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P62899 · RL31_HUMAN

  • Protein
    Large ribosomal subunit protein eL31
  • Gene
    RPL31
  • 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:23636399, PubMed:32669547).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (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 Componentfocal adhesion
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 eL31
  • Alternative names
    • 60S ribosomal protein L31

Gene names

    • Name
      RPL31

Organism names

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

Accessions

  • Primary accession
    P62899
  • Secondary accessions
    • B7Z4K2
    • D3DVJ4
    • P12947
    • Q53SQ5
    • Q6IRZ0
    • Q6LBJ6

Proteomes

Organism-specific databases

Disease & Variants

Variants

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

The viewer provides 117 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 modified residue, chain, modified residue (large scale data).

Type
IDPosition(s)Source
Description
Modified residue1UniProtN-acetylmethionine
ChainPRO_00001537631-125UniProtLarge ribosomal subunit protein eL31
Modified residue15UniProtPhosphoserine
Modified residue (large scale data)15PRIDEPhosphoserine
Modified residue55UniProtN6-succinyllysine
Modified residue70UniProtN6-succinyllysine
Modified residue75UniProtN6-acetyllysine; alternate
Modified residue75UniProtN6-succinyllysine; alternate
Modified residue98UniProtPhosphoserine
Modified residue (large scale data)98PRIDEPhosphoserine
Modified residue (large scale data)103PRIDEPhosphotyrosine
Modified residue (large scale data)108PRIDEPhosphotyrosine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the large ribosomal subunit.

Binary interactions

Type
Entry 1Entry 2Number of experimentsIntAct
BINARY P62899CHAT P28329-33EBI-1053664, EBI-25837549
BINARY P62899CTCF P497113EBI-1053664, EBI-932887
BINARY P62899FGFR3 P226073EBI-1053664, EBI-348399
BINARY P62899GSN P063963EBI-1053664, EBI-351506
BINARY P62899HTT P428583EBI-1053664, EBI-466029
XENO P62899N P0DTC96EBI-1053664, EBI-25475856
BINARY P62899 Q9Y6493EBI-1053664, EBI-25900580
BINARY P62899UBQLN1 Q9UMX03EBI-1053664, EBI-741480

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 & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

P62899-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    125
  • Mass (Da)
    14,463
  • Last updated
    2004-08-31 v1
  • MD5 Checksum
    BBAD9FA9F2882D0A50BF6CB07141C653
MAPAKKGGEKKKGRSAINEVVTREYTINIHKRIHGVGFKKRAPRALKEIRKFAMKEMGTPDVRIDTRLNKAVWAKGIRNVPYRIRVRLSRKRNEDEDSPNKLYTLVTYVPVTTFKNLQTVNVDEN

P62899-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 116-125: NLQTVNVDEN → ISVLNSVTVAKSP

P62899-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9JU56C9JU56_HUMANRPL31115
B7Z4C8B7Z4C8_HUMANRPL31130
B7Z4E3B7Z4E3_HUMANRPL31120
B8ZZK4B8ZZK4_HUMANRPL3179
H7C2W9H7C2W9_HUMANRPL31108

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_042572116-125in isoform 2
Alternative sequenceVSP_043224116-125in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X15940
EMBL· GenBank· DDBJ
CAA34066.1
EMBL· GenBank· DDBJ
mRNA
AB061830
EMBL· GenBank· DDBJ
BAB79468.1
EMBL· GenBank· DDBJ
Genomic DNA
AK297483
EMBL· GenBank· DDBJ
BAH12588.1
EMBL· GenBank· DDBJ
mRNA
AC016738
EMBL· GenBank· DDBJ
AAY14823.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471127
EMBL· GenBank· DDBJ
EAX01826.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471127
EMBL· GenBank· DDBJ
EAX01827.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471127
EMBL· GenBank· DDBJ
EAX01829.1
EMBL· GenBank· DDBJ
Genomic DNA
BC017343
EMBL· GenBank· DDBJ
AAH17343.1
EMBL· GenBank· DDBJ
mRNA
BC070210
EMBL· GenBank· DDBJ
AAH70210.1
EMBL· GenBank· DDBJ
mRNA
BC070373
EMBL· GenBank· DDBJ
AAH70373.1
EMBL· GenBank· DDBJ
mRNA
X69181
EMBL· GenBank· DDBJ
CAA48925.1
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.
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