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P62266

- RS23_HUMAN

UniProt

P62266 - RS23_HUMAN

Protein

40S ribosomal protein S23

Gene

RPS23

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 binding Source: IntAct
    3. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. RNA metabolic process Source: Reactome
    6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    7. translation Source: UniProtKB
    8. translational elongation Source: Reactome
    9. translational initiation Source: Reactome
    10. translational termination Source: Reactome
    11. viral life cycle Source: Reactome
    12. viral process Source: Reactome
    13. 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 S23
    Gene namesi
    Name:RPS23
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:10410. RPS23.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic small ribosomal subunit Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nucleolus Source: HPA
    6. ribosome Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34813.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 14314240S ribosomal protein S23PRO_0000146457Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541N6-succinyllysineBy similarity
    Modified residuei62 – 6213-hydroxyproline2 Publications
    Modified residuei135 – 1351N6-acetyllysine1 Publication

    Post-translational modificationi

    Hydroxylation at Pro-62 affects translation termination efficiency.2 Publications

    Keywords - PTMi

    Acetylation, Hydroxylation

    Proteomic databases

    MaxQBiP62266.
    PaxDbiP62266.
    PRIDEiP62266.

    PTM databases

    PhosphoSiteiP62266.

    Expressioni

    Gene expression databases

    ArrayExpressiP62266.
    BgeeiP62266.
    CleanExiHS_RPS23.
    GenevestigatoriP62266.

    Organism-specific databases

    HPAiHPA054853.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCCP431462EBI-353072,EBI-1222919
    LRRK2Q5S0072EBI-353072,EBI-5323863

    Protein-protein interaction databases

    BioGridi112142. 129 interactions.
    IntActiP62266. 22 interactions.
    MINTiMINT-5000369.
    STRINGi9606.ENSP00000296674.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00X1-143[»]
    ProteinModelPortaliP62266.
    SMRiP62266. Positions 1-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S12P family.Curated

    Phylogenomic databases

    eggNOGiCOG0048.
    HOGENOMiHOG000040064.
    HOVERGENiHBG054200.
    InParanoidiP62266.
    KOiK02973.
    OMAiWHDKDYK.
    OrthoDBiEOG77DJ7H.
    PhylomeDBiP62266.
    TreeFamiTF300871.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR006032. Ribosomal_S12/S23.
    IPR005680. Ribosomal_S23_euk/arc.
    [Graphical view]
    PANTHERiPTHR11652. PTHR11652. 1 hit.
    PfamiPF00164. Ribosom_S12_S23. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00982. S23_S12_E_A. 1 hit.
    PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P62266-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI    50
    VLEKVGVEAK QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV 100
    LVAGFGRKGH AVGDIPGVRF KVVKVANVSL LALYKGKKER PRS 143
    Length:143
    Mass (Da):15,808
    Last modified:January 23, 2007 - v3
    Checksum:i8417A48B8CF0A8E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14530 mRNA. Translation: BAA03400.1.
    CR456996 mRNA. Translation: CAG33277.1.
    BC070221 mRNA. Translation: AAH70221.1.
    AB007158 Genomic DNA. Translation: BAA25822.1.
    CCDSiCCDS47241.1.
    PIRiS42105.
    RefSeqiNP_001016.1. NM_001025.4.
    UniGeneiHs.527193.

    Genome annotation databases

    EnsembliENST00000296674; ENSP00000296674; ENSG00000186468.
    GeneIDi6228.
    KEGGihsa:6228.
    UCSCiuc003khu.3. human.

    Polymorphism databases

    DMDMi50403755.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14530 mRNA. Translation: BAA03400.1 .
    CR456996 mRNA. Translation: CAG33277.1 .
    BC070221 mRNA. Translation: AAH70221.1 .
    AB007158 Genomic DNA. Translation: BAA25822.1 .
    CCDSi CCDS47241.1.
    PIRi S42105.
    RefSeqi NP_001016.1. NM_001025.4.
    UniGenei Hs.527193.

    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 X 1-143 [» ]
    ProteinModelPortali P62266.
    SMRi P62266. Positions 1-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112142. 129 interactions.
    IntActi P62266. 22 interactions.
    MINTi MINT-5000369.
    STRINGi 9606.ENSP00000296674.

    PTM databases

    PhosphoSitei P62266.

    Polymorphism databases

    DMDMi 50403755.

    Proteomic databases

    MaxQBi P62266.
    PaxDbi P62266.
    PRIDEi P62266.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296674 ; ENSP00000296674 ; ENSG00000186468 .
    GeneIDi 6228.
    KEGGi hsa:6228.
    UCSCi uc003khu.3. human.

    Organism-specific databases

    CTDi 6228.
    GeneCardsi GC05M081569.
    HGNCi HGNC:10410. RPS23.
    HPAi HPA054853.
    MIMi 603683. gene.
    neXtProti NX_P62266.
    PharmGKBi PA34813.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0048.
    HOGENOMi HOG000040064.
    HOVERGENi HBG054200.
    InParanoidi P62266.
    KOi K02973.
    OMAi WHDKDYK.
    OrthoDBi EOG77DJ7H.
    PhylomeDBi P62266.
    TreeFami TF300871.

    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 RPS23. human.
    GeneWikii RPS23.
    GenomeRNAii 6228.
    NextBioi 24175.
    PROi P62266.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62266.
    Bgeei P62266.
    CleanExi HS_RPS23.
    Genevestigatori P62266.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR006032. Ribosomal_S12/S23.
    IPR005680. Ribosomal_S23_euk/arc.
    [Graphical view ]
    PANTHERi PTHR11652. PTHR11652. 1 hit.
    Pfami PF00164. Ribosom_S12_S23. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002133. Ribosomal_S12/S23. 1 hit.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00982. S23_S12_E_A. 1 hit.
    PROSITEi PS00055. RIBOSOMAL_S12. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cDNA sequence of human ribosomal protein, homologue of yeast S28."
      Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.
      Nucleic Acids Res. 21:4394-4394(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    4. "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 2-10.
      Tissue: Placenta.
    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 84-142.
    6. "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-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
    9. Cited for: HYDROXYLATION AT PRO-62.
    10. Cited for: HYDROXYLATION AT PRO-62.

    Entry informationi

    Entry nameiRS23_HUMAN
    AccessioniPrimary (citable) accession number: P62266
    Secondary accession number(s): P39028, Q6IB08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 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 5
      Human chromosome 5: 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