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P32969

- RL9_HUMAN

UniProt

P32969 - RL9_HUMAN

Protein

60S ribosomal protein L9

Gene

RPL9

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. RNA binding Source: ProtInc
    2. rRNA binding Source: InterPro
    3. structural constituent of ribosome 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. 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_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    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_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S ribosomal protein L9
    Gene namesi
    Name:RPL9
    ORF Names:OK/SW-cl.103
    AND
    Name:RPL9P7
    AND
    Name:RPL9P8
    AND
    Name:RPL9P9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:10369. RPL9.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic large ribosomal subunit Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nucleolus Source: HPA
    6. nucleus Source: UniProt
    7. ribosome Source: ProtInc

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34769.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19219260S ribosomal protein L9PRO_0000131097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei121 – 1211N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP32969.
    PaxDbiP32969.
    PeptideAtlasiP32969.
    PRIDEiP32969.

    2D gel databases

    SWISS-2DPAGEP32969.

    PTM databases

    PhosphoSiteiP32969.

    Expressioni

    Gene expression databases

    BgeeiP32969.
    CleanExiHS_RPL9.
    GenevestigatoriP32969.

    Organism-specific databases

    HPAiHPA003372.

    Interactioni

    Protein-protein interaction databases

    BioGridi112053. 102 interactions.
    IntActiP32969. 18 interactions.
    MINTiMINT-5000985.
    STRINGi9606.ENSP00000346022.

    Structurei

    Secondary structure

    1
    192
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Beta strandi17 – 215
    Beta strandi24 – 296
    Beta strandi32 – 376
    Beta strandi44 – 485
    Beta strandi50 – 523
    Beta strandi54 – 585
    Beta strandi61 – 633
    Helixi65 – 8521

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQLNMR-A1-87[»]
    3J3Belectron microscopy5.00H1-192[»]
    ProteinModelPortaliP32969.
    SMRiP32969. Positions 1-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32969.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L6P family.Curated

    Phylogenomic databases

    eggNOGiCOG0097.
    HOGENOMiHOG000039905.
    HOVERGENiHBG000942.
    InParanoidiP32969.
    KOiK02940.
    OMAiEFVGQTA.
    OrthoDBiEOG7353Z4.
    PhylomeDBiP32969.
    TreeFamiTF300033.

    Family and domain databases

    Gene3Di3.90.930.12. 2 hits.
    InterProiIPR000702. Ribosomal_L6.
    IPR020040. Ribosomal_L6_a/b-dom.
    IPR002359. Ribosomal_L6_CS2.
    [Graphical view]
    PANTHERiPTHR11655. PTHR11655. 1 hit.
    PfamiPF00347. Ribosomal_L6. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
    SUPFAMiSSF56053. SSF56053. 2 hits.
    PROSITEiPS00700. RIBOSOMAL_L6_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32969-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTILSNQTV DIPENVDITL KGRTVIVKGP RGTLRRDFNH INVELSLLGK    50
    KKKRLRVDKW WGNRKELATV RTICSHVQNM IKGVTLGFRY KMRSVYAHFP 100
    INVVIQENGS LVEIRNFLGE KYIRRVRMRP GVACSVSQAQ KDELILEGND 150
    IELVSNSAAL IQQATTVKNK DIRKFLDGIY VSEKGTVQQA DE 192
    Length:192
    Mass (Da):21,863
    Last modified:October 1, 1993 - v1
    Checksum:i0249E6CA12F77934
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111D → E in AAB01040. (PubMed:8597601)Curated
    Sequence conflicti11 – 111D → E in AAB01041. (PubMed:8597601)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14531 mRNA. Translation: BAA03401.1.
    U09953 mRNA. Translation: AAB01040.1.
    U09954 Genomic DNA. Translation: AAB01041.1.
    U21138 mRNA. Translation: AAA63752.1.
    AB062431 mRNA. Translation: BAB93494.1.
    BC000483 mRNA. Translation: AAH00483.1.
    BC004156 mRNA. Translation: AAH04156.1.
    BC004206 mRNA. Translation: AAH04206.1.
    BC007967 mRNA. Translation: AAH07967.1.
    BC012149 mRNA. Translation: AAH12149.1.
    BC031906 mRNA. Translation: AAH31906.1.
    BC066318 mRNA. Translation: AAH66318.1.
    BC070214 mRNA. Translation: AAH70214.1.
    AB007169 Genomic DNA. Translation: BAA25830.1.
    CCDSiCCDS3452.1.
    PIRiS65792.
    RefSeqiNP_000652.2. NM_000661.4.
    NP_001020092.1. NM_001024921.2.
    XP_005262718.1. XM_005262661.1.
    UniGeneiHs.412370.
    Hs.513083.
    Hs.730597.

    Genome annotation databases

    EnsembliENST00000295955; ENSP00000346022; ENSG00000163682.
    ENST00000449470; ENSP00000400467; ENSG00000163682.
    GeneIDi6133.
    KEGGihsa:6133.
    UCSCiuc003gub.3. human.

    Polymorphism databases

    DMDMi417677.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14531 mRNA. Translation: BAA03401.1 .
    U09953 mRNA. Translation: AAB01040.1 .
    U09954 Genomic DNA. Translation: AAB01041.1 .
    U21138 mRNA. Translation: AAA63752.1 .
    AB062431 mRNA. Translation: BAB93494.1 .
    BC000483 mRNA. Translation: AAH00483.1 .
    BC004156 mRNA. Translation: AAH04156.1 .
    BC004206 mRNA. Translation: AAH04206.1 .
    BC007967 mRNA. Translation: AAH07967.1 .
    BC012149 mRNA. Translation: AAH12149.1 .
    BC031906 mRNA. Translation: AAH31906.1 .
    BC066318 mRNA. Translation: AAH66318.1 .
    BC070214 mRNA. Translation: AAH70214.1 .
    AB007169 Genomic DNA. Translation: BAA25830.1 .
    CCDSi CCDS3452.1.
    PIRi S65792.
    RefSeqi NP_000652.2. NM_000661.4.
    NP_001020092.1. NM_001024921.2.
    XP_005262718.1. XM_005262661.1.
    UniGenei Hs.412370.
    Hs.513083.
    Hs.730597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQL NMR - A 1-87 [» ]
    3J3B electron microscopy 5.00 H 1-192 [» ]
    ProteinModelPortali P32969.
    SMRi P32969. Positions 1-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112053. 102 interactions.
    IntActi P32969. 18 interactions.
    MINTi MINT-5000985.
    STRINGi 9606.ENSP00000346022.

    PTM databases

    PhosphoSitei P32969.

    Polymorphism databases

    DMDMi 417677.

    2D gel databases

    SWISS-2DPAGE P32969.

    Proteomic databases

    MaxQBi P32969.
    PaxDbi P32969.
    PeptideAtlasi P32969.
    PRIDEi P32969.

    Protocols and materials databases

    DNASUi 6133.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295955 ; ENSP00000346022 ; ENSG00000163682 .
    ENST00000449470 ; ENSP00000400467 ; ENSG00000163682 .
    GeneIDi 6133.
    KEGGi hsa:6133.
    UCSCi uc003gub.3. human.

    Organism-specific databases

    CTDi 6133.
    HGNCi HGNC:10369. RPL9.
    HPAi HPA003372.
    MIMi 603686. gene.
    neXtProti NX_P32969.
    PharmGKBi PA34769.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0097.
    HOGENOMi HOG000039905.
    HOVERGENi HBG000942.
    InParanoidi P32969.
    KOi K02940.
    OMAi EFVGQTA.
    OrthoDBi EOG7353Z4.
    PhylomeDBi P32969.
    TreeFami TF300033.

    Enzyme and pathway databases

    Reactomei 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_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_9491. Viral mRNA Translation.

    Miscellaneous databases

    EvolutionaryTracei P32969.
    GeneWikii RPL9.
    GenomeRNAii 6133.
    NextBioi 23821.
    PROi P32969.
    SOURCEi Search...

    Gene expression databases

    Bgeei P32969.
    CleanExi HS_RPL9.
    Genevestigatori P32969.

    Family and domain databases

    Gene3Di 3.90.930.12. 2 hits.
    InterProi IPR000702. Ribosomal_L6.
    IPR020040. Ribosomal_L6_a/b-dom.
    IPR002359. Ribosomal_L6_CS2.
    [Graphical view ]
    PANTHERi PTHR11655. PTHR11655. 1 hit.
    Pfami PF00347. Ribosomal_L6. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002162. Ribosomal_L6. 1 hit.
    SUPFAMi SSF56053. SSF56053. 2 hits.
    PROSITEi PS00700. RIBOSOMAL_L6_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new human ribosomal protein sequence, homologue of rat L9."
      Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.
      Nucleic Acids Res. 21:4395-4395(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural organization and chromosomal localization of the human ribosomal protein L9 gene."
      Mazuruk K., Schoen T.J., Chader G.J., Iwata T., Rodriguez I.R.
      Biochim. Biophys. Acta 1305:151-162(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Retina.
    3. "Human homolog of rat ribosomal protein L9."
      Williams J.H., Pearse M.J., Power D.A.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon adenocarcinoma.
    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 Uterus.
    6. Bienvenut W.V., Bilsland A.E., Keith W.N.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-21; 36-51; 94-115; 142-168 AND 174-184, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    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 146-192.
    8. "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-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the N-terminal domain of human ribosomal protein L9."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-87.
    12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL9_HUMAN
    AccessioniPrimary (citable) accession number: P32969
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 153 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 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    3. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    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