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Protein

60S acidic ribosomal protein P2-beta

Gene

RPP2B

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: SGD
  3. translational elongation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-29930-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P2-beta
Short name:
P2B
Alternative name(s):
L12EIA
L45
YL44C
YP2beta
YPA1
Gene namesi
Name:RPP2B
Synonyms:L12EIA, RPL45, RPLA4
Ordered Locus Names:YDR382W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR382w.
SGDiS000002790. RPP2B.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11011060S acidic ribosomal protein P2-betaPRO_0000157682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei100 – 1001Phosphoserine3 Publications

Post-translational modificationi

The N-terminus is not modified.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP02400.
PaxDbiP02400.
PeptideAtlasiP02400.

Expressioni

Gene expression databases

GenevestigatoriP02400.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPP1AP053182EBI-15464,EBI-15452

Protein-protein interaction databases

BioGridi32443. 204 interactions.
DIPiDIP-580N.
IntActiP02400. 31 interactions.
MINTiMINT-411356.
STRINGi4932.YDR382W.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2DX-ray2.22B100-105[»]
3N3XX-ray1.70B100-105[»]
DisProtiDP00002.
ProteinModelPortaliP02400.
SMRiP02400. Positions 1-70.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02400.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiCOG2058.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
InParanoidiP02400.
KOiK02943.
OMAiAEIDETK.
OrthoDBiEOG708WC9.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYLAAYLLL VQGGNAAPSA ADIKAVVESV GAEVDEARIN ELLSSLEGKG
60 70 80 90 100
SLEEIIAEGQ KKFATVPTGG ASSAAAGAAG AAAGGDAAEE EKEEEAKEES
110
DDDMGFGLFD
Length:110
Mass (Da):11,050
Last modified:June 30, 1989 - v2
Checksum:iEC45406CB5F199F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 784AAGA → GPAS AA sequence (PubMed:7030402).Curated
Sequence conflicti86 – 872DA → GD AA sequence (PubMed:7030402).Curated
Sequence conflicti89 – 891E → A AA sequence (PubMed:7030402).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA35109. R5BYA1.
RefSeqiNP_010670.3. NM_001180690.3.

Genome annotation databases

EnsemblFungiiYDR382W; YDR382W; YDR382W.
GeneIDi851990.
KEGGisce:YDR382W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA35109. R5BYA1.
RefSeqiNP_010670.3. NM_001180690.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2DX-ray2.22B100-105[»]
3N3XX-ray1.70B100-105[»]
DisProtiDP00002.
ProteinModelPortaliP02400.
SMRiP02400. Positions 1-70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32443. 204 interactions.
DIPiDIP-580N.
IntActiP02400. 31 interactions.
MINTiMINT-411356.
STRINGi4932.YDR382W.

Proteomic databases

MaxQBiP02400.
PaxDbiP02400.
PeptideAtlasiP02400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR382W; YDR382W; YDR382W.
GeneIDi851990.
KEGGisce:YDR382W.

Organism-specific databases

CYGDiYDR382w.
SGDiS000002790. RPP2B.

Phylogenomic databases

eggNOGiCOG2058.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
InParanoidiP02400.
KOiK02943.
OMAiAEIDETK.
OrthoDBiEOG708WC9.

Enzyme and pathway databases

BioCyciYEAST:G3O-29930-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

EvolutionaryTraceiP02400.
NextBioi970154.

Gene expression databases

GenevestigatoriP02400.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1987) [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(1989) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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(1980) [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(1992) [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(1997) [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(1998) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPP1A.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. 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(2005) [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(2006) [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(2006) [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(2007) [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(2008) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRLA4_YEAST
AccessioniPrimary (citable) accession number: P02400
Secondary accession number(s): D6VT16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: June 30, 1989
Last modified: March 31, 2015
This is version 152 of the entry and version 2 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 602000 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.