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P46782

- RS5_HUMAN

UniProt

P46782 - RS5_HUMAN

Protein

40S ribosomal protein S5

Gene

RPS5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. mRNA binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. RNA binding Source: UniProtKB
    4. 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. regulation of translational fidelity Source: UniProtKB
    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: UniProtKB
    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 S5
    Cleaved into the following chain:
    Gene namesi
    Name:RPS5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10426. RPS5.

    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. ribonucleoprotein complex Source: MGI

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34841.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20420440S ribosomal protein S5PRO_0000370369Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate2 Publications
    Chaini2 – 20420340S ribosomal protein S5, N-terminally processedPRO_0000124526Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in 40S ribosomal protein S5; alternate3 Publications
    Modified residuei2 – 21N-acetylthreonine; in 40S ribosomal protein S5, N-terminally processed4 Publications
    Modified residuei47 – 471N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP46782.
    PaxDbiP46782.
    PeptideAtlasiP46782.
    PRIDEiP46782.

    2D gel databases

    SWISS-2DPAGEP46782.

    PTM databases

    PhosphoSiteiP46782.

    Expressioni

    Gene expression databases

    ArrayExpressiP46782.
    BgeeiP46782.
    CleanExiHS_RPS5.
    GenevestigatoriP46782.

    Organism-specific databases

    HPAiHPA055878.

    Interactioni

    Protein-protein interaction databases

    BioGridi112107. 119 interactions.
    IntActiP46782. 16 interactions.
    MINTiMINT-1142463.
    STRINGi9606.ENSP00000196551.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00F1-204[»]
    ProteinModelPortaliP46782.
    SMRiP46782. Positions 14-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S7P family.Curated

    Phylogenomic databases

    eggNOGiCOG0049.
    HOGENOMiHOG000039066.
    HOVERGENiHBG028547.
    InParanoidiP46782.
    KOiK02989.
    OrthoDBiEOG7PZRZS.
    PhylomeDBiP46782.
    TreeFamiTF300872.

    Family and domain databases

    Gene3Di1.10.455.10. 1 hit.
    InterProiIPR000235. Ribosomal_S5/S7.
    IPR005716. Ribosomal_S5/S7_euk/arc.
    IPR020606. Ribosomal_S7_CS.
    IPR023798. Ribosomal_S7_dom.
    [Graphical view]
    PANTHERiPTHR11205. PTHR11205. 1 hit.
    PfamiPF00177. Ribosomal_S7. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
    SUPFAMiSSF47973. SSF47973. 1 hit.
    TIGRFAMsiTIGR01028. S7_S5_E_A. 1 hit.
    PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P46782-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP    50
    HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII 100
    HLLTGENPLQ VLVNAIINSG PREDSTRIGR AGTVRRQAVD VSPLRRVNQA 150
    IWLLCTGARE AAFRNIKTIA ECLADELINA AKGSSNSYAI KKKDELERVA 200
    KSNR 204
    Length:204
    Mass (Da):22,876
    Last modified:January 23, 2007 - v4
    Checksum:iDFE2FD5AAFCFD894
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 602KR → NA in AAA85658. (PubMed:7772601)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14970 mRNA. Translation: AAA85658.1.
    AB061853 Genomic DNA. Translation: BAB79493.1.
    AK311938 mRNA. Translation: BAG34879.1.
    CH471135 Genomic DNA. Translation: EAW72581.1.
    BC015405 mRNA. Translation: AAH15405.1.
    BC018151 mRNA. Translation: AAH18151.1.
    AB007149 Genomic DNA. Translation: BAA25815.1.
    CCDSiCCDS12978.1.
    PIRiS55916.
    RefSeqiNP_001000.2. NM_001009.3.
    UniGeneiHs.378103.

    Genome annotation databases

    EnsembliENST00000196551; ENSP00000196551; ENSG00000083845.
    ENST00000596046; ENSP00000472985; ENSG00000083845.
    ENST00000601521; ENSP00000470114; ENSG00000083845.
    GeneIDi6193.
    KEGGihsa:6193.
    UCSCiuc002qsn.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14970 mRNA. Translation: AAA85658.1 .
    AB061853 Genomic DNA. Translation: BAB79493.1 .
    AK311938 mRNA. Translation: BAG34879.1 .
    CH471135 Genomic DNA. Translation: EAW72581.1 .
    BC015405 mRNA. Translation: AAH15405.1 .
    BC018151 mRNA. Translation: AAH18151.1 .
    AB007149 Genomic DNA. Translation: BAA25815.1 .
    CCDSi CCDS12978.1.
    PIRi S55916.
    RefSeqi NP_001000.2. NM_001009.3.
    UniGenei Hs.378103.

    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 F 1-204 [» ]
    ProteinModelPortali P46782.
    SMRi P46782. Positions 14-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112107. 119 interactions.
    IntActi P46782. 16 interactions.
    MINTi MINT-1142463.
    STRINGi 9606.ENSP00000196551.

    PTM databases

    PhosphoSitei P46782.

    2D gel databases

    SWISS-2DPAGE P46782.

    Proteomic databases

    MaxQBi P46782.
    PaxDbi P46782.
    PeptideAtlasi P46782.
    PRIDEi P46782.

    Protocols and materials databases

    DNASUi 6193.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000196551 ; ENSP00000196551 ; ENSG00000083845 .
    ENST00000596046 ; ENSP00000472985 ; ENSG00000083845 .
    ENST00000601521 ; ENSP00000470114 ; ENSG00000083845 .
    GeneIDi 6193.
    KEGGi hsa:6193.
    UCSCi uc002qsn.3. human.

    Organism-specific databases

    CTDi 6193.
    GeneCardsi GC19P059246.
    H-InvDB HIX0020415.
    HGNCi HGNC:10426. RPS5.
    HPAi HPA055878.
    MIMi 603630. gene.
    neXtProti NX_P46782.
    PharmGKBi PA34841.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0049.
    HOGENOMi HOG000039066.
    HOVERGENi HBG028547.
    InParanoidi P46782.
    KOi K02989.
    OrthoDBi EOG7PZRZS.
    PhylomeDBi P46782.
    TreeFami TF300872.

    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 RPS5. human.
    GeneWikii RPS5.
    GenomeRNAii 6193.
    NextBioi 24049.
    PROi P46782.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46782.
    Bgeei P46782.
    CleanExi HS_RPS5.
    Genevestigatori P46782.

    Family and domain databases

    Gene3Di 1.10.455.10. 1 hit.
    InterProi IPR000235. Ribosomal_S5/S7.
    IPR005716. Ribosomal_S5/S7_euk/arc.
    IPR020606. Ribosomal_S7_CS.
    IPR023798. Ribosomal_S7_dom.
    [Graphical view ]
    PANTHERi PTHR11205. PTHR11205. 1 hit.
    Pfami PF00177. Ribosomal_S7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
    SUPFAMi SSF47973. SSF47973. 1 hit.
    TIGRFAMsi TIGR01028. S7_S5_E_A. 1 hit.
    PROSITEi PS00052. RIBOSOMAL_S7. 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. "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: Tongue.
    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: Bone and Ovary.
    6. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-18; 23-42; 48-55; 137-145 AND 168-182, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-18; 23-42; 137-159 AND 168-182, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix 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 150-204.
    9. "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 192-197.
      Tissue: Placenta.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS5_HUMAN
    AccessioniPrimary (citable) accession number: P46782
    Secondary accession number(s): B2R4T2, Q96BN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 4 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. 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