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Entry version 72 (13 Feb 2019)
Sequence version 1 (28 Jun 2011)
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Protein

60S ribosomal protein L19-A

Gene

RPL19A

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. eL19 may play a role in the last stages of translation initiation, in particular sububit joining and shedding/releasing factors.1 Publication

Miscellaneous

Present with 97700 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL19 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

  • RNA binding Source: InterPro
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

  • cytoplasmic translation 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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29228-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-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:
60S ribosomal protein L19-A1 Publication
Alternative name(s):
L23
RP15L
RP33
YL14
<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:RPL19A1 Publication
Synonyms:RPL23A, YL14A
Ordered Locus Names:YBR084C-A
ORF Names:YBR084BC
<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 II

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002156 RPL19A

<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 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1741172

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001311842 – 18960S ribosomal protein L19-AAdd BLAST188

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<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 residuei30PhosphoserineCombined sources1
Modified residuei37PhosphoserineCombined sources1
Cross-linki53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei91PhosphoserineCombined sources1
Cross-linki146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P0CX82

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

More...
PaxDbi
P0CX82

PRoteomics IDEntifications database

More...
PRIDEi
P0CX82

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P0CX82

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P0CX82

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0CX82

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P0CX82 differential

<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 large ribosomal subunit (LSU). 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). eL19 lies in close proximity to the binding site for eukaryotic initiation factor eIF4G (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32671, 281 interactors
32789, 127 interactors

Protein interaction database and analysis system

More...
IntActi
P0CX82, 2 interactors

Molecular INTeraction database

More...
MINTi
P0CX82

STRING: functional protein association networks

More...
STRINGi
4932.YBR084C-A

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0CX82

<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

1189
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
1K5Ymodel-P3-143[»]
2WW9electron microscopy8.60J1-189[»]
2WWAelectron microscopy8.90J1-189[»]
3J6Xelectron microscopy6.10591-189[»]
3J6Yelectron microscopy6.10591-189[»]
3J77electron microscopy6.20691-189[»]
3J78electron microscopy6.30691-189[»]
3JCTelectron microscopy3.08R1-189[»]
4U3MX-ray3.00M9/m92-189[»]
4U3NX-ray3.20M9/m92-189[»]
4U3UX-ray2.90M9/m92-189[»]
4U4NX-ray3.10M9/m92-189[»]
4U4OX-ray3.60M9/m92-189[»]
4U4QX-ray3.00M9/m92-189[»]
4U4RX-ray2.80M9/m92-189[»]
4U4UX-ray3.00M9/m92-189[»]
4U4YX-ray3.20M9/m92-189[»]
4U4ZX-ray3.10M9/m92-189[»]
4U50X-ray3.20M9/m92-189[»]
4U51X-ray3.20M9/m92-189[»]
4U52X-ray3.00M9/m92-189[»]
4U53X-ray3.30M9/m92-189[»]
4U55X-ray3.20M9/m92-189[»]
4U56X-ray3.45M9/m92-189[»]
4U6FX-ray3.10M9/m92-189[»]
4V4Belectron microscopy11.70BP2-143[»]
4V6Ielectron microscopy8.80BT1-189[»]
4V7Felectron microscopy8.70R1-189[»]
4V7RX-ray4.00BS/DS1-189[»]
4V88X-ray3.00BR/DR1-189[»]
4V91electron microscopy3.70R1-189[»]
5APNelectron microscopy3.91R1-189[»]
5APOelectron microscopy3.41R1-189[»]
5DATX-ray3.15M9/m92-189[»]
5DC3X-ray3.25M9/m92-189[»]
5DGEX-ray3.45M9/m92-189[»]
5DGFX-ray3.30M9/m92-189[»]
5DGVX-ray3.10M9/m92-189[»]
5FCIX-ray3.40M9/m92-189[»]
5FCJX-ray3.10M9/m92-189[»]
5FL8electron microscopy9.50R1-189[»]
5GAKelectron microscopy3.88T1-189[»]
5H4Pelectron microscopy3.07R1-189[»]
5I4LX-ray3.10M9/m92-189[»]
5JCSelectron microscopy9.50R1-189[»]
5JUOelectron microscopy4.00W1-189[»]
5JUPelectron microscopy3.50W1-189[»]
5JUSelectron microscopy4.20W1-189[»]
5JUTelectron microscopy4.00W1-189[»]
5JUUelectron microscopy4.00W1-189[»]
5LYBX-ray3.25M9/m92-189[»]
5M1Jelectron microscopy3.30R52-189[»]
5MC6electron microscopy3.80BF1-189[»]
5MEIX-ray3.50CT/z2-189[»]
5NDGX-ray3.70M9/m92-189[»]
5NDVX-ray3.30M9/m92-189[»]
5NDWX-ray3.70M9/m92-189[»]
5OBMX-ray3.40M9/m92-189[»]
5ON6X-ray3.10CT/z2-189[»]
5T62electron microscopy3.30e1-189[»]
5T6Relectron microscopy4.50e1-189[»]
5TBWX-ray3.00CT/z2-189[»]
5TGAX-ray3.30M9/m92-189[»]
5TGMX-ray3.50M9/m92-189[»]
6ELZelectron microscopy3.30R1-189[»]
6EM5electron microscopy4.30R1-189[»]
6FT6electron microscopy3.90R1-189[»]
6GQ1electron microscopy4.40R2-189[»]
6GQBelectron microscopy3.90R2-189[»]
6GQVelectron microscopy4.00R2-189[»]
6HD7electron microscopy3.40T1-189[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0CX82

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

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SMRi
P0CX82

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0CX82

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CX82

KEGG Orthology (KO)

More...
KOi
K02885

Identification of Orthologs from Complete Genome Data

More...
OMAi
NRVWIDP

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01417 Ribosomal_L19e_E, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1650.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01475 Ribosomal_L19e, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035970 60S_ribosomal_L19/L19e_sf
IPR000196 Ribosomal_L19/L19e
IPR023638 Ribosomal_L19/L19e_CS
IPR015972 Ribosomal_L19/L19e_dom1
IPR033935 Ribosomal_L19_euka
IPR039547 RPL19

The PANTHER Classification System

More...
PANTHERi
PTHR10722 PTHR10722, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01280 Ribosomal_L19e, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01416 Ribosomal_L19e, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48140 SSF48140, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00526 RIBOSOMAL_L19E, 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.

P0CX82-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANLRTQKRL AASVVGVGKR KVWLDPNETS EIAQANSRNA IRKLVKNGTI
60 70 80 90 100
VKKAVTVHSK SRTRAHAQSK REGRHSGYGK RKGTREARLP SQVVWIRRLR
110 120 130 140 150
VLRRLLAKYR DAGKIDKHLY HVLYKESKGN AFKHKRALVE HIIQAKADAQ
160 170 180
REKALNEEAE ARRLKNRAAR DRRAQRVAEK RDALLKEDA
Length:189
Mass (Da):21,704
Last modified:June 28, 2011 - 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:i776C3AB3D348EE99
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 conflicti54A → S in J03724 (PubMed:2836393).Curated1

<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 21573.159 Da from positions 2 - 189. Determined by ESI. Average mass.1 Publication

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
Z36751 Genomic DNA Translation: CAA85322.1
D17337 mRNA Translation: BAA04155.1
Z35953 Genomic DNA Translation: CAA85030.1
Z35954 Genomic DNA Translation: CAA85032.1
J03724 Genomic DNA No translation available.
BK006936 Genomic DNA Translation: DAA07204.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S44597

NCBI Reference Sequences

More...
RefSeqi
NP_009526.1, NM_001178267.1
NP_009641.1, NM_001180057.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBL027W_mRNA; YBL027W_mRNA; YBL027W
YBR084C-A_mRNA; YBR084C-A_mRNA; YBR084C-A

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852254
852379

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBL027W
sce:YBR084C-A

<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
Z36751 Genomic DNA Translation: CAA85322.1
D17337 mRNA Translation: BAA04155.1
Z35953 Genomic DNA Translation: CAA85030.1
Z35954 Genomic DNA Translation: CAA85032.1
J03724 Genomic DNA No translation available.
BK006936 Genomic DNA Translation: DAA07204.1
PIRiS44597
RefSeqiNP_009526.1, NM_001178267.1
NP_009641.1, NM_001180057.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-P3-143[»]
2WW9electron microscopy8.60J1-189[»]
2WWAelectron microscopy8.90J1-189[»]
3J6Xelectron microscopy6.10591-189[»]
3J6Yelectron microscopy6.10591-189[»]
3J77electron microscopy6.20691-189[»]
3J78electron microscopy6.30691-189[»]
3JCTelectron microscopy3.08R1-189[»]
4U3MX-ray3.00M9/m92-189[»]
4U3NX-ray3.20M9/m92-189[»]
4U3UX-ray2.90M9/m92-189[»]
4U4NX-ray3.10M9/m92-189[»]
4U4OX-ray3.60M9/m92-189[»]
4U4QX-ray3.00M9/m92-189[»]
4U4RX-ray2.80M9/m92-189[»]
4U4UX-ray3.00M9/m92-189[»]
4U4YX-ray3.20M9/m92-189[»]
4U4ZX-ray3.10M9/m92-189[»]
4U50X-ray3.20M9/m92-189[»]
4U51X-ray3.20M9/m92-189[»]
4U52X-ray3.00M9/m92-189[»]
4U53X-ray3.30M9/m92-189[»]
4U55X-ray3.20M9/m92-189[»]
4U56X-ray3.45M9/m92-189[»]
4U6FX-ray3.10M9/m92-189[»]
4V4Belectron microscopy11.70BP2-143[»]
4V6Ielectron microscopy8.80BT1-189[»]
4V7Felectron microscopy8.70R1-189[»]
4V7RX-ray4.00BS/DS1-189[»]
4V88X-ray3.00BR/DR1-189[»]
4V91electron microscopy3.70R1-189[»]
5APNelectron microscopy3.91R1-189[»]
5APOelectron microscopy3.41R1-189[»]
5DATX-ray3.15M9/m92-189[»]
5DC3X-ray3.25M9/m92-189[»]
5DGEX-ray3.45M9/m92-189[»]
5DGFX-ray3.30M9/m92-189[»]
5DGVX-ray3.10M9/m92-189[»]
5FCIX-ray3.40M9/m92-189[»]
5FCJX-ray3.10M9/m92-189[»]
5FL8electron microscopy9.50R1-189[»]
5GAKelectron microscopy3.88T1-189[»]
5H4Pelectron microscopy3.07R1-189[»]
5I4LX-ray3.10M9/m92-189[»]
5JCSelectron microscopy9.50R1-189[»]
5JUOelectron microscopy4.00W1-189[»]
5JUPelectron microscopy3.50W1-189[»]
5JUSelectron microscopy4.20W1-189[»]
5JUTelectron microscopy4.00W1-189[»]
5JUUelectron microscopy4.00W1-189[»]
5LYBX-ray3.25M9/m92-189[»]
5M1Jelectron microscopy3.30R52-189[»]
5MC6electron microscopy3.80BF1-189[»]
5MEIX-ray3.50CT/z2-189[»]
5NDGX-ray3.70M9/m92-189[»]
5NDVX-ray3.30M9/m92-189[»]
5NDWX-ray3.70M9/m92-189[»]
5OBMX-ray3.40M9/m92-189[»]
5ON6X-ray3.10CT/z2-189[»]
5T62electron microscopy3.30e1-189[»]
5T6Relectron microscopy4.50e1-189[»]
5TBWX-ray3.00CT/z2-189[»]
5TGAX-ray3.30M9/m92-189[»]
5TGMX-ray3.50M9/m92-189[»]
6ELZelectron microscopy3.30R1-189[»]
6EM5electron microscopy4.30R1-189[»]
6FT6electron microscopy3.90R1-189[»]
6GQ1electron microscopy4.40R2-189[»]
6GQBelectron microscopy3.90R2-189[»]
6GQVelectron microscopy4.00R2-189[»]
6HD7electron microscopy3.40T1-189[»]
ProteinModelPortaliP0CX82
SMRiP0CX82
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32671, 281 interactors
32789, 127 interactors
IntActiP0CX82, 2 interactors
MINTiP0CX82
STRINGi4932.YBR084C-A

Chemistry databases

BindingDBiP0CX82
ChEMBLiCHEMBL1741172

PTM databases

CarbonylDBiP0CX82
iPTMnetiP0CX82

Proteomic databases

MaxQBiP0CX82
PaxDbiP0CX82
PRIDEiP0CX82
TopDownProteomicsiP0CX82

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL027W_mRNA; YBL027W_mRNA; YBL027W
YBR084C-A_mRNA; YBR084C-A_mRNA; YBR084C-A
GeneIDi852254
852379
KEGGisce:YBL027W
sce:YBR084C-A

Organism-specific databases

SGDiS000002156 RPL19A

Phylogenomic databases

InParanoidiP0CX82
KOiK02885
OMAiNRVWIDP

Enzyme and pathway databases

BioCyciYEAST:G3O-29228-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-72689 Formation of a pool of free 40S subunits
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

EvolutionaryTraceiP0CX82

Protein Ontology

More...
PROi
PR:P0CX82

Gene expression databases

ExpressionAtlasiP0CX82 differential

Family and domain databases

CDDicd01417 Ribosomal_L19e_E, 1 hit
Gene3Di1.10.1650.10, 1 hit
HAMAPiMF_01475 Ribosomal_L19e, 1 hit
InterProiView protein in InterPro
IPR035970 60S_ribosomal_L19/L19e_sf
IPR000196 Ribosomal_L19/L19e
IPR023638 Ribosomal_L19/L19e_CS
IPR015972 Ribosomal_L19/L19e_dom1
IPR033935 Ribosomal_L19_euka
IPR039547 RPL19
PANTHERiPTHR10722 PTHR10722, 1 hit
PfamiView protein in Pfam
PF01280 Ribosomal_L19e, 1 hit
SMARTiView protein in SMART
SM01416 Ribosomal_L19e, 1 hit
SUPFAMiSSF48140 SSF48140, 1 hit
PROSITEiView protein in PROSITE
PS00526 RIBOSOMAL_L19E, 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 nameiRL19A_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: P0CX82
Secondary accession number(s): D6VPX3, P05735
<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: June 28, 2011
Last sequence update: June 28, 2011
Last modified: February 13, 2019
This is version 72 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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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