:545-556(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A PCG COMPLEX WITH PC; PH AND PSC.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    6. "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins."
      Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.
      Nature 412:655-660(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC1 COMPLEX WITH PC; PSC AND PH.
    7. "Molecular and genetic analysis of the Polycomb group gene Sex combs extra/Ring in Drosophila."
      Fritsch C., Beuchle D., Mueller J.
      Mech. Dev. 120:949-954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTANT SCE33M2.
    8. "The Drosophila Polycomb group gene Sex combs extra encodes the ortholog of mammalian Ring1 proteins."
      Gorfinkiel N., Fanti L., Melgar T., Garcia E., Pimpinelli S., Guerrero I., Vidal M.
      Mech. Dev. 121:449-462(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH PSC.
    9. "Chromatin compaction by a polycomb group protein complex."
      Francis N.J., Kingston R.E., Woodcock C.L.
      Science 306:1574-1577(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE PCG COMPLEX.
    10. "Propagation of silencing; recruitment and repression of naive chromatin in trans by polycomb repressed chromatin."
      Lavigne M., Francis N.J., King I.F., Kingston R.E.
      Mol. Cell 13:415-425(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE PCG COMPLEX.
    11. "Role of histone H2A ubiquitination in Polycomb silencing."
      Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
      Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-65.
    12. "A proposed role for the Polycomb group protein dRING in meiotic sister-chromatid cohesion."
      Balicky E.M., Young L., Orr-Weaver T.L., Bickel S.E.
      Chromosoma 112:231-239(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ORD.
    13. "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-202; SER-266; THR-267 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiRING1_DROME
    AccessioniPrimary (citable) accession number: Q9VB08
    Secondary accession number(s): O18380
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 106 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3