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Protein

60S acidic ribosomal protein P2-alpha

Gene

RPP2A

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

Plays an important role in the elongation step of protein synthesis.

GO - Molecular functioni

  1. protein kinase activator activity Source: SGD
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. positive regulation of protein kinase activity Source: GOC
  3. translational elongation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-33453-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P2-alpha
Short name:
P2A
Alternative name(s):
A2
L12EIB
L44
YP2alpha
Gene namesi
Name:RPP2A
Synonyms:L12EIB, RPA2, RPL44, RPLA2
Ordered Locus Names:YOL039W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL039w.
SGDiS000005399. RPP2A.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Protein family/group databases

Allergomei9537. Sac c P2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10610660S acidic ribosomal protein P2-alphaPRO_0000157681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphothreonine1 Publication
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei43 – 431Phosphoserine1 Publication
Modified residuei49 – 491Phosphoserine2 Publications
Modified residuei96 – 961Phosphoserine3 Publications

Post-translational modificationi

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.
The N-terminus is not modified.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05319.
PaxDbiP05319.
PeptideAtlasiP05319.

Expressioni

Gene expression databases

GenevestigatoriP05319.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPP0P053172EBI-15456,EBI-15447
RPP1BP106222EBI-15456,EBI-15460

Protein-protein interaction databases

BioGridi34363. 65 interactions.
DIPiDIP-2506N.
IntActiP05319. 22 interactions.
MINTiMINT-531798.
STRINGi4932.YOL039W.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Ielectron microscopy8.80Bv/Bw1-106[»]
ProteinModelPortaliP05319.
SMRiP05319. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiCOG2058.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
InParanoidiP05319.
KOiK02943.
OMAiDDGGMMS.
OrthoDBiEOG708WC9.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR001813. Ribosomal_L10/L12.
IPR027534. Ribosomal_L12.
[Graphical view]
PfamiPF00428. Ribosomal_60s. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05319-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYLAAYLLL NAAGNTPDAT KIKAILESVG IEIEDEKVSS VLSALEGKSV
60 70 80 90 100
DELITEGNEK LAAVPAAGPA SAGGAAAASG DAAAEEEKEE EAAEESDDDM

GFGLFD
Length:106
Mass (Da):10,746
Last modified:November 1, 1988 - v1
Checksum:i22275AFA35E1A32E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB28104. R5BYIB.
RefSeqiNP_014603.1. NM_001183293.1.

Genome annotation databases

EnsemblFungiiYOL039W; YOL039W; YOL039W.
GeneIDi854118.
KEGGisce:YOL039W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB28104. R5BYIB.
RefSeqiNP_014603.1. NM_001183293.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Ielectron microscopy8.80Bv/Bw1-106[»]
ProteinModelPortaliP05319.
SMRiP05319. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34363. 65 interactions.
DIPiDIP-2506N.
IntActiP05319. 22 interactions.
MINTiMINT-531798.
STRINGi4932.YOL039W.

Protein family/group databases

Allergomei9537. Sac c P2.

Proteomic databases

MaxQBiP05319.
PaxDbiP05319.
PeptideAtlasiP05319.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL039W; YOL039W; YOL039W.
GeneIDi854118.
KEGGisce:YOL039W.

Organism-specific databases

CYGDiYOL039w.
SGDiS000005399. RPP2A.

Phylogenomic databases

eggNOGiCOG2058.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
InParanoidiP05319.
KOiK02943.
OMAiDDGGMMS.
OrthoDBiEOG708WC9.

Enzyme and pathway databases

BioCyciYEAST:G3O-33453-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

NextBioi975819.

Gene expression databases

GenevestigatoriP05319.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR001813. Ribosomal_L10/L12.
IPR027534. Ribosomal_L12.
[Graphical view]
PfamiPF00428. Ribosomal_60s. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. 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].

Entry informationi

Entry nameiRLA2_YEAST
AccessioniPrimary (citable) accession number: P05319
Secondary accession number(s): D6W227
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: March 4, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

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 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.