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Protein

40S ribosomal protein S21

Gene

RPS21

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein N-terminus binding Source: UniProtKB
  3. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: GO_Central
  3. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: GO_Central
  4. gene expression Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  6. ribosomal small subunit biogenesis Source: GO_Central
  7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  8. translation Source: UniProtKB
  9. translational elongation Source: Reactome
  10. translational initiation Source: Reactome
  11. translational termination Source: Reactome
  12. viral life cycle Source: Reactome
  13. viral process Source: Reactome
  14. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S21
Gene namesi
Name:RPS21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:10409. RPS21.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic small ribosomal subunit Source: UniProtKB
  4. small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34812.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838340S ribosomal protein S21PRO_0000194730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei81 – 811N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP63220.
PaxDbiP63220.
PRIDEiP63220.

PTM databases

PhosphoSiteiP63220.

Miscellaneous databases

PMAP-CutDBP63220.

Expressioni

Gene expression databases

BgeeiP63220.
CleanExiHS_RPS21.
ExpressionAtlasiP63220. baseline and differential.
GenevestigatoriP63220.

Organism-specific databases

HPAiHPA003371.

Interactioni

Protein-protein interaction databases

BioGridi112141. 100 interactions.
IntActiP63220. 5 interactions.
MINTiMINT-4656636.
STRINGi9606.ENSP00000324438.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AV1-83[»]
ProteinModelPortaliP63220.
SMRiP63220. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S21e family.Curated

Phylogenomic databases

eggNOGiNOG301320.
HOGENOMiHOG000183557.
InParanoidiP63220.
KOiK02971.
OMAiIQINIAE.
OrthoDBiEOG7HQNBQ.
PhylomeDBiP63220.
TreeFamiTF300167.

Family and domain databases

InterProiIPR001931. Ribosomal_S21e.
IPR018279. Ribosomal_S21e_CS.
[Graphical view]
PANTHERiPTHR10442. PTHR10442. 1 hit.
PfamiPF01249. Ribosomal_S21e. 1 hit.
[Graphical view]
PIRSFiPIRSF002148. Ribosomal_S21e. 1 hit.
ProDomiPD006584. Ribosomal_S21e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00996. RIBOSOMAL_S21E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63220-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNDAGEFVD LYVPRKCSAS NRIIGAKDHA SIQMNVAEVD KVTGRFNGQF
60 70 80
KTYAICGAIR RMGESDDSIL RLAKADGIVS KNF
Length:83
Mass (Da):9,111
Last modified:September 27, 2004 - v1
Checksum:i6794AC1292A06BD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04483 mRNA. Translation: AAA99893.1.
AJ250907 Genomic DNA. Translation: CAB83213.1.
AB061843 Genomic DNA. Translation: BAB79481.1.
AL121832 Genomic DNA. Translation: CAC21458.1.
AB007157 Genomic DNA. Translation: BAA25821.1.
CCDSiCCDS13497.1.
PIRiS34108.
RefSeqiNP_001015.1. NM_001024.3.
UniGeneiHs.190968.

Genome annotation databases

EnsembliENST00000343986; ENSP00000345957; ENSG00000171858.
GeneIDi6227.
KEGGihsa:6227.
UCSCiuc002ycr.3. human.

Polymorphism databases

DMDMi52783792.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04483 mRNA. Translation: AAA99893.1.
AJ250907 Genomic DNA. Translation: CAB83213.1.
AB061843 Genomic DNA. Translation: BAB79481.1.
AL121832 Genomic DNA. Translation: CAC21458.1.
AB007157 Genomic DNA. Translation: BAA25821.1.
CCDSiCCDS13497.1.
PIRiS34108.
RefSeqiNP_001015.1. NM_001024.3.
UniGeneiHs.190968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AV1-83[»]
ProteinModelPortaliP63220.
SMRiP63220. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112141. 100 interactions.
IntActiP63220. 5 interactions.
MINTiMINT-4656636.
STRINGi9606.ENSP00000324438.

PTM databases

PhosphoSiteiP63220.

Polymorphism databases

DMDMi52783792.

Proteomic databases

MaxQBiP63220.
PaxDbiP63220.
PRIDEiP63220.

Protocols and materials databases

DNASUi6227.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343986; ENSP00000345957; ENSG00000171858.
GeneIDi6227.
KEGGihsa:6227.
UCSCiuc002ycr.3. human.

Organism-specific databases

CTDi6227.
GeneCardsiGC20P060962.
HGNCiHGNC:10409. RPS21.
HPAiHPA003371.
MIMi180477. gene.
neXtProtiNX_P63220.
PharmGKBiPA34812.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG301320.
HOGENOMiHOG000183557.
InParanoidiP63220.
KOiK02971.
OMAiIQINIAE.
OrthoDBiEOG7HQNBQ.
PhylomeDBiP63220.
TreeFamiTF300167.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPS21. human.
GeneWikiiRPS21.
GenomeRNAii6227.
NextBioi24171.
PMAP-CutDBP63220.
PROiP63220.
SOURCEiSearch...

Gene expression databases

BgeeiP63220.
CleanExiHS_RPS21.
ExpressionAtlasiP63220. baseline and differential.
GenevestigatoriP63220.

Family and domain databases

InterProiIPR001931. Ribosomal_S21e.
IPR018279. Ribosomal_S21e_CS.
[Graphical view]
PANTHERiPTHR10442. PTHR10442. 1 hit.
PfamiPF01249. Ribosomal_S21e. 1 hit.
[Graphical view]
PIRSFiPIRSF002148. Ribosomal_S21e. 1 hit.
ProDomiPD006584. Ribosomal_S21e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00996. RIBOSOMAL_S21E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of human ribosomal protein S21."
    Bhat K.S., Morrison S.G.
    Nucleic Acids Res. 21:2939-2939(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and characterization of the human ribosomal protein S21 gene."
    Smirnova E.V., Rakitina T.V., Evtodienko A.Y., Kostanian I.A., Lipkin V.M.
    Bioorg. Khim. 26:392-396(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-74.
  6. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-15, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  7. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
    Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
    Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 42-47.
    Tissue: Placenta.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS21_HUMAN
AccessioniPrimary (citable) accession number: P63220
Secondary accession number(s): P35265
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: March 4, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.