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Entry version 179 (13 Feb 2019)
Sequence version 3 (23 Jan 2007)
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Protein

40S ribosomal protein S2

Gene

RPS2

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 (PubMed:22096102). uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).1 Publication1 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

  • small ribosomal subunit rRNA binding Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • positive regulation of translational fidelity Source: SGD
  • rRNA export from nucleus Source: SGD
  • rRNA methylation Source: Reactome
  • translation Source: InterPro

<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
Biological processRibosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-30620-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-3214858 RMTs methylate histone arginines
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-8876725 Protein methylation
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 S21 Publication
Alternative name(s):
Omnipotent suppressor protein SUP44
RP12
S4
YS5
<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:RPS21 Publication
Synonyms:RPS4, SUP38, SUP44
Ordered Locus Names:YGL123W
ORF Names:G2893
<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 VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGL123W

Saccharomyces Genome Database

More...
SGDi
S000003091 RPS2

<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, Nucleus

<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 methionineiRemovedCombined sources2 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_00001316842 – 25440S ribosomal protein S2Add BLAST253

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-acetylserineCombined sources2 Publications1
Modified residuei11Asymmetric dimethylarginine; by HMT1; alternate2 Publications1
Modified residuei11Omega-N-methylarginine; by HMT1; alternate2 Publications1
<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-linki33Glycyl 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, Methylation, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P25443

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

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PaxDbi
P25443

PRoteomics IDEntifications database

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PRIDEi
P25443

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P25443

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P25443

<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). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).1 Publication2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
33128, 357 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1599 40S cytosolic small ribosomal subunit

Protein interaction database and analysis system

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IntActi
P25443, 12 interactors

Molecular INTeraction database

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MINTi
P25443

STRING: functional protein association networks

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STRINGi
4932.YGL123W

<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

1254
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-E75-223[»]
3J6Xelectron microscopy6.10S21-254[»]
3J6Yelectron microscopy6.10S21-254[»]
3J77electron microscopy6.20S21-254[»]
3J78electron microscopy6.30S21-254[»]
4U3MX-ray3.00S2/s22-254[»]
4U3NX-ray3.20S2/s22-254[»]
4U3UX-ray2.90S2/s22-254[»]
4U4NX-ray3.10S2/s22-254[»]
4U4OX-ray3.60S2/s22-254[»]
4U4QX-ray3.00S2/s22-254[»]
4U4RX-ray2.80S2/s22-254[»]
4U4UX-ray3.00S2/s22-254[»]
4U4YX-ray3.20S2/s22-254[»]
4U4ZX-ray3.10S2/s22-254[»]
4U50X-ray3.20S2/s22-254[»]
4U51X-ray3.20S2/s22-254[»]
4U52X-ray3.00S2/s22-254[»]
4U53X-ray3.30S2/s22-254[»]
4U55X-ray3.20S2/s22-254[»]
4U56X-ray3.45S2/s22-254[»]
4U6FX-ray3.10S2/s22-254[»]
4V4Belectron microscopy11.70AE75-223[»]
4V6Ielectron microscopy8.80AE1-254[»]
4V7RX-ray4.00AB/CB1-254[»]
4V88X-ray3.00AC/CC1-254[»]
4V8Yelectron microscopy4.30AC1-254[»]
4V8Zelectron microscopy6.60AC1-254[»]
4V92electron microscopy3.70C34-249[»]
5DATX-ray3.15S2/s22-254[»]
5DC3X-ray3.25S2/s22-254[»]
5DGEX-ray3.45S2/s22-254[»]
5DGFX-ray3.30S2/s22-254[»]
5DGVX-ray3.10S2/s22-254[»]
5FCIX-ray3.40S2/s22-254[»]
5FCJX-ray3.10S2/s22-254[»]
5I4LX-ray3.10S2/s234-250[»]
5JUOelectron microscopy4.00ZA1-254[»]
5JUPelectron microscopy3.50ZA1-254[»]
5JUSelectron microscopy4.20ZA1-254[»]
5JUTelectron microscopy4.00ZA1-254[»]
5JUUelectron microscopy4.00ZA1-254[»]
5LL6electron microscopy3.90R1-254[»]
5LYBX-ray3.25S2/s234-250[»]
5M1Jelectron microscopy3.30C234-250[»]
5MC6electron microscopy3.80R1-254[»]
5MEIX-ray3.50D/s234-250[»]
5NDGX-ray3.70S2/s234-250[»]
5NDVX-ray3.30S2/s234-250[»]
5NDWX-ray3.70S2/s234-250[»]
5OBMX-ray3.40S2/s234-250[»]
5ON6X-ray3.10D/s234-250[»]
5TBWX-ray3.00D/s234-250[»]
5TGAX-ray3.30S2/s234-250[»]
5TGMX-ray3.50S2/s234-250[»]
6EMLelectron microscopy3.60R1-254[»]
6FAIelectron microscopy3.40C1-254[»]
6GQ1electron microscopy4.40s34-250[»]
6GQBelectron microscopy3.90s34-250[»]
6GQVelectron microscopy4.00s34-250[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P25443

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

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SMRi
P25443

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
P25443

<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>Domaini76 – 139S5 DRBMPROSITE-ProRule annotationAdd BLAST64

<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
ENSGT00940000161636

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000072596

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P25443

KEGG Orthology (KO)

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KOi
K02981

Identification of Orthologs from Complete Genome Data

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OMAi
EDCYTQS

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.230.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000851 Ribosomal_S5
IPR005324 Ribosomal_S5_C
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR005711 Ribosomal_S5_euk/arc
IPR013810 Ribosomal_S5_N
IPR018192 Ribosomal_S5_N_CS

The PANTHER Classification System

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PANTHERi
PTHR13718 PTHR13718, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00333 Ribosomal_S5, 1 hit
PF03719 Ribosomal_S5_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54211 SSF54211, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01020 uS5_euk_arch, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00585 RIBOSOMAL_S5, 1 hit
PS50881 S5_DSRBD, 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.

P25443-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAPEAQQQK RGGFGGRNRG RPNRRGPRNT EEKGWVPVTK LGRLVKAGKI
60 70 80 90 100
TTIEEIFLHS LPVKEFQIID TLLPGLQDEV MNIKPVQKQT RAGQRTRFKA
110 120 130 140 150
VVVVGDSNGH VGLGIKTAKE VAGAIRAGII IAKLSVIPIR RGYWGTNLGQ
160 170 180 190 200
PHSLATKTTG KCGSVTVRLI PAPRGSGIVA SPAVKKLLQL AGVEDVYTQS
210 220 230 240 250
NGKTRTLENT LKAAFVAIGN TYGFLTPNLW AEQPLPVSPL DIYSDEASAQ

KKRF
Length:254
Mass (Da):27,450
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:i5EFDA4C7DE7BDFFB
GO

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
M59375 Genomic DNA Translation: AAA63576.1
X94106 Genomic DNA Translation: CAA63835.1
Z72645 Genomic DNA Translation: CAA96831.1
AY557815 Genomic DNA Translation: AAS56141.1
BK006941 Genomic DNA Translation: DAA07986.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A36363 R3BYS2

NCBI Reference Sequences

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RefSeqi
NP_011392.1, NM_001180988.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL123W_mRNA; YGL123W_mRNA; YGL123W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852754

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL123W

<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
M59375 Genomic DNA Translation: AAA63576.1
X94106 Genomic DNA Translation: CAA63835.1
Z72645 Genomic DNA Translation: CAA96831.1
AY557815 Genomic DNA Translation: AAS56141.1
BK006941 Genomic DNA Translation: DAA07986.1
PIRiA36363 R3BYS2
RefSeqiNP_011392.1, NM_001180988.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-E75-223[»]
3J6Xelectron microscopy6.10S21-254[»]
3J6Yelectron microscopy6.10S21-254[»]
3J77electron microscopy6.20S21-254[»]
3J78electron microscopy6.30S21-254[»]
4U3MX-ray3.00S2/s22-254[»]
4U3NX-ray3.20S2/s22-254[»]
4U3UX-ray2.90S2/s22-254[»]
4U4NX-ray3.10S2/s22-254[»]
4U4OX-ray3.60S2/s22-254[»]
4U4QX-ray3.00S2/s22-254[»]
4U4RX-ray2.80S2/s22-254[»]
4U4UX-ray3.00S2/s22-254[»]
4U4YX-ray3.20S2/s22-254[»]
4U4ZX-ray3.10S2/s22-254[»]
4U50X-ray3.20S2/s22-254[»]
4U51X-ray3.20S2/s22-254[»]
4U52X-ray3.00S2/s22-254[»]
4U53X-ray3.30S2/s22-254[»]
4U55X-ray3.20S2/s22-254[»]
4U56X-ray3.45S2/s22-254[»]
4U6FX-ray3.10S2/s22-254[»]
4V4Belectron microscopy11.70AE75-223[»]
4V6Ielectron microscopy8.80AE1-254[»]
4V7RX-ray4.00AB/CB1-254[»]
4V88X-ray3.00AC/CC1-254[»]
4V8Yelectron microscopy4.30AC1-254[»]
4V8Zelectron microscopy6.60AC1-254[»]
4V92electron microscopy3.70C34-249[»]
5DATX-ray3.15S2/s22-254[»]
5DC3X-ray3.25S2/s22-254[»]
5DGEX-ray3.45S2/s22-254[»]
5DGFX-ray3.30S2/s22-254[»]
5DGVX-ray3.10S2/s22-254[»]
5FCIX-ray3.40S2/s22-254[»]
5FCJX-ray3.10S2/s22-254[»]
5I4LX-ray3.10S2/s234-250[»]
5JUOelectron microscopy4.00ZA1-254[»]
5JUPelectron microscopy3.50ZA1-254[»]
5JUSelectron microscopy4.20ZA1-254[»]
5JUTelectron microscopy4.00ZA1-254[»]
5JUUelectron microscopy4.00ZA1-254[»]
5LL6electron microscopy3.90R1-254[»]
5LYBX-ray3.25S2/s234-250[»]
5M1Jelectron microscopy3.30C234-250[»]
5MC6electron microscopy3.80R1-254[»]
5MEIX-ray3.50D/s234-250[»]
5NDGX-ray3.70S2/s234-250[»]
5NDVX-ray3.30S2/s234-250[»]
5NDWX-ray3.70S2/s234-250[»]
5OBMX-ray3.40S2/s234-250[»]
5ON6X-ray3.10D/s234-250[»]
5TBWX-ray3.00D/s234-250[»]
5TGAX-ray3.30S2/s234-250[»]
5TGMX-ray3.50S2/s234-250[»]
6EMLelectron microscopy3.60R1-254[»]
6FAIelectron microscopy3.40C1-254[»]
6GQ1electron microscopy4.40s34-250[»]
6GQBelectron microscopy3.90s34-250[»]
6GQVelectron microscopy4.00s34-250[»]
ProteinModelPortaliP25443
SMRiP25443
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33128, 357 interactors
ComplexPortaliCPX-1599 40S cytosolic small ribosomal subunit
IntActiP25443, 12 interactors
MINTiP25443
STRINGi4932.YGL123W

PTM databases

CarbonylDBiP25443
iPTMnetiP25443

Proteomic databases

MaxQBiP25443
PaxDbiP25443
PRIDEiP25443

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL123W_mRNA; YGL123W_mRNA; YGL123W
GeneIDi852754
KEGGisce:YGL123W

Organism-specific databases

EuPathDBiFungiDB:YGL123W
SGDiS000003091 RPS2

Phylogenomic databases

GeneTreeiENSGT00940000161636
HOGENOMiHOG000072596
InParanoidiP25443
KOiK02981
OMAiEDCYTQS

Enzyme and pathway databases

BioCyciYEAST:G3O-30620-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-3214858 RMTs methylate histone arginines
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-8876725 Protein methylation
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

EvolutionaryTraceiP25443

Protein Ontology

More...
PROi
PR:P25443

Family and domain databases

Gene3Di3.30.230.10, 1 hit
InterProiView protein in InterPro
IPR000851 Ribosomal_S5
IPR005324 Ribosomal_S5_C
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR005711 Ribosomal_S5_euk/arc
IPR013810 Ribosomal_S5_N
IPR018192 Ribosomal_S5_N_CS
PANTHERiPTHR13718 PTHR13718, 1 hit
PfamiView protein in Pfam
PF00333 Ribosomal_S5, 1 hit
PF03719 Ribosomal_S5_C, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
TIGRFAMsiTIGR01020 uS5_euk_arch, 1 hit
PROSITEiView protein in PROSITE
PS00585 RIBOSOMAL_S5, 1 hit
PS50881 S5_DSRBD, 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 nameiRS2_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: P25443
Secondary accession number(s): D6VU25
<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: May 1, 1992
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 179 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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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