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P05319 (RLA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 140. 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-alpha

Short name=P2A
Alternative name(s):
A2
L12EIB
L44
YP2alpha
Gene names
Name:RPP2A
Synonyms:L12EIB, RPA2, RPL44, RPLA2
Ordered Locus Names:YOL039W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length106 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 P1B-P2A. 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.8 Ref.11 Ref.14

Subcellular location

Cytoplasm Ref.12.

Post-translational modification

Phosphorylation is not involved in the interaction of the acidic P proteins with the ribosome, however it is suggested to affect the ribosome activity and to participate in a possible ribosome regulatory mechanism. HAMAP-Rule MF_01478

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 428000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ribosomal protein L12P family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPP0P053172EBI-15456,EBI-15447
RPP1BP106222EBI-15456,EBI-15460

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10610660S acidic ribosomal protein P2-alpha HAMAP-Rule MF_01478
PRO_0000157681

Amino acid modifications

Modified residue161Phosphothreonine Ref.16
Modified residue401Phosphoserine Ref.17
Modified residue431Phosphoserine Ref.17
Modified residue491Phosphoserine Ref.16 Ref.17
Modified residue961Phosphoserine Ref.15 Ref.16 Ref.17

Sequences

Sequence LengthMass (Da)Tools
P05319 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 22275AFA35E1A32E

FASTA10610,746
        10         20         30         40         50         60 
MKYLAAYLLL NAAGNTPDAT KIKAILESVG IEIEDEKVSS VLSALEGKSV DELITEGNEK 

        70         80         90        100 
LAAVPAAGPA SAGGAAAASG DAAAEEEKEE EAAEESDDDM GFGLFD 

« Hide

References

« Hide 'large scale' references
[1]"cDNA and deduced amino acid sequence of acidic ribosomal protein A2 from Saccharomyces cerevisiae."
Mitsui K., Tsurugi K.
Nucleic Acids Res. 16:3575-3575(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: IFO 40028.
[2]"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].
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"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.
[8]"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.
[9]"Phosphorylation of the yeast ribosomal stalk. Functional effects and enzymes involved in the process."
Ballesta J.P.G., Rodriguez-Gabriel M.A., Bou G., Briones E., Zambrano R., Remacha M.
FEMS Microbiol. Rev. 23:537-550(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE OF PHOSPHORYLATION.
[10]"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.
[11]"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 RPP1B.
[12]"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].
[13]"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].
[14]"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 RPP1B.
[15]"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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[16]"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 THR-16; SER-49 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-40; SER-43; SER-49 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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
X06958 mRNA. Translation: CAA30028.1.
J03760 Genomic DNA. Translation: AAA34971.1.
M26503 Genomic DNA. Translation: AAA34735.1.
Z74781 Genomic DNA. Translation: CAA99041.1.
AY692793 Genomic DNA. Translation: AAT92812.1.
BK006948 Genomic DNA. Translation: DAA10743.1.
PIRR5BYIB. B28104.
RefSeqNP_014603.1. NM_001183293.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IZSelectron microscopy-v/w1-106[»]
ProteinModelPortalP05319.
SMRP05319. Positions 1-68.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34363. 64 interactions.
DIPDIP-2506N.
IntActP05319. 22 interactions.
MINTMINT-531798.
STRING4932.YOL039W.

Protein family/group databases

Allergome9537. Sac c P2.

Proteomic databases

MaxQBP05319.
PaxDbP05319.
PeptideAtlasP05319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL039W; YOL039W; YOL039W.
GeneID854118.
KEGGsce:YOL039W.

Organism-specific databases

CYGDYOL039w.
SGDS000005399. RPP2A.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycYEAST:G3O-33453-MONOMER.

Gene expression databases

GenevestigatorP05319.

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

NextBio975819.

Entry information

Entry nameRLA2_YEAST
AccessionPrimary (citable) accession number: P05319
Secondary accession number(s): D6W227
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 11, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: 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