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P62854 · RS26_HUMAN

  • Protein
    Small ribosomal subunit protein eS26
  • Gene
    RPS26
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the small ribosomal subunit (PubMed:23636399, PubMed:25901680, PubMed:25957688).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:25901680, PubMed:25957688).

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 Componentcytoplasmic side of rough endoplasmic reticulum membrane
Cellular Componentcytosol
Cellular Componentcytosolic small ribosomal subunit
Cellular Componentextracellular exosome
Cellular Componentmembrane
Cellular Componentnucleoplasm
Cellular Componentribosome
Cellular Componentsmall ribosomal subunit
Cellular Componentsynapse
Molecular Functioncadherin binding
Molecular FunctionmRNA binding
Molecular FunctionRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processcytoplasmic translation
Biological Processnegative regulation of RNA splicing
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Small ribosomal subunit protein eS26
  • Alternative names
    • 40S ribosomal protein S26

Gene names

    • Name
      RPS26

Organism names

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

Accessions

  • Primary accession
    P62854
  • Secondary accessions
    • P02383
    • P70394
    • Q06722
    • Q3MHD8
    • Q6IRY4

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Cytoplasm
Note: Detected on cytosolic polysomes (PubMed:25957688).
Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).

Keywords

Disease & Variants

Involvement in disease

Diamond-Blackfan anemia 10 (DBA10)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
  • See also
    MIM:613309
Natural variants in DBA10
Variant IDPosition(s)ChangeDescription
VAR_06358033D>Nin DBA10; dbSNP:rs267607023
VAR_063581115M>Tin DBA10

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_06358033in DBA10; dbSNP:rs267607023
Natural variantVAR_063581115in DBA10

Variants

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

The viewer provides 91 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

Type
IDPosition(s)Source
Description
Initiator methionine1UniProtRemoved
ChainPRO_00002045092-115UniProtSmall ribosomal subunit protein eS26
Modified residue54UniProtPhosphoserine
Modified residue (large scale data)54PRIDEPhosphoserine
Modified residue (large scale data)57PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the 40S small ribosomal subunit.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P62854OTX2 P32243-23EBI-353438, EBI-9087860
BINARY P62854SDCBP O005603EBI-353438, EBI-727004
BINARY P62854TSR2 Q969E817EBI-353438, EBI-746981

Complex viewer

View interactors in UniProtKB
View CPX-5223 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias85-99Basic and acidic residues
Region85-115Disordered
Compositional bias101-115Pro residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    115
  • Mass (Da)
    13,015
  • Last updated
    2007-01-23 v3
  • MD5 Checksum
    F36A1CA722713CCA71D35723C920F54E
MTKKRRNNGRAKKGRGHVQPIRCTNCARCVPKDKAIKKFVIRNIVEAAAVRDISEASVFDAYVLPKLYVKLHYCVSCAIHSKVVRNRSREARKDRTPPPRFRPAGAAPRPPPKPM

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict78in Ref. 2; CAA54808
Compositional bias85-99Basic and acidic residues
Compositional bias101-115Pro residues
Sequence conflict109in Ref. 1; CAA49345

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X69654
EMBL· GenBank· DDBJ
CAA49345.1
EMBL· GenBank· DDBJ
mRNA
X77770
EMBL· GenBank· DDBJ
CAA54808.1
EMBL· GenBank· DDBJ
mRNA
X79236
EMBL· GenBank· DDBJ
CAA55818.1
EMBL· GenBank· DDBJ
Genomic DNA
U41448
EMBL· GenBank· DDBJ
AAC26987.1
EMBL· GenBank· DDBJ
Genomic DNA
BC002604
EMBL· GenBank· DDBJ
AAH02604.1
EMBL· GenBank· DDBJ
mRNA
BC015832
EMBL· GenBank· DDBJ
AAH15832.1
EMBL· GenBank· DDBJ
mRNA
BC070220
EMBL· GenBank· DDBJ
AAH70220.1
EMBL· GenBank· DDBJ
mRNA
BC105276
EMBL· GenBank· DDBJ
AAI05277.1
EMBL· GenBank· DDBJ
mRNA
BC105798
EMBL· GenBank· DDBJ
AAI05799.1
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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