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P26321

- RL5_YEAST

UniProt

P26321 - RL5_YEAST

Protein

60S ribosomal protein L5

Gene

RPL5

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 135 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Binds 5S RNA and is required for 60S subunit assembly.

    GO - Molecular functioni

    1. 5S 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

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34030-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 ribosomal protein L5
    Alternative name(s):
    L1
    L1a
    Ribosomal 5S RNA-binding protein
    YL3
    Gene namesi
    Name:RPL5
    Synonyms:RPL1, RPL1A
    Ordered Locus Names:YPL131W
    ORF Names:LPI14W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    SGDiS000006052. RPL5.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: The SYO1/RPL11/RPL5 complex is transported into the nucleus by KAP104.

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: SGD
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 29729660S ribosomal protein L5PRO_0000131454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei167 – 1671Phosphoserine1 Publication
    Modified residuei176 – 1761Phosphoserine1 Publication
    Modified residuei235 – 2351Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP26321.
    PaxDbiP26321.
    PeptideAtlasiP26321.

    Expressioni

    Gene expression databases

    GenevestigatoriP26321.

    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). Forms a heterotrimeric complex with SYO1 and RPL11A or RPL11B. Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NOG1Q028922EBI-15398,EBI-12105

    Protein-protein interaction databases

    BioGridi36050. 135 interactions.
    DIPiDIP-1790N.
    IntActiP26321. 163 interactions.
    MINTiMINT-8285488.
    STRINGi4932.YPL131W.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K5Ymodel-E11-232[»]
    1S1Ielectron microscopy11.70E11-232[»]
    1VW8electron microscopy6.10E1-297[»]
    1VWUelectron microscopy6.10E1-297[»]
    3IZSelectron microscopy-Q1-297[»]
    3J65electron microscopy8.70P1-297[»]
    3O58X-ray4.00E1-297[»]
    3O5HX-ray4.00E1-297[»]
    3U5EX-ray3.00D1-297[»]
    3U5IX-ray3.00D1-297[»]
    4B6Aelectron microscopy8.10D1-297[»]
    4BYNelectron microscopy4.30D2-297[»]
    4BYUelectron microscopy6.60D2-297[»]
    4CUWelectron microscopy3.70D1-297[»]
    ProteinModelPortaliP26321.
    SMRiP26321. Positions 2-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26321.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L18P family.Curated

    Phylogenomic databases

    eggNOGiCOG0256.
    GeneTreeiENSGT00390000008456.
    HOGENOMiHOG000105947.
    KOiK02932.
    OMAiKAYGITH.
    OrthoDBiEOG7DJSXQ.

    Family and domain databases

    HAMAPiMF_01337_A. Ribosomal_L18_A.
    InterProiIPR005485. Rbsml_L5_euk/L18_arc.
    IPR025607. Rbsml_L5e/L18P_C.
    IPR005484. Ribosomal_L18/L5.
    [Graphical view]
    PANTHERiPTHR23410. PTHR23410. 1 hit.
    PfamiPF14204. Ribosomal_L18_c. 1 hit.
    PF00861. Ribosomal_L18p. 1 hit.
    [Graphical view]
    PRINTSiPR00058. RIBOSOMALL5.

    Sequencei

    Sequence statusi: Complete.

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

    P26321-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR    50
    LVVRFTNKDI ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA 100
    TGLLIARRTL QKLGLDETYK GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL 150
    QRTTTGARVF GALKGASDGG LYVPHSENRF PGWDFETEEI DPELLRSYIF 200
    GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY TSAHEAIRAD 250
    PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ 297
    Length:297
    Mass (Da):33,715
    Last modified:October 5, 2010 - v4
    Checksum:i14E3B2931C3CAE2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181T → Y AA sequence (PubMed:393511)Curated
    Sequence conflicti112 – 1121K → R in AAA35234. (PubMed:2007570)Curated
    Sequence conflicti112 – 1121K → R in AAA35236. (PubMed:1325447)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65056 Genomic DNA. Translation: AAA35234.1.
    M94864 Genomic DNA. Translation: AAA35236.1.
    L01796 Genomic DNA. Translation: AAA34979.1.
    U43703 Genomic DNA. Translation: AAB68228.1.
    BK006949 Genomic DNA. Translation: DAA11302.1.
    PIRiS42144.
    RefSeqiNP_015194.1. NM_001183945.1.

    Genome annotation databases

    EnsemblFungiiYPL131W; YPL131W; YPL131W.
    GeneIDi855972.
    KEGGisce:YPL131W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65056 Genomic DNA. Translation: AAA35234.1 .
    M94864 Genomic DNA. Translation: AAA35236.1 .
    L01796 Genomic DNA. Translation: AAA34979.1 .
    U43703 Genomic DNA. Translation: AAB68228.1 .
    BK006949 Genomic DNA. Translation: DAA11302.1 .
    PIRi S42144.
    RefSeqi NP_015194.1. NM_001183945.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K5Y model - E 11-232 [» ]
    1S1I electron microscopy 11.70 E 11-232 [» ]
    1VW8 electron microscopy 6.10 E 1-297 [» ]
    1VWU electron microscopy 6.10 E 1-297 [» ]
    3IZS electron microscopy - Q 1-297 [» ]
    3J65 electron microscopy 8.70 P 1-297 [» ]
    3O58 X-ray 4.00 E 1-297 [» ]
    3O5H X-ray 4.00 E 1-297 [» ]
    3U5E X-ray 3.00 D 1-297 [» ]
    3U5I X-ray 3.00 D 1-297 [» ]
    4B6A electron microscopy 8.10 D 1-297 [» ]
    4BYN electron microscopy 4.30 D 2-297 [» ]
    4BYU electron microscopy 6.60 D 2-297 [» ]
    4CUW electron microscopy 3.70 D 1-297 [» ]
    ProteinModelPortali P26321.
    SMRi P26321. Positions 2-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36050. 135 interactions.
    DIPi DIP-1790N.
    IntActi P26321. 163 interactions.
    MINTi MINT-8285488.
    STRINGi 4932.YPL131W.

    Proteomic databases

    MaxQBi P26321.
    PaxDbi P26321.
    PeptideAtlasi P26321.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL131W ; YPL131W ; YPL131W .
    GeneIDi 855972.
    KEGGi sce:YPL131W.

    Organism-specific databases

    SGDi S000006052. RPL5.

    Phylogenomic databases

    eggNOGi COG0256.
    GeneTreei ENSGT00390000008456.
    HOGENOMi HOG000105947.
    KOi K02932.
    OMAi KAYGITH.
    OrthoDBi EOG7DJSXQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34030-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

    EvolutionaryTracei P26321.
    NextBioi 980789.
    PROi P26321.

    Gene expression databases

    Genevestigatori P26321.

    Family and domain databases

    HAMAPi MF_01337_A. Ribosomal_L18_A.
    InterProi IPR005485. Rbsml_L5_euk/L18_arc.
    IPR025607. Rbsml_L5e/L18P_C.
    IPR005484. Ribosomal_L18/L5.
    [Graphical view ]
    PANTHERi PTHR23410. PTHR23410. 1 hit.
    Pfami PF14204. Ribosomal_L18_c. 1 hit.
    PF00861. Ribosomal_L18p. 1 hit.
    [Graphical view ]
    PRINTSi PR00058. RIBOSOMALL5.
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the yeast ribosomal 5 S RNA-binding protein YL3."
      Tang B., Nazar R.N.
      J. Biol. Chem. 266:6120-6123(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Unbalanced regulation of the ribosomal 5 S RNA-binding protein in Saccharomyces cerevisiae expressing mutant 5 S rRNAs."
      Tang B., Nazar R.N.
      J. Biol. Chem. 267:17738-17742(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits."
      Deshmukh M.P., Tsay Y.F., Paulovich A.G., Woolford J.L. Jr.
      Mol. Cell. Biol. 13:2835-2845(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(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. "The 5-S RNA binding protein from yeast (Saccharomyces cerevisiae) ribosomes. Evolution of the eukaryotic 5-S RNA binding protein."
      Nazar R.N., Yaguchi M., Willick G.E., Rollin C.F., Roy C.
      Eur. J. Biochem. 102:573-582(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31 AND 219-253.
    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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. "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-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-167; SER-176 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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].
    14. Cited for: INTERACTION WITH RPL11A; RPL11B AND SYO1, SUBCELLULAR LOCATION.
    15. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
      Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
      Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 11-232, ELECTRON MICROSCOPY.
    16. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
      Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
      EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 11-232, ELECTRON MICROSCOPY.
    17. "Crystal structure of the eukaryotic ribosome."
      Ben-Shem A., Jenner L., Yusupova G., Yusupov M.
      Science 330:1203-1209(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL5_YEAST
    AccessioniPrimary (citable) accession number: P26321
    Secondary accession number(s): D6W3N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 135 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3