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P06367

- RS14A_YEAST

UniProt

P06367 - RS14A_YEAST

Protein

40S ribosomal protein S14-A

Gene

RPS14A

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 141 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.1 Publication

    GO - Molecular functioni

    1. mRNA binding Source: SGD
    2. structural constituent of ribosome Source: SGD

    GO - Biological processi

    1. cytoplasmic translation Source: SGD
    2. maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
    3. ribosomal small subunit assembly Source: SGD

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29345-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 S14-A
    Alternative name(s):
    RP59A
    Gene namesi
    Name:RPS14A
    Synonyms:CRY1, RPL59
    Ordered Locus Names:YCR031C
    ORF Names:YCR31C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    SGDiS000000627. RPS14A.

    Subcellular locationi

    Cytoplasm By similarity. Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: SGD
    2. nucleolus Source: UniProtKB-SubCell
    3. small-subunit processome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 13713640S ribosomal protein S14-APRO_0000123359Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications

    Post-translational modificationi

    N-terminally acetylated by acetyltransferase NatA.3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP06367.

    Expressioni

    Gene expression databases

    GenevestigatoriP06367.

    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). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESS1P226961EBI-14460,EBI-6679
    PRP40P332031EBI-14460,EBI-701
    SET2P469951EBI-14460,EBI-16985
    URN1Q065251EBI-14460,EBI-35138
    YFL010CP435821EBI-14460,EBI-22766

    Protein-protein interaction databases

    BioGridi31014. 138 interactions.
    IntActiP06367. 22 interactions.
    MINTiMINT-4083975.
    STRINGi4932.YCR031C.

    Structurei

    Secondary structure

    1
    137
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 163
    Beta strandi19 – 224
    Beta strandi25 – 284
    Beta strandi35 – 373
    Turni44 – 474
    Turni52 – 554
    Helixi57 – 7418
    Beta strandi78 – 803
    Beta strandi82 – 843
    Helixi96 – 983
    Helixi99 – 1068
    Turni107 – 1093
    Beta strandi111 – 1177

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K5Xmodel-K9-133[»]
    1S1Helectron microscopy11.70K2-137[»]
    1VW9electron microscopy6.10P1-137[»]
    1VWVelectron microscopy6.10P1-137[»]
    3IZBelectron microscopy-K1-137[»]
    3O2ZX-ray4.00H1-137[»]
    3O30X-ray4.00H1-137[»]
    3U5CX-ray3.00O1-137[»]
    3U5GX-ray3.00O1-137[»]
    4BYLelectron microscopy4.30O1-137[»]
    4BYTelectron microscopy6.60O1-137[»]
    4CUYelectron microscopy3.70O11-137[»]
    ProteinModelPortaliP06367.
    SMRiP06367. Positions 10-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06367.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S11P family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000000703.
    HOGENOMiHOG000111598.
    KOiK02955.
    OMAiNDRDEAS.
    OrthoDBiEOG7WHHPF.

    Family and domain databases

    Gene3Di3.30.420.80. 1 hit.
    HAMAPiMF_01310. Ribosomal_S11.
    InterProiIPR001971. Ribosomal_S11.
    IPR018102. Ribosomal_S11_CS.
    [Graphical view]
    PANTHERiPTHR11759. PTHR11759. 1 hit.
    PfamiPF00411. Ribosomal_S11. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
    PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06367-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNVVQARDN SQVFGVARIY ASFNDTFVHV TDLSGKETIA RVTGGMKVKA    50
    DRDESSPYAA MLAAQDVAAK CKEVGITAVH VKIRATGGTR TKTPGPGGQA 100
    ALRALARSGL RIGRIEDVTP VPSDSTRKKG GRRGRRL 137
    Length:137
    Mass (Da):14,537
    Last modified:January 23, 2007 - v5
    Checksum:i65A9212E10340A95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721K → R in AAA34530. (PubMed:3037334)Curated
    Sequence conflicti123 – 1231S → C in AAA34530. (PubMed:3037334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16126 Genomic DNA. Translation: AAA34530.1.
    X59720 Genomic DNA. Translation: CAC42981.1.
    BK006937 Genomic DNA. Translation: DAA07510.1.
    PIRiA02726. R5BY59.
    RefSeqiNP_009960.2. NM_001178745.1.

    Genome annotation databases

    EnsemblFungiiYCR031C; YCR031C; YCR031C.
    GeneIDi850397.
    KEGGisce:YCR031C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16126 Genomic DNA. Translation: AAA34530.1 .
    X59720 Genomic DNA. Translation: CAC42981.1 .
    BK006937 Genomic DNA. Translation: DAA07510.1 .
    PIRi A02726. R5BY59.
    RefSeqi NP_009960.2. NM_001178745.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K5X model - K 9-133 [» ]
    1S1H electron microscopy 11.70 K 2-137 [» ]
    1VW9 electron microscopy 6.10 P 1-137 [» ]
    1VWV electron microscopy 6.10 P 1-137 [» ]
    3IZB electron microscopy - K 1-137 [» ]
    3O2Z X-ray 4.00 H 1-137 [» ]
    3O30 X-ray 4.00 H 1-137 [» ]
    3U5C X-ray 3.00 O 1-137 [» ]
    3U5G X-ray 3.00 O 1-137 [» ]
    4BYL electron microscopy 4.30 O 1-137 [» ]
    4BYT electron microscopy 6.60 O 1-137 [» ]
    4CUY electron microscopy 3.70 O 11-137 [» ]
    ProteinModelPortali P06367.
    SMRi P06367. Positions 10-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31014. 138 interactions.
    IntActi P06367. 22 interactions.
    MINTi MINT-4083975.
    STRINGi 4932.YCR031C.

    Proteomic databases

    MaxQBi P06367.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR031C ; YCR031C ; YCR031C .
    GeneIDi 850397.
    KEGGi sce:YCR031C.

    Organism-specific databases

    SGDi S000000627. RPS14A.

    Phylogenomic databases

    GeneTreei ENSGT00390000000703.
    HOGENOMi HOG000111598.
    KOi K02955.
    OMAi NDRDEAS.
    OrthoDBi EOG7WHHPF.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29345-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 P06367.
    NextBioi 965926.

    Gene expression databases

    Genevestigatori P06367.

    Family and domain databases

    Gene3Di 3.30.420.80. 1 hit.
    HAMAPi MF_01310. Ribosomal_S11.
    InterProi IPR001971. Ribosomal_S11.
    IPR018102. Ribosomal_S11_CS.
    [Graphical view ]
    PANTHERi PTHR11759. PTHR11759. 1 hit.
    Pfami PF00411. Ribosomal_S11. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002131. Ribosomal_S11. 1 hit.
    PROSITEi PS00054. RIBOSOMAL_S11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene."
      Larkin J.C., Thompson J.R., Woolford J.L. Jr.
      Mol. Cell. Biol. 7:1764-1775(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Valles G., Volckaerts G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 72 AND 123.
    4. Cited for: GENOME REANNOTATION.
      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: 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "The small-subunit processome is a ribosome assembly intermediate."
      Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., Baserga S.J.
      Eukaryot. Cell 3:1619-1626(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME, SUBCELLULAR LOCATION.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 9-133, ELECTRON MICROSCOPY.
    12. "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, ELECTRON MICROSCOPY.

    Entry informationi

    Entry nameiRS14A_YEAST
    AccessioniPrimary (citable) accession number: P06367
    Secondary accession number(s): D6VR41, Q96VG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 29600 molecules/cell in log phase SD medium.1 Publication
    There are 2 genes for S14 in yeast.

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

    External Data

    Dasty 3