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Protein

40S ribosomal protein S15

Gene

RPS15

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. RNA binding Source: InterPro
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Ribosome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-33454-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_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S15
Alternative name(s):
RIG protein
RP52
S21
YS21
Gene namesi
Name:RPS15
Synonyms:RPS21
Ordered Locus Names:YOL040C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL040c.
SGDiS000005400. RPS15.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 14214140S ribosomal protein S15PRO_0000130051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ01855.
PaxDbiQ01855.
PeptideAtlasiQ01855.

Expressioni

Gene expression databases

GenevestigatoriQ01855.

Interactioni

Subunit structurei

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).1 Publication

Protein-protein interaction databases

BioGridi34362. 74 interactions.
IntActiQ01855. 5 interactions.
MINTiMINT-4986189.
STRINGi4932.YOL040C.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 194Combined sources
Helixi22 – 265Combined sources
Helixi30 – 345Combined sources
Helixi39 – 468Combined sources
Beta strandi50 – 534Combined sources
Helixi54 – 629Combined sources
Beta strandi65 – 673Combined sources
Beta strandi69 – 713Combined sources
Beta strandi76 – 783Combined sources
Helixi87 – 893Combined sources
Beta strandi93 – 10614Combined sources
Helixi109 – 1113Combined sources
Helixi116 – 1194Combined sources
Beta strandi131 – 1333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-S47-126[»]
3J6Xelectron microscopy6.10151-142[»]
3J6Yelectron microscopy6.10151-142[»]
3J77electron microscopy6.20151-142[»]
3J78electron microscopy6.30151-142[»]
3V88X-ray3.00P1-142[»]
4U3MX-ray3.00C5/c52-142[»]
4U3NX-ray3.20C5/c52-142[»]
4U3UX-ray2.90C5/c52-142[»]
4U4NX-ray3.10C5/c52-142[»]
4U4OX-ray3.60C5/c52-142[»]
4U4QX-ray3.00C5/c52-142[»]
4U4RX-ray2.80C5/c52-142[»]
4U4UX-ray3.00C5/c52-142[»]
4U4YX-ray3.20C5/c52-142[»]
4U4ZX-ray3.10C5/c52-142[»]
4U50X-ray3.20C5/c52-142[»]
4U51X-ray3.20C5/c52-142[»]
4U52X-ray3.00C5/c52-142[»]
4U53X-ray3.30C5/c52-142[»]
4U55X-ray3.20C5/c52-142[»]
4U56X-ray3.45C5/c52-142[»]
4U6FX-ray3.10C5/c52-142[»]
4V4Belectron microscopy11.70AS47-126[»]
4V6Ielectron microscopy8.80AR1-142[»]
4V7RX-ray4.00AI/CI1-142[»]
4V88X-ray3.00AP/CP1-142[»]
4V8Yelectron microscopy4.30AP1-142[»]
4V8Zelectron microscopy6.60AP1-142[»]
4V92electron microscopy3.70P12-126[»]
ProteinModelPortaliQ01855.
SMRiQ01855. Positions 4-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01855.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S19P family.Curated

Phylogenomic databases

eggNOGiCOG0185.
GeneTreeiENSGT00390000000475.
HOGENOMiHOG000111561.
InParanoidiQ01855.
KOiK02958.
OMAiHGSPGMG.
OrthoDBiEOG7FBRW1.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19.
InterProiIPR002222. Ribosomal_S19.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
IPR005713. Ribosomal_S19A/S15e.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01025. rpsS_arch. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01855-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAVNAKKR VFKTHSYRGV DLEKLLEMST EDFVKLAPAR VRRRFARGMT
60 70 80 90 100
SKPAGFMKKL RAAKLAAPEN EKPAPVRTHM RNMIIVPEMI GSVVGIYNGK
110 120 130 140
AFNQVEIRPE MLGHYLGEFS ITYTPVRHGR AGATTSRFIP LK
Length:142
Mass (Da):16,002
Last modified:April 1, 1993 - v1
Checksum:i06B564FD68051CD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS24053.
RefSeqiNP_014602.1. NM_001183294.1.

Genome annotation databases

EnsemblFungiiYOL040C; YOL040C; YOL040C.
GeneIDi854117.
KEGGisce:YOL040C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS24053.
RefSeqiNP_014602.1. NM_001183294.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-S47-126[»]
3J6Xelectron microscopy6.10151-142[»]
3J6Yelectron microscopy6.10151-142[»]
3J77electron microscopy6.20151-142[»]
3J78electron microscopy6.30151-142[»]
3V88X-ray3.00P1-142[»]
4U3MX-ray3.00C5/c52-142[»]
4U3NX-ray3.20C5/c52-142[»]
4U3UX-ray2.90C5/c52-142[»]
4U4NX-ray3.10C5/c52-142[»]
4U4OX-ray3.60C5/c52-142[»]
4U4QX-ray3.00C5/c52-142[»]
4U4RX-ray2.80C5/c52-142[»]
4U4UX-ray3.00C5/c52-142[»]
4U4YX-ray3.20C5/c52-142[»]
4U4ZX-ray3.10C5/c52-142[»]
4U50X-ray3.20C5/c52-142[»]
4U51X-ray3.20C5/c52-142[»]
4U52X-ray3.00C5/c52-142[»]
4U53X-ray3.30C5/c52-142[»]
4U55X-ray3.20C5/c52-142[»]
4U56X-ray3.45C5/c52-142[»]
4U6FX-ray3.10C5/c52-142[»]
4V4Belectron microscopy11.70AS47-126[»]
4V6Ielectron microscopy8.80AR1-142[»]
4V7RX-ray4.00AI/CI1-142[»]
4V88X-ray3.00AP/CP1-142[»]
4V8Yelectron microscopy4.30AP1-142[»]
4V8Zelectron microscopy6.60AP1-142[»]
4V92electron microscopy3.70P12-126[»]
ProteinModelPortaliQ01855.
SMRiQ01855. Positions 4-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34362. 74 interactions.
IntActiQ01855. 5 interactions.
MINTiMINT-4986189.
STRINGi4932.YOL040C.

Proteomic databases

MaxQBiQ01855.
PaxDbiQ01855.
PeptideAtlasiQ01855.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL040C; YOL040C; YOL040C.
GeneIDi854117.
KEGGisce:YOL040C.

Organism-specific databases

CYGDiYOL040c.
SGDiS000005400. RPS15.

Phylogenomic databases

eggNOGiCOG0185.
GeneTreeiENSGT00390000000475.
HOGENOMiHOG000111561.
InParanoidiQ01855.
KOiK02958.
OMAiHGSPGMG.
OrthoDBiEOG7FBRW1.

Enzyme and pathway databases

BioCyciYEAST:G3O-33454-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_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Miscellaneous databases

EvolutionaryTraceiQ01855.
NextBioi975816.
PROiQ01855.

Gene expression databases

GenevestigatoriQ01855.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19.
InterProiIPR002222. Ribosomal_S19.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
IPR005713. Ribosomal_S19A/S15e.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01025. rpsS_arch. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1991) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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(1997) [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(1998) [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(2003) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2011) [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(2000) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 47-126, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiRS15_YEAST
AccessioniPrimary (citable) accession number: Q01855
Secondary accession number(s): D6W226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 1, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.