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Protein

40S ribosomal protein S5

Gene

RPS5

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

GO - Molecular functioni

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

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. regulation of translational fidelity Source: SGD
  3. rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-31744-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 S5
Alternative name(s):
RP14
S2
YS8
Gene namesi
Name:RPS5
Synonyms:RPS2
Ordered Locus Names:YJR123W
ORF Names:J2045
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

SGDiS000003884. RPS5.

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 – 22522440S ribosomal protein S5PRO_0000124540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei27 – 271Phosphothreonine1 Publication

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26783.
PaxDbiP26783.
PeptideAtlasiP26783.
PRIDEiP26783.

2D gel databases

UCD-2DPAGEP26783.

Expressioni

Gene expression databases

GenevestigatoriP26783.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
BUL1P485243EBI-16150,EBI-3881

Protein-protein interaction databases

BioGridi33879. 158 interactions.
DIPiDIP-5092N.
IntActiP26783. 66 interactions.
MINTiMINT-480795.
STRINGi4932.YJR123W.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 388Combined sources
Beta strandi43 – 453Combined sources
Beta strandi48 – 503Combined sources
Turni56 – 583Combined sources
Turni59 – 613Combined sources
Beta strandi69 – 713Combined sources
Beta strandi78 – 803Combined sources
Helixi83 – 864Combined sources
Helixi89 – 957Combined sources
Helixi101 – 1033Combined sources
Helixi107 – 12317Combined sources
Helixi129 – 13810Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi157 – 1615Combined sources
Helixi164 – 18320Combined sources
Beta strandi186 – 1883Combined sources
Helixi190 – 20213Combined sources
Beta strandi206 – 2083Combined sources
Helixi209 – 22214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-G76-225[»]
2NOQelectron microscopy7.30F76-225[»]
3J6Xelectron microscopy6.10S51-225[»]
3J6Yelectron microscopy6.10S51-225[»]
3J77electron microscopy6.20S51-225[»]
3J78electron microscopy6.30S51-225[»]
3V88X-ray3.00F1-225[»]
4U3MX-ray3.00S5/s52-225[»]
4U3NX-ray3.20S5/s52-225[»]
4U3UX-ray2.90S5/s52-225[»]
4U4NX-ray3.10S5/s52-225[»]
4U4OX-ray3.60S5/s52-225[»]
4U4QX-ray3.00S5/s52-225[»]
4U4RX-ray2.80S5/s52-225[»]
4U4UX-ray3.00S5/s52-225[»]
4U4YX-ray3.20S5/s52-225[»]
4U4ZX-ray3.10S5/s52-225[»]
4U50X-ray3.20S5/s52-225[»]
4U51X-ray3.20S5/s52-225[»]
4U52X-ray3.00S5/s52-225[»]
4U53X-ray3.30S5/s52-225[»]
4U55X-ray3.20S5/s52-225[»]
4U56X-ray3.45S5/s52-225[»]
4U6FX-ray3.10S5/s52-225[»]
4V4Belectron microscopy11.70AG76-225[»]
4V6Ielectron microscopy8.80AF1-225[»]
4V7RX-ray4.00AD/CD1-225[»]
4V88X-ray3.00AF/CF1-225[»]
4V8Yelectron microscopy4.30AF1-225[»]
4V8Zelectron microscopy6.60AF1-225[»]
4V92electron microscopy3.70F20-225[»]
ProteinModelPortaliP26783.
SMRiP26783. Positions 20-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26783.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S7P family.Curated

Phylogenomic databases

eggNOGiCOG0049.
GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
InParanoidiP26783.
KOiK02989.
OMAiDSLMMKG.
OrthoDBiEOG7MD52N.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. S7_S5_E_A. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDTEAPVEV QEDFEVVEEF TPVVLATPIP EEVQQAQTEI KLFNKWSFEE
60 70 80 90 100
VEVKDASLVD YVQVRQPIFV AHTAGRYANK RFRKAQCPII ERLTNSLMMN
110 120 130 140 150
GRNNGKKLKA VRIIKHTLDI INVLTDQNPI QVVVDAITNT GPREDTTRVG
160 170 180 190 200
GGGAARRQAV DVSPLRRVNQ AIALLTIGAR EAAFRNIKTI AETLAEELIN
210 220
AAKGSSTSYA IKKKDELERV AKSNR
Length:225
Mass (Da):25,039
Last modified:January 22, 2007 - v3
Checksum:iCD3F743B56CB1127
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211T → E AA sequence (PubMed:1544921).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89368 Genomic DNA. Translation: CAA61550.1.
Z49623 Genomic DNA. Translation: CAA89654.1.
AY692868 Genomic DNA. Translation: AAT92887.1.
BK006943 Genomic DNA. Translation: DAA08908.1.
PIRiS55720.
RefSeqiNP_012657.1. NM_001181781.1.

Genome annotation databases

EnsemblFungiiYJR123W; YJR123W; YJR123W.
GeneIDi853587.
KEGGisce:YJR123W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89368 Genomic DNA. Translation: CAA61550.1.
Z49623 Genomic DNA. Translation: CAA89654.1.
AY692868 Genomic DNA. Translation: AAT92887.1.
BK006943 Genomic DNA. Translation: DAA08908.1.
PIRiS55720.
RefSeqiNP_012657.1. NM_001181781.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-G76-225[»]
2NOQelectron microscopy7.30F76-225[»]
3J6Xelectron microscopy6.10S51-225[»]
3J6Yelectron microscopy6.10S51-225[»]
3J77electron microscopy6.20S51-225[»]
3J78electron microscopy6.30S51-225[»]
3V88X-ray3.00F1-225[»]
4U3MX-ray3.00S5/s52-225[»]
4U3NX-ray3.20S5/s52-225[»]
4U3UX-ray2.90S5/s52-225[»]
4U4NX-ray3.10S5/s52-225[»]
4U4OX-ray3.60S5/s52-225[»]
4U4QX-ray3.00S5/s52-225[»]
4U4RX-ray2.80S5/s52-225[»]
4U4UX-ray3.00S5/s52-225[»]
4U4YX-ray3.20S5/s52-225[»]
4U4ZX-ray3.10S5/s52-225[»]
4U50X-ray3.20S5/s52-225[»]
4U51X-ray3.20S5/s52-225[»]
4U52X-ray3.00S5/s52-225[»]
4U53X-ray3.30S5/s52-225[»]
4U55X-ray3.20S5/s52-225[»]
4U56X-ray3.45S5/s52-225[»]
4U6FX-ray3.10S5/s52-225[»]
4V4Belectron microscopy11.70AG76-225[»]
4V6Ielectron microscopy8.80AF1-225[»]
4V7RX-ray4.00AD/CD1-225[»]
4V88X-ray3.00AF/CF1-225[»]
4V8Yelectron microscopy4.30AF1-225[»]
4V8Zelectron microscopy6.60AF1-225[»]
4V92electron microscopy3.70F20-225[»]
ProteinModelPortaliP26783.
SMRiP26783. Positions 20-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33879. 158 interactions.
DIPiDIP-5092N.
IntActiP26783. 66 interactions.
MINTiMINT-480795.
STRINGi4932.YJR123W.

2D gel databases

UCD-2DPAGEP26783.

Proteomic databases

MaxQBiP26783.
PaxDbiP26783.
PeptideAtlasiP26783.
PRIDEiP26783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR123W; YJR123W; YJR123W.
GeneIDi853587.
KEGGisce:YJR123W.

Organism-specific databases

SGDiS000003884. RPS5.

Phylogenomic databases

eggNOGiCOG0049.
GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
InParanoidiP26783.
KOiK02989.
OMAiDSLMMKG.
OrthoDBiEOG7MD52N.

Enzyme and pathway databases

BioCyciYEAST:G3O-31744-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

EvolutionaryTraceiP26783.
NextBioi974388.
PROiP26783.

Gene expression databases

GenevestigatoriP26783.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. S7_S5_E_A. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae."
    Ignatovich O., Cooper M., Kulesza H.M., Beggs J.D.
    Nucleic Acids Res. 23:4616-4619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1995) [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. "NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae."
    Takakura H., Tsunasawa S., Miyagi M., Warner J.R.
    J. Biol. Chem. 267:5442-5445(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, ACETYLATION AT SER-2 BY NATA.
  6. "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.
  7. "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.
  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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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].
  10. "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 76-225, ELECTRON MICROSCOPY.
  11. "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 76-225, ELECTRON MICROSCOPY.
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 76-225.

Entry informationi

Entry nameiRS5_YEAST
AccessioniPrimary (citable) accession number: P26783
Secondary accession number(s): D6VWU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.