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P02400 (RLA4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S acidic ribosomal protein P2-beta

Short name=P2B
Alternative name(s):
L12EIA
L45
YL44C
YP2beta
YPA1
Gene names
Name:RPP2B
Synonyms:L12EIA, RPL45, RPLA4
Ordered Locus Names:YDR382W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the elongation step of protein synthesis. HAMAP-Rule MF_01478

Subunit structure

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. Ref.7 Ref.9 Ref.12

Subcellular location

Cytoplasm Ref.10.

Post-translational modification

The N-terminus is not modified. HAMAP-Rule MF_01478

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.

Sequence similarities

Belongs to the ribosomal protein L12P family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPP1AP053182EBI-15464,EBI-15452

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11011060S acidic ribosomal protein P2-beta HAMAP-Rule MF_01478
PRO_0000157682

Amino acid modifications

Modified residue291Phosphoserine Ref.14
Modified residue1001Phosphoserine Ref.13 Ref.15 Ref.16

Experimental info

Sequence conflict75 – 784AAGA → GPAS AA sequence Ref.5
Sequence conflict86 – 872DA → GD AA sequence Ref.5
Sequence conflict891E → A AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P02400 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: EC45406CB5F199F4

FASTA11011,050
        10         20         30         40         50         60 
MKYLAAYLLL VQGGNAAPSA ADIKAVVESV GAEVDEARIN ELLSSLEGKG SLEEIIAEGQ 

        70         80         90        100        110 
KKFATVPTGG ASSAAAGAAG AAAGGDAAEE EKEEEAKEES DDDMGFGLFD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRR5BYA1. A35109.
RefSeqNP_010670.3. NM_001180690.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2DX-ray2.22B100-105[»]
DisProtDP00002.
ProteinModelPortalP02400.
SMRP02400. Positions 1-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32443. 203 interactions.
DIPDIP-580N.
IntActP02400. 31 interactions.
MINTMINT-411356.
STRING4932.YDR382W.

Proteomic databases

PaxDbP02400.
PeptideAtlasP02400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR382W; YDR382W; YDR382W.
GeneID851990.
KEGGsce:YDR382W.

Organism-specific databases

CYGDYDR382w.
SGDS000002790. RPP2B.

Phylogenomic databases

eggNOGCOG2058.
GeneTreeENSGT00550000074828.
HOGENOMHOG000229897.
KOK02943.
OMAAEIDETK.
OrthoDBEOG708WC9.

Enzyme and pathway databases

BioCycYEAST:G3O-29930-MONOMER.

Gene expression databases

GenevestigatorP02400.

Family and domain databases

HAMAPMF_01478. Ribosomal_L12_arch.
InterProIPR001813. Ribosomal_L10/L12.
IPR027534. Ribosomal_L12.
[Graphical view]
PfamPF00428. Ribosomal_60s. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02400.
NextBio970154.

Entry information

Entry nameRLA4_YEAST
AccessionPrimary (citable) accession number: P02400
Secondary accession number(s): D6VT16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references