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Protein

60S acidic ribosomal protein P0

Gene

RPP0

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

GO - Molecular functioni

  1. large ribosomal subunit rRNA binding Source: SGD
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. ribosomal large subunit assembly Source: SGD
  3. translational elongation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32417-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.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P0
Short name:
A0
Alternative name(s):
L10E
Gene namesi
Name:RPP0
Synonyms:L10E, RPA0, RPL10E, RPLA0
Ordered Locus Names:YLR340W
ORF Names:L8300.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000004332. RPP0.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. cytosolic large ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31231260S acidic ribosomal protein P0PRO_0000154786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei302 – 3021Phosphoserine; by CK24 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05317.
PaxDbiP05317.
PeptideAtlasiP05317.

2D gel databases

SWISS-2DPAGEP05317.

Expressioni

Gene expression databases

GenevestigatoriP05317.

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). 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. P0 directly interacts with 28S rRNA. Interacts with YFL034W.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EFT2P323242EBI-15447,EBI-6333
RPP1AP053184EBI-15447,EBI-15452
RPP1BP106223EBI-15447,EBI-15460
RPP2AP053192EBI-15447,EBI-15456

Protein-protein interaction databases

BioGridi31602. 150 interactions.
DIPiDIP-1582N.
IntActiP05317. 267 interactions.
MINTiMINT-384116.
STRINGi4932.YLR340W.

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2118Combined sources
Beta strandi23 – 297Combined sources
Helixi35 – 439Combined sources
Beta strandi46 – 483Combined sources
Beta strandi50 – 534Combined sources
Helixi56 – 649Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 743Combined sources
Helixi77 – 793Combined sources
Beta strandi82 – 898Combined sources
Helixi93 – 10210Combined sources
Beta strandi186 – 1949Combined sources
Beta strandi195 – 1973Combined sources
Turni200 – 2023Combined sources
Helixi210 – 2134Combined sources
Turni214 – 2196Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VXVelectron microscopy6.20r1-312[»]
1VXYelectron microscopy6.30r1-312[»]
3IZSelectron microscopy-s1-312[»]
3J16electron microscopy-G1-312[»]
3O5HX-ray4.00M1-312[»]
3U5IX-ray3.00q1-312[»]
4B6Aelectron microscopy8.10q1-312[»]
4BYNelectron microscopy4.30q1-312[»]
4BYUelectron microscopy6.60q1-237[»]
4UJJX-ray3.20i2-312[»]
4UJOX-ray3.00i2-312[»]
4UJTX-ray2.80i2-312[»]
4UJYX-ray3.10h2-312[»]
4UK3X-ray3.00i2-311[»]
4UK8X-ray3.20i2-312[»]
4UKEX-ray2.90i2-312[»]
4UKJX-ray3.45h2-312[»]
4UKOX-ray3.20h2-312[»]
4UKTX-ray3.30i2-312[»]
4UKYX-ray3.10i2-312[»]
4UL3X-ray3.60i2-312[»]
4UL8X-ray3.00i2-312[»]
4ULDX-ray3.00i2-312[»]
4ULIX-ray3.20i2-312[»]
4ULOX-ray3.10i2-312[»]
4ULTX-ray3.20h2-312[»]
4V8Telectron microscopy8.10q1-312[»]
ProteinModelPortaliP05317.
SMRiP05317. Positions 3-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 23032Interaction with P1A-P2BAdd
BLAST
Regioni231 – 25828Interaction with P1B-P2AAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

eggNOGiCOG0244.
GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
InParanoidiP05317.
KOiK02941.
OMAiSTHVINA.
OrthoDBiEOG7PS1RV.

Family and domain databases

InterProiIPR001790. Ribosomal_L10/acidic_P0.
IPR001813. Ribosomal_L10/L12.
[Graphical view]
PfamiPF00428. Ribosomal_60s. 1 hit.
PF00466. Ribosomal_L10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05317-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGGIREKKAE YFAKLREYLE EYKSLFVVGV DNVSSQQMHE VRKELRGRAV
60 70 80 90 100
VLMGKNTMVR RAIRGFLSDL PDFEKLLPFV KGNVGFVFTN EPLTEIKNVI
110 120 130 140 150
VSNRVAAPAR AGAVAPEDIW VRAVNTGMEP GKTSFFQALG VPTKIARGTI
160 170 180 190 200
EIVSDVKVVD AGNKVGQSEA SLLNLLNISP FTFGLTVVQV YDNGQVFPSS
210 220 230 240 250
ILDITDEELV SHFVSAVSTI ASISLAIGYP TLPSVGHTLI NNYKDLLAVA
260 270 280 290 300
IAASYHYPEI EDLVDRIENP EKYAAAAPAA TSAASGDAAP AEEAAAEEEE
310
ESDDDMGFGL FD
Length:312
Mass (Da):33,717
Last modified:October 5, 2010 - v2
Checksum:i109ECC90F7C8B68E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831N → Y in CAA30029. (PubMed:3287327)Curated
Sequence conflicti83 – 831N → Y in BAA00415. (PubMed:2681177)Curated
Sequence conflicti83 – 831N → Y in CAA31703. (PubMed:2681177)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06959 mRNA. Translation: CAA30029.1.
D00529 Genomic DNA. Translation: BAA00415.1.
X13328 Genomic DNA. Translation: CAA31703.1.
M26506 Genomic DNA. Translation: AAA34730.1.
M37326 Genomic DNA. Translation: AAA34729.1.
U19028 Genomic DNA. Translation: AAB67258.1.
BK006945 Genomic DNA. Translation: DAA09644.1.
PIRiS51343. R5BY0E.
RefSeqiNP_013444.1. NM_001182229.1.

Genome annotation databases

EnsemblFungiiYLR340W; YLR340W; YLR340W.
GeneIDi851052.
KEGGisce:YLR340W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06959 mRNA. Translation: CAA30029.1.
D00529 Genomic DNA. Translation: BAA00415.1.
X13328 Genomic DNA. Translation: CAA31703.1.
M26506 Genomic DNA. Translation: AAA34730.1.
M37326 Genomic DNA. Translation: AAA34729.1.
U19028 Genomic DNA. Translation: AAB67258.1.
BK006945 Genomic DNA. Translation: DAA09644.1.
PIRiS51343. R5BY0E.
RefSeqiNP_013444.1. NM_001182229.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VXVelectron microscopy6.20r1-312[»]
1VXYelectron microscopy6.30r1-312[»]
3IZSelectron microscopy-s1-312[»]
3J16electron microscopy-G1-312[»]
3O5HX-ray4.00M1-312[»]
3U5IX-ray3.00q1-312[»]
4B6Aelectron microscopy8.10q1-312[»]
4BYNelectron microscopy4.30q1-312[»]
4BYUelectron microscopy6.60q1-237[»]
4UJJX-ray3.20i2-312[»]
4UJOX-ray3.00i2-312[»]
4UJTX-ray2.80i2-312[»]
4UJYX-ray3.10h2-312[»]
4UK3X-ray3.00i2-311[»]
4UK8X-ray3.20i2-312[»]
4UKEX-ray2.90i2-312[»]
4UKJX-ray3.45h2-312[»]
4UKOX-ray3.20h2-312[»]
4UKTX-ray3.30i2-312[»]
4UKYX-ray3.10i2-312[»]
4UL3X-ray3.60i2-312[»]
4UL8X-ray3.00i2-312[»]
4ULDX-ray3.00i2-312[»]
4ULIX-ray3.20i2-312[»]
4ULOX-ray3.10i2-312[»]
4ULTX-ray3.20h2-312[»]
4V8Telectron microscopy8.10q1-312[»]
ProteinModelPortaliP05317.
SMRiP05317. Positions 3-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31602. 150 interactions.
DIPiDIP-1582N.
IntActiP05317. 267 interactions.
MINTiMINT-384116.
STRINGi4932.YLR340W.

2D gel databases

SWISS-2DPAGEP05317.

Proteomic databases

MaxQBiP05317.
PaxDbiP05317.
PeptideAtlasiP05317.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR340W; YLR340W; YLR340W.
GeneIDi851052.
KEGGisce:YLR340W.

Organism-specific databases

SGDiS000004332. RPP0.

Phylogenomic databases

eggNOGiCOG0244.
GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
InParanoidiP05317.
KOiK02941.
OMAiSTHVINA.
OrthoDBiEOG7PS1RV.

Enzyme and pathway databases

BioCyciYEAST:G3O-32417-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.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

NextBioi967667.

Gene expression databases

GenevestigatoriP05317.

Family and domain databases

InterProiIPR001790. Ribosomal_L10/acidic_P0.
IPR001813. Ribosomal_L10/L12.
[Graphical view]
PfamiPF00428. Ribosomal_60s. 1 hit.
PF00466. Ribosomal_L10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA and deduced amino acid sequence of 38 kDa-type acidic ribosomal protein A0 from Saccharomyces cerevisiae."
    Mitsui K., Tsurugi K.
    Nucleic Acids Res. 16:3573-3573(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: IFO 40028.
  2. "The gene and the primary structure of acidic ribosomal protein A0 from yeast Saccharomyces cerevisiae which shows partial homology to bacterial ribosomal protein L10."
    Mitsui K., Nakagawa T., Tsurugi K.
    J. Biochem. 106:223-227(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Erratum
    Newton C.H., Shimmin L.C., Yee J., Dennis P.P.
    J. Bacteriol. 172:3535-3535(1990) [PubMed] [Europe PMC] [Abstract]
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  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. "Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation."
    Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G.
    Biochemistry 37:16620-16626(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-302.
  9. "Identification of a hypothetical membrane protein interactor of ribosomal phosphoprotein P0."
    Aruna K., Chakraborty T., Nambeesan S., Mannan A.B., Sehgal A., Balachandara S.R., Sharma S.
    J. Biosci. 29:33-43(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YFL034W.
  10. "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 RPP1A; RPP1B; RPP2A AND RPP2B.
  11. "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-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, 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-68 AND SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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 nameiRLA0_YEAST
AccessioniPrimary (citable) accession number: P05317
Secondary accession number(s): D6VYX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 5, 2010
Last modified: February 4, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.