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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

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • regulation of translational fidelity Source: SGD
  • rRNA export from nucleus Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-31744-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 S51 Publication
Alternative name(s):
RP14
S2
Small ribosomal subunit protein uS71 Publication
YS8
Gene namesi
Name:RPS51 Publication
Synonyms:RPS2
Ordered Locus Names:YJR123W
ORF Names:J2045
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR123W.
SGDiS000003884. RPS5.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001245402 – 22540S ribosomal protein S5Add BLAST224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
Modified residuei27PhosphothreonineCombined sources1
Cross-linki45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26783.
PRIDEiP26783.

2D gel databases

UCD-2DPAGEiP26783.

PTM databases

iPTMnetiP26783.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi33879. 90 interactors.
DIPiDIP-5092N.
IntActiP26783. 68 interactors.
MINTiMINT-480795.

Structurei

Secondary structure

1225
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 38Combined sources8
Beta strandi43 – 45Combined sources3
Beta strandi48 – 50Combined sources3
Turni56 – 58Combined sources3
Turni59 – 61Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi78 – 80Combined sources3
Helixi83 – 86Combined sources4
Helixi89 – 95Combined sources7
Helixi101 – 103Combined sources3
Helixi107 – 123Combined sources17
Helixi129 – 138Combined sources10
Beta strandi143 – 148Combined sources6
Beta strandi151 – 154Combined sources4
Beta strandi157 – 161Combined sources5
Helixi164 – 183Combined sources20
Beta strandi186 – 188Combined sources3
Helixi190 – 202Combined sources13
Beta strandi206 – 208Combined sources3
Helixi209 – 222Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DATX-ray3.15S5/s52-225[»]
5DC3X-ray3.25S5/s52-225[»]
5DGEX-ray3.45S5/s52-225[»]
5DGFX-ray3.30S5/s52-225[»]
5DGVX-ray3.10S5/s52-225[»]
5FCIX-ray3.40S5/s52-225[»]
5FCJX-ray3.10S5/s52-225[»]
5I4LX-ray3.10S5/s520-225[»]
5JPQelectron microscopy7.30q1-225[»]
5JUOelectron microscopy4.00CB1-225[»]
5JUPelectron microscopy3.50CB1-225[»]
5JUSelectron microscopy4.20CB1-225[»]
5JUTelectron microscopy4.00CB1-225[»]
5JUUelectron microscopy4.00CB1-225[»]
5LYBX-ray3.25S5/s520-225[»]
5M1Jelectron microscopy3.30F220-225[»]
5MC6electron microscopy3.80B1-225[»]
5TGAX-ray3.30S5/s520-225[»]
5TGMX-ray3.50S5/s520-225[»]
5TZSelectron microscopy5.1061-225[»]
ProteinModelPortaliP26783.
SMRiP26783.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26783.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
InParanoidiP26783.
KOiK02989.
OMAiVDYIQIR.
OrthoDBiEOG092C50PJ.

Family and domain databases

CDDicd14867. uS7_Eukaryote. 1 hit.
Gene3Di1.10.455.10. 1 hit.
InterProiView protein in InterPro
IPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
PANTHERiPTHR11205. PTHR11205. 1 hit.
PTHR11205:SF30. PTHR11205:SF30. 1 hit.
PfamiView protein in Pfam
PF00177. Ribosomal_S7. 1 hit.
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. uS7_euk_arch. 1 hit.
PROSITEiView protein in PROSITE
PS00052. RIBOSOMAL_S7. 1 hit.

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 23, 2007 - v3
Checksum:iCD3F743B56CB1127
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21T → E AA sequence (PubMed:1544921).Curated1

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
PDB 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[»]
5DATX-ray3.15S5/s52-225[»]
5DC3X-ray3.25S5/s52-225[»]
5DGEX-ray3.45S5/s52-225[»]
5DGFX-ray3.30S5/s52-225[»]
5DGVX-ray3.10S5/s52-225[»]
5FCIX-ray3.40S5/s52-225[»]
5FCJX-ray3.10S5/s52-225[»]
5I4LX-ray3.10S5/s520-225[»]
5JPQelectron microscopy7.30q1-225[»]
5JUOelectron microscopy4.00CB1-225[»]
5JUPelectron microscopy3.50CB1-225[»]
5JUSelectron microscopy4.20CB1-225[»]
5JUTelectron microscopy4.00CB1-225[»]
5JUUelectron microscopy4.00CB1-225[»]
5LYBX-ray3.25S5/s520-225[»]
5M1Jelectron microscopy3.30F220-225[»]
5MC6electron microscopy3.80B1-225[»]
5TGAX-ray3.30S5/s520-225[»]
5TGMX-ray3.50S5/s520-225[»]
5TZSelectron microscopy5.1061-225[»]
ProteinModelPortaliP26783.
SMRiP26783.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33879. 90 interactors.
DIPiDIP-5092N.
IntActiP26783. 68 interactors.
MINTiMINT-480795.

PTM databases

iPTMnetiP26783.

2D gel databases

UCD-2DPAGEiP26783.

Proteomic databases

MaxQBiP26783.
PRIDEiP26783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YJR123W.
SGDiS000003884. RPS5.

Phylogenomic databases

GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
InParanoidiP26783.
KOiK02989.
OMAiVDYIQIR.
OrthoDBiEOG092C50PJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31744-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

EvolutionaryTraceiP26783.
PROiPR:P26783.

Family and domain databases

CDDicd14867. uS7_Eukaryote. 1 hit.
Gene3Di1.10.455.10. 1 hit.
InterProiView protein in InterPro
IPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
PANTHERiPTHR11205. PTHR11205. 1 hit.
PTHR11205:SF30. PTHR11205:SF30. 1 hit.
PfamiView protein in Pfam
PF00177. Ribosomal_S7. 1 hit.
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. uS7_euk_arch. 1 hit.
PROSITEiView protein in PROSITE
PS00052. RIBOSOMAL_S7. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRS5_YEAST
AccessioniPrimary (citable) accession number: P26783
Secondary accession number(s): D6VWU2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 12, 2017
This is version 158 of the entry and version 3 of the sequence. See 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

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.