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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

  • large ribosomal subunit rRNA binding Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • ribosomal large subunit assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32417-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR340W.
SGDiS000004332. RPP0.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001547861 – 31260S acidic ribosomal protein P0Add BLAST312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei68PhosphoserineCombined sources1
Cross-linki97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei302Phosphoserine; by CK2Combined sources1 Publication1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05317.
PRIDEiP05317.
TopDownProteomicsiP05317.

2D gel databases

SWISS-2DPAGEP05317.

PTM databases

iPTMnetiP05317.

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. 123 interactors.
DIPiDIP-1582N.
IntActiP05317. 269 interactors.
MINTiMINT-384116.

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 21Combined sources18
Beta strandi23 – 29Combined sources7
Helixi35 – 43Combined sources9
Beta strandi46 – 48Combined sources3
Beta strandi50 – 53Combined sources4
Helixi56 – 64Combined sources9
Beta strandi68 – 70Combined sources3
Helixi72 – 74Combined sources3
Helixi77 – 79Combined sources3
Beta strandi82 – 89Combined sources8
Helixi93 – 102Combined sources10
Beta strandi186 – 194Combined sources9
Beta strandi195 – 197Combined sources3
Turni200 – 202Combined sources3
Helixi210 – 213Combined sources4
Turni214 – 219Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-G1-312[»]
3J77electron microscopy6.20P01-312[»]
3J78electron microscopy6.30P01-312[»]
4U3MX-ray3.00p02-311[»]
4U3NX-ray3.20p02-312[»]
4U3UX-ray2.90p02-312[»]
4U4NX-ray3.10p02-312[»]
4U4OX-ray3.60p02-312[»]
4U4QX-ray3.00p02-312[»]
4U4RX-ray2.80p02-312[»]
4U4UX-ray3.00p02-312[»]
4U4YX-ray3.20p02-312[»]
4U4ZX-ray3.10p02-312[»]
4U50X-ray3.20p02-312[»]
4U51X-ray3.20p02-312[»]
4U52X-ray3.00p02-312[»]
4U53X-ray3.30p02-312[»]
4U55X-ray3.20p02-312[»]
4U56X-ray3.45p02-312[»]
4U6FX-ray3.10p02-312[»]
4V6Ielectron microscopy8.80Bs1-312[»]
4V7RX-ray4.00DM1-312[»]
4V88X-ray3.00Dq1-312[»]
4V8Telectron microscopy8.10q1-312[»]
4V8Yelectron microscopy4.30Bq1-312[»]
4V8Zelectron microscopy6.60Bq1-237[»]
5APNelectron microscopy3.91q1-312[»]
5APOelectron microscopy3.41q1-312[»]
5DATX-ray3.15p02-221[»]
5DC3X-ray3.25p02-312[»]
5FCIX-ray3.40p02-311[»]
5FCJX-ray3.10p02-312[»]
5I4LX-ray3.10p01-312[»]
5JUOelectron microscopy4.00VA1-312[»]
5JUPelectron microscopy3.50VA1-312[»]
5JUSelectron microscopy4.20VA1-312[»]
5JUTelectron microscopy4.00VA1-312[»]
5JUUelectron microscopy4.00VA1-312[»]
ProteinModelPortaliP05317.
SMRiP05317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 230Interaction with P1A-P2BAdd BLAST32
Regioni231 – 258Interaction with P1B-P2AAdd BLAST28

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
InParanoidiP05317.
KOiK02941.
OMAiKTGNQAF.
OrthoDBiEOG092C4JUE.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti83N → Y in CAA30029 (PubMed:3287327).Curated1
Sequence conflicti83N → Y in BAA00415 (PubMed:2681177).Curated1
Sequence conflicti83N → Y in CAA31703 (PubMed:2681177).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-G1-312[»]
3J77electron microscopy6.20P01-312[»]
3J78electron microscopy6.30P01-312[»]
4U3MX-ray3.00p02-311[»]
4U3NX-ray3.20p02-312[»]
4U3UX-ray2.90p02-312[»]
4U4NX-ray3.10p02-312[»]
4U4OX-ray3.60p02-312[»]
4U4QX-ray3.00p02-312[»]
4U4RX-ray2.80p02-312[»]
4U4UX-ray3.00p02-312[»]
4U4YX-ray3.20p02-312[»]
4U4ZX-ray3.10p02-312[»]
4U50X-ray3.20p02-312[»]
4U51X-ray3.20p02-312[»]
4U52X-ray3.00p02-312[»]
4U53X-ray3.30p02-312[»]
4U55X-ray3.20p02-312[»]
4U56X-ray3.45p02-312[»]
4U6FX-ray3.10p02-312[»]
4V6Ielectron microscopy8.80Bs1-312[»]
4V7RX-ray4.00DM1-312[»]
4V88X-ray3.00Dq1-312[»]
4V8Telectron microscopy8.10q1-312[»]
4V8Yelectron microscopy4.30Bq1-312[»]
4V8Zelectron microscopy6.60Bq1-237[»]
5APNelectron microscopy3.91q1-312[»]
5APOelectron microscopy3.41q1-312[»]
5DATX-ray3.15p02-221[»]
5DC3X-ray3.25p02-312[»]
5FCIX-ray3.40p02-311[»]
5FCJX-ray3.10p02-312[»]
5I4LX-ray3.10p01-312[»]
5JUOelectron microscopy4.00VA1-312[»]
5JUPelectron microscopy3.50VA1-312[»]
5JUSelectron microscopy4.20VA1-312[»]
5JUTelectron microscopy4.00VA1-312[»]
5JUUelectron microscopy4.00VA1-312[»]
ProteinModelPortaliP05317.
SMRiP05317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31602. 123 interactors.
DIPiDIP-1582N.
IntActiP05317. 269 interactors.
MINTiMINT-384116.

PTM databases

iPTMnetiP05317.

2D gel databases

SWISS-2DPAGEP05317.

Proteomic databases

MaxQBiP05317.
PRIDEiP05317.
TopDownProteomicsiP05317.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR340W.
SGDiS000004332. RPP0.

Phylogenomic databases

GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
InParanoidiP05317.
KOiK02941.
OMAiKTGNQAF.
OrthoDBiEOG092C4JUE.

Enzyme and pathway databases

BioCyciYEAST:G3O-32417-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP05317.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 165 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

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 one 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.