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.

P62857 · RS28_HUMAN

  • Protein
    Small ribosomal subunit protein eS28
  • Gene
    RPS28
  • 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).
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).

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 Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentribosome
Cellular Componentsmall ribosomal subunit
Cellular Componentsmall-subunit processome
Cellular Componentsynapse
Molecular FunctionRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processcytoplasmic translation
Biological Processmaturation of SSU-rRNA
Biological Processribosomal small subunit assembly
Biological Processribosomal small subunit biogenesis
Biological Processribosome biogenesis
Biological ProcessrRNA processing
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Small ribosomal subunit protein eS28
  • Alternative names
    • 40S ribosomal protein S28

Gene names

    • Name
      RPS28

Organism names

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

Accessions

  • Primary accession
    P62857
  • Secondary accessions
    • P25112

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Cytoplasm
Nucleus, nucleolus
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 15, with mandibulofacial dysostosis (DBA15)

  • 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:606164

Variants

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

The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

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_00001368221-69UniProtSmall ribosomal subunit protein eS28
Modified residue (large scale data)21PRIDEPhosphothreonine
Modified residue (large scale data)23PRIDEPhosphoserine
Modified residue (large scale data)38PRIDEPhosphothreonine
Modified residue (large scale data)39PRIDEPhosphoserine
Modified residue41UniProtPhosphoserine
Modified residue (large scale data)41PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the 40S small ribosomal subunit (PubMed:23636399, PubMed:25901680, PubMed:25957688).
Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P62857CCNDBP1 O952733EBI-353027, EBI-748961
BINARY P62857HSF2BP O750313EBI-353027, EBI-7116203
BINARY P62857KRTAP1-1 Q076273EBI-353027, EBI-11959885
BINARY P62857KRTAP10-7 P604093EBI-353027, EBI-10172290
BINARY P62857KRTAP10-8 P604103EBI-353027, EBI-10171774
BINARY P62857KRTAP2-3 P0C7H83EBI-353027, EBI-10196781
BINARY P62857NOTCH2NLA Q7Z3S93EBI-353027, EBI-945833

Complex viewer

View interactors in UniProtKB
View CPX-5223 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    69
  • Mass (Da)
    7,841
  • Last updated
    2004-08-16 v1
  • MD5 Checksum
    A94F14E12E9C2D0C3885D7DB26DDDF2E
MDTSRVQPIKLARVTKVLGRTGSQGQCTQVRVEFMDDTSRSIIRNVKGPVREGDVLTLLESEREARRLR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict66in Ref. 6; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L05091
EMBL· GenBank· DDBJ
AAC15855.1
EMBL· GenBank· DDBJ
mRNA
U58682
EMBL· GenBank· DDBJ
AAB07066.1
EMBL· GenBank· DDBJ
mRNA
AB061846
EMBL· GenBank· DDBJ
BAB79484.1
EMBL· GenBank· DDBJ
Genomic DNA
CR457055
EMBL· GenBank· DDBJ
CAG33336.1
EMBL· GenBank· DDBJ
mRNA
BC000354
EMBL· GenBank· DDBJ
AAH00354.1
EMBL· GenBank· DDBJ
mRNA
BC021239
EMBL· GenBank· DDBJ
AAH21239.1
EMBL· GenBank· DDBJ
mRNA
BC070217
EMBL· GenBank· DDBJ
AAH70217.1
EMBL· GenBank· DDBJ
mRNA
BC070218
EMBL· GenBank· DDBJ
AAH70218.1
EMBL· GenBank· DDBJ
mRNA
AB007164
EMBL· GenBank· DDBJ
BAA28594.1
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.
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