Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P26783

- RS5_YEAST

UniProt

P26783 - RS5_YEAST

Protein

40S ribosomal protein S5

Gene

RPS5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: InterPro
    3. structural constituent of ribosome Source: SGD

    GO - Biological processi

    1. cytoplasmic translation Source: SGD
    2. regulation of translational fidelity Source: SGD
    3. rRNA export from nucleus Source: SGD

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31744-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:
    40S ribosomal protein S5
    Alternative name(s):
    RP14
    S2
    YS8
    Gene namesi
    Name:RPS5
    Synonyms:RPS2
    Ordered Locus Names:YJR123W
    ORF Names:J2045
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    SGDiS000003884. RPS5.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 22522440S ribosomal protein S5PRO_0000124540Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei27 – 271Phosphothreonine1 Publication

    Post-translational modificationi

    N-terminally acetylated by acetyltransferase NatA.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26783.
    PaxDbiP26783.
    PeptideAtlasiP26783.
    PRIDEiP26783.

    2D gel databases

    UCD-2DPAGEP26783.

    Expressioni

    Gene expression databases

    GenevestigatoriP26783.

    Interactioni

    Subunit structurei

    Component of the small 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).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUL1P485243EBI-16150,EBI-3881

    Protein-protein interaction databases

    BioGridi33879. 157 interactions.
    DIPiDIP-5092N.
    IntActiP26783. 66 interactions.
    MINTiMINT-480795.
    STRINGi4932.YJR123W.

    Structurei

    Secondary structure

    1
    225
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 388
    Beta strandi43 – 453
    Turni56 – 583
    Beta strandi69 – 713
    Beta strandi78 – 803
    Helixi83 – 864
    Helixi89 – 979
    Helixi101 – 1033
    Helixi107 – 12317
    Helixi129 – 13810
    Beta strandi143 – 1475
    Beta strandi151 – 1544
    Beta strandi158 – 1614
    Helixi164 – 18320
    Beta strandi186 – 1883
    Helixi190 – 20213
    Beta strandi206 – 2083
    Helixi209 – 22315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K5Xmodel-G76-225[»]
    1S1Helectron microscopy11.70G76-225[»]
    1VW9electron microscopy6.10G1-225[»]
    1VWVelectron microscopy6.10G1-225[»]
    2NOQelectron microscopy7.30F76-225[»]
    3IZBelectron microscopy-F1-225[»]
    3O2ZX-ray4.00D1-225[»]
    3O30X-ray4.00D1-225[»]
    3U5CX-ray3.00F1-225[»]
    3U5GX-ray3.00F1-225[»]
    4BYLelectron microscopy4.30F1-225[»]
    4BYTelectron microscopy6.60F1-225[»]
    4CUYelectron microscopy3.70F20-225[»]
    ProteinModelPortaliP26783.
    SMRiP26783. Positions 20-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26783.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S7P family.Curated

    Phylogenomic databases

    eggNOGiCOG0049.
    GeneTreeiENSGT00390000010806.
    HOGENOMiHOG000039066.
    KOiK02989.
    OMAiKEHHISH.
    OrthoDBiEOG7MD52N.

    Family and domain databases

    Gene3Di1.10.455.10. 1 hit.
    InterProiIPR000235. Ribosomal_S5/S7.
    IPR005716. Ribosomal_S5/S7_euk/arc.
    IPR020606. Ribosomal_S7_CS.
    IPR023798. Ribosomal_S7_dom.
    [Graphical view]
    PANTHERiPTHR11205. PTHR11205. 1 hit.
    PfamiPF00177. Ribosomal_S7. 1 hit.
    [Graphical view]
    SUPFAMiSSF47973. SSF47973. 1 hit.
    TIGRFAMsiTIGR01028. S7_S5_E_A. 1 hit.
    PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P26783-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDTEAPVEV QEDFEVVEEF TPVVLATPIP EEVQQAQTEI KLFNKWSFEE    50
    VEVKDASLVD YVQVRQPIFV AHTAGRYANK RFRKAQCPII ERLTNSLMMN 100
    GRNNGKKLKA VRIIKHTLDI INVLTDQNPI QVVVDAITNT GPREDTTRVG 150
    GGGAARRQAV DVSPLRRVNQ AIALLTIGAR EAAFRNIKTI AETLAEELIN 200
    AAKGSSTSYA IKKKDELERV AKSNR 225
    Length:225
    Mass (Da):25,039
    Last modified:January 23, 2007 - v3
    Checksum:iCD3F743B56CB1127
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211T → E AA sequence (PubMed:1544921)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89368 Genomic DNA. Translation: CAA61550.1.
    Z49623 Genomic DNA. Translation: CAA89654.1.
    AY692868 Genomic DNA. Translation: AAT92887.1.
    BK006943 Genomic DNA. Translation: DAA08908.1.
    PIRiS55720.
    RefSeqiNP_012657.1. NM_001181781.1.

    Genome annotation databases

    EnsemblFungiiYJR123W; YJR123W; YJR123W.
    GeneIDi853587.
    KEGGisce:YJR123W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89368 Genomic DNA. Translation: CAA61550.1 .
    Z49623 Genomic DNA. Translation: CAA89654.1 .
    AY692868 Genomic DNA. Translation: AAT92887.1 .
    BK006943 Genomic DNA. Translation: DAA08908.1 .
    PIRi S55720.
    RefSeqi NP_012657.1. NM_001181781.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K5X model - G 76-225 [» ]
    1S1H electron microscopy 11.70 G 76-225 [» ]
    1VW9 electron microscopy 6.10 G 1-225 [» ]
    1VWV electron microscopy 6.10 G 1-225 [» ]
    2NOQ electron microscopy 7.30 F 76-225 [» ]
    3IZB electron microscopy - F 1-225 [» ]
    3O2Z X-ray 4.00 D 1-225 [» ]
    3O30 X-ray 4.00 D 1-225 [» ]
    3U5C X-ray 3.00 F 1-225 [» ]
    3U5G X-ray 3.00 F 1-225 [» ]
    4BYL electron microscopy 4.30 F 1-225 [» ]
    4BYT electron microscopy 6.60 F 1-225 [» ]
    4CUY electron microscopy 3.70 F 20-225 [» ]
    ProteinModelPortali P26783.
    SMRi P26783. Positions 20-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33879. 157 interactions.
    DIPi DIP-5092N.
    IntActi P26783. 66 interactions.
    MINTi MINT-480795.
    STRINGi 4932.YJR123W.

    2D gel databases

    UCD-2DPAGE P26783.

    Proteomic databases

    MaxQBi P26783.
    PaxDbi P26783.
    PeptideAtlasi P26783.
    PRIDEi P26783.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR123W ; YJR123W ; YJR123W .
    GeneIDi 853587.
    KEGGi sce:YJR123W.

    Organism-specific databases

    SGDi S000003884. RPS5.

    Phylogenomic databases

    eggNOGi COG0049.
    GeneTreei ENSGT00390000010806.
    HOGENOMi HOG000039066.
    KOi K02989.
    OMAi KEHHISH.
    OrthoDBi EOG7MD52N.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31744-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 P26783.
    NextBioi 974388.
    PROi P26783.

    Gene expression databases

    Genevestigatori P26783.

    Family and domain databases

    Gene3Di 1.10.455.10. 1 hit.
    InterProi IPR000235. Ribosomal_S5/S7.
    IPR005716. Ribosomal_S5/S7_euk/arc.
    IPR020606. Ribosomal_S7_CS.
    IPR023798. Ribosomal_S7_dom.
    [Graphical view ]
    PANTHERi PTHR11205. PTHR11205. 1 hit.
    Pfami PF00177. Ribosomal_S7. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47973. SSF47973. 1 hit.
    TIGRFAMsi TIGR01028. S7_S5_E_A. 1 hit.
    PROSITEi PS00052. RIBOSOMAL_S7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae."
      Ignatovich O., Cooper M., Kulesza H.M., Beggs J.D.
      Nucleic Acids Res. 23:4616-4619(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae."
      Takakura H., Tsunasawa S., Miyagi M., Warner J.R.
      J. Biol. Chem. 267:5442-5445(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, ACETYLATION AT SER-2 BY NATA.
    6. "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.
    7. "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.
    8. "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 THR-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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].
    10. "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 76-225, ELECTRON MICROSCOPY.
    11. "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 76-225, ELECTRON MICROSCOPY.
    12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 76-225.

    Entry informationi

    Entry nameiRS5_YEAST
    AccessioniPrimary (citable) accession number: P26783
    Secondary accession number(s): D6VWU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3