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Entry version 122 (13 Feb 2019)
Sequence version 1 (20 Dec 2005)
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Protein

40S ribosomal protein S21-A

Gene

RPS21A

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). eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability (PubMed:14627813).1 Publication1 Publication

Miscellaneous

Present with 27400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS21 in yeast.Curated

<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

  • structural constituent of ribosome Source: SGD

GO - Biological processi

<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 processrRNA processing

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32026-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 S21-A1 Publication
Alternative name(s):
S26
YS25
<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:RPS21A1 Publication
Synonyms:RPS25, RPS25A, RPS26A
Ordered Locus Names:YKR057W
<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 XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKR057W

Saccharomyces Genome Database

More...
SGDi
S000001765 RPS21A

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Reduction in growth rate, a decrease in free 40S subunits, an increase in the amount of free 60S subunits and a decrease in polysome size.1 Publication

<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 ‘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_00001947611 – 8740S ribosomal protein S21-AAdd BLAST87

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 residuei1N-acetylmethionine1 Publication1

<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 NatB.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P0C0V8

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

More...
PaxDbi
P0C0V8

PRoteomics IDEntifications database

More...
PRIDEi
P0C0V8

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P0C0V8

2D gel databases

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P0C0V8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0C0V8

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34188, 231 interactors

Protein interaction database and analysis system

More...
IntActi
P0C0V8, 8 interactors

Molecular INTeraction database

More...
MINTi
P0C0V8

STRING: functional protein association networks

More...
STRINGi
4932.YKR057W

<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

187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10211-87[»]
3J6Yelectron microscopy6.10211-87[»]
3J77electron microscopy6.20211-87[»]
3J78electron microscopy6.30211-87[»]
4U3MX-ray3.00D1/d11-87[»]
4U3NX-ray3.20D1/d11-87[»]
4U3UX-ray2.90D1/d11-87[»]
4U4NX-ray3.10D1/d11-87[»]
4U4OX-ray3.60D1/d11-87[»]
4U4QX-ray3.00D1/d11-87[»]
4U4RX-ray2.80D1/d11-87[»]
4U4UX-ray3.00D1/d11-87[»]
4U4YX-ray3.20D1/d11-87[»]
4U4ZX-ray3.10D1/d11-87[»]
4U50X-ray3.20D1/d11-87[»]
4U51X-ray3.20D1/d11-87[»]
4U52X-ray3.00D1/d11-87[»]
4U53X-ray3.30D1/d11-87[»]
4U55X-ray3.20D1/d11-87[»]
4U56X-ray3.45D1/d11-87[»]
4U6FX-ray3.10D1/d11-87[»]
4V6Ielectron microscopy8.80AT1-87[»]
4V88X-ray3.00AV/CV1-87[»]
4V8Yelectron microscopy4.30AV1-87[»]
4V8Zelectron microscopy6.60AV1-87[»]
4V92electron microscopy3.70V1-87[»]
5DATX-ray3.15D1/d11-87[»]
5DC3X-ray3.25D1/d11-87[»]
5DGEX-ray3.45D1/d11-87[»]
5DGFX-ray3.30D1/d11-87[»]
5DGVX-ray3.10D1/d11-87[»]
5FCIX-ray3.40D1/d11-87[»]
5FCJX-ray3.10D1/d11-87[»]
5I4LX-ray3.10D1/d11-87[»]
5JUOelectron microscopy4.00SB1-87[»]
5JUPelectron microscopy3.50SB1-87[»]
5JUSelectron microscopy4.20SB1-87[»]
5JUTelectron microscopy4.00SB1-87[»]
5JUUelectron microscopy4.00SB1-87[»]
5LL6electron microscopy3.90a1-87[»]
5LYBX-ray3.25D1/d11-87[»]
5M1Jelectron microscopy3.30V21-87[»]
5MC6electron microscopy3.80a1-87[»]
5MEIX-ray3.50W/d11-87[»]
5NDGX-ray3.70D1/d11-87[»]
5NDVX-ray3.30D1/d11-87[»]
5NDWX-ray3.70D1/d11-87[»]
5OBMX-ray3.40D1/d11-87[»]
5ON6X-ray3.10W/d11-87[»]
5TBWX-ray3.00W/d11-87[»]
5TGAX-ray3.30D1/d11-87[»]
5TGMX-ray3.50D1/d11-87[»]
6EMLelectron microscopy3.60a1-87[»]
6FAIelectron microscopy3.40V1-87[»]
6GQ1electron microscopy4.40AL1-87[»]
6GQBelectron microscopy3.90AL1-87[»]
6GQVelectron microscopy4.00AL1-87[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0C0V8

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

More...
SMRi
P0C0V8

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

More...
GeneTreei
ENSGT00390000017515

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000183557

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0C0V8

KEGG Orthology (KO)

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KOi
K02971

Identification of Orthologs from Complete Genome Data

More...
OMAi
IELYIPR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1230.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001931 Ribosomal_S21e
IPR018279 Ribosomal_S21e_CS
IPR038579 Ribosomal_S21e_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10442 PTHR10442, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01249 Ribosomal_S21e, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002148 Ribosomal_S21e, 1 hit

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD006584 Ribosomal_S21e, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00996 RIBOSOMAL_S21E, 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.

P0C0V8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MENDKGQLVE LYVPRKCSAT NRIIKADDHA SVQINVAKVD EEGRAIPGEY
60 70 80
VTYALSGYVR SRGESDDSLN RLAQNDGLLK NVWSYSR
Length:87
Mass (Da):9,746
Last modified:December 20, 2005 - v1
<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:i52E1C24744E24F80
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X07811 Genomic DNA Translation: CAA30671.1
Z28282 Genomic DNA Translation: CAA82135.1
Z28283 Genomic DNA Translation: CAA82137.1
BK006944 Genomic DNA Translation: DAA09208.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S00975 R3BY1E

NCBI Reference Sequences

More...
RefSeqi
NP_012983.3, NM_001179847.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKR057W_mRNA; YKR057W_mRNA; YKR057W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853931

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKR057W

<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
X07811 Genomic DNA Translation: CAA30671.1
Z28282 Genomic DNA Translation: CAA82135.1
Z28283 Genomic DNA Translation: CAA82137.1
BK006944 Genomic DNA Translation: DAA09208.1
PIRiS00975 R3BY1E
RefSeqiNP_012983.3, NM_001179847.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10211-87[»]
3J6Yelectron microscopy6.10211-87[»]
3J77electron microscopy6.20211-87[»]
3J78electron microscopy6.30211-87[»]
4U3MX-ray3.00D1/d11-87[»]
4U3NX-ray3.20D1/d11-87[»]
4U3UX-ray2.90D1/d11-87[»]
4U4NX-ray3.10D1/d11-87[»]
4U4OX-ray3.60D1/d11-87[»]
4U4QX-ray3.00D1/d11-87[»]
4U4RX-ray2.80D1/d11-87[»]
4U4UX-ray3.00D1/d11-87[»]
4U4YX-ray3.20D1/d11-87[»]
4U4ZX-ray3.10D1/d11-87[»]
4U50X-ray3.20D1/d11-87[»]
4U51X-ray3.20D1/d11-87[»]
4U52X-ray3.00D1/d11-87[»]
4U53X-ray3.30D1/d11-87[»]
4U55X-ray3.20D1/d11-87[»]
4U56X-ray3.45D1/d11-87[»]
4U6FX-ray3.10D1/d11-87[»]
4V6Ielectron microscopy8.80AT1-87[»]
4V88X-ray3.00AV/CV1-87[»]
4V8Yelectron microscopy4.30AV1-87[»]
4V8Zelectron microscopy6.60AV1-87[»]
4V92electron microscopy3.70V1-87[»]
5DATX-ray3.15D1/d11-87[»]
5DC3X-ray3.25D1/d11-87[»]
5DGEX-ray3.45D1/d11-87[»]
5DGFX-ray3.30D1/d11-87[»]
5DGVX-ray3.10D1/d11-87[»]
5FCIX-ray3.40D1/d11-87[»]
5FCJX-ray3.10D1/d11-87[»]
5I4LX-ray3.10D1/d11-87[»]
5JUOelectron microscopy4.00SB1-87[»]
5JUPelectron microscopy3.50SB1-87[»]
5JUSelectron microscopy4.20SB1-87[»]
5JUTelectron microscopy4.00SB1-87[»]
5JUUelectron microscopy4.00SB1-87[»]
5LL6electron microscopy3.90a1-87[»]
5LYBX-ray3.25D1/d11-87[»]
5M1Jelectron microscopy3.30V21-87[»]
5MC6electron microscopy3.80a1-87[»]
5MEIX-ray3.50W/d11-87[»]
5NDGX-ray3.70D1/d11-87[»]
5NDVX-ray3.30D1/d11-87[»]
5NDWX-ray3.70D1/d11-87[»]
5OBMX-ray3.40D1/d11-87[»]
5ON6X-ray3.10W/d11-87[»]
5TBWX-ray3.00W/d11-87[»]
5TGAX-ray3.30D1/d11-87[»]
5TGMX-ray3.50D1/d11-87[»]
6EMLelectron microscopy3.60a1-87[»]
6FAIelectron microscopy3.40V1-87[»]
6GQ1electron microscopy4.40AL1-87[»]
6GQBelectron microscopy3.90AL1-87[»]
6GQVelectron microscopy4.00AL1-87[»]
ProteinModelPortaliP0C0V8
SMRiP0C0V8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34188, 231 interactors
IntActiP0C0V8, 8 interactors
MINTiP0C0V8
STRINGi4932.YKR057W

PTM databases

iPTMnetiP0C0V8

2D gel databases

UCD-2DPAGEiP0C0V8

Proteomic databases

MaxQBiP0C0V8
PaxDbiP0C0V8
PRIDEiP0C0V8
TopDownProteomicsiP0C0V8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR057W_mRNA; YKR057W_mRNA; YKR057W
GeneIDi853931
KEGGisce:YKR057W

Organism-specific databases

EuPathDBiFungiDB:YKR057W
SGDiS000001765 RPS21A

Phylogenomic databases

GeneTreeiENSGT00390000017515
HOGENOMiHOG000183557
InParanoidiP0C0V8
KOiK02971
OMAiIELYIPR

Enzyme and pathway databases

BioCyciYEAST:G3O-32026-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

Protein Ontology

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PROi
PR:P0C0V8

Family and domain databases

Gene3Di3.30.1230.20, 1 hit
InterProiView protein in InterPro
IPR001931 Ribosomal_S21e
IPR018279 Ribosomal_S21e_CS
IPR038579 Ribosomal_S21e_sf
PANTHERiPTHR10442 PTHR10442, 1 hit
PfamiView protein in Pfam
PF01249 Ribosomal_S21e, 1 hit
PIRSFiPIRSF002148 Ribosomal_S21e, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD006584 Ribosomal_S21e, 1 hit
PROSITEiView protein in PROSITE
PS00996 RIBOSOMAL_S21E, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiRS21A_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: P0C0V8
Secondary accession number(s): D6VXB8, P05760
<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: December 20, 2005
Last sequence update: December 20, 2005
Last modified: February 13, 2019
This is version 122 of the entry and version 1 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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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