Q9W5R8 · RL5_DROME

Function

function

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.

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 Componentcytosolic large ribosomal subunit
Cellular Componentcytosolic ribosome
Cellular Componentnucleus
Molecular Function5S rRNA binding
Molecular FunctionRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processcytoplasmic translation
Biological Processribosomal large subunit assembly

Keywords

Enzyme and pathway databases

    • R-DME-156827L13a-mediated translational silencing of Ceruloplasmin expression
    • R-DME-1799339SRP-dependent cotranslational protein targeting to membrane
    • R-DME-72689Formation of a pool of free 40S subunits
    • R-DME-72706GTP hydrolysis and joining of the 60S ribosomal subunit
    • R-DME-975956Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
    • R-DME-975957Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Names & Taxonomy

Protein names

  • Recommended name
    Large ribosomal subunit protein uL18
  • Alternative names
    • 60S ribosomal protein L5

Gene names

    • Name
      RpL5
    • Synonyms
      yip6
    • ORF names
      CG17489

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9W5R8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002915591-299Large ribosomal subunit protein uL18

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Component of the large ribosomal subunit (LSU) (By similarity).
Interacts with Fmr1 to form the RNA-induced silencing complex (RISC), a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are Rm62, RpL11, AGO2 and Dcr-1 (PubMed:12368261).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    299
  • Mass (Da)
    34,037
  • Last updated
    2001-03-01 v2
  • Checksum
    523F50ED67E7841A
MGFVKVVKNKQYFKRYQVKFRRRREGKTDYYARKRLTFQDKNKYNTPKYRLIVRLSNKDITVQIAYARIEGDRVVCAAYSHELPKYGIQVGLTNYAAAYCTGLLVARRVLNKLGLDSLYAGCTEVTGEEFNVEPVDDGPGAFRCFLDVGLARTTTGARVFGAMKGAVDGGLNIPHSVKRFPGYSAETKSFNADVHRAHIFGQHVADYMRSLEEEDEESFKRQFSRYIKLGIRADDLEDIYKKAHQAIRNDPTHKVTAKKSSAVTKKRWNAKKLTNEQRKTKIAAHKAAYVAKLQSETEA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
R9Q794R9Q794_DROMERpL5299

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014134
EMBL· GenBank· DDBJ
EAA46016.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014134
EMBL· GenBank· DDBJ
EAA46019.1
EMBL· GenBank· DDBJ
Genomic DNA
AY071305
EMBL· GenBank· DDBJ
AAL48927.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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