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Entry version 174 (13 Feb 2019)
Sequence version 3 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • mRNA binding Source: GO_Central
  • rRNA binding Source: GO_Central
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • regulation of translational fidelity Source: SGD
  • ribosomal small subunit assembly Source: GO_Central
  • rRNA export from nucleus Source: SGD
  • translation Source: GO_Central

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31744-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
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)

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
40S ribosomal protein S51 Publication
Alternative name(s):
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPS51 Publication
Synonyms:RPS2
Ordered Locus Names:YJR123W
ORF Names:J2045
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YJR123W

Saccharomyces Genome Database

More...
SGDi
S000003884 RPS5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001245402 – 22540S ribosomal protein S5Add BLAST224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine2 Publications1
Modified residuei27PhosphothreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P26783

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P26783

PRoteomics IDEntifications database

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PRIDEi
P26783

2D gel databases

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P26783

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P26783

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P26783

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33879, 110 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1599 40S cytosolic small ribosomal subunit

Database of interacting proteins

More...
DIPi
DIP-5092N

Protein interaction database and analysis system

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IntActi
P26783, 68 interactors

Molecular INTeraction database

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MINTi
P26783

STRING: functional protein association networks

More...
STRINGi
4932.YJR123W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1225
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
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[»]
5MEIX-ray3.50G/s520-225[»]
5NDGX-ray3.70S5/s520-225[»]
5NDVX-ray3.30S5/s520-225[»]
5NDWX-ray3.70S5/s520-225[»]
5OBMX-ray3.40S5/s520-225[»]
5ON6X-ray3.10G/s520-225[»]
5TBWX-ray3.00G/s520-225[»]
5TGAX-ray3.30S5/s520-225[»]
5TGMX-ray3.50S5/s520-225[»]
5TZSelectron microscopy5.1061-225[»]
5WYJelectron microscopy8.70SG1-225[»]
5WYKelectron microscopy4.50SG1-225[»]
6EMLelectron microscopy3.60B1-225[»]
6FAIelectron microscopy3.40F1-225[»]
6GQ1electron microscopy4.40v20-225[»]
6GQBelectron microscopy3.90v20-225[»]
6GQVelectron microscopy4.00v20-225[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P26783

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P26783

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P26783

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00390000010806

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000039066

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P26783

KEGG Orthology (KO)

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KOi
K02989

Identification of Orthologs from Complete Genome Data

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OMAi
DSLMMKG

Family and domain databases

Conserved Domains Database

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CDDi
cd14867 uS7_Eukaryote, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.455.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

The PANTHER Classification System

More...
PANTHERi
PTHR11205 PTHR11205, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00177 Ribosomal_S7, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002122 RPS7p_RPS7a_RPS5e_RPS7o, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47973 SSF47973, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01028 uS7_euk_arch, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00052 RIBOSOMAL_S7, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCD3F743B56CB1127
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21T → E AA sequence (PubMed:1544921).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S55720

NCBI Reference Sequences

More...
RefSeqi
NP_012657.1, NM_001181781.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJR123W_mRNA; YJR123W_mRNA; YJR123W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853587

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJR123W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
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[»]
5MEIX-ray3.50G/s520-225[»]
5NDGX-ray3.70S5/s520-225[»]
5NDVX-ray3.30S5/s520-225[»]
5NDWX-ray3.70S5/s520-225[»]
5OBMX-ray3.40S5/s520-225[»]
5ON6X-ray3.10G/s520-225[»]
5TBWX-ray3.00G/s520-225[»]
5TGAX-ray3.30S5/s520-225[»]
5TGMX-ray3.50S5/s520-225[»]
5TZSelectron microscopy5.1061-225[»]
5WYJelectron microscopy8.70SG1-225[»]
5WYKelectron microscopy4.50SG1-225[»]
6EMLelectron microscopy3.60B1-225[»]
6FAIelectron microscopy3.40F1-225[»]
6GQ1electron microscopy4.40v20-225[»]
6GQBelectron microscopy3.90v20-225[»]
6GQVelectron microscopy4.00v20-225[»]
ProteinModelPortaliP26783
SMRiP26783
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33879, 110 interactors
ComplexPortaliCPX-1599 40S cytosolic small ribosomal subunit
DIPiDIP-5092N
IntActiP26783, 68 interactors
MINTiP26783
STRINGi4932.YJR123W

PTM databases

CarbonylDBiP26783
iPTMnetiP26783

2D gel databases

UCD-2DPAGEiP26783

Proteomic databases

MaxQBiP26783
PaxDbiP26783
PRIDEiP26783

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR123W_mRNA; YJR123W_mRNA; YJR123W
GeneIDi853587
KEGGisce:YJR123W

Organism-specific databases

EuPathDBiFungiDB:YJR123W
SGDiS000003884 RPS5

Phylogenomic databases

GeneTreeiENSGT00390000010806
HOGENOMiHOG000039066
InParanoidiP26783
KOiK02989
OMAiDSLMMKG

Enzyme and pathway databases

BioCyciYEAST:G3O-31744-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
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

Protein Ontology

More...
PROi
PR: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
IPR036823 Ribosomal_S7_dom_sf
PANTHERiPTHR11205 PTHR11205, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRS5_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P26783
Secondary accession number(s): D6VWU2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 174 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Ribosomal proteins
    Ribosomal proteins families and list of entries
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