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P62280

- RS11_HUMAN

UniProt

P62280 - RS11_HUMAN

Protein

40S ribosomal protein S11

Gene

RPS11

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. protein binding Source: IntAct
    3. rRNA binding Source: UniProtKB-KW
    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. 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

    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 S11
    Gene namesi
    Name:RPS11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10384. RPS11.

    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. ribosome Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi60 – 601C → S: Abolishes S-acylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA34782.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 15815740S ribosomal protein S11PRO_0000128509Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei22 – 221CitrullineBy similarity
    Modified residuei38 – 381N6-acetyllysine1 Publication
    Modified residuei45 – 451N6-acetyllysine1 Publication
    Modified residuei58 – 581N6-acetyllysineBy similarity
    Lipidationi60 – 601S-palmitoyl cysteine1 Publication

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiP62280.
    PaxDbiP62280.
    PeptideAtlasiP62280.
    PRIDEiP62280.

    2D gel databases

    SWISS-2DPAGEP62280.

    PTM databases

    PhosphoSiteiP62280.

    Miscellaneous databases

    PMAP-CutDBP62280.

    Expressioni

    Gene expression databases

    ArrayExpressiP62280.
    BgeeiP62280.
    CleanExiHS_RPS11.
    GenevestigatoriP62280.

    Organism-specific databases

    HPAiHPA049719.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0073EBI-1047710,EBI-5323863

    Protein-protein interaction databases

    BioGridi112119. 116 interactions.
    IntActiP62280. 34 interactions.
    MINTiMINT-1154341.
    STRINGi9606.ENSP00000270625.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00L1-158[»]
    ProteinModelPortaliP62280.
    SMRiP62280. Positions 1-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S17P family.Curated

    Phylogenomic databases

    eggNOGiCOG0186.
    HOGENOMiHOG000231341.
    HOVERGENiHBG004670.
    InParanoidiP62280.
    KOiK02949.
    OMAiGAKKQFQ.
    OrthoDBiEOG78H3VQ.
    PhylomeDBiP62280.
    TreeFamiTF300126.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    HAMAPiMF_01345_B. Ribosomal_S17_B.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR000266. Ribosomal_S17.
    IPR028333. Ribosomal_S17_arc-typ.
    IPR019979. Ribosomal_S17_CS.
    [Graphical view]
    PANTHERiPTHR10744. PTHR10744. 1 hit.
    PfamiPF00366. Ribosomal_S17. 1 hit.
    [Graphical view]
    PRINTSiPR00973. RIBOSOMALS17.
    ProDomiPD001295. Ribosomal_S17. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR03630. arch_S17P. 1 hit.
    PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62280-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA    50
    IEGTYIDKKC PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN 100
    RFEKRHKNMS VHLSPCFRDV QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG 150
    TKKQFQKF 158
    Length:158
    Mass (Da):18,431
    Last modified:January 23, 2007 - v3
    Checksum:i9FB75DC1D99614B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06617 mRNA. Translation: CAA29834.1.
    AB028893 Genomic DNA. Translation: BAA88215.1.
    AK311809 mRNA. Translation: BAG34752.1.
    CH471177 Genomic DNA. Translation: EAW52497.1.
    BC007283 mRNA. Translation: AAH07283.1.
    BC007603 mRNA. Translation: AAH07603.1.
    BC007945 mRNA. Translation: AAH07945.1.
    BC010028 mRNA. Translation: AAH10028.1.
    BC016378 mRNA. Translation: AAH16378.1.
    BC070224 mRNA. Translation: AAH70224.1.
    BC100025 mRNA. Translation: AAI00026.1.
    AB007152 Genomic DNA. Translation: BAA25818.1.
    CCDSiCCDS12769.1.
    PIRiS02133. R3HU11.
    RefSeqiNP_001006.1. NM_001015.4.
    UniGeneiHs.433529.

    Genome annotation databases

    EnsembliENST00000270625; ENSP00000270625; ENSG00000142534.
    GeneIDi6205.
    KEGGihsa:6205.
    UCSCiuc002pob.2. human.

    Polymorphism databases

    DMDMi50403609.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06617 mRNA. Translation: CAA29834.1 .
    AB028893 Genomic DNA. Translation: BAA88215.1 .
    AK311809 mRNA. Translation: BAG34752.1 .
    CH471177 Genomic DNA. Translation: EAW52497.1 .
    BC007283 mRNA. Translation: AAH07283.1 .
    BC007603 mRNA. Translation: AAH07603.1 .
    BC007945 mRNA. Translation: AAH07945.1 .
    BC010028 mRNA. Translation: AAH10028.1 .
    BC016378 mRNA. Translation: AAH16378.1 .
    BC070224 mRNA. Translation: AAH70224.1 .
    BC100025 mRNA. Translation: AAI00026.1 .
    AB007152 Genomic DNA. Translation: BAA25818.1 .
    CCDSi CCDS12769.1.
    PIRi S02133. R3HU11.
    RefSeqi NP_001006.1. NM_001015.4.
    UniGenei Hs.433529.

    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 L 1-158 [» ]
    ProteinModelPortali P62280.
    SMRi P62280. Positions 1-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112119. 116 interactions.
    IntActi P62280. 34 interactions.
    MINTi MINT-1154341.
    STRINGi 9606.ENSP00000270625.

    PTM databases

    PhosphoSitei P62280.

    Polymorphism databases

    DMDMi 50403609.

    2D gel databases

    SWISS-2DPAGE P62280.

    Proteomic databases

    MaxQBi P62280.
    PaxDbi P62280.
    PeptideAtlasi P62280.
    PRIDEi P62280.

    Protocols and materials databases

    DNASUi 6205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270625 ; ENSP00000270625 ; ENSG00000142534 .
    GeneIDi 6205.
    KEGGi hsa:6205.
    UCSCi uc002pob.2. human.

    Organism-specific databases

    CTDi 6205.
    GeneCardsi GC19P049999.
    H-InvDB HIX0037158.
    HGNCi HGNC:10384. RPS11.
    HPAi HPA049719.
    MIMi 180471. gene.
    neXtProti NX_P62280.
    PharmGKBi PA34782.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0186.
    HOGENOMi HOG000231341.
    HOVERGENi HBG004670.
    InParanoidi P62280.
    KOi K02949.
    OMAi GAKKQFQ.
    OrthoDBi EOG78H3VQ.
    PhylomeDBi P62280.
    TreeFami TF300126.

    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 RPS11. human.
    GeneWikii RPS11.
    GenomeRNAii 6205.
    NextBioi 24099.
    PMAP-CutDB P62280.
    PROi P62280.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62280.
    Bgeei P62280.
    CleanExi HS_RPS11.
    Genevestigatori P62280.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    HAMAPi MF_01345_B. Ribosomal_S17_B.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR000266. Ribosomal_S17.
    IPR028333. Ribosomal_S17_arc-typ.
    IPR019979. Ribosomal_S17_CS.
    [Graphical view ]
    PANTHERi PTHR10744. PTHR10744. 1 hit.
    Pfami PF00366. Ribosomal_S17. 1 hit.
    [Graphical view ]
    PRINTSi PR00973. RIBOSOMALS17.
    ProDomi PD001295. Ribosomal_S17. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR03630. arch_S17P. 1 hit.
    PROSITEi PS00056. RIBOSOMAL_S17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a cloned cDNA encoding human ribosomal protein S11."
      Lott J.B., Mackie G.A.
      Nucleic Acids Res. 16:1205-1205(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Gene organization and sequence of the region containing the ribosomal protein genes RPL13A and RPS11 in the human genome and conserved features in the mouse genome."
      Higa S., Yoshihama M., Tanaka T., Kenmochi N.
      Gene 240:371-377(1999) [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: Thymus.
    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: B-cell, Eye, Lung and Prostate.
    6. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    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 39-45 AND 137-143.
      Tissue: Placenta.
    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 76-158.
    9. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-38 AND LYS-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Site-specific analysis of protein S-acylation by resin-assisted capture."
      Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J.
      J. Lipid Res. 52:393-398(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-60, PALMITOYLATION AT CYS-60.
    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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS11_HUMAN
    AccessioniPrimary (citable) accession number: P62280
    Secondary accession number(s): B2R4F5
    , P04643, Q498Y6, Q6IRY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 119 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. 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