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P05318 (RLA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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 P1-alpha

Short name=P1A
Alternative name(s):
A1
L12EIIA
YP1alpha
Gene names
Name:RPP1A
Synonyms:L12EIIA, RPA1, RPLA1
Ordered Locus Names:YDL081C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length106 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.8 Ref.9 Ref.11

Subcellular location

Cytoplasm Ref.12.

Post-translational modification

N-terminally acetylated by acetyltransferase NatA. Ref.7 Ref.10

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.

Sequence similarities

Belongs to the ribosomal protein L12P family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPP0P053174EBI-15452,EBI-15447
RPP2BP024002EBI-15452,EBI-15464

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.10
Chain2 – 10610560S acidic ribosomal protein P1-alpha HAMAP-Rule MF_01478
PRO_0000157705

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.10
Modified residue961Phosphoserine Ref.13 Ref.14

Experimental info

Sequence conflict371V → D in CAA30027. Ref.1
Sequence conflict371V → D in CAA31976. Ref.2
Sequence conflict371V → D in BAA14113. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P05318 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: 9A2FE94D28640ACC

FASTA10610,908
        10         20         30         40         50         60 
MSTESALSYA ALILADSEIE ISSEKLLTLT NAANVPVENI WADIFAKALD GQNLKDLLVN 

        70         80         90        100 
FSAGAAAPAG VAGGVAGGEA GEAEAEKEEE EAKEESDDDM GFGLFD 

« Hide

References

« Hide 'large scale' references
[1]"cDNA and deduced amino acid sequence of acidic ribosomal protein A1 from Saccharomyces cerevisiae."
Tsurugi K., Mitsui K.
Nucleic Acids Res. 16:3574-3574(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: IFO 40028.
[2]"Identification of A1 protein as the fourth member of 13 kDa-type acidic ribosomal protein family in yeast Saccharomyces cerevisiae."
Mitsui K., Tsurugi K.
Biochem. Biophys. Res. Commun. 161:1001-1006(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IFO 40028.
[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 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.
[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 2-5, ACETYLATION AT SER-2, PHOSPHORYLATION.
[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]"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 RPP2B.
[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: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
[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 RPP2B.
[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]"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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06957 mRNA. Translation: CAA30027.1.
X13682 Genomic DNA. Translation: CAA31976.1.
D90072 Genomic DNA. Translation: BAA14113.1.
M26504 Genomic DNA. Translation: AAA34733.1.
Z74129 Genomic DNA. Translation: CAA98647.1.
AY558526 Genomic DNA. Translation: AAS56852.1.
BK006938 Genomic DNA. Translation: DAA11778.1.
PIRR5BY2A. S67617.
RefSeqNP_010202.1. NM_001180140.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IZSelectron microscopy-t/u1-106[»]
DisProtDP00164.
ProteinModelPortalP05318.
SMRP05318. Positions 3-106.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31980. 125 interactions.
DIPDIP-1583N.
IntActP05318. 19 interactions.
MINTMINT-384141.
STRING4932.YDL081C.

Proteomic databases

MaxQBP05318.
PaxDbP05318.
PeptideAtlasP05318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL081C; YDL081C; YDL081C.
GeneID851478.
KEGGsce:YDL081C.

Organism-specific databases

SGDS000002239. RPP1A.

Phylogenomic databases

eggNOGCOG2058.
GeneTreeENSGT00730000113211.
HOGENOMHOG000229898.
KOK02942.
OMASIESYWP.
OrthoDBEOG7J70V7.

Enzyme and pathway databases

BioCycYEAST:G3O-29490-MONOMER.

Gene expression databases

GenevestigatorP05318.

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

NextBio968786.

Entry information

Entry nameRLA1_YEAST
AccessionPrimary (citable) accession number: P05318
Secondary accession number(s): D6VRR8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 130 of the entry and version 4 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