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P46781

- RS9_HUMAN

UniProt

P46781 - RS9_HUMAN

Protein

40S ribosomal protein S9

Gene

RPS9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. rRNA binding Source: UniProtKB-KW
    4. structural constituent of ribosome Source: InterPro
    5. translation regulator activity Source: UniProtKB

    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. positive regulation of cell proliferation Source: UniProtKB
    6. regulation of translation Source: GOC
    7. RNA metabolic process Source: Reactome
    8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    9. translation Source: UniProtKB
    10. translational elongation Source: Reactome
    11. translational initiation Source: Reactome
    12. translational termination Source: Reactome
    13. viral life cycle Source: Reactome
    14. viral process Source: Reactome
    15. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    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 S9
    Gene namesi
    Name:RPS9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10442. RPS9.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. cytosolic small ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. nucleolus Source: UniProtKB
    7. nucleus Source: UniProt
    8. ribonucleoprotein complex Source: UniProtKB
    9. ribosome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34857.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 19419340S ribosomal protein S9PRO_0000132689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysineBy similarity
    Modified residuei116 – 1161N6-acetyllysineBy similarity
    Modified residuei155 – 1551N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP46781.
    PaxDbiP46781.
    PeptideAtlasiP46781.
    PRIDEiP46781.

    PTM databases

    PhosphoSiteiP46781.

    Expressioni

    Gene expression databases

    ArrayExpressiP46781.
    BgeeiP46781.
    CleanExiHS_RPS9.
    GenevestigatoriP46781.

    Organism-specific databases

    HPAiHPA048746.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAT3P407632EBI-351206,EBI-518675

    Protein-protein interaction databases

    BioGridi112117. 108 interactions.
    IntActiP46781. 46 interactions.
    MINTiMINT-5001013.
    STRINGi9606.ENSP00000302896.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00J1-194[»]
    ProteinModelPortaliP46781.
    SMRiP46781. Positions 7-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini108 – 18275S4 RNA-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein S4P family.Curated
    Contains 1 S4 RNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0522.
    HOGENOMiHOG000194525.
    HOVERGENiHBG001135.
    InParanoidiP46781.
    KOiK02997.
    OMAiVXSLERR.
    PhylomeDBiP46781.
    TreeFamiTF300795.

    Family and domain databases

    Gene3Di3.10.290.10. 1 hit.
    InterProiIPR022801. Ribosomal_S4/S9.
    IPR005710. Ribosomal_S4/S9_euk/arc.
    IPR001912. Ribosomal_S4/S9_N.
    IPR018079. Ribosomal_S4_CS.
    IPR002942. S4_RNA-bd.
    [Graphical view]
    PANTHERiPTHR11831. PTHR11831. 1 hit.
    PfamiPF00163. Ribosomal_S4. 1 hit.
    PF01479. S4. 1 hit.
    [Graphical view]
    SMARTiSM00363. S4. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01018. rpsD_arch. 1 hit.
    PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
    PS50889. S4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P46781-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL    50
    AKIRKAAREL LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL 100
    KIEDFLERRL QTQVFKLGLA KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR 150
    LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK GQGGAGAGDD EEED 194
    Length:194
    Mass (Da):22,591
    Last modified:January 23, 2007 - v3
    Checksum:iE9CE3CBD59524F81
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841I → L in AAA85659. (PubMed:7772601)Curated
    Sequence conflicti165 – 1673YGG → TGV in AAA85659. (PubMed:7772601)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251L → F.
    Corresponds to variant rs41423149 [ dbSNP | Ensembl ].
    VAR_052069
    Natural varianti137 – 1371V → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036543

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14971 mRNA. Translation: AAA85659.1.
    AB061839 Genomic DNA. Translation: BAB79477.1.
    CU457734 Genomic DNA. Translation: CAP19125.1.
    CU151838 Genomic DNA. Translation: CAQ09597.1.
    CH471135 Genomic DNA. Translation: EAW72209.1.
    BC000802 mRNA. Translation: AAH00802.1.
    BC007410 mRNA. Translation: AAH07410.1.
    BC007434 mRNA. Translation: AAH07434.1.
    BC007857 mRNA. Translation: AAH07857.1.
    BC068055 mRNA. Translation: AAH68055.1.
    BC071940 mRNA. Translation: AAH71940.1.
    BC096756 mRNA. Translation: AAH96756.1.
    AB007150 Genomic DNA. Translation: BAA25816.1.
    CCDSiCCDS12884.1.
    PIRiS55917.
    RefSeqiNP_001004.2. NM_001013.3.
    XP_005259192.1. XM_005259135.1.
    XP_005259193.1. XM_005259136.2.
    XP_005277141.1. XM_005277084.2.
    XP_005277142.1. XM_005277085.1.
    XP_005277331.1. XM_005277274.1.
    XP_005277372.1. XM_005277315.1.
    XP_005277373.1. XM_005277316.2.
    XP_005278344.1. XM_005278287.2.
    XP_005278345.1. XM_005278288.1.
    XP_006725939.1. XM_006725876.1.
    XP_006725940.1. XM_006725877.1.
    XP_006726027.1. XM_006725964.1.
    XP_006726028.1. XM_006725965.1.
    XP_006726126.1. XM_006726063.1.
    XP_006726127.1. XM_006726064.1.
    XP_006726227.1. XM_006726164.1.
    XP_006726228.1. XM_006726165.1.
    XP_006726264.1. XM_006726201.1.
    XP_006726265.1. XM_006726202.1.
    UniGeneiHs.467284.
    Hs.546288.

    Genome annotation databases

    EnsembliENST00000302907; ENSP00000302896; ENSG00000170889.
    ENST00000391752; ENSP00000375632; ENSG00000170889.
    ENST00000391753; ENSP00000375633; ENSG00000170889.
    GeneIDi6203.
    KEGGihsa:6203.
    UCSCiuc002qdx.3. human.

    Polymorphism databases

    DMDMi20178311.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14971 mRNA. Translation: AAA85659.1 .
    AB061839 Genomic DNA. Translation: BAB79477.1 .
    CU457734 Genomic DNA. Translation: CAP19125.1 .
    CU151838 Genomic DNA. Translation: CAQ09597.1 .
    CH471135 Genomic DNA. Translation: EAW72209.1 .
    BC000802 mRNA. Translation: AAH00802.1 .
    BC007410 mRNA. Translation: AAH07410.1 .
    BC007434 mRNA. Translation: AAH07434.1 .
    BC007857 mRNA. Translation: AAH07857.1 .
    BC068055 mRNA. Translation: AAH68055.1 .
    BC071940 mRNA. Translation: AAH71940.1 .
    BC096756 mRNA. Translation: AAH96756.1 .
    AB007150 Genomic DNA. Translation: BAA25816.1 .
    CCDSi CCDS12884.1.
    PIRi S55917.
    RefSeqi NP_001004.2. NM_001013.3.
    XP_005259192.1. XM_005259135.1.
    XP_005259193.1. XM_005259136.2.
    XP_005277141.1. XM_005277084.2.
    XP_005277142.1. XM_005277085.1.
    XP_005277331.1. XM_005277274.1.
    XP_005277372.1. XM_005277315.1.
    XP_005277373.1. XM_005277316.2.
    XP_005278344.1. XM_005278287.2.
    XP_005278345.1. XM_005278288.1.
    XP_006725939.1. XM_006725876.1.
    XP_006725940.1. XM_006725877.1.
    XP_006726027.1. XM_006725964.1.
    XP_006726028.1. XM_006725965.1.
    XP_006726126.1. XM_006726063.1.
    XP_006726127.1. XM_006726064.1.
    XP_006726227.1. XM_006726164.1.
    XP_006726228.1. XM_006726165.1.
    XP_006726264.1. XM_006726201.1.
    XP_006726265.1. XM_006726202.1.
    UniGenei Hs.467284.
    Hs.546288.

    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 J 1-194 [» ]
    ProteinModelPortali P46781.
    SMRi P46781. Positions 7-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112117. 108 interactions.
    IntActi P46781. 46 interactions.
    MINTi MINT-5001013.
    STRINGi 9606.ENSP00000302896.

    PTM databases

    PhosphoSitei P46781.

    Polymorphism databases

    DMDMi 20178311.

    Proteomic databases

    MaxQBi P46781.
    PaxDbi P46781.
    PeptideAtlasi P46781.
    PRIDEi P46781.

    Protocols and materials databases

    DNASUi 6203.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302907 ; ENSP00000302896 ; ENSG00000170889 .
    ENST00000391752 ; ENSP00000375632 ; ENSG00000170889 .
    ENST00000391753 ; ENSP00000375633 ; ENSG00000170889 .
    GeneIDi 6203.
    KEGGi hsa:6203.
    UCSCi uc002qdx.3. human.

    Organism-specific databases

    CTDi 6203.
    GeneCardsi GC19P054851.
    HGNCi HGNC:10442. RPS9.
    HPAi HPA048746.
    MIMi 603631. gene.
    neXtProti NX_P46781.
    PharmGKBi PA34857.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0522.
    HOGENOMi HOG000194525.
    HOVERGENi HBG001135.
    InParanoidi P46781.
    KOi K02997.
    OMAi VXSLERR.
    PhylomeDBi P46781.
    TreeFami TF300795.

    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 RPS9. human.
    GeneWikii RPS9.
    GenomeRNAii 6203.
    NextBioi 24091.
    PROi P46781.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46781.
    Bgeei P46781.
    CleanExi HS_RPS9.
    Genevestigatori P46781.

    Family and domain databases

    Gene3Di 3.10.290.10. 1 hit.
    InterProi IPR022801. Ribosomal_S4/S9.
    IPR005710. Ribosomal_S4/S9_euk/arc.
    IPR001912. Ribosomal_S4/S9_N.
    IPR018079. Ribosomal_S4_CS.
    IPR002942. S4_RNA-bd.
    [Graphical view ]
    PANTHERi PTHR11831. PTHR11831. 1 hit.
    Pfami PF00163. Ribosomal_S4. 1 hit.
    PF01479. S4. 1 hit.
    [Graphical view ]
    SMARTi SM00363. S4. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01018. rpsD_arch. 1 hit.
    PROSITEi PS00632. RIBOSOMAL_S4. 1 hit.
    PS50889. S4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
      Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
      Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon.
    2. "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].
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain, Muscle, Placenta and Skin.
    6. "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 2-19.
      Tissue: Placenta.
    7. "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 10-73.
    8. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-137.

    Entry informationi

    Entry nameiRS9_HUMAN
    AccessioniPrimary (citable) accession number: P46781
    Secondary accession number(s): A9C4C1, Q4QRK7, Q9BVZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Ribosomal proteins
      Ribosomal proteins families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3