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P05317

- RLA0_YEAST

UniProt

P05317 - RLA0_YEAST

Protein

60S acidic ribosomal protein P0

Gene

RPP0

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. large ribosomal subunit rRNA binding Source: SGD
    2. protein binding Source: IntAct
    3. structural constituent of ribosome Source: SGD

    GO - Biological processi

    1. cytoplasmic translation Source: SGD
    2. ribosomal large subunit assembly Source: SGD
    3. translational elongation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32417-MONOMER.
    ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
    REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_217188. Formation of a pool of free 40S subunits.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S acidic ribosomal protein P0
    Short name:
    A0
    Alternative name(s):
    L10E
    Gene namesi
    Name:RPP0
    Synonyms:L10E, RPA0, RPL10E, RPLA0
    Ordered Locus Names:YLR340W
    ORF Names:L8300.8
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004332. RPP0.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytosolic large ribosomal subunit Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31231260S acidic ribosomal protein P0PRO_0000154786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681Phosphoserine1 Publication
    Modified residuei302 – 3021Phosphoserine; by CK24 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP05317.
    PaxDbiP05317.
    PeptideAtlasiP05317.

    2D gel databases

    SWISS-2DPAGEP05317.

    Expressioni

    Gene expression databases

    GenevestigatoriP05317.

    Interactioni

    Subunit structurei

    Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S). The 5 acidic ribosomal P-proteins form the stalk structure of the 60S subunit. They are organized as a pentameric complex in which P0 interacts with 2 heterodimers, P1A-P2B and P1B-P2A. P0 directly interacts with 28S rRNA. Interacts with YFL034W.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EFT2P323242EBI-15447,EBI-6333
    RPP1AP053184EBI-15447,EBI-15452
    RPP1BP106223EBI-15447,EBI-15460
    RPP2AP053192EBI-15447,EBI-15456

    Protein-protein interaction databases

    BioGridi31602. 149 interactions.
    DIPiDIP-1582N.
    IntActiP05317. 267 interactions.
    MINTiMINT-384116.
    STRINGi4932.YLR340W.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IZSelectron microscopy-s1-312[»]
    3J16electron microscopy-G1-312[»]
    3O5HX-ray4.00M1-312[»]
    3U5IX-ray3.00q1-312[»]
    4B6Aelectron microscopy8.10q1-312[»]
    4BYNelectron microscopy4.30q1-312[»]
    4BYUelectron microscopy6.60q1-237[»]
    ProteinModelPortaliP05317.
    SMRiP05317. Positions 3-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 23032Interaction with P1A-P2BAdd
    BLAST
    Regioni231 – 25828Interaction with P1B-P2AAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein L10P family.Curated

    Phylogenomic databases

    eggNOGiCOG0244.
    GeneTreeiENSGT00390000017839.
    HOGENOMiHOG000210987.
    KOiK02941.
    OMAiLATEYSF.
    OrthoDBiEOG7PS1RV.

    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.

    P05317-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGIREKKAE YFAKLREYLE EYKSLFVVGV DNVSSQQMHE VRKELRGRAV    50
    VLMGKNTMVR RAIRGFLSDL PDFEKLLPFV KGNVGFVFTN EPLTEIKNVI 100
    VSNRVAAPAR AGAVAPEDIW VRAVNTGMEP GKTSFFQALG VPTKIARGTI 150
    EIVSDVKVVD AGNKVGQSEA SLLNLLNISP FTFGLTVVQV YDNGQVFPSS 200
    ILDITDEELV SHFVSAVSTI ASISLAIGYP TLPSVGHTLI NNYKDLLAVA 250
    IAASYHYPEI EDLVDRIENP EKYAAAAPAA TSAASGDAAP AEEAAAEEEE 300
    ESDDDMGFGL FD 312
    Length:312
    Mass (Da):33,717
    Last modified:October 5, 2010 - v2
    Checksum:i109ECC90F7C8B68E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831N → Y in CAA30029. (PubMed:3287327)Curated
    Sequence conflicti83 – 831N → Y in BAA00415. (PubMed:2681177)Curated
    Sequence conflicti83 – 831N → Y in CAA31703. (PubMed:2681177)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06959 mRNA. Translation: CAA30029.1.
    D00529 Genomic DNA. Translation: BAA00415.1.
    X13328 Genomic DNA. Translation: CAA31703.1.
    M26506 Genomic DNA. Translation: AAA34730.1.
    M37326 Genomic DNA. Translation: AAA34729.1.
    U19028 Genomic DNA. Translation: AAB67258.1.
    BK006945 Genomic DNA. Translation: DAA09644.1.
    PIRiS51343. R5BY0E.
    RefSeqiNP_013444.1. NM_001182229.1.

    Genome annotation databases

    EnsemblFungiiYLR340W; YLR340W; YLR340W.
    GeneIDi851052.
    KEGGisce:YLR340W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06959 mRNA. Translation: CAA30029.1 .
    D00529 Genomic DNA. Translation: BAA00415.1 .
    X13328 Genomic DNA. Translation: CAA31703.1 .
    M26506 Genomic DNA. Translation: AAA34730.1 .
    M37326 Genomic DNA. Translation: AAA34729.1 .
    U19028 Genomic DNA. Translation: AAB67258.1 .
    BK006945 Genomic DNA. Translation: DAA09644.1 .
    PIRi S51343. R5BY0E.
    RefSeqi NP_013444.1. NM_001182229.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IZS electron microscopy - s 1-312 [» ]
    3J16 electron microscopy - G 1-312 [» ]
    3O5H X-ray 4.00 M 1-312 [» ]
    3U5I X-ray 3.00 q 1-312 [» ]
    4B6A electron microscopy 8.10 q 1-312 [» ]
    4BYN electron microscopy 4.30 q 1-312 [» ]
    4BYU electron microscopy 6.60 q 1-237 [» ]
    ProteinModelPortali P05317.
    SMRi P05317. Positions 3-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31602. 149 interactions.
    DIPi DIP-1582N.
    IntActi P05317. 267 interactions.
    MINTi MINT-384116.
    STRINGi 4932.YLR340W.

    2D gel databases

    SWISS-2DPAGE P05317.

    Proteomic databases

    MaxQBi P05317.
    PaxDbi P05317.
    PeptideAtlasi P05317.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR340W ; YLR340W ; YLR340W .
    GeneIDi 851052.
    KEGGi sce:YLR340W.

    Organism-specific databases

    SGDi S000004332. RPP0.

    Phylogenomic databases

    eggNOGi COG0244.
    GeneTreei ENSGT00390000017839.
    HOGENOMi HOG000210987.
    KOi K02941.
    OMAi LATEYSF.
    OrthoDBi EOG7PS1RV.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32417-MONOMER.
    Reactomei REACT_188965. SRP-dependent cotranslational protein targeting to membrane.
    REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_217188. Formation of a pool of free 40S subunits.

    Miscellaneous databases

    NextBioi 967667.

    Gene expression databases

    Genevestigatori P05317.

    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. "cDNA and deduced amino acid sequence of 38 kDa-type acidic ribosomal protein A0 from Saccharomyces cerevisiae."
      Mitsui K., Tsurugi K.
      Nucleic Acids Res. 16:3573-3573(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: IFO 40028.
    2. "The gene and the primary structure of acidic ribosomal protein A0 from yeast Saccharomyces cerevisiae which shows partial homology to bacterial ribosomal protein L10."
      Mitsui K., Nakagawa T., Tsurugi K.
      J. Biochem. 106:223-227(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coli L12 protein and a single form of the L10-equivalent ribosomal protein."
      Newton C.H., Shimmin L.C., Yee J., Dennis P.P.
      J. Bacteriol. 172:579-588(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SR26-12C.
    4. Erratum
      Newton C.H., Shimmin L.C., Yee J., Dennis P.P.
      J. Bacteriol. 172:3535-3535(1990) [PubMed] [Europe PMC] [Abstract]
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
      Planta R.J., Mager W.H.
      Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE, SUBUNIT.
    8. "Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation."
      Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G.
      Biochemistry 37:16620-16626(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-302.
    9. "Identification of a hypothetical membrane protein interactor of ribosomal phosphoprotein P0."
      Aruna K., Chakraborty T., Nambeesan S., Mannan A.B., Sehgal A., Balachandara S.R., Sharma S.
      J. Biosci. 29:33-43(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YFL034W.
    10. "Yeast ribosomal P0 protein has two separate binding sites for P1/P2 proteins."
      Krokowski D., Boguszewska A., Abramczyk D., Liljas A., Tchorzewski M., Grankowski N.
      Mol. Microbiol. 60:386-400(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPP1A; RPP1B; RPP2A AND RPP2B.
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRLA0_YEAST
    AccessioniPrimary (citable) accession number: P05317
    Secondary accession number(s): D6VYX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3