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P14126

- RL3_YEAST

UniProt

P14126 - RL3_YEAST

Protein

60S ribosomal protein L3

Gene

RPL3

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 146 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. 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

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33603-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 L3
    Alternative name(s):
    Maintenance of killer protein 8
    RP1
    Trichodermin resistance protein
    YL1
    Gene namesi
    Name:RPL3
    Synonyms:MAK8, TCM1
    Ordered Locus Names:YOR063W
    ORF Names:YOR29-14
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    SGDiS000005589. RPL3.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    A mutant confers resistance to trichodermin, a trichotecene toxin produced by plant-pathogenic fungi.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 38738660S ribosomal protein L3PRO_0000077251Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphoserine1 Publication
    Modified residuei103 – 1031Phosphothreonine1 Publication
    Modified residuei156 – 1561Phosphoserine1 Publication
    Modified residuei243 – 2431Pros-methylhistidine1 Publication
    Modified residuei297 – 2971Phosphoserine1 Publication

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP14126.
    PaxDbiP14126.
    PeptideAtlasiP14126.
    PRIDEiP14126.

    Expressioni

    Gene expression databases

    GenevestigatoriP14126.

    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).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRV2P175553EBI-15364,EBI-4024

    Protein-protein interaction databases

    BioGridi34462. 198 interactions.
    DIPiDIP-6264N.
    IntActiP14126. 104 interactions.
    MINTiMINT-604187.
    STRINGi4932.YOR063W.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K5Ymodel-C8-366[»]
    1S1Ielectron microscopy11.70C2-387[»]
    1VW8electron microscopy6.10C1-387[»]
    1VWUelectron microscopy6.10C1-387[»]
    3IZSelectron microscopy-C1-387[»]
    3J65electron microscopy8.70C1-387[»]
    3O58X-ray4.00C1-387[»]
    3O5HX-ray4.00C1-387[»]
    3U5EX-ray3.00B1-387[»]
    3U5IX-ray3.00B1-387[»]
    4B6Aelectron microscopy8.10B1-387[»]
    4BYNelectron microscopy4.30B2-387[»]
    4BYUelectron microscopy6.60B2-387[»]
    4CUWelectron microscopy3.70B1-387[»]
    ProteinModelPortaliP14126.
    SMRiP14126. Positions 2-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14126.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L3P family.Curated

    Phylogenomic databases

    eggNOGiCOG0087.
    GeneTreeiENSGT00390000017606.
    HOGENOMiHOG000107319.
    KOiK02925.
    OMAiFQTFEEK.
    OrthoDBiEOG7KQ2B9.

    Family and domain databases

    InterProiIPR000597. Ribosomal_L3.
    IPR019926. Ribosomal_L3_CS.
    IPR009000. Transl_B-barrel.
    [Graphical view]
    PfamiPF00297. Ribosomal_L3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14126-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHRKYEAPR HGHLGFLPRK RAASIRARVK AFPKDDRSKP VALTSFLGYK    50
    AGMTTIVRDL DRPGSKFHKR EVVEAVTVVD TPPVVVVGVV GYVETPRGLR 100
    SLTTVWAEHL SDEVKRRFYK NWYKSKKKAF TKYSAKYAQD GAGIERELAR 150
    IKKYASVVRV LVHTQIRKTP LAQKKAHLAE IQLNGGSISE KVDWAREHFE 200
    KTVAVDSVFE QNEMIDAIAV TKGHGFEGVT HRWGTKKLPR KTHRGLRKVA 250
    CIGAWHPAHV MWSVARAGQR GYHSRTSINH KIYRVGKGDD EANGATSFDR 300
    TKKTITPMGG FVHYGEIKND FIMVKGCIPG NRKRIVTLRK SLYTNTSRKA 350
    LEEVSLKWID TASKFGKGRF QTPAEKHAFM GTLKKDL 387
    Length:387
    Mass (Da):43,758
    Last modified:January 23, 2007 - v4
    Checksum:i986769A218E9698A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551W → C in AAA88732. (PubMed:6305925)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01351 Genomic DNA. Translation: AAA88732.1.
    Z74971 Genomic DNA. Translation: CAA99256.1.
    Z70678 Genomic DNA. Translation: CAA94548.1.
    BK006948 Genomic DNA. Translation: DAA10842.1.
    PIRiS66946. R5BY4E.
    RefSeqiNP_014706.1. NM_001183482.1.

    Genome annotation databases

    EnsemblFungiiYOR063W; YOR063W; YOR063W.
    GeneIDi854229.
    KEGGisce:YOR063W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01351 Genomic DNA. Translation: AAA88732.1 .
    Z74971 Genomic DNA. Translation: CAA99256.1 .
    Z70678 Genomic DNA. Translation: CAA94548.1 .
    BK006948 Genomic DNA. Translation: DAA10842.1 .
    PIRi S66946. R5BY4E.
    RefSeqi NP_014706.1. NM_001183482.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K5Y model - C 8-366 [» ]
    1S1I electron microscopy 11.70 C 2-387 [» ]
    1VW8 electron microscopy 6.10 C 1-387 [» ]
    1VWU electron microscopy 6.10 C 1-387 [» ]
    3IZS electron microscopy - C 1-387 [» ]
    3J65 electron microscopy 8.70 C 1-387 [» ]
    3O58 X-ray 4.00 C 1-387 [» ]
    3O5H X-ray 4.00 C 1-387 [» ]
    3U5E X-ray 3.00 B 1-387 [» ]
    3U5I X-ray 3.00 B 1-387 [» ]
    4B6A electron microscopy 8.10 B 1-387 [» ]
    4BYN electron microscopy 4.30 B 2-387 [» ]
    4BYU electron microscopy 6.60 B 2-387 [» ]
    4CUW electron microscopy 3.70 B 1-387 [» ]
    ProteinModelPortali P14126.
    SMRi P14126. Positions 2-387.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34462. 198 interactions.
    DIPi DIP-6264N.
    IntActi P14126. 104 interactions.
    MINTi MINT-604187.
    STRINGi 4932.YOR063W.

    Proteomic databases

    MaxQBi P14126.
    PaxDbi P14126.
    PeptideAtlasi P14126.
    PRIDEi P14126.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR063W ; YOR063W ; YOR063W .
    GeneIDi 854229.
    KEGGi sce:YOR063W.

    Organism-specific databases

    SGDi S000005589. RPL3.

    Phylogenomic databases

    eggNOGi COG0087.
    GeneTreei ENSGT00390000017606.
    HOGENOMi HOG000107319.
    KOi K02925.
    OMAi FQTFEEK.
    OrthoDBi EOG7KQ2B9.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33603-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 P14126.
    NextBioi 976109.
    PROi P14126.

    Gene expression databases

    Genevestigatori P14126.

    Family and domain databases

    InterProi IPR000597. Ribosomal_L3.
    IPR019926. Ribosomal_L3_CS.
    IPR009000. Transl_B-barrel.
    [Graphical view ]
    Pfami PF00297. Ribosomal_L3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the tcm1 gene (ribosomal protein L3) of Saccharomyces cerevisiae."
      Schultz L.D., Friesen J.D.
      J. Bacteriol. 155:8-14(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
      Strain: CLP1.
    2. "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the presence of two tRNAs and 24 new open reading frames."
      Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.
      Yeast 13:379-390(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from Schizosaccharomyces pombe."
      Otaka E., Higo K., Itoh T.
      Mol. Gen. Genet. 191:519-524(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20.
    6. "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 2-10.
    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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "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 THR-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: 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-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is dependent upon the YIL110W methyltransferase."
      Webb K.J., Zurita-Lopez C.I., Al-Hadid Q., Laganowsky A., Young B.D., Lipson R.S., Souda P., Faull K.F., Whitelegge J.P., Clarke S.G.
      J. Biol. Chem. 285:37598-37606(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT HIS-243.
    15. "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].
    16. "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 8-366, ELECTRON MICROSCOPY.
    17. "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.
    18. "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.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL3_YEAST
    AccessioniPrimary (citable) accession number: P14126
    Secondary accession number(s): D6W2C6, Q08459
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 450 molecules/cell in log phase SD medium.1 Publication

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

    External Data

    Dasty 3