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P50914 · RL14_HUMAN

  • Protein
    Large ribosomal subunit protein eL14
  • Gene
    RPL14
  • 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 (PubMed:12962325, PubMed:23636399, PubMed:32669547).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547).

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 Componentextracellular exosome
Cellular Componentmembrane
Cellular Componentpostsynaptic density
Molecular Functioncadherin binding
Molecular FunctionRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processcytoplasmic translation
Biological Processribosomal large subunit biogenesis
Biological ProcessrRNA processing
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Large ribosomal subunit protein eL14
  • Alternative names
    • 60S ribosomal protein L14
    • CAG-ISL 7

Gene names

    • Name
      RPL14

Organism names

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

Accessions

  • Primary accession
    P50914
  • Secondary accessions
    • Q45RF0
    • Q53G20
    • Q8TBD5
    • Q8WUT0
    • Q92579

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_013633138in dbSNP:rs929099541
Natural variantVAR_047109158-159
Natural variantVAR_013634159
Natural variantVAR_014070159
Natural variantVAR_013635159
Natural variantVAR_013636159
Natural variantVAR_006923159
Natural variantVAR_013637159

Variants

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

The viewer provides 261 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

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

Type
IDPosition(s)Source
Description
Initiator methionine1UniProtRemoved
ChainPRO_00001320312-215UniProtLarge ribosomal subunit protein eL14
Modified residue79UniProtN6-acetyllysine
Modified residue85UniProtN6-acetyllysine; alternate
Modified residue85UniProtN6-succinyllysine; alternate
Cross-link124UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue139UniProtPhosphoserine
Modified residue (large scale data)139PRIDEPhosphoserine
Modified residue204UniProtN6-succinyllysine
Modified residue (large scale data)211PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P50914H1-4 P104122EBI-356746, EBI-358163
BINARY P50914LRRK2 Q5S0072EBI-356746, EBI-5323863
BINARY P50914PHLDA1 Q8WV242EBI-356746, EBI-738731
BINARY P50914RPL4 P365784EBI-356746, EBI-348313

Complex viewer

View interactors in UniProtKB
View CPX-5183 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, repeat.

Type
IDPosition(s)Description
Region161-215Disordered
Repeat171-1751-1
Region171-1904 X 5 AA tandem repeats of Q-K-A-[PAS]-X
Repeat176-1801-2
Repeat181-1851-3
Repeat186-1901-4
Repeat193-1952-1
Region193-1982 X 3 AA tandem repeats of K-[GA]-Q
Repeat196-1982-2

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    215
  • Mass (Da)
    23,432
  • Last updated
    2008-11-04 v4
  • MD5 Checksum
    9BAD67F1538FD42DE5688C52DD1F6F90
MVFRRFVEVGRVAYVSFGPHAGKLVAIVDVIDQNRALVDGPCTQVRRQAMPFKCMQLTDFILKFPHSAHQKYVRQAWQKADINTKWAATRWAKKIEARERKAKMTDFDRFKVMKAKKMRNRIIKNEVKKLQKAALLKASPKKAPGTKGTAAAAAAAAAAKVPAKKITAASKKAPAQKVPAQKATGQKAAPAPKAQKGQKAPAQKAPAPKASGKKA

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E7EPB3E7EPB3_HUMANRPL14124
F8WDZ7F8WDZ7_HUMANRPL1452

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict65in Ref. 2; BAA13443

Polymorphism

The poly-Ala stretch is highly polymorphic.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U16738
EMBL· GenBank· DDBJ
AAC16021.1
EMBL· GenBank· DDBJ
mRNA
D87735
EMBL· GenBank· DDBJ
BAA13443.1
EMBL· GenBank· DDBJ
mRNA
AB061822
EMBL· GenBank· DDBJ
BAB79460.1
EMBL· GenBank· DDBJ
Genomic DNA
DQ118667
EMBL· GenBank· DDBJ
AAZ38460.1
EMBL· GenBank· DDBJ
mRNA
AK223111
EMBL· GenBank· DDBJ
BAD96831.1
EMBL· GenBank· DDBJ
mRNA
AC104186
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC000606
EMBL· GenBank· DDBJ
AAH00606.1
EMBL· GenBank· DDBJ
mRNA
BC005134
EMBL· GenBank· DDBJ
AAH05134.1
EMBL· GenBank· DDBJ
mRNA
BC009294
EMBL· GenBank· DDBJ
AAH09294.1
EMBL· GenBank· DDBJ
mRNA
BC019651
EMBL· GenBank· DDBJ
AAH19651.1
EMBL· GenBank· DDBJ
mRNA
BC022805
EMBL· GenBank· DDBJ
AAH22805.1
EMBL· GenBank· DDBJ
mRNA
BC029036
EMBL· GenBank· DDBJ
AAH29036.1
EMBL· GenBank· DDBJ
mRNA
AB046407
EMBL· GenBank· DDBJ
BAB21253.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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