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Entry version 80 (17 Jun 2020)
Sequence version 1 (28 Jun 2011)
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Protein

60S ribosomal protein L18-A

Gene

RPL18A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

Miscellaneous

There are 2 genes for eL18 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

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33516-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-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%5Fand%5Ftaxonomy%5Fsection">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 L18-A1 Publication
Alternative name(s):
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:RPL18A1 Publication
Synonyms:RP28A
Ordered Locus Names:YOL120C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Saccharomyces Genome Database

More...
SGDi
S000005480 RPL18A

<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 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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001327842 – 18660S ribosomal protein L18-AAdd BLAST185

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 residuei50N6,N6,N6-trimethyllysine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P0CX49

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

More...
PaxDbi
P0CX49

PRoteomics IDEntifications database

More...
PRIDEi
P0CX49

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0CX49

<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
P0CX49 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%5Fsection">'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%5Fsection">'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) (PubMed:9559554, PubMed:22096102). eL18 interacts with NAP1 (PubMed:18086883).

1 Publication2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
34281, 93 interactors
35537, 128 interactors

Protein interaction database and analysis system

More...
IntActi
P0CX49, 1 interactor

Molecular INTeraction database

More...
MINTi
P0CX49

STRING: functional protein association networks

More...
STRINGi
4932.YOL120C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P0CX49 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

1186
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

More...
SMRi
P0CX49

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0CX49

<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
CLU_080024_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CX49

KEGG Orthology (KO)

More...
KOi
K02883

Identification of Orthologs from Complete Genome Data

More...
OMAi
TNRPPMS

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036227 L18e/L15P_sf
IPR000039 Ribosomal_L18e
IPR021131 Ribosomal_L18e/L15P
IPR021132 Ribosomal_L18e_CS

The PANTHER Classification System

More...
PANTHERi
PTHR10934 PTHR10934, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17135 Ribosomal_L18, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52080 SSF52080, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01106 RIBOSOMAL_L18E, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0CX49-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGIDHTSKQH KRSGHRTAPK SDNVYLKLLV KLYTFLARRT DAPFNKVVLK
60 70 80 90 100
ALFLSKINRP PVSVSRIARA LKQEGAANKT VVVVGTVTDD ARIFEFPKTT
110 120 130 140 150
VAALRFTAGA RAKIVKAGGE CITLDQLAVR APKGQNTLIL RGPRNSREAV
160 170 180
RHFGMGPHKG KAPRILSTGR KFERARGRRR SKGFKV
Length:186
Mass (Da):20,563
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:iD097B187F369EACD
GO

<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 20419.431 Da. Determined by ESI. Monoisotopic 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
X01099 Genomic DNA Translation: CAA25573.1
X02635 Genomic DNA Translation: CAA26481.1
X95258 Genomic DNA Translation: CAA64550.1
Z74862 Genomic DNA Translation: CAA99139.1
BK006948 Genomic DNA Translation: DAA10664.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S05867 R5BY8E

NCBI Reference Sequences

More...
RefSeqi
NP_014098.1, NM_001183139.1
NP_014521.1, NM_001183374.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL301C_mRNA; YNL301C; YNL301C
YOL120C_mRNA; YOL120C; YOL120C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854029
855415

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL301C
sce:YOL120C

<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
X01099 Genomic DNA Translation: CAA25573.1
X02635 Genomic DNA Translation: CAA26481.1
X95258 Genomic DNA Translation: CAA64550.1
Z74862 Genomic DNA Translation: CAA99139.1
BK006948 Genomic DNA Translation: DAA10664.1
PIRiS05867 R5BY8E
RefSeqiNP_014098.1, NM_001183139.1
NP_014521.1, NM_001183374.1

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
1K5Ymodel-O22-141[»]
3J6Xelectron microscopy6.10581-186[»]
3J6Yelectron microscopy6.10581-186[»]
3J77electron microscopy6.20681-186[»]
3J78electron microscopy6.30681-186[»]
3JCTelectron microscopy3.08Q1-186[»]
4U3MX-ray3.00M8/m82-186[»]
4U3NX-ray3.20M8/m82-186[»]
4U3UX-ray2.90M8/m82-186[»]
4U4NX-ray3.10M8/m82-186[»]
4U4OX-ray3.60M8/m82-186[»]
4U4QX-ray3.00M8/m82-186[»]
4U4RX-ray2.80M8/m82-186[»]
4U4UX-ray3.00M8/m82-186[»]
4U4YX-ray3.20M8/m82-186[»]
4U4ZX-ray3.10M8/m82-186[»]
4U50X-ray3.20M8/m82-186[»]
4U51X-ray3.20M8/m82-186[»]
4U52X-ray3.00M8/m82-186[»]
4U53X-ray3.30M8/m82-186[»]
4U55X-ray3.20M8/m82-186[»]
4U56X-ray3.45M8/m82-186[»]
4U6FX-ray3.10M8/m82-186[»]
4V4Belectron microscopy11.70BO22-141[»]
4V6Ielectron microscopy8.80BR1-186[»]
4V7Felectron microscopy8.70Q1-186[»]
4V7RX-ray4.00BR/DR1-186[»]
4V88X-ray3.00BQ/DQ1-186[»]
4V8Yelectron microscopy4.30BQ2-186[»]
4V8Zelectron microscopy6.60BQ2-186[»]
4V91electron microscopy3.70Q1-186[»]
5APNelectron microscopy3.91Q1-186[»]
5APOelectron microscopy3.41Q1-186[»]
5DATX-ray3.15M8/m82-186[»]
5DC3X-ray3.25M8/m82-186[»]
5DGEX-ray3.45M8/m82-186[»]
5DGFX-ray3.30M8/m82-186[»]
5DGVX-ray3.10M8/m82-186[»]
5FCIX-ray3.40M8/m82-186[»]
5FCJX-ray3.10M8/m82-186[»]
5FL8electron microscopy9.50Q1-186[»]
5GAKelectron microscopy3.88S1-186[»]
5H4Pelectron microscopy3.07Q1-186[»]
5I4LX-ray3.10M8/m82-186[»]
5JCSelectron microscopy9.50Q1-186[»]
5JUOelectron microscopy4.00V1-186[»]
5JUPelectron microscopy3.50V1-186[»]
5JUSelectron microscopy4.20V1-186[»]
5JUTelectron microscopy4.00V1-186[»]
5JUUelectron microscopy4.00V1-186[»]
5LYBX-ray3.25M8/m82-186[»]
5M1Jelectron microscopy3.30Q52-186[»]
5MC6electron microscopy3.80BB1-186[»]
5MEIX-ray3.50CS/y2-186[»]
5NDGX-ray3.70M8/m82-186[»]
5NDVX-ray3.30M8/m82-186[»]
5NDWX-ray3.70M8/m82-186[»]
5OBMX-ray3.40M8/m82-186[»]
5ON6X-ray3.10CS/y2-186[»]
5T62electron microscopy3.30d1-186[»]
5T6Relectron microscopy4.50d1-186[»]
5TBWX-ray3.00CS/y2-186[»]
5TGAX-ray3.30M8/m82-186[»]
5TGMX-ray3.50M8/m82-186[»]
5Z3Gelectron microscopy3.65U1-186[»]
6C0Felectron microscopy3.70Q1-186[»]
6CB1electron microscopy4.60Q1-186[»]
6ELZelectron microscopy3.30Q1-186[»]
6EM1electron microscopy3.60Q1-186[»]
6EM3electron microscopy3.20Q1-186[»]
6EM4electron microscopy4.10Q1-186[»]
6EM5electron microscopy4.30Q1-186[»]
6FT6electron microscopy3.90Q1-186[»]
6GQ1electron microscopy4.40Q2-186[»]
6GQBelectron microscopy3.90Q2-186[»]
6GQVelectron microscopy4.00Q2-186[»]
6HD7electron microscopy3.40S1-186[»]
6HHQX-ray3.10CS/y1-186[»]
6I7Oelectron microscopy5.30BB/YB2-186[»]
6N8Jelectron microscopy3.50Q1-186[»]
6N8Kelectron microscopy3.60Q1-186[»]
6N8Lelectron microscopy3.60Q1-186[»]
6N8Melectron microscopy3.50d1-186[»]
6N8Nelectron microscopy3.80d1-186[»]
6N8Oelectron microscopy3.50d1-186[»]
6Q8Yelectron microscopy3.10BB2-186[»]
6QIKelectron microscopy3.10Q1-186[»]
6QT0electron microscopy3.40Q1-186[»]
6QTZelectron microscopy3.50Q1-186[»]
6R84electron microscopy3.60S2-186[»]
6R86electron microscopy3.40S2-186[»]
6R87electron microscopy3.40S2-186[»]
6RI5electron microscopy3.30Q1-186[»]
6RZZelectron microscopy3.20Q1-186[»]
6S05electron microscopy3.90Q1-186[»]
6S47electron microscopy3.28AS2-186[»]
6SNTelectron microscopy2.80w1-186[»]
6SV4electron microscopy3.30BB/YB/ZB1-186[»]
6T4Qelectron microscopy2.60LQ2-186[»]
6T7Ielectron microscopy3.20LQ1-186[»]
6T7Telectron microscopy3.10LQ1-186[»]
6T83electron microscopy4.00B/Qy1-186[»]
SMRiP0CX49
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34281, 93 interactors
35537, 128 interactors
IntActiP0CX49, 1 interactor
MINTiP0CX49
STRINGi4932.YOL120C

PTM databases

iPTMnetiP0CX49

Proteomic databases

MaxQBiP0CX49
PaxDbiP0CX49
PRIDEiP0CX49

Genome annotation databases

EnsemblFungiiYNL301C_mRNA; YNL301C; YNL301C
YOL120C_mRNA; YOL120C; YOL120C
GeneIDi854029
855415
KEGGisce:YNL301C
sce:YOL120C

Organism-specific databases

SGDiS000005480 RPL18A

Phylogenomic databases

HOGENOMiCLU_080024_0_1_1
InParanoidiP0CX49
KOiK02883
OMAiTNRPPMS

Enzyme and pathway databases

BioCyciYEAST:G3O-33516-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-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

EvolutionaryTraceiP0CX49

Protein Ontology

More...
PROi
PR:P0CX49
RNActiP0CX49 protein

Gene expression databases

ExpressionAtlasiP0CX49 differential

Family and domain databases

InterProiView protein in InterPro
IPR036227 L18e/L15P_sf
IPR000039 Ribosomal_L18e
IPR021131 Ribosomal_L18e/L15P
IPR021132 Ribosomal_L18e_CS
PANTHERiPTHR10934 PTHR10934, 1 hit
PfamiView protein in Pfam
PF17135 Ribosomal_L18, 1 hit
SUPFAMiSSF52080 SSF52080, 1 hit
PROSITEiView protein in PROSITE
PS01106 RIBOSOMAL_L18E, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiRL18A_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: P0CX49
Secondary accession number(s): D6W0P3, P07279
<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%5Fand%5Fisoforms">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: June 17, 2020
This is version 80 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, 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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