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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: 5 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

  • RNA binding Source: InterPro
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • ribosomal small subunit assembly Source: GO_Central
  • 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.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL040C.
SGDiS000005400. RPS15.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001300512 – 14240S ribosomal protein S15Add BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Cross-linki24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ01855.
PRIDEiQ01855.
TopDownProteomicsiQ01855.

PTM databases

iPTMnetiQ01855.

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. 35 interactors.
IntActiQ01855. 6 interactors.
MINTiMINT-4986189.

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Helixi22 – 26Combined sources5
Helixi30 – 34Combined sources5
Helixi39 – 46Combined sources8
Beta strandi50 – 53Combined sources4
Helixi54 – 62Combined sources9
Beta strandi65 – 67Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi76 – 78Combined sources3
Helixi87 – 89Combined sources3
Beta strandi93 – 106Combined sources14
Helixi109 – 111Combined sources3
Helixi116 – 119Combined sources4
Beta strandi131 – 133Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DATX-ray3.15C5/c52-138[»]
5DC3X-ray3.25C5/c52-142[»]
5FCIX-ray3.40C5/c52-142[»]
5FCJX-ray3.10C5/c52-142[»]
5I4LX-ray3.10C5/c51-142[»]
5JUOelectron microscopy4.00MB1-142[»]
5JUPelectron microscopy3.50MB1-142[»]
5JUSelectron microscopy4.20MB1-142[»]
5JUTelectron microscopy4.00MB1-142[»]
5JUUelectron microscopy4.00MB1-142[»]
ProteinModelPortaliQ01855.
SMRiQ01855.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01855.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S19P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000000475.
HOGENOMiHOG000111561.
InParanoidiQ01855.
KOiK02958.
OMAiARVRRKF.
OrthoDBiEOG092C5E45.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19. 1 hit.
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. uS19_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
PDB 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[»]
5DATX-ray3.15C5/c52-138[»]
5DC3X-ray3.25C5/c52-142[»]
5FCIX-ray3.40C5/c52-142[»]
5FCJX-ray3.10C5/c52-142[»]
5I4LX-ray3.10C5/c51-142[»]
5JUOelectron microscopy4.00MB1-142[»]
5JUPelectron microscopy3.50MB1-142[»]
5JUSelectron microscopy4.20MB1-142[»]
5JUTelectron microscopy4.00MB1-142[»]
5JUUelectron microscopy4.00MB1-142[»]
ProteinModelPortaliQ01855.
SMRiQ01855.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34362. 35 interactors.
IntActiQ01855. 6 interactors.
MINTiMINT-4986189.

PTM databases

iPTMnetiQ01855.

Proteomic databases

MaxQBiQ01855.
PRIDEiQ01855.
TopDownProteomicsiQ01855.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YOL040C.
SGDiS000005400. RPS15.

Phylogenomic databases

GeneTreeiENSGT00390000000475.
HOGENOMiHOG000111561.
InParanoidiQ01855.
KOiK02958.
OMAiARVRRKF.
OrthoDBiEOG092C5E45.

Enzyme and pathway databases

BioCyciYEAST:G3O-33454-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiQ01855.
PROiQ01855.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19. 1 hit.
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. uS19_arch. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 147 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

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 one 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.