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Entry version 166 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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Protein

40S ribosomal protein S19-A

Gene

RPS19A

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). eS19 is required for proper maturation of the small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA (PubMed:16159874, PubMed:17726054).1 Publication2 Publications

Miscellaneous

Present with 29000 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS19 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 processRibosome biogenesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33517-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 S19-A1 Publication
Alternative name(s):
RP55A
S16a
YP45
YS16A
<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:RPS19A1 Publication
Synonyms:RP55A, RPS16AA
Ordered Locus Names:YOL121C
<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 XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOL121C

Saccharomyces Genome Database

More...
SGDi
S000005481 RPS19A

<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

Disruption of a single RPS19 gene reduces cell growth; a double disruption is lethal. Depletion experiments show the proteins are required for correct maturation of precursor rRNA to generate the 18S small rRNA. A specific site between the 18S and 5.8S precursors (site A2 in ETS1) is not cleaved in disruption mutants. Partially assembled ribosomes are retained in the nucleolus rather than being exported to the cytoplasm. All effects are exacerbated in the double disruption. Increases association of NOC4 with 20S/21S pre-rRNA, decreases association of ENP1, TSR1 and RIO2 with 20S/21S pre-rRNA.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi15I → F: Partial loss of function; decreased 18S rRNA, decreases binding to 20S pre-rRNA complex, slow growth in double RPS19A/RPS19B mutant. 1 Publication1
Mutagenesisi57R → E or Q: Loss of mature 18S rRNA, protein doesn't bind 20S pre-RNA complex. Lethal in double RPS19A/RPS19B mutant. 1 Publication1
Mutagenesisi63R → E: Loss of mature 18S rRNA, protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. 1 Publication1
Mutagenesisi65I → P: Lethal in double RPS19A/RPS19B mutant, considerable decrease in 18S rRNA production. 2 Publications1
Mutagenesisi102R → E: Decreases mature 18S rRNA, protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. 1 Publication1
Mutagenesisi122R → E: Decreases mature 18S rRNA, protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. 1 Publication1

<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 methionineiRemoved1 Publication
<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_00001538352 – 14440S ribosomal protein S19-AAdd BLAST143

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P07280

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

More...
PaxDbi
P07280

PRoteomics IDEntifications database

More...
PRIDEi
P07280

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P07280

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07280

<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
34280, 194 interactors

Protein interaction database and analysis system

More...
IntActi
P07280, 33 interactors

Molecular INTeraction database

More...
MINTi
P07280

STRING: functional protein association networks

More...
STRINGi
4932.YOL121C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P07280 protein

<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

1144
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P07280

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230649

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07280

KEGG Orthology (KO)

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KOi
K02966

Identification of Orthologs from Complete Genome Data

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OMAi
YIDGPVG

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.2700, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001266 Ribosomal_S19e
IPR018277 Ribosomal_S19e_CS
IPR038111 Ribosomal_S19e_sf
IPR036390 WH_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11710 PTHR11710, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01090 Ribosomal_S19e, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01413 Ribosomal_S19e, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00628 RIBOSOMAL_S19E, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P07280-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPGVSVRDVA AQDFINAYAS FLQRQGKLEV PGYVDIVKTS SGNEMPPQDA
60 70 80 90 100
EGWFYKRAAS VARHIYMRKQ VGVGKLNKLY GGAKSRGVRP YKHIDASGSI
110 120 130 140
NRKVLQALEK IGIVEISPKG GRRISENGQR DLDRIAAQTL EEDE
Length:144
Mass (Da):15,917
Last modified:January 23, 2007 - v2
<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:iFE06D94B993B11B2
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
X02635 Genomic DNA Translation: CAA26482.1
X95258 Genomic DNA Translation: CAA64549.1
Z74863 Genomic DNA Translation: CAA99140.1
BK006948 Genomic DNA Translation: DAA10663.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S05868 R3BY9E

NCBI Reference Sequences

More...
RefSeqi
NP_014520.1, NM_001183375.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOL121C_mRNA; YOL121C; YOL121C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854028

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOL121C

<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
X02635 Genomic DNA Translation: CAA26482.1
X95258 Genomic DNA Translation: CAA64549.1
Z74863 Genomic DNA Translation: CAA99140.1
BK006948 Genomic DNA Translation: DAA10663.1
PIRiS05868 R3BY9E
RefSeqiNP_014520.1, NM_001183375.1

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 microscopy6.10191-144[»]
3J6Yelectron microscopy6.10191-144[»]
3J77electron microscopy6.20191-144[»]
3J78electron microscopy6.30191-144[»]
4U3MX-ray3.00C9/c92-144[»]
4U3NX-ray3.20C9/c92-144[»]
4U3UX-ray2.90C9/c92-144[»]
4U4NX-ray3.10C9/c92-144[»]
4U4OX-ray3.60C9/c92-144[»]
4U4QX-ray3.00C9/c92-144[»]
4U4RX-ray2.80C9/c92-144[»]
4U4UX-ray3.00C9/c92-144[»]
4U4YX-ray3.20C9/c92-144[»]
4U4ZX-ray3.10C9/c92-144[»]
4U50X-ray3.20C9/c92-144[»]
4U51X-ray3.20C9/c92-144[»]
4U52X-ray3.00C9/c92-144[»]
4U53X-ray3.30C9/c92-144[»]
4U55X-ray3.20C9/c92-144[»]
4U56X-ray3.45C9/c92-144[»]
4U6FX-ray3.10C9/c92-144[»]
4V6Ielectron microscopy8.80AS1-144[»]
4V7RX-ray4.00AM/CM1-144[»]
4V88X-ray3.00AT/CT1-144[»]
4V8Yelectron microscopy4.30AT1-144[»]
4V8Zelectron microscopy6.60AT1-144[»]
4V92electron microscopy3.70T3-144[»]
5DATX-ray3.15C9/c92-144[»]
5DC3X-ray3.25C9/c92-144[»]
5DGEX-ray3.45C9/c92-144[»]
5DGFX-ray3.30C9/c92-144[»]
5DGVX-ray3.10C9/c92-144[»]
5FCIX-ray3.40C9/c92-144[»]
5FCJX-ray3.10C9/c92-144[»]
5I4LX-ray3.10C9/c92-144[»]
5JUOelectron microscopy4.00QB1-144[»]
5JUPelectron microscopy3.50QB1-144[»]
5JUSelectron microscopy4.20QB1-144[»]
5JUTelectron microscopy4.00QB1-144[»]
5JUUelectron microscopy4.00QB1-144[»]
5LYBX-ray3.25C9/c92-144[»]
5M1Jelectron microscopy3.30T22-144[»]
5MC6electron microscopy3.80I1-144[»]
5MEIX-ray3.50U/c92-144[»]
5NDGX-ray3.70C9/c92-144[»]
5NDVX-ray3.30C9/c92-144[»]
5NDWX-ray3.70C9/c92-144[»]
5OBMX-ray3.40C9/c92-144[»]
5ON6X-ray3.10U/c92-144[»]
5TBWX-ray3.00U/c92-144[»]
5TGAX-ray3.30C9/c92-144[»]
5TGMX-ray3.50C9/c92-144[»]
6EMLelectron microscopy3.60I1-144[»]
6FAIelectron microscopy3.40T1-144[»]
6GQ1electron microscopy4.40AJ2-144[»]
6GQBelectron microscopy3.90AJ2-144[»]
6GQVelectron microscopy4.00AJ2-144[»]
6HHQX-ray3.10U/c91-144[»]
6I7Oelectron microscopy5.30I/Ib2-144[»]
6Q8Yelectron microscopy3.10I2-144[»]
6RBDelectron microscopy3.47T1-144[»]
6RBEelectron microscopy3.80T1-144[»]
6S47electron microscopy3.28BU2-144[»]
SMRiP07280
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi34280, 194 interactors
IntActiP07280, 33 interactors
MINTiP07280
STRINGi4932.YOL121C

PTM databases

iPTMnetiP07280

Proteomic databases

MaxQBiP07280
PaxDbiP07280
PRIDEiP07280
TopDownProteomicsiP07280

Genome annotation databases

EnsemblFungiiYOL121C_mRNA; YOL121C; YOL121C
GeneIDi854028
KEGGisce:YOL121C

Organism-specific databases

EuPathDBiFungiDB:YOL121C
SGDiS000005481 RPS19A

Phylogenomic databases

HOGENOMiHOG000230649
InParanoidiP07280
KOiK02966
OMAiYIDGPVG

Enzyme and pathway databases

BioCyciYEAST:G3O-33517-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

Protein Ontology

More...
PROi
PR:P07280
RNActiP07280 protein

Family and domain databases

Gene3Di1.10.10.2700, 1 hit
InterProiView protein in InterPro
IPR001266 Ribosomal_S19e
IPR018277 Ribosomal_S19e_CS
IPR038111 Ribosomal_S19e_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR11710 PTHR11710, 1 hit
PfamiView protein in Pfam
PF01090 Ribosomal_S19e, 1 hit
SMARTiView protein in SMART
SM01413 Ribosomal_S19e, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00628 RIBOSOMAL_S19E, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiRS19A_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: P07280
Secondary accession number(s): D6W1U7
<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: April 1, 1988
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 166 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

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