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P63220

- RS21_HUMAN

UniProt

P63220 - RS21_HUMAN

Protein

40S ribosomal protein S21

Gene

RPS21

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

    GO - Molecular functioni

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

    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: RefGenome
    3. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: RefGenome
    4. gene expression Source: Reactome
    5. mRNA metabolic process Source: Reactome
    6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    7. ribosomal small subunit biogenesis Source: RefGenome
    8. RNA metabolic process Source: Reactome
    9. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    10. translation Source: UniProtKB
    11. translational elongation Source: Reactome
    12. translational initiation Source: Reactome
    13. translational termination Source: Reactome
    14. viral life cycle Source: Reactome
    15. viral process Source: Reactome
    16. viral transcription Source: Reactome

    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

    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

    ArrayExpressiP63220.
    BgeeiP63220.
    CleanExiHS_RPS21.
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00V1-83[»]
    ProteinModelPortaliP63220.
    SMRiP63220. Positions 1-82.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S21e family.Curated

    Phylogenomic databases

    eggNOGiNOG301320.
    HOGENOMiHOG000183557.
    KOiK02971.
    OMAiGISSAKQ.
    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

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13497.1.
    PIRi S34108.
    RefSeqi NP_001015.1. NM_001024.3.
    UniGenei Hs.190968.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3A electron microscopy 5.00 V 1-83 [» ]
    ProteinModelPortali P63220.
    SMRi P63220. Positions 1-82.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112141. 100 interactions.
    IntActi P63220. 5 interactions.
    MINTi MINT-4656636.
    STRINGi 9606.ENSP00000324438.

    PTM databases

    PhosphoSitei P63220.

    Polymorphism databases

    DMDMi 52783792.

    Proteomic databases

    MaxQBi P63220.
    PaxDbi P63220.
    PRIDEi P63220.

    Protocols and materials databases

    DNASUi 6227.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343986 ; ENSP00000345957 ; ENSG00000171858 .
    GeneIDi 6227.
    KEGGi hsa:6227.
    UCSCi uc002ycr.3. human.

    Organism-specific databases

    CTDi 6227.
    GeneCardsi GC20P060962.
    HGNCi HGNC:10409. RPS21.
    HPAi HPA003371.
    MIMi 180477. gene.
    neXtProti NX_P63220.
    PharmGKBi PA34812.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301320.
    HOGENOMi HOG000183557.
    KOi K02971.
    OMAi GISSAKQ.
    OrthoDBi EOG7HQNBQ.
    PhylomeDBi P63220.
    TreeFami TF300167.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi RpS21. human.
    GeneWikii RPS21.
    GenomeRNAii 6227.
    NextBioi 24171.
    PMAP-CutDB P63220.
    PROi P63220.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63220.
    Bgeei P63220.
    CleanExi HS_RPS21.
    Genevestigatori P63220.

    Family and domain databases

    InterProi IPR001931. Ribosomal_S21e.
    IPR018279. Ribosomal_S21e_CS.
    [Graphical view ]
    PANTHERi PTHR10442. PTHR10442. 1 hit.
    Pfami PF01249. Ribosomal_S21e. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002148. Ribosomal_S21e. 1 hit.
    ProDomi PD006584. Ribosomal_S21e. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    PROSITEi PS00996. RIBOSOMAL_S21E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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: October 1, 2014
    This is version 97 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