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P62277

- RS13_HUMAN

UniProt

P62277 - RS13_HUMAN

Protein

40S ribosomal protein S13

Gene

RPS13

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

    GO - Molecular functioni

    1. mRNA binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. 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. negative regulation of RNA splicing Source: UniProtKB
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    8. translation Source: UniProtKB
    9. translational elongation Source: Reactome
    10. translational initiation Source: Reactome
    11. translational termination Source: Reactome
    12. viral life cycle Source: Reactome
    13. viral process Source: Reactome
    14. 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 S13
    Gene namesi
    Name:RPS13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10386. RPS13.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34785.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 15115040S ribosomal protein S13PRO_0000115661Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271N6-acetyllysine; alternate1 Publication
    Modified residuei27 – 271N6-succinyllysine; alternateBy similarity
    Modified residuei34 – 341N6-succinyllysineBy similarity
    Modified residuei38 – 381Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62277.
    PaxDbiP62277.
    PeptideAtlasiP62277.
    PRIDEiP62277.

    PTM databases

    PhosphoSiteiP62277.

    Expressioni

    Gene expression databases

    ArrayExpressiP62277.
    BgeeiP62277.
    CleanExiHS_RPS13.
    GenevestigatoriP62277.

    Organism-specific databases

    HPAiHPA005985.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDCD4Q53EL62EBI-351850,EBI-935824

    Protein-protein interaction databases

    BioGridi112121. 137 interactions.
    IntActiP62277. 27 interactions.
    MINTiMINT-4999984.
    STRINGi9606.ENSP00000228140.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00N1-151[»]
    ProteinModelPortaliP62277.
    SMRiP62277. Positions 2-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S15P family.Curated

    Phylogenomic databases

    eggNOGiCOG0184.
    HOGENOMiHOG000180723.
    HOVERGENiHBG000938.
    InParanoidiP62277.
    KOiK02953.
    OMAiNWKYESA.
    PhylomeDBiP62277.
    TreeFamiTF300190.

    Family and domain databases

    HAMAPiMF_01343_A. Ribosomal_S15_A.
    InterProiIPR012606. Ribosomal_S13/S15_N.
    IPR000589. Ribosomal_S15.
    IPR023029. Ribosomal_S15P.
    IPR009068. S15_NS1_RNA-bd.
    [Graphical view]
    PfamiPF08069. Ribosomal_S13_N. 1 hit.
    PF00312. Ribosomal_S15. 1 hit.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 1 hit.
    PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62277-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI    50
    GVILRDSHGV AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK 100
    HLERNRKDKD AKFRLILIES RIHRLARYYK TKRVLPPNWK YESSTASALV 150
    A 151
    Length:151
    Mass (Da):17,222
    Last modified:January 23, 2007 - v2
    Checksum:i23F94D38F87B8D53
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821P → S in AAC15854. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01124 mRNA. Translation: AAA60283.1.
    X79239 mRNA. Translation: CAA55821.1.
    D88010 Genomic DNA. Translation: BAA13528.1.
    AK312060 mRNA. Translation: BAG34996.1.
    CH471064 Genomic DNA. Translation: EAW68448.1.
    BC000475 mRNA. Translation: AAH00475.1.
    BC006772 mRNA. Translation: AAH06772.1.
    BC029732 mRNA. Translation: AAH29732.1.
    BC066322 mRNA. Translation: AAH66322.1.
    BC100032 mRNA. Translation: AAI00033.1.
    L05090 mRNA. Translation: AAC15854.1.
    CCDSiCCDS7823.1.
    PIRiS34109.
    RefSeqiNP_001008.1. NM_001017.2.
    UniGeneiHs.446588.

    Genome annotation databases

    EnsembliENST00000525634; ENSP00000435777; ENSG00000110700.
    GeneIDi6207.
    KEGGihsa:6207.
    UCSCiuc001mmp.3. human.

    Polymorphism databases

    DMDMi50403608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01124 mRNA. Translation: AAA60283.1 .
    X79239 mRNA. Translation: CAA55821.1 .
    D88010 Genomic DNA. Translation: BAA13528.1 .
    AK312060 mRNA. Translation: BAG34996.1 .
    CH471064 Genomic DNA. Translation: EAW68448.1 .
    BC000475 mRNA. Translation: AAH00475.1 .
    BC006772 mRNA. Translation: AAH06772.1 .
    BC029732 mRNA. Translation: AAH29732.1 .
    BC066322 mRNA. Translation: AAH66322.1 .
    BC100032 mRNA. Translation: AAI00033.1 .
    L05090 mRNA. Translation: AAC15854.1 .
    CCDSi CCDS7823.1.
    PIRi S34109.
    RefSeqi NP_001008.1. NM_001017.2.
    UniGenei Hs.446588.

    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 N 1-151 [» ]
    ProteinModelPortali P62277.
    SMRi P62277. Positions 2-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112121. 137 interactions.
    IntActi P62277. 27 interactions.
    MINTi MINT-4999984.
    STRINGi 9606.ENSP00000228140.

    PTM databases

    PhosphoSitei P62277.

    Polymorphism databases

    DMDMi 50403608.

    Proteomic databases

    MaxQBi P62277.
    PaxDbi P62277.
    PeptideAtlasi P62277.
    PRIDEi P62277.

    Protocols and materials databases

    DNASUi 6207.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000525634 ; ENSP00000435777 ; ENSG00000110700 .
    GeneIDi 6207.
    KEGGi hsa:6207.
    UCSCi uc001mmp.3. human.

    Organism-specific databases

    CTDi 6207.
    GeneCardsi GC11M017055.
    HGNCi HGNC:10386. RPS13.
    HPAi HPA005985.
    MIMi 180476. gene.
    neXtProti NX_P62277.
    PharmGKBi PA34785.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0184.
    HOGENOMi HOG000180723.
    HOVERGENi HBG000938.
    InParanoidi P62277.
    KOi K02953.
    OMAi NWKYESA.
    PhylomeDBi P62277.
    TreeFami TF300190.

    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 RPS13. human.
    GeneWikii RPS13.
    GenomeRNAii 6207.
    NextBioi 24107.
    PROi P62277.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62277.
    Bgeei P62277.
    CleanExi HS_RPS13.
    Genevestigatori P62277.

    Family and domain databases

    HAMAPi MF_01343_A. Ribosomal_S15_A.
    InterProi IPR012606. Ribosomal_S13/S15_N.
    IPR000589. Ribosomal_S15.
    IPR023029. Ribosomal_S15P.
    IPR009068. S15_NS1_RNA-bd.
    [Graphical view ]
    Pfami PF08069. Ribosomal_S13_N. 1 hit.
    PF00312. Ribosomal_S15. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 1 hit.
    PROSITEi PS00362. RIBOSOMAL_S15. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and analysis of the human S13 ribosomal protein cDNA."
      Chadeneau C., Lemoullac B., Denis M.G.
      Nucleic Acids Res. 21:2945-2945(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Filipenko M.L.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    3. "U14 snoRNAs are encoded in introns of human ribosomal protein S13 gene."
      Kenmochi N., Higa S., Yoshihama M., Tanaka T.
      Biochem. Biophys. Res. Commun. 228:371-374(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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: Uterus.
    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: Bone, Brain, Muscle, Pancreas and Placenta.
    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 2-8, CLEAVAGE OF INITIATOR METHIONINE.
      Tissue: Placenta.
    8. Bhat K.S.
      Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-127.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS13_HUMAN
    AccessioniPrimary (citable) accession number: P62277
    Secondary accession number(s): B2R549
    , P19116, Q02546, Q29200, Q498Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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 11
      Human chromosome 11: 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