Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

Q02543 · RL18A_HUMAN

  • Protein
    Large ribosomal subunit protein eL20
  • Gene
    RPL18A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentcytosolic large ribosomal subunit
Cellular Componentcytosolic ribosome
Cellular Componentmembrane
Molecular FunctionRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processcytoplasmic translation
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Large ribosomal subunit protein eL20
  • Alternative names
    • 60S ribosomal protein L18a

Gene names

    • Name
      RPL18A

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q02543

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 183 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, cross-link, modified residue, modified residue (large scale data).

Type
IDPosition(s)Source
Description
ChainPRO_00002139251-176UniProtLarge ribosomal subunit protein eL20
Cross-link11UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue63UniProtPhosphotyrosine
Modified residue (large scale data)63PRIDEPhosphotyrosine
Modified residue71UniProtPhosphoserine
Modified residue (large scale data)71PRIDEPhosphoserine
Modified residue76UniProtN6-succinyllysine
Modified residue123UniProtPhosphoserine
Modified residue (large scale data)123PRIDEPhosphoserine
Cross-link128UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link170UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547).
Binds IPO9 with high affinity (PubMed:11823430).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q02543RPL4 P365783EBI-350523, EBI-348313

Complex viewer

View interactors in UniProtKB
View CPX-5183 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    176
  • Mass (Da)
    20,762
  • Last updated
    1995-02-01 v2
  • MD5 Checksum
    403E21A8903C673F2287CAF0CF7E6A21
MKASGTLREYKVVGRCLPTPKCHTPPLYRMRIFAPNHVVAKSRFWYFVSQLKKMKKSSGEIVYCGQVFEKSPLRVKNFGIWLRYDSRSGTHNMYREYRDLTTAGAVTQCYRDMGARHRARAHSIQIMKVEEIAASKCRRPAVKQFHDSKIKFPLPHRVLRRQHKPRFTTKRPNTFF

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
M0R1A7M0R1A7_HUMANRPL18A147
M0R0P7M0R0P7_HUMANRPL18A137
M0R117M0R117_HUMANRPL18A154
M0R3D6M0R3D6_HUMANRPL18A141

Sequence caution

The sequence CAA56788.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict83in Ref. 2; CAA56788
Sequence conflict134in Ref. 2; CAA56788

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L05093
EMBL· GenBank· DDBJ
AAC18781.1
EMBL· GenBank· DDBJ
mRNA
X80822
EMBL· GenBank· DDBJ
CAA56788.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AC005796
EMBL· GenBank· DDBJ
AAC62828.1
EMBL· GenBank· DDBJ
Genomic DNA
BC007512
EMBL· GenBank· DDBJ
AAH07512.1
EMBL· GenBank· DDBJ
mRNA
BC066319
EMBL· GenBank· DDBJ
AAH66319.1
EMBL· GenBank· DDBJ
mRNA
BC071920
EMBL· GenBank· DDBJ
AAH71920.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help