60S acidic ribosomal protein P0 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P05317 (RLA0_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
60S acidic ribosomal protein P0
Short name=A0

Alternative name(s):
L10E

Gene names

Name:	RPP0
Synonyms:	L10E, RPA0, RPL10E, RPLA0
Ordered Locus Names:	YLR340W
ORF Names:	L8300.8

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Subunit structure	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. Ref.7 Ref.9 Ref.10
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ribosomal protein L10P family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic translation Traceable author statement Ref.7. Source: SGD ribosomal large subunit assembly Inferred from mutant phenotype PubMed 8195220. Source: SGD translational elongation Inferred from sequence or structural similarity PubMed 9175862 Ref.7. Source: SGD
Cellular_component	90S preribosome Inferred from direct assay PubMed 12150911. Source: SGD cytosolic large ribosomal subunit Traceable author statement Ref.7. Source: SGD
Molecular_function	LSU rRNA binding Inferred from direct assay PubMed 16164560. Source: SGD structural constituent of ribosome Traceable author statement Ref.7. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
EFT2	P32324	2	EBI-15447,EBI-6333
RPP1A	P05318	4	EBI-15447,EBI-15452
RPP1B	P10622	3	EBI-15447,EBI-15460
RPP2A	P05319	2	EBI-15447,EBI-15456

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 312

312

60S acidic ribosomal protein P0

PRO_0000154786

Regions

Region

199 – 230

Interaction with P1A-P2B

Region

231 – 258

Interaction with P1B-P2A

Amino acid modifications

Modified residue

Phosphoserine Ref.12

Modified residue

302

Phosphoserine; by CK2 Ref.8 Ref.11 Ref.13

Experimental info

Sequence conflict

N → Y in CAA30029. Ref.1

Sequence conflict

N → Y in BAA00415. Ref.2

Sequence conflict

N → Y in CAA31703. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P05317 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 109ECC90F7C8B68E
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FASTA

312

33,717

        10         20         30         40         50         60 
MGGIREKKAE YFAKLREYLE EYKSLFVVGV DNVSSQQMHE VRKELRGRAV VLMGKNTMVR 

        70         80         90        100        110        120 
RAIRGFLSDL PDFEKLLPFV KGNVGFVFTN EPLTEIKNVI VSNRVAAPAR AGAVAPEDIW 

       130        140        150        160        170        180 
VRAVNTGMEP GKTSFFQALG VPTKIARGTI EIVSDVKVVD AGNKVGQSEA SLLNLLNISP 

       190        200        210        220        230        240 
FTFGLTVVQV YDNGQVFPSS ILDITDEELV SHFVSAVSTI ASISLAIGYP TLPSVGHTLI 

       250        260        270        280        290        300 
NNYKDLLAVA IAASYHYPEI EDLVDRIENP EKYAAAAPAA TSAASGDAAP AEEAAAEEEE 

       310 
ESDDDMGFGL FD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. Strain: ADR376.
[12]	"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-34, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

R5BY0E. S51343.

RefSeq

NP_013444.1. NM_001182229.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IZS	electron microscopy	-	s	1-312	[»]
3J16	electron microscopy	-	G	1-312	[»]
3O5H	X-ray	4.00	M	1-312	[»]
3U5I	X-ray	3.00	q	1-312	[»]
4B6A	electron microscopy	8.10	q	1-312	[»]

ProteinModelPortal

P05317.

SMR

P05317. Positions 3-257.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1582N.

IntAct

P05317. 270 interactions.

MINT

MINT-384116.

STRING

4932.YLR340W.

2D gel databases

SWISS-2DPAGE

P05317.

Proteomic databases

PaxDb

P05317.

PeptideAtlas

P05317.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR340W; YLR340W; YLR340W.

GeneID

851052.

KEGG

sce:YLR340W.

Organism-specific databases

SGD

S000004332. RPP0.

Phylogenomic databases

eggNOG

COG0244.

GeneTree

ENSGT00390000017839.

HOGENOM

HOG000210987.

K02941.

OMA

PILSTFG.

OrthoDB

EOG4Z39PT.

Gene expression databases

Genevestigator

P05317.

GermOnline

YLR340W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001813. Ribosomal_60S.
IPR001790. Ribosomal_L10/acidic_P0.
[Graphical view]

Pfam

PF00428. Ribosomal_60s. 1 hit.
PF00466. Ribosomal_L10. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967667.

Entry information

Entry name

RLA0_YEAST

Accession

Primary (citable) accession number: P05317
Secondary accession number(s): D6VYX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

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

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents