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Q01855 (RS15_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S15
Alternative name(s):
RIG protein
RP52
S21
YS21
Gene names
Name:RPS15
Synonyms:RPS21
Ordered Locus Names:YOL040C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm. Ref.7

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.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00531.

Sequence similarities

Belongs to the ribosomal protein S19P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 14214140S ribosomal protein S15 HAMAP-Rule MF_00531
PRO_0000130051

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.10

Secondary structure

....................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01855 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 06B564FD68051CD2

FASTA14216,002
        10         20         30         40         50         60 
MSQAVNAKKR VFKTHSYRGV DLEKLLEMST EDFVKLAPAR VRRRFARGMT SKPAGFMKKL 

        70         80         90        100        110        120 
RAAKLAAPEN EKPAPVRTHM RNMIIVPEMI GSVVGIYNGK AFNQVEIRPE MLGHYLGEFS 

       130        140 
ITYTPVRHGR AGATTSRFIP LK 

« Hide

References

« Hide 'large scale' references
[1]"Structural determination of Saccharomyces cerevisiae rig gene and identification of its product as ribosomal protein S21."
Takasawa S., Tohgo A., Unno M., Yonekura H., Okamoto H.
FEBS Lett. 307:318-323(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"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.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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.
[5]"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.
[6]"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.
[7]"The ribosomal protein Rps15p is required for nuclear exit of the 40S subunit precursors in yeast."
Leger-Silvestre I., Milkereit P., Ferreira-Cerca S., Saveanu C., Rousselle J.-C., Choesmel V., Guinefoleau C., Gas N., Gleizes P.-E.
EMBO J. 23:2336-2347(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 47-126, ELECTRON MICROSCOPY.
[13]"Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 47-126, ELECTRON MICROSCOPY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11386 mRNA. Translation: BAA01982.1.
D11387 Genomic DNA. Translation: BAA01983.1.
Z74782 Genomic DNA. Translation: CAA99042.1.
AY558426 Genomic DNA. Translation: AAS56752.1.
BK006948 Genomic DNA. Translation: DAA10742.1.
PIRS24053.
RefSeqNP_014602.1. NM_001183294.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-S47-126[»]
1S1Helectron microscopy11.70S47-126[»]
3IZBelectron microscopy-R1-142[»]
3O2ZX-ray4.00I1-142[»]
3O30X-ray4.00I1-142[»]
3U5CX-ray3.00P1-142[»]
3U5GX-ray3.00P1-142[»]
4BYLelectron microscopy4.30P1-142[»]
4BYTelectron microscopy6.60P1-142[»]
ProteinModelPortalQ01855.
SMRQ01855. Positions 4-138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34362. 73 interactions.
IntActQ01855. 5 interactions.
MINTMINT-4986189.
STRING4932.YOL040C.

Proteomic databases

PaxDbQ01855.
PeptideAtlasQ01855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL040C; YOL040C; YOL040C.
GeneID854117.
KEGGsce:YOL040C.

Organism-specific databases

CYGDYOL040c.
SGDS000005400. RPS15.

Phylogenomic databases

eggNOGCOG0185.
GeneTreeENSGT00390000000475.
HOGENOMHOG000111561.
KOK02958.
OMAMVILPEM.
OrthoDBEOG7FBRW1.

Enzyme and pathway databases

BioCycYEAST:G3O-33454-MONOMER.

Gene expression databases

GenevestigatorQ01855.

Family and domain databases

Gene3D3.30.860.10. 1 hit.
HAMAPMF_00531. Ribosomal_S19.
InterProIPR002222. Ribosomal_S19.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
IPR005713. Ribosomal_S19A/S15e.
[Graphical view]
PANTHERPTHR11880. PTHR11880. 1 hit.
PfamPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSPR00975. RIBOSOMALS19.
SUPFAMSSF54570. SSF54570. 1 hit.
TIGRFAMsTIGR01025. rpsS_arch. 1 hit.
PROSITEPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01855.
NextBio975816.
PROQ01855.

Entry information

Entry nameRS15_YEAST
AccessionPrimary (citable) accession number: Q01855
Secondary accession number(s): D6W226
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: March 19, 2014
This is version 120 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