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P19889

- RLA0_DROME

UniProt

P19889 - RLA0_DROME

Protein

60S acidic ribosomal protein P0

Gene

RpLP0

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 141 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

    Catalytic activityi

    The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

    GO - Molecular functioni

    1. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
    2. structural constituent of ribosome Source: FlyBase

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. ribosome biogenesis Source: InterPro
    3. translational elongation Source: InterPro

    Keywords - Molecular functioni

    Lyase, Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    ReactomeiREACT_180232. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_180235. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_180780. SRP-dependent cotranslational protein targeting to membrane.
    REACT_205240. Formation of a pool of free 40S subunits.
    REACT_207008. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_209554. Eukaryotic Translation Termination.
    REACT_213100. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_222675. Peptide chain elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S acidic ribosomal protein P0
    Alternative name(s):
    Apurinic-apyrimidinic endonuclease
    DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.18)
    Gene namesi
    Name:RpLP0
    Synonyms:AP3, Ape, RpP0
    ORF Names:CG7490
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0000100. RpLP0.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. ribosome Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31731760S acidic ribosomal protein P0PRO_0000154769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei302 – 3021Phosphoserine1 Publication
    Modified residuei304 – 3041Phosphoserine; by CK1Sequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP19889.
    PRIDEiP19889.

    Expressioni

    Developmental stagei

    All stages of development. A larger transcript is restricted to the embryonic and early larval stages.

    Gene expression databases

    BgeeiP19889.

    Interactioni

    Subunit structurei

    P0 forms a pentameric complex by interaction with dimers of P1 and P2.By similarity

    Protein-protein interaction databases

    BioGridi65690. 23 interactions.
    DIPiDIP-21968N.
    IntActiP19889. 4 interactions.
    MINTiMINT-235412.

    Structurei

    3D structure databases

    ProteinModelPortaliP19889.
    SMRiP19889. Positions 5-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L10P family.Curated

    Phylogenomic databases

    eggNOGiCOG0244.
    GeneTreeiENSGT00390000017839.
    InParanoidiP19889.
    KOiK02941.
    OMAiWKKDEIE.
    OrthoDBiEOG71K63M.
    PhylomeDBiP19889.

    Family and domain databases

    InterProiIPR001790. Ribosomal_L10/acidic_P0.
    IPR001813. Ribosomal_L10/L12.
    [Graphical view]
    PfamiPF00428. Ribosomal_60s. 1 hit.
    PF00466. Ribosomal_L10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19889-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL    50
    AVVLMGKNTM MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD 100
    KLLESKVRAP ARPGAIAPLH VIIPAQNTGL GPEKTSFFQA LSIPTKISKG 150
    TIEIINDVPI LKPGDKVGAS EATLLNMLNI SPFSYGLIVN QVYDSGSIFS 200
    PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS IANGFKNLLA 250
    IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP 300
    ESESEEEDDD MGFGLFD 317
    Length:317
    Mass (Da):34,202
    Last modified:February 1, 1991 - v1
    Checksum:i36E9DD5DD8CF7E1F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25772 mRNA. Translation: AAA53372.1.
    AE014296 Genomic DNA. Translation: AAF51807.1.
    AY075528 mRNA. Translation: AAL68335.1.
    BT021447 mRNA. Translation: AAX33595.1.
    PIRiA30223. R5FFP0.
    RefSeqiNP_001262202.1. NM_001275273.1.
    NP_524211.1. NM_079487.4.
    UniGeneiDm.7933.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078481; FBpp0078134; FBgn0000100.
    FBtr0334113; FBpp0306232; FBgn0000100.
    GeneIDi40451.
    KEGGidme:Dmel_CG7490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25772 mRNA. Translation: AAA53372.1 .
    AE014296 Genomic DNA. Translation: AAF51807.1 .
    AY075528 mRNA. Translation: AAL68335.1 .
    BT021447 mRNA. Translation: AAX33595.1 .
    PIRi A30223. R5FFP0.
    RefSeqi NP_001262202.1. NM_001275273.1.
    NP_524211.1. NM_079487.4.
    UniGenei Dm.7933.

    3D structure databases

    ProteinModelPortali P19889.
    SMRi P19889. Positions 5-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65690. 23 interactions.
    DIPi DIP-21968N.
    IntActi P19889. 4 interactions.
    MINTi MINT-235412.

    Proteomic databases

    PaxDbi P19889.
    PRIDEi P19889.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078481 ; FBpp0078134 ; FBgn0000100 .
    FBtr0334113 ; FBpp0306232 ; FBgn0000100 .
    GeneIDi 40451.
    KEGGi dme:Dmel_CG7490.

    Organism-specific databases

    CTDi 6175.
    FlyBasei FBgn0000100. RpLP0.

    Phylogenomic databases

    eggNOGi COG0244.
    GeneTreei ENSGT00390000017839.
    InParanoidi P19889.
    KOi K02941.
    OMAi WKKDEIE.
    OrthoDBi EOG71K63M.
    PhylomeDBi P19889.

    Enzyme and pathway databases

    Reactomei REACT_180232. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_180235. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_180780. SRP-dependent cotranslational protein targeting to membrane.
    REACT_205240. Formation of a pool of free 40S subunits.
    REACT_207008. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_209554. Eukaryotic Translation Termination.
    REACT_213100. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_222675. Peptide chain elongation.

    Miscellaneous databases

    GenomeRNAii 40451.
    NextBioi 818852.
    PROi P19889.

    Gene expression databases

    Bgeei P19889.

    Family and domain databases

    InterProi IPR001790. Ribosomal_L10/acidic_P0.
    IPR001813. Ribosomal_L10/L12.
    [Graphical view ]
    Pfami PF00428. Ribosomal_60s. 1 hit.
    PF00466. Ribosomal_L10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Antibody to a human DNA repair protein allows for cloning of a Drosophila cDNA that encodes an apurinic endonuclease."
      Kelley M.R., Venugopal S., Harless J., Deutsch W.A.
      Mol. Cell. Biol. 9:965-973(1989) [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: Embryo.
    5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    6. "Drosophila AP3, a presumptive DNA repair protein, is homologous to human ribosomal associated protein P0."
      Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R.
      Nucleic Acids Res. 19:4297-4297(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO RIBOSOMAL PROTEIN P0.
    7. "Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity."
      Yacoub A., Kelley M.R., Deutsch W.A.
      Nucleic Acids Res. 24:4298-4303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA REPAIR ACTIVITY.
    8. "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-302 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiRLA0_DROME
    AccessioniPrimary (citable) accession number: P19889
    Secondary accession number(s): Q5BHX7, Q9VNV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 141 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. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3