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P02400

- RLA4_YEAST

UniProt

P02400 - RLA4_YEAST

Protein

60S acidic ribosomal protein P2-beta

Gene

RPP2B

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-29930-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S acidic ribosomal protein P2-beta
    Short name:
    P2B
    Alternative name(s):
    L12EIA
    L45
    YL44C
    YP2beta
    YPA1
    Gene namesi
    Name:RPP2B
    Synonyms:L12EIA, RPL45, RPLA4
    Ordered Locus Names:YDR382W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR382w.
    SGDiS000002790. RPP2B.

    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
    Chaini1 – 11011060S acidic ribosomal protein P2-betaPRO_0000157682Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei100 – 1001Phosphoserine3 Publications

    Post-translational modificationi

    The N-terminus is not modified.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP02400.
    PaxDbiP02400.
    PeptideAtlasiP02400.

    Expressioni

    Gene expression databases

    GenevestigatoriP02400.

    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
    RPP1AP053182EBI-15464,EBI-15452

    Protein-protein interaction databases

    BioGridi32443. 203 interactions.
    DIPiDIP-580N.
    IntActiP02400. 31 interactions.
    MINTiMINT-411356.
    STRINGi4932.YDR382W.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N2DX-ray2.22B100-105[»]
    3N3XX-ray1.70B100-105[»]
    DisProtiDP00002.
    ProteinModelPortaliP02400.
    SMRiP02400. Positions 1-70.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02400.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L12P family.Curated

    Phylogenomic databases

    eggNOGiCOG2058.
    GeneTreeiENSGT00550000074828.
    HOGENOMiHOG000229897.
    KOiK02943.
    OMAiWTEEQHA.
    OrthoDBiEOG708WC9.

    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.

    P02400-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKYLAAYLLL VQGGNAAPSA ADIKAVVESV GAEVDEARIN ELLSSLEGKG    50
    SLEEIIAEGQ KKFATVPTGG ASSAAAGAAG AAAGGDAAEE EKEEEAKEES 100
    DDDMGFGLFD 110
    Length:110
    Mass (Da):11,050
    Last modified:July 1, 1989 - v2
    Checksum:iEC45406CB5F199F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 784AAGA → GPAS AA sequence (PubMed:7030402)Curated
    Sequence conflicti86 – 872DA → GD AA sequence (PubMed:7030402)Curated
    Sequence conflicti89 – 891E → A AA sequence (PubMed:7030402)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03761 Genomic DNA. Translation: AAA34972.1.
    M26505 Genomic DNA. Translation: AAA34732.1.
    U28373 Genomic DNA. Translation: AAB64818.1.
    U32274 Genomic DNA. Translation: AAB64824.1.
    BK006938 Genomic DNA. Translation: DAA12226.1.
    PIRiA35109. R5BYA1.
    RefSeqiNP_010670.3. NM_001180690.3.

    Genome annotation databases

    EnsemblFungiiYDR382W; YDR382W; YDR382W.
    GeneIDi851990.
    KEGGisce:YDR382W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03761 Genomic DNA. Translation: AAA34972.1 .
    M26505 Genomic DNA. Translation: AAA34732.1 .
    U28373 Genomic DNA. Translation: AAB64818.1 .
    U32274 Genomic DNA. Translation: AAB64824.1 .
    BK006938 Genomic DNA. Translation: DAA12226.1 .
    PIRi A35109. R5BYA1.
    RefSeqi NP_010670.3. NM_001180690.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3N2D X-ray 2.22 B 100-105 [» ]
    3N3X X-ray 1.70 B 100-105 [» ]
    DisProti DP00002.
    ProteinModelPortali P02400.
    SMRi P02400. Positions 1-70.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32443. 203 interactions.
    DIPi DIP-580N.
    IntActi P02400. 31 interactions.
    MINTi MINT-411356.
    STRINGi 4932.YDR382W.

    Proteomic databases

    MaxQBi P02400.
    PaxDbi P02400.
    PeptideAtlasi P02400.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR382W ; YDR382W ; YDR382W .
    GeneIDi 851990.
    KEGGi sce:YDR382W.

    Organism-specific databases

    CYGDi YDR382w.
    SGDi S000002790. RPP2B.

    Phylogenomic databases

    eggNOGi COG2058.
    GeneTreei ENSGT00550000074828.
    HOGENOMi HOG000229897.
    KOi K02943.
    OMAi WTEEQHA.
    OrthoDBi EOG708WC9.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29930-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P02400.
    NextBioi 970154.

    Gene expression databases

    Genevestigatori P02400.

    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. "Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae."
      Remacha M., Saenz-Robles M.T., Vilella M.D., Ballesta J.P.G.
      J. Biol. Chem. 263:9094-9101(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Primary structure of an acidic ribosomal protein YPA1 from Saccharomyces cerevisiae. Isolation and characterization of peptides and the complete amino acid sequence."
      Itoh T.
      Biochim. Biophys. Acta 671:16-24(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    6. "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 1-6.
    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. "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: ANALYSIS OF N-TERMINUS.
    9. "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 RPP1A.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "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 RPP1A.
    13. "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-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    14. "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-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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].

    Entry informationi

    Entry nameiRLA4_YEAST
    AccessioniPrimary (citable) accession number: P02400
    Secondary accession number(s): D6VT16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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.
    Present with 602000 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3