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P05318

- RLA1_YEAST

UniProt

P05318 - RLA1_YEAST

Protein

60S acidic ribosomal protein P1-alpha

Gene

RPP1A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays an important role in the elongation step of protein synthesis.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase activator activity Source: SGD
    3. structural constituent of ribosome Source: SGD

    GO - Biological processi

    1. cytoplasmic translation Source: SGD
    2. positive regulation of protein kinase activity Source: SGD
    3. translational elongation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29490-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 P1-alpha
    Short name:
    P1A
    Alternative name(s):
    A1
    L12EIIA
    YP1alpha
    Gene namesi
    Name:RPP1A
    Synonyms:L12EIIA, RPA1, RPLA1
    Ordered Locus Names:YDL081C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002239. RPP1A.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 10610560S acidic ribosomal protein P1-alphaPRO_0000157705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei96 – 961Phosphoserine3 Publications

    Post-translational modificationi

    N-terminally acetylated by acetyltransferase NatA.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05318.
    PaxDbiP05318.
    PeptideAtlasiP05318.

    Expressioni

    Gene expression databases

    GenevestigatoriP05318.

    Interactioni

    Subunit structurei

    Heterodimer of P1A-P2B. 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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RPP0P053174EBI-15452,EBI-15447
    RPP2BP024002EBI-15452,EBI-15464

    Protein-protein interaction databases

    BioGridi31980. 125 interactions.
    DIPiDIP-1583N.
    IntActiP05318. 19 interactions.
    MINTiMINT-384141.
    STRINGi4932.YDL081C.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IZSelectron microscopy-t/u1-106[»]
    DisProtiDP00164.
    ProteinModelPortaliP05318.
    SMRiP05318. Positions 3-106.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L12P family.Curated

    Phylogenomic databases

    eggNOGiCOG2058.
    GeneTreeiENSGT00730000113211.
    HOGENOMiHOG000229898.
    KOiK02942.
    OMAiSIESYWP.
    OrthoDBiEOG7J70V7.

    Family and domain databases

    HAMAPiMF_01478. Ribosomal_L12_arch.
    InterProiIPR001813. Ribosomal_L10/L12.
    IPR027534. Ribosomal_L12.
    [Graphical view]
    PfamiPF00428. Ribosomal_60s. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05318-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTESALSYA ALILADSEIE ISSEKLLTLT NAANVPVENI WADIFAKALD    50
    GQNLKDLLVN FSAGAAAPAG VAGGVAGGEA GEAEAEKEEE EAKEESDDDM 100
    GFGLFD 106
    Length:106
    Mass (Da):10,908
    Last modified:October 5, 2010 - v4
    Checksum:i9A2FE94D28640ACC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371V → D in CAA30027. (PubMed:3287328)Curated
    Sequence conflicti37 – 371V → D in CAA31976. (PubMed:2662969)Curated
    Sequence conflicti37 – 371V → D in BAA14113. (PubMed:2662969)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06957 mRNA. Translation: CAA30027.1.
    X13682 Genomic DNA. Translation: CAA31976.1.
    D90072 Genomic DNA. Translation: BAA14113.1.
    M26504 Genomic DNA. Translation: AAA34733.1.
    Z74129 Genomic DNA. Translation: CAA98647.1.
    AY558526 Genomic DNA. Translation: AAS56852.1.
    BK006938 Genomic DNA. Translation: DAA11778.1.
    PIRiS67617. R5BY2A.
    RefSeqiNP_010202.1. NM_001180140.1.

    Genome annotation databases

    EnsemblFungiiYDL081C; YDL081C; YDL081C.
    GeneIDi851478.
    KEGGisce:YDL081C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06957 mRNA. Translation: CAA30027.1 .
    X13682 Genomic DNA. Translation: CAA31976.1 .
    D90072 Genomic DNA. Translation: BAA14113.1 .
    M26504 Genomic DNA. Translation: AAA34733.1 .
    Z74129 Genomic DNA. Translation: CAA98647.1 .
    AY558526 Genomic DNA. Translation: AAS56852.1 .
    BK006938 Genomic DNA. Translation: DAA11778.1 .
    PIRi S67617. R5BY2A.
    RefSeqi NP_010202.1. NM_001180140.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IZS electron microscopy - t/u 1-106 [» ]
    DisProti DP00164.
    ProteinModelPortali P05318.
    SMRi P05318. Positions 3-106.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31980. 125 interactions.
    DIPi DIP-1583N.
    IntActi P05318. 19 interactions.
    MINTi MINT-384141.
    STRINGi 4932.YDL081C.

    Proteomic databases

    MaxQBi P05318.
    PaxDbi P05318.
    PeptideAtlasi P05318.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL081C ; YDL081C ; YDL081C .
    GeneIDi 851478.
    KEGGi sce:YDL081C.

    Organism-specific databases

    SGDi S000002239. RPP1A.

    Phylogenomic databases

    eggNOGi COG2058.
    GeneTreei ENSGT00730000113211.
    HOGENOMi HOG000229898.
    KOi K02942.
    OMAi SIESYWP.
    OrthoDBi EOG7J70V7.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29490-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 968786.

    Gene expression databases

    Genevestigatori P05318.

    Family and domain databases

    HAMAPi MF_01478. Ribosomal_L12_arch.
    InterProi IPR001813. Ribosomal_L10/L12.
    IPR027534. Ribosomal_L12.
    [Graphical view ]
    Pfami PF00428. Ribosomal_60s. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA and deduced amino acid sequence of acidic ribosomal protein A1 from Saccharomyces cerevisiae."
      Tsurugi K., Mitsui K.
      Nucleic Acids Res. 16:3574-3574(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: IFO 40028.
    2. "Identification of A1 protein as the fourth member of 13 kDa-type acidic ribosomal protein family in yeast Saccharomyces cerevisiae."
      Mitsui K., Tsurugi K.
      Biochem. Biophys. Res. Commun. 161:1001-1006(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IFO 40028.
    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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "The acidic phosphoproteins from Saccharomyces cerevisiae ribosomes. NH2-terminal acetylation is a conserved difference between P1 and P2 proteins."
      Santos C., Ortiz-Reyes B., Naranda T., Remacha M., Ballesta J.P.G.
      Biochemistry 32:4231-4236(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-5, ACETYLATION AT SER-2, PHOSPHORYLATION.
    8. "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.
    9. "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 RPP0 AND RPP2B.
    10. "The action of N-terminal acetyltransferases on yeast ribosomal proteins."
      Arnold R.J., Polevoda B., Reilly J.P., Sherman F.
      J. Biol. Chem. 274:37035-37040(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
    11. "Asymmetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk."
      Guarinos E., Remacha M., Ballesta J.P.G.
      J. Biol. Chem. 276:32474-32479(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPP2B.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. "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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRLA1_YEAST
    AccessioniPrimary (citable) accession number: P05318
    Secondary accession number(s): D6VRR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 132 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Yeasts contain 4 individual small ribosomal A proteins (RPA) which can be classified into two couples of similar but not identical sequences. Each couple is distinctly related to one of the two A proteins present in multicellular organisms.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3