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P83731

- RL24_HUMAN

UniProt

P83731 - RL24_HUMAN

Protein

60S ribosomal protein L24

Gene

RPL24

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. RNA binding Source: ProtInc
    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 L24
    Alternative name(s):
    60S ribosomal protein L30
    Gene namesi
    Name:RPL24
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10325. RPL24.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34701.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15715760S ribosomal protein L24PRO_0000136867Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271N6-acetyllysine1 Publication
    Modified residuei77 – 771N6-acetyllysine1 Publication
    Modified residuei83 – 831Phosphothreonine2 Publications
    Modified residuei86 – 861Phosphoserine2 Publications
    Modified residuei93 – 931N6-acetyllysine1 Publication
    Modified residuei131 – 1311N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP83731.
    PaxDbiP83731.
    PRIDEiP83731.

    PTM databases

    PhosphoSiteiP83731.

    Expressioni

    Gene expression databases

    BgeeiP83731.
    CleanExiHS_RPL24.
    GenevestigatoriP83731.

    Organism-specific databases

    HPAiHPA051653.

    Interactioni

    Protein-protein interaction databases

    BioGridi112071. 115 interactions.
    IntActiP83731. 25 interactions.
    MINTiMINT-5000278.
    STRINGi9606.ENSP00000377640.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00W1-157[»]
    ProteinModelPortaliP83731.
    SMRiP83731. Positions 1-107.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L24e family.Curated

    Phylogenomic databases

    eggNOGiCOG2075.
    HOGENOMiHOG000184343.
    HOVERGENiHBG001066.
    InParanoidiP83731.
    KOiK02896.
    OMAiNQTEDFR.
    OrthoDBiEOG77HDH1.
    PhylomeDBiP83731.
    TreeFamiTF312933.

    Family and domain databases

    Gene3Di2.30.170.20. 1 hit.
    InterProiIPR023442. Ribosomal_L24e_CS.
    IPR023441. Ribosomal_L24e_dom.
    IPR000988. Ribosomal_L24e_rel.
    IPR011017. TRASH_dom.
    [Graphical view]
    PANTHERiPTHR10792. PTHR10792. 1 hit.
    PfamiPF01246. Ribosomal_L24e. 1 hit.
    [Graphical view]
    SMARTiSM00746. TRASH. 1 hit.
    [Graphical view]
    PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P83731-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN    50
    WTVLYRRKHK KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV 100
    RKAQREQAIR AAKEAKKAKQ ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA 150
    PRVGGKR 157
    Length:157
    Mass (Da):17,779
    Last modified:January 16, 2004 - v1
    Checksum:i1D48EEB7C0652574
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94314 mRNA. Translation: AAC28251.1.
    AB061828 Genomic DNA. Translation: BAB79466.1.
    CR456729 mRNA. Translation: CAG33010.1.
    AK311992 mRNA. Translation: BAG34930.1.
    CH471052 Genomic DNA. Translation: EAW79780.1.
    BC000690 mRNA. Translation: AAH00690.1.
    BC070193 mRNA. Translation: AAH70193.1.
    AB007177 Genomic DNA. Translation: BAA25836.1.
    CCDSiCCDS33809.1.
    PIRiJN0549.
    RefSeqiNP_000977.1. NM_000986.3.
    UniGeneiHs.477028.
    Hs.649475.

    Genome annotation databases

    EnsembliENST00000394077; ENSP00000377640; ENSG00000114391.
    GeneIDi6152.
    KEGGihsa:6152.
    UCSCiuc003dvh.1. human.

    Polymorphism databases

    DMDMi41393532.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94314 mRNA. Translation: AAC28251.1 .
    AB061828 Genomic DNA. Translation: BAB79466.1 .
    CR456729 mRNA. Translation: CAG33010.1 .
    AK311992 mRNA. Translation: BAG34930.1 .
    CH471052 Genomic DNA. Translation: EAW79780.1 .
    BC000690 mRNA. Translation: AAH00690.1 .
    BC070193 mRNA. Translation: AAH70193.1 .
    AB007177 Genomic DNA. Translation: BAA25836.1 .
    CCDSi CCDS33809.1.
    PIRi JN0549.
    RefSeqi NP_000977.1. NM_000986.3.
    UniGenei Hs.477028.
    Hs.649475.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3B electron microscopy 5.00 W 1-157 [» ]
    ProteinModelPortali P83731.
    SMRi P83731. Positions 1-107.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112071. 115 interactions.
    IntActi P83731. 25 interactions.
    MINTi MINT-5000278.
    STRINGi 9606.ENSP00000377640.

    PTM databases

    PhosphoSitei P83731.

    Polymorphism databases

    DMDMi 41393532.

    Proteomic databases

    MaxQBi P83731.
    PaxDbi P83731.
    PRIDEi P83731.

    Protocols and materials databases

    DNASUi 6152.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394077 ; ENSP00000377640 ; ENSG00000114391 .
    GeneIDi 6152.
    KEGGi hsa:6152.
    UCSCi uc003dvh.1. human.

    Organism-specific databases

    CTDi 6152.
    GeneCardsi GC03M101399.
    HGNCi HGNC:10325. RPL24.
    HPAi HPA051653.
    MIMi 604180. gene.
    neXtProti NX_P83731.
    PharmGKBi PA34701.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2075.
    HOGENOMi HOG000184343.
    HOVERGENi HBG001066.
    InParanoidi P83731.
    KOi K02896.
    OMAi NQTEDFR.
    OrthoDBi EOG77HDH1.
    PhylomeDBi P83731.
    TreeFami TF312933.

    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

    ChiTaRSi RPL24. human.
    GeneWikii RPL24.
    GenomeRNAii 6152.
    NextBioi 23893.
    PROi P83731.
    SOURCEi Search...

    Gene expression databases

    Bgeei P83731.
    CleanExi HS_RPL24.
    Genevestigatori P83731.

    Family and domain databases

    Gene3Di 2.30.170.20. 1 hit.
    InterProi IPR023442. Ribosomal_L24e_CS.
    IPR023441. Ribosomal_L24e_dom.
    IPR000988. Ribosomal_L24e_rel.
    IPR011017. TRASH_dom.
    [Graphical view ]
    PANTHERi PTHR10792. PTHR10792. 1 hit.
    Pfami PF01246. Ribosomal_L24e. 1 hit.
    [Graphical view ]
    SMARTi SM00746. TRASH. 1 hit.
    [Graphical view ]
    PROSITEi PS01073. RIBOSOMAL_L24E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones encoding the human homologue of Saccharomyces cerevisiae ribosomal protein L30."
      Johnson K.R.
      Gene 123:283-285(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. "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].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Colon.
    7. Bienvenut W.V., Bilsland A.E., Keith W.N.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-12; 28-44; 48-56 AND 81-93, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    8. "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 132-157.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-27; LYS-77 AND LYS-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL24_HUMAN
    AccessioniPrimary (citable) accession number: P83731
    Secondary accession number(s): B2R4Y3, P38663, Q6IBS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 113 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 3
      Human chromosome 3: 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