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P48589 (RS12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S12
Gene names
Name:RPS12
Ordered Locus Names:YOR369C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Component of the small 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). Ref.6

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ribosomal protein S12e family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcytoplasmic translation

Inferred by curator. Source: SGD

   Cellular componentcytosolic small ribosomal subunit

Inferred from direct assay. Source: SGD

   Molecular functionstructural constituent of ribosome

Inferred from direct assay. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14314340S ribosomal protein S12
PRO_0000122340

Amino acid modifications

Modified residue641Phosphoserine Ref.7
Modified residue651Phosphoserine Ref.7 Ref.8
Modified residue1191Phosphoserine Ref.8

Experimental info

Sequence conflict90 – 923KVA → EGLP in AAA69926. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48589 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 7BD0434EB06A26B3

FASTA14315,472
        10         20         30         40         50         60 
MSDVEEVVEV QEETVVEQTA EVTIEDALKV VLRTALVHDG LARGLRESTK ALTRGEALLV 

        70         80         90        100        110        120 
VLVSSVTEAN IIKLVEGLAN DPENKVPLIK VADAKQLGEW AGLGKIDREG NARKVVGASV 

       130        140 
VVVKNWGAET DELSMIMEHF SQQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of RAD17, a gene controlling cell cycle responses to DNA damage in Saccharomyces cerevisiae."
Siede W., Nusspaumer G., Portillo V., Rodriguez R., Friedberg E.C.
Nucleic Acids Res. 24:1669-1675(1996) [PubMed: 8649984] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Yeast homologue of ribosomal protein S12."
Teply R.
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 44774 / DBY747.
[3]"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: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]Moore J., Jacobs H.T., Kaiser K.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 29-126.
Strain: ATCC 204660 / DBY746.
[6]"The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
Planta R.J., Mager W.H.
Yeast 14:471-477(1998) [PubMed: 9559554] [Abstract]
Cited for: NOMENCLATURE, SUBUNIT.
[7]"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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-65, MASS SPECTROMETRY.
[8]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-119, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37460 Genomic DNA. Translation: AAA80546.1.
U01049 Genomic DNA. Translation: AAA69926.1.
Z75277 Genomic DNA. Translation: CAA99700.1.
U24143 mRNA. Translation: AAA65439.1. Sequence problems.
BK006948 Genomic DNA. Translation: DAA11128.1.
PIRS62102.
RefSeqNP_015014.1. NM_001183789.1.

3D structure databases

ProteinModelPortalP48589.
SMRP48589. Positions 13-142.
ModBaseSearch...

Protein-protein interaction databases

IntActP48589. 4 interactions.
MINTMINT-1325368.
STRINGP48589.

Proteomic databases

PeptideAtlasP48589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR369C; YOR369C; YOR369C.
GeneID854551.
KEGGsce:YOR369C.
NMPDRfig|4932.3.peg.6133.

Organism-specific databases

CYGDYOR369c.
SGDS000005896. RPS12.

Phylogenomic databases

eggNOGfuNOG10041.
GeneTreeEFGT00050000004062.
HOGENOMHBG319268.
OMACVLAENC.
OrthoDBEOG4TB7MV.

Gene expression databases

ArrayExpressP48589.
GenevestigatorP48589.
GermOnlineYOR369C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR000530. Ribosomal_S12e.
[Graphical view]
KOK02951.
PANTHERPTHR11843. Ribosomal_S12e. 1 hit.
PfamPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSPR00972. RIBSOMALS12E.
PROSITEPS01189. RIBOSOMAL_S12E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976970.

Entry information

Entry nameRS12_YEAST
AccessionPrimary (citable) accession number: P48589
Secondary accession number(s): D6W362, Q02545
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families