UniProtKB - P26783 (RS5_YEAST)
40S ribosomal protein S5
RPS5
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 PublicationGO - Molecular functioni
- mRNA binding Source: GO_Central
- rRNA binding Source: GO_Central
- structural constituent of ribosome Source: SGD
GO - Biological processi
- regulation of translational fidelity Source: SGD
- ribosomal small subunit assembly Source: GO_Central
- rRNA export from nucleus Source: SGD
- translation Source: GO_Central
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein |
Enzyme and pathway databases
Reactomei | R-SCE-156827, L13a-mediated translational silencing of Ceruloplasmin expression R-SCE-1799339, SRP-dependent cotranslational protein targeting to membrane R-SCE-6791226, Major pathway of rRNA processing in the nucleolus and cytosol 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 PublicationAlternative name(s): RP14 S2 Small ribosomal subunit protein uS71 Publication YS8 |
Gene namesi | Ordered Locus Names:YJR123W ORF Names:J2045 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000003884, RPS5 |
VEuPathDBi | FungiDB:YJR123W |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: Reactome
- cytosolic small ribosomal subunit Source: SGD
Other locations
- 90S preribosome Source: SGD
- cytoplasm Source: ComplexPortal
- ribosome Source: GO_Central
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000124540 | 2 – 225 | 40S ribosomal protein S5Add BLAST | 224 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine2 Publications | 1 | |
Modified residuei | 27 | PhosphothreonineCombined sources | 1 | |
Cross-linki | 45 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources | ||
Cross-linki | 203 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | P26783 |
PaxDbi | P26783 |
PRIDEi | P26783 |
2D gel databases
UCD-2DPAGEi | P26783 |
PTM databases
CarbonylDBi | P26783 |
iPTMneti | P26783 |
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 PublicationBinary interactionsi
P26783
With | #Exp. | IntAct |
---|---|---|
BUL1 [P48524] | 3 | EBI-16150,EBI-3881 |
Protein-protein interaction databases
BioGRIDi | 33879, 148 interactors |
ComplexPortali | CPX-1599, 40S cytosolic small ribosomal subunit |
DIPi | DIP-5092N |
IntActi | P26783, 73 interactors |
MINTi | P26783 |
STRINGi | 4932.YJR123W |
Miscellaneous databases
RNActi | P26783, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P26783 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P26783 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3291, Eukaryota |
GeneTreei | ENSGT00390000010806 |
HOGENOMi | CLU_063975_0_0_1 |
InParanoidi | P26783 |
OMAi | KMNIVER |
Family and domain databases
CDDi | cd14867, uS7_Eukaryote, 1 hit |
Gene3Di | 1.10.455.10, 1 hit |
InterProi | View protein in InterPro IPR000235, Ribosomal_S5/S7 IPR005716, Ribosomal_S5/S7_euk/arc IPR020606, Ribosomal_S7_CS IPR023798, Ribosomal_S7_dom IPR036823, Ribosomal_S7_dom_sf |
PANTHERi | PTHR11205, PTHR11205, 1 hit |
Pfami | View protein in Pfam PF00177, Ribosomal_S7, 1 hit |
PIRSFi | PIRSF002122, RPS7p_RPS7a_RPS5e_RPS7o, 1 hit |
SUPFAMi | SSF47973, SSF47973, 1 hit |
TIGRFAMsi | TIGR01028, uS7_euk_arch, 1 hit |
PROSITEi | View protein in PROSITE PS00052, RIBOSOMAL_S7, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 21 | T → E AA sequence (PubMed:1544921).Curated | 1 |
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 |
PIRi | S55720 |
RefSeqi | NP_012657.1, NM_001181781.1 |
Genome annotation databases
EnsemblFungii | YJR123W_mRNA; YJR123W; YJR123W |
GeneIDi | 853587 |
KEGGi | sce:YJR123W |
Similar proteinsi
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 |
PIRi | S55720 |
RefSeqi | NP_012657.1, NM_001181781.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2NOQ | electron microscopy | 7.30 | F | 76-225 | [»] | |
3J6X | electron microscopy | 6.10 | S5 | 1-225 | [»] | |
3J6Y | electron microscopy | 6.10 | S5 | 1-225 | [»] | |
3J77 | electron microscopy | 6.20 | S5 | 1-225 | [»] | |
3J78 | electron microscopy | 6.30 | S5 | 1-225 | [»] | |
4U3M | X-ray | 3.00 | S5/s5 | 2-225 | [»] | |
4U3N | X-ray | 3.20 | S5/s5 | 2-225 | [»] | |
4U3U | X-ray | 2.90 | S5/s5 | 2-225 | [»] | |
4U4N | X-ray | 3.10 | S5/s5 | 2-225 | [»] | |
4U4O | X-ray | 3.60 | S5/s5 | 2-225 | [»] | |
4U4Q | X-ray | 3.00 | S5/s5 | 2-225 | [»] | |
4U4R | X-ray | 2.80 | S5/s5 | 2-225 | [»] | |
4U4U | X-ray | 3.00 | S5/s5 | 2-225 | [»] | |
4U4Y | X-ray | 3.20 | S5/s5 | 2-225 | [»] | |
4U4Z | X-ray | 3.10 | S5/s5 | 2-225 | [»] | |
4U50 | X-ray | 3.20 | S5/s5 | 2-225 | [»] | |
4U51 | X-ray | 3.20 | S5/s5 | 2-225 | [»] | |
4U52 | X-ray | 3.00 | S5/s5 | 2-225 | [»] | |
4U53 | X-ray | 3.30 | S5/s5 | 2-225 | [»] | |
4U55 | X-ray | 3.20 | S5/s5 | 2-225 | [»] | |
4U56 | X-ray | 3.45 | S5/s5 | 2-225 | [»] | |
4U6F | X-ray | 3.10 | S5/s5 | 2-225 | [»] | |
4V4B | electron microscopy | 11.70 | AG | 76-225 | [»] | |
4V6I | electron microscopy | 8.80 | AF | 1-225 | [»] | |
4V7R | X-ray | 4.00 | AD/CD | 1-225 | [»] | |
4V88 | X-ray | 3.00 | AF/CF | 1-225 | [»] | |
4V8Y | electron microscopy | 4.30 | AF | 1-225 | [»] | |
4V8Z | electron microscopy | 6.60 | AF | 1-225 | [»] | |
4V92 | electron microscopy | 3.70 | F | 20-225 | [»] | |
5DAT | X-ray | 3.15 | S5/s5 | 2-225 | [»] | |
5DC3 | X-ray | 3.25 | S5/s5 | 2-225 | [»] | |
5DGE | X-ray | 3.45 | S5/s5 | 2-225 | [»] | |
5DGF | X-ray | 3.30 | S5/s5 | 2-225 | [»] | |
5DGV | X-ray | 3.10 | S5/s5 | 2-225 | [»] | |
5FCI | X-ray | 3.40 | S5/s5 | 2-225 | [»] | |
5FCJ | X-ray | 3.10 | S5/s5 | 2-225 | [»] | |
5I4L | X-ray | 3.10 | S5/s5 | 20-225 | [»] | |
5JPQ | electron microscopy | 7.30 | q | 1-225 | [»] | |
5JUO | electron microscopy | 4.00 | CB | 1-225 | [»] | |
5JUP | electron microscopy | 3.50 | CB | 1-225 | [»] | |
5JUS | electron microscopy | 4.20 | CB | 1-225 | [»] | |
5JUT | electron microscopy | 4.00 | CB | 1-225 | [»] | |
5JUU | electron microscopy | 4.00 | CB | 1-225 | [»] | |
5LYB | X-ray | 3.25 | S5/s5 | 20-225 | [»] | |
5M1J | electron microscopy | 3.30 | F2 | 20-225 | [»] | |
5MC6 | electron microscopy | 3.80 | B | 1-225 | [»] | |
5MEI | X-ray | 3.50 | G/s5 | 20-225 | [»] | |
5NDG | X-ray | 3.70 | S5/s5 | 20-225 | [»] | |
5NDV | X-ray | 3.30 | S5/s5 | 20-225 | [»] | |
5NDW | X-ray | 3.70 | S5/s5 | 20-225 | [»] | |
5OBM | X-ray | 3.40 | S5/s5 | 20-225 | [»] | |
5ON6 | X-ray | 3.10 | G/s5 | 20-225 | [»] | |
5TBW | X-ray | 3.00 | G/s5 | 20-225 | [»] | |
5TGA | X-ray | 3.30 | S5/s5 | 20-225 | [»] | |
5TGM | X-ray | 3.50 | S5/s5 | 20-225 | [»] | |
5TZS | electron microscopy | 5.10 | 6 | 1-225 | [»] | |
5WYJ | electron microscopy | 8.70 | SG | 1-225 | [»] | |
5WYK | electron microscopy | 4.50 | SG | 1-225 | [»] | |
6EML | electron microscopy | 3.60 | B | 1-225 | [»] | |
6FAI | electron microscopy | 3.40 | F | 1-225 | [»] | |
6GQ1 | electron microscopy | 4.40 | v | 20-225 | [»] | |
6GQB | electron microscopy | 3.90 | v | 20-225 | [»] | |
6GQV | electron microscopy | 4.00 | v | 20-225 | [»] | |
6HHQ | X-ray | 3.10 | G/s5 | 1-225 | [»] | |
6I7O | electron microscopy | 5.30 | B/Bb | 20-225 | [»] | |
6KE6 | electron microscopy | 3.40 | SG | 1-225 | [»] | |
6LQP | electron microscopy | 3.20 | SG | 1-225 | [»] | |
6LQQ | electron microscopy | 4.10 | SG | 1-225 | [»] | |
6LQR | electron microscopy | 8.60 | SG | 1-225 | [»] | |
6LQS | electron microscopy | 3.80 | SG | 1-225 | [»] | |
6LQT | electron microscopy | 4.90 | SG | 1-225 | [»] | |
6LQU | electron microscopy | 3.70 | SG | 1-225 | [»] | |
6LQV | electron microscopy | 4.80 | SG | 1-225 | [»] | |
6RBD | electron microscopy | 3.47 | F | 1-225 | [»] | |
6RBE | electron microscopy | 3.80 | F | 1-225 | [»] | |
6SNT | electron microscopy | 2.80 | F | 1-225 | [»] | |
6WDR | electron microscopy | 3.70 | F | 20-225 | [»] | |
6Y7C | electron microscopy | 3.80 | F | 1-225 | [»] | |
6Z6J | electron microscopy | 3.40 | SF | 1-225 | [»] | |
6ZCE | electron microscopy | 5.30 | G | 1-225 | [»] | |
6ZQA | electron microscopy | 4.40 | DF | 1-225 | [»] | |
6ZQB | electron microscopy | 3.90 | DF | 1-225 | [»] | |
6ZQC | electron microscopy | 3.80 | DF | 1-225 | [»] | |
6ZQE | electron microscopy | 7.10 | DF | 1-225 | [»] | |
6ZQF | electron microscopy | 4.90 | DF | 1-225 | [»] | |
6ZQG | electron microscopy | 3.50 | DF | 1-225 | [»] | |
6ZU9 | electron microscopy | 6.20 | C | 1-225 | [»] | |
6ZVI | electron microscopy | 3.00 | n | 20-225 | [»] | |
7A1G | electron microscopy | 3.00 | B | 20-225 | [»] | |
7AJT | electron microscopy | 4.60 | DF | 1-225 | [»] | |
7AJU | electron microscopy | 3.80 | DF | 1-225 | [»] | |
7B7D | electron microscopy | 3.30 | B | 20-225 | [»] | |
7D4I | electron microscopy | 4.00 | SG | 1-225 | [»] | |
7D5S | electron microscopy | 4.60 | SG | 1-225 | [»] | |
7D5T | electron microscopy | 6.00 | SG | 1-225 | [»] | |
7D63 | electron microscopy | 12.30 | SG | 1-225 | [»] | |
7NRC | electron microscopy | 3.90 | SB | 20-225 | [»] | |
7NRD | electron microscopy | 4.36 | SB | 20-225 | [»] | |
SMRi | P26783 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 33879, 148 interactors |
ComplexPortali | CPX-1599, 40S cytosolic small ribosomal subunit |
DIPi | DIP-5092N |
IntActi | P26783, 73 interactors |
MINTi | P26783 |
STRINGi | 4932.YJR123W |
PTM databases
CarbonylDBi | P26783 |
iPTMneti | P26783 |
2D gel databases
UCD-2DPAGEi | P26783 |
Proteomic databases
MaxQBi | P26783 |
PaxDbi | P26783 |
PRIDEi | P26783 |
Genome annotation databases
EnsemblFungii | YJR123W_mRNA; YJR123W; YJR123W |
GeneIDi | 853587 |
KEGGi | sce:YJR123W |
Organism-specific databases
SGDi | S000003884, RPS5 |
VEuPathDBi | FungiDB:YJR123W |
Phylogenomic databases
eggNOGi | KOG3291, Eukaryota |
GeneTreei | ENSGT00390000010806 |
HOGENOMi | CLU_063975_0_0_1 |
InParanoidi | P26783 |
OMAi | KMNIVER |
Enzyme and pathway databases
Reactomei | R-SCE-156827, L13a-mediated translational silencing of Ceruloplasmin expression R-SCE-1799339, SRP-dependent cotranslational protein targeting to membrane R-SCE-6791226, Major pathway of rRNA processing in the nucleolus and cytosol 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
EvolutionaryTracei | P26783 |
PROi | PR:P26783 |
RNActi | P26783, protein |
Family and domain databases
CDDi | cd14867, uS7_Eukaryote, 1 hit |
Gene3Di | 1.10.455.10, 1 hit |
InterProi | View protein in InterPro IPR000235, Ribosomal_S5/S7 IPR005716, Ribosomal_S5/S7_euk/arc IPR020606, Ribosomal_S7_CS IPR023798, Ribosomal_S7_dom IPR036823, Ribosomal_S7_dom_sf |
PANTHERi | PTHR11205, PTHR11205, 1 hit |
Pfami | View protein in Pfam PF00177, Ribosomal_S7, 1 hit |
PIRSFi | PIRSF002122, RPS7p_RPS7a_RPS5e_RPS7o, 1 hit |
SUPFAMi | SSF47973, SSF47973, 1 hit |
TIGRFAMsi | TIGR01028, uS7_euk_arch, 1 hit |
PROSITEi | View protein in PROSITE PS00052, RIBOSOMAL_S7, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RS5_YEAST | |
Accessioni | P26783Primary (citable) accession number: P26783 Secondary accession number(s): D6VWU2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 192 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome X
Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names - Ribosomal proteins
Ribosomal proteins families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families