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Protein

40S ribosomal protein S3

Gene

RPS3

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

Miscellaneous

Present with 146000 molecules/cell in log phase SD medium.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

  • damaged DNA binding Source: GO_Central
  • DNA-(apurinic or apyrimidinic site) endonuclease activity Source: SGD
  • oxidized purine DNA binding Source: GO_Central
  • oxidized purine nucleobase lesion DNA N-glycosylase activity Source: GO_Central
  • protein kinase A catalytic subunit binding Source: SGD
  • RNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • DNA repair Source: GO_Central
  • positive regulation of DNA repair Source: GO_Central
  • ribosomal small subunit export from nucleus Source: SGD
  • rRNA export from nucleus Source: SGD

<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, RNA-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33190-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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)

<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 S31 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:RPS31 Publication
Synonyms:SUF14
Ordered Locus Names:YNL178W
ORF Names:N1653
<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 XIV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000005122 RPS3

<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; 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 methionineiRemoved3 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_00001303322 – 24040S ribosomal protein S3Add BLAST239

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 residuei44PhosphothreonineCombined sources1
Modified residuei70PhosphothreonineCombined sources1
Modified residuei97PhosphoserineCombined 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-linki106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei129PhosphoserineCombined sources1
Cross-linki132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei146Omega-N-methylarginine; by SFM11 Publication1
Cross-linki151Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei221PhosphoserineCombined sources1
Modified residuei231PhosphothreonineCombined sources1

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P05750

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

More...
PaxDbi
P05750

PRoteomics IDEntifications database

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PRIDEi
P05750

2D gel databases

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P05750

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P05750

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P05750

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35653, 293 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1599 40S cytosolic small ribosomal subunit

Database of interacting proteins

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DIPi
DIP-4328N

Protein interaction database and analysis system

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IntActi
P05750, 104 interactors

Molecular INTeraction database

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MINTi
P05750

STRING: functional protein association networks

More...
STRINGi
4932.YNL178W

<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

1240
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-C6-193[»]
3J6Xelectron microscopy6.10S31-240[»]
3J6Yelectron microscopy6.10S31-240[»]
3J77electron microscopy6.20S31-240[»]
3J78electron microscopy6.30S31-240[»]
4BSZX-ray2.84A1-240[»]
4U3MX-ray3.00S3/s32-240[»]
4U3NX-ray3.20S3/s32-240[»]
4U3UX-ray2.90S3/s32-240[»]
4U4NX-ray3.10S3/s32-240[»]
4U4OX-ray3.60S3/s32-240[»]
4U4QX-ray3.00S3/s32-240[»]
4U4RX-ray2.80S3/s32-240[»]
4U4UX-ray3.00S3/s32-240[»]
4U4YX-ray3.20S3/s32-240[»]
4U4ZX-ray3.10S3/s32-240[»]
4U50X-ray3.20S3/s32-240[»]
4U51X-ray3.20S3/s32-240[»]
4U52X-ray3.00S3/s32-240[»]
4U53X-ray3.30S3/s32-240[»]
4U55X-ray3.20S3/s32-240[»]
4U56X-ray3.45S3/s32-240[»]
4U6FX-ray3.10S3/s32-240[»]
4V4Belectron microscopy11.70AC2-193[»]
4V6Ielectron microscopy8.80AB1-240[»]
4V7RX-ray4.00AC/CC1-240[»]
4V88X-ray3.00AD/CD1-240[»]
4V8Yelectron microscopy4.30AD1-240[»]
4V8Zelectron microscopy6.60AD1-240[»]
4V92electron microscopy3.70D4-225[»]
5DATX-ray3.15S3/s32-240[»]
5DC3X-ray3.25S3/s32-240[»]
5DGEX-ray3.45S3/s32-240[»]
5DGFX-ray3.30S3/s32-240[»]
5DGVX-ray3.10S3/s32-240[»]
5FCIX-ray3.40S3/s32-240[»]
5FCJX-ray3.10S3/s32-240[»]
5I4LX-ray3.10S3/s33-225[»]
5JUOelectron microscopy4.00AB1-240[»]
5JUPelectron microscopy3.50AB1-240[»]
5JUSelectron microscopy4.20AB1-240[»]
5JUTelectron microscopy4.00AB1-240[»]
5JUUelectron microscopy4.00AB1-240[»]
5LYBX-ray3.25S3/s33-225[»]
5M1Jelectron microscopy3.30D23-225[»]
5MC6electron microscopy3.80A1-240[»]
5MEIX-ray3.50E/s33-225[»]
5NDGX-ray3.70S3/s33-225[»]
5NDVX-ray3.30S3/s33-225[»]
5NDWX-ray3.70S3/s33-225[»]
5OBMX-ray3.40S3/s33-225[»]
5ON6X-ray3.10E/s33-225[»]
5TBWX-ray3.00E/s33-225[»]
5TGAX-ray3.30S3/s33-225[»]
5TGMX-ray3.50S3/s33-225[»]
6FAIelectron microscopy3.40D1-240[»]
6GQ1electron microscopy4.40t3-225[»]
6GQBelectron microscopy3.90t3-225[»]
6GQVelectron microscopy4.00t3-225[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P05750

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

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SMRi
P05750

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

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EvolutionaryTracei
P05750

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini21 – 92KH type-2PROSITE-ProRule annotationAdd BLAST72

<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
ENSGT00390000008610

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000210611

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P05750

KEGG Orthology (KO)

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KOi
K02985

Identification of Orthologs from Complete Genome Data

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OMAi
AVRHVLM

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1140.32, 1 hit
3.30.300.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR015946 KH_dom-like_a/b
IPR004044 KH_dom_type_2
IPR009019 KH_sf_prok-type
IPR001351 Ribosomal_S3_C
IPR036419 Ribosomal_S3_C_sf
IPR018280 Ribosomal_S3_CS
IPR005703 Ribosomal_S3_euk/arc

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07650 KH_2, 1 hit
PF00189 Ribosomal_S3_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54814 SSF54814, 1 hit
SSF54821 SSF54821, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01008 uS3_euk_arch, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50823 KH_TYPE_2, 1 hit
PS00548 RIBOSOMAL_S3, 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.

P05750-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVALISKKRK LVADGVFYAE LNEFFTRELA EEGYSGVEVR VTPTKTEVII
60 70 80 90 100
RATRTQDVLG ENGRRINELT LLVQKRFKYA PGTIVLYAER VQDRGLSAVA
110 120 130 140 150
QAESMKFKLL NGLAIRRAAY GVVRYVMESG AKGCEVVVSG KLRAARAKAM
160 170 180 190 200
KFADGFLIHS GQPVNDFIDT ATRHVLMRQG VLGIKVKIMR DPAKSRTGPK
210 220 230 240
ALPDAVTIIE PKEEEPILAP SVKDYRPAEE TEAQAEPVEA
Length:240
Mass (Da):26,503
Last modified:January 23, 2007 - v5
<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:iB85C0DFEB011745F
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 conflicti17F → N in AAA35010 (Ref. 3) Curated1
Sequence conflicti223 – 224KD → NH in AAA35010 (Ref. 3) Curated2

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 26384.3 Da from positions 2 - 240. Determined by ESI. The measured mass is that of the monomethylated protein.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U34347 Genomic DNA Translation: AAC49380.1
D25285 mRNA Translation: BAA04973.1
L31405 Genomic DNA Translation: AAA35010.1
Z71454 Genomic DNA Translation: CAA96070.1
BK006947 Genomic DNA Translation: DAA10373.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S48510

NCBI Reference Sequences

More...
RefSeqi
NP_014221.3, NM_001183016.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL178W_mRNA; YNL178W_mRNA; YNL178W

Database of genes from NCBI RefSeq genomes

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GeneIDi
855543

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL178W

<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
U34347 Genomic DNA Translation: AAC49380.1
D25285 mRNA Translation: BAA04973.1
L31405 Genomic DNA Translation: AAA35010.1
Z71454 Genomic DNA Translation: CAA96070.1
BK006947 Genomic DNA Translation: DAA10373.1
PIRiS48510
RefSeqiNP_014221.3, NM_001183016.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-C6-193[»]
3J6Xelectron microscopy6.10S31-240[»]
3J6Yelectron microscopy6.10S31-240[»]
3J77electron microscopy6.20S31-240[»]
3J78electron microscopy6.30S31-240[»]
4BSZX-ray2.84A1-240[»]
4U3MX-ray3.00S3/s32-240[»]
4U3NX-ray3.20S3/s32-240[»]
4U3UX-ray2.90S3/s32-240[»]
4U4NX-ray3.10S3/s32-240[»]
4U4OX-ray3.60S3/s32-240[»]
4U4QX-ray3.00S3/s32-240[»]
4U4RX-ray2.80S3/s32-240[»]
4U4UX-ray3.00S3/s32-240[»]
4U4YX-ray3.20S3/s32-240[»]
4U4ZX-ray3.10S3/s32-240[»]
4U50X-ray3.20S3/s32-240[»]
4U51X-ray3.20S3/s32-240[»]
4U52X-ray3.00S3/s32-240[»]
4U53X-ray3.30S3/s32-240[»]
4U55X-ray3.20S3/s32-240[»]
4U56X-ray3.45S3/s32-240[»]
4U6FX-ray3.10S3/s32-240[»]
4V4Belectron microscopy11.70AC2-193[»]
4V6Ielectron microscopy8.80AB1-240[»]
4V7RX-ray4.00AC/CC1-240[»]
4V88X-ray3.00AD/CD1-240[»]
4V8Yelectron microscopy4.30AD1-240[»]
4V8Zelectron microscopy6.60AD1-240[»]
4V92electron microscopy3.70D4-225[»]
5DATX-ray3.15S3/s32-240[»]
5DC3X-ray3.25S3/s32-240[»]
5DGEX-ray3.45S3/s32-240[»]
5DGFX-ray3.30S3/s32-240[»]
5DGVX-ray3.10S3/s32-240[»]
5FCIX-ray3.40S3/s32-240[»]
5FCJX-ray3.10S3/s32-240[»]
5I4LX-ray3.10S3/s33-225[»]
5JUOelectron microscopy4.00AB1-240[»]
5JUPelectron microscopy3.50AB1-240[»]
5JUSelectron microscopy4.20AB1-240[»]
5JUTelectron microscopy4.00AB1-240[»]
5JUUelectron microscopy4.00AB1-240[»]
5LYBX-ray3.25S3/s33-225[»]
5M1Jelectron microscopy3.30D23-225[»]
5MC6electron microscopy3.80A1-240[»]
5MEIX-ray3.50E/s33-225[»]
5NDGX-ray3.70S3/s33-225[»]
5NDVX-ray3.30S3/s33-225[»]
5NDWX-ray3.70S3/s33-225[»]
5OBMX-ray3.40S3/s33-225[»]
5ON6X-ray3.10E/s33-225[»]
5TBWX-ray3.00E/s33-225[»]
5TGAX-ray3.30S3/s33-225[»]
5TGMX-ray3.50S3/s33-225[»]
6FAIelectron microscopy3.40D1-240[»]
6GQ1electron microscopy4.40t3-225[»]
6GQBelectron microscopy3.90t3-225[»]
6GQVelectron microscopy4.00t3-225[»]
ProteinModelPortaliP05750
SMRiP05750
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35653, 293 interactors
ComplexPortaliCPX-1599 40S cytosolic small ribosomal subunit
DIPiDIP-4328N
IntActiP05750, 104 interactors
MINTiP05750
STRINGi4932.YNL178W

PTM databases

CarbonylDBiP05750
iPTMnetiP05750

2D gel databases

UCD-2DPAGEiP05750

Proteomic databases

MaxQBiP05750
PaxDbiP05750
PRIDEiP05750

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL178W_mRNA; YNL178W_mRNA; YNL178W
GeneIDi855543
KEGGisce:YNL178W

Organism-specific databases

SGDiS000005122 RPS3

Phylogenomic databases

GeneTreeiENSGT00390000008610
HOGENOMiHOG000210611
InParanoidiP05750
KOiK02985
OMAiAVRHVLM

Enzyme and pathway databases

BioCyciYEAST:G3O-33190-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

EvolutionaryTraceiP05750

Protein Ontology

More...
PROi
PR:P05750

Family and domain databases

Gene3Di3.30.1140.32, 1 hit
3.30.300.20, 1 hit
InterProiView protein in InterPro
IPR015946 KH_dom-like_a/b
IPR004044 KH_dom_type_2
IPR009019 KH_sf_prok-type
IPR001351 Ribosomal_S3_C
IPR036419 Ribosomal_S3_C_sf
IPR018280 Ribosomal_S3_CS
IPR005703 Ribosomal_S3_euk/arc
PfamiView protein in Pfam
PF07650 KH_2, 1 hit
PF00189 Ribosomal_S3_C, 1 hit
SUPFAMiSSF54814 SSF54814, 1 hit
SSF54821 SSF54821, 1 hit
TIGRFAMsiTIGR01008 uS3_euk_arch, 1 hit
PROSITEiView protein in PROSITE
PS50823 KH_TYPE_2, 1 hit
PS00548 RIBOSOMAL_S3, 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 nameiRS3_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: P05750
Secondary accession number(s): D6W107
<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: November 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 203 of the entry and version 5 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
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