60S acidic ribosomal protein P0 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P05317 (RLA0_YEAST)

Last modified September 2, 2008. Version 83. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the ribosomal protein L10P family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ribosomal large subunit assembly and maintenance Inferred from mutant phenotype. Source: SGD translation Ref.6 Traceable author statement. Source: SGD
Cellular component	90S preribosome Inferred from direct assay. Source: SGD cytosolic large ribosomal subunit Ref.6 Traceable author statement. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural constituent of ribosome Ref.6 Traceable author statement. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
EFT1	P32324	1	EBI-15447,EBI-6333
RPP1A	P05318	4	EBI-15447,EBI-15452
RPP1B	P10622	2	EBI-15447,EBI-15460
RPP2A	P05319	1	EBI-15447,EBI-15456
RPP2B	P02400	1	EBI-15447,EBI-15464

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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

Modified residue

302

Phosphoserine; by CK2

Experimental info

Sequence conflict

Y → N Ref.2 Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P05317-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: D5FE0F9CC70C603C
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FASTA

312

33,766

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

        70         80         90        100        110        120 
RAIRGFLSDL PDFEKLLPFV KGYVGFVFTN 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

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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: 3287327] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: IFO 40028.
[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: 2404943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SR26-12C.
[3]	Erratum Newton C.H., Shimmin L.C., Yee J., Dennis P.P. J. Bacteriol. 172:3535-3535(1990) [PubMed: 2188966] [Abstract]
[4]	"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: 2681177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[6]	"The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae." Planta R.J., Mager W.H. Yeast 14:471-477(1998) [PubMed: 9559554] [Abstract] Cited for: NOMENCLATURE, SUBUNIT.
[7]	"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: 9843429] [Abstract] Cited for: PHOSPHORYLATION AT SER-302.
[8]	"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: 15286401] [Abstract] Cited for: INTERACTION WITH YFL034W.
[9]	"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: 16573688] [Abstract] Cited for: INTERACTION WITH RPP1A; RPP1B; RPP2A AND RPP2B.
[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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, MASS SPECTROMETRY.
[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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X06959 mRNA. Translation: CAA30029.1. M26506 Genomic DNA. Translation: AAA34730.1. M37326 Genomic DNA. Translation: AAA34729.1. D00529 Genomic DNA. Translation: BAA00415.1. X13328 Genomic DNA. Translation: CAA31703.1. U19028 Genomic DNA. Translation: AAB67258.1.
PIR	R5BY0E. S51343.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1582N.
IntAct	P05317.
2-D gel databases
SWISS-2DPAGE	P05317.
Proteomic databases
PeptideAtlas	P05317.
Genome annotation databases
Ensembl	YLR340W. Saccharomyces cerevisiae. [Contig view]
GenomeReviews	Gene locus YLR340W in contig Y13138_GR.
Organism-specific databases
CYGD	YLR340w.
SGD	S000004332. RPP0.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P05317.
Gene expression databases
GermOnline	YLR340W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001813. Ribosomal_60S. IPR001790. Ribosomal_L10. [Graphical view]
Pfam	PF00428. Ribosomal_60s. 1 hit. PF00466. Ribosomal_L10. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...
Other Resources
LinkHub	P05317.

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Entry information

Entry name

RLA0_YEAST

Accession

Primary (citable) accession number: P05317

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	September 2, 2008
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

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

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents