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P62269

- RS18_HUMAN

UniProt

P62269 - RS18_HUMAN

Protein

40S ribosomal protein S18

Gene

RPS18

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

    Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProt
    3. rRNA binding Source: UniProtKB-KW
    4. structural constituent of ribosome Source: RefGenome

    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. ribosome biogenesis Source: RefGenome
    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

    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 S18
    Alternative name(s):
    Ke-3
    Short name:
    Ke3
    Gene namesi
    Name:RPS18
    Synonyms:D6S218E
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10401. RPS18.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34801.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 15215140S ribosomal protein S18PRO_0000132212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei94 – 941N6-acetyllysine1 Publication
    Modified residuei106 – 1061N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62269.
    PaxDbiP62269.
    PeptideAtlasiP62269.
    PRIDEiP62269.

    PTM databases

    PhosphoSiteiP62269.

    Expressioni

    Gene expression databases

    BgeeiP62269.
    CleanExiHS_RPS18.
    GenevestigatoriP62269.

    Organism-specific databases

    HPAiHPA050159.

    Interactioni

    Protein-protein interaction databases

    BioGridi112136. 90 interactions.
    IntActiP62269. 33 interactions.
    MINTiMINT-1151113.
    STRINGi9606.ENSP00000403175.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00S1-152[»]
    ProteinModelPortaliP62269.
    SMRiP62269. Positions 6-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S13P family.Curated

    Phylogenomic databases

    eggNOGiCOG0099.
    HOGENOMiHOG000039877.
    HOVERGENiHBG000200.
    InParanoidiP62269.
    KOiK02964.
    OMAiQHILRVM.
    PhylomeDBiP62269.
    TreeFamiTF317649.

    Family and domain databases

    Gene3Di4.10.910.10. 1 hit.
    HAMAPiMF_01315. Ribosomal_S13_S18.
    InterProiIPR027437. 30s_Rbsml_prot_S13_C.
    IPR001892. Ribosomal_S13.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR018269. Ribosomal_S13_CS.
    [Graphical view]
    PfamiPF00416. Ribosomal_S13. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
    SUPFAMiSSF46946. SSF46946. 1 hit.
    PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
    PS50159. RIBOSOMAL_S13_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62269-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI    50
    DLTKRAGELT EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA 100
    NGLDNKLRED LERLKKIRAH RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK 150
    KK 152
    Length:152
    Mass (Da):17,719
    Last modified:January 23, 2007 - v3
    Checksum:i4DAF0662C3F37F22
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551R → S AA sequence (PubMed:8706699)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69150 mRNA. Translation: CAB56794.1.
    AL031228 Genomic DNA. Translation: CAA20231.1.
    AL662827, AL713971 Genomic DNA. Translation: CAI17530.1.
    AL713971, AL662827 Genomic DNA. Translation: CAI17656.1.
    AL645940, AL662820 Genomic DNA. Translation: CAI18076.1.
    AL662820, AL645940 Genomic DNA. Translation: CAI18127.1.
    AL844527 Genomic DNA. Translation: CAI41848.1.
    CR759817 Genomic DNA. Translation: CAQ08021.1.
    CR759786 Genomic DNA. Translation: CAQ08251.1.
    CH471081 Genomic DNA. Translation: EAX03695.1.
    BC101786 mRNA. Translation: AAI01787.1.
    BC101788 mRNA. Translation: AAI01789.1.
    BC106063 mRNA. Translation: AAI06064.1.
    CCDSiCCDS4771.1.
    PIRiS30393.
    RefSeqiNP_072045.1. NM_022551.2.
    UniGeneiHs.448854.
    Hs.627414.

    Genome annotation databases

    EnsembliENST00000211372; ENSP00000211372; ENSG00000096150.
    ENST00000434122; ENSP00000403175; ENSG00000226225.
    ENST00000439602; ENSP00000393241; ENSG00000231500.
    ENST00000454021; ENSP00000416110; ENSG00000235650.
    ENST00000457341; ENSP00000412583; ENSG00000223367.
    GeneIDi6222.
    KEGGihsa:6222.
    UCSCiuc003odp.1. human.

    Polymorphism databases

    DMDMi50403625.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69150 mRNA. Translation: CAB56794.1 .
    AL031228 Genomic DNA. Translation: CAA20231.1 .
    AL662827 , AL713971 Genomic DNA. Translation: CAI17530.1 .
    AL713971 , AL662827 Genomic DNA. Translation: CAI17656.1 .
    AL645940 , AL662820 Genomic DNA. Translation: CAI18076.1 .
    AL662820 , AL645940 Genomic DNA. Translation: CAI18127.1 .
    AL844527 Genomic DNA. Translation: CAI41848.1 .
    CR759817 Genomic DNA. Translation: CAQ08021.1 .
    CR759786 Genomic DNA. Translation: CAQ08251.1 .
    CH471081 Genomic DNA. Translation: EAX03695.1 .
    BC101786 mRNA. Translation: AAI01787.1 .
    BC101788 mRNA. Translation: AAI01789.1 .
    BC106063 mRNA. Translation: AAI06064.1 .
    CCDSi CCDS4771.1.
    PIRi S30393.
    RefSeqi NP_072045.1. NM_022551.2.
    UniGenei Hs.448854.
    Hs.627414.

    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 S 1-152 [» ]
    ProteinModelPortali P62269.
    SMRi P62269. Positions 6-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112136. 90 interactions.
    IntActi P62269. 33 interactions.
    MINTi MINT-1151113.
    STRINGi 9606.ENSP00000403175.

    PTM databases

    PhosphoSitei P62269.

    Polymorphism databases

    DMDMi 50403625.

    Proteomic databases

    MaxQBi P62269.
    PaxDbi P62269.
    PeptideAtlasi P62269.
    PRIDEi P62269.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000211372 ; ENSP00000211372 ; ENSG00000096150 .
    ENST00000434122 ; ENSP00000403175 ; ENSG00000226225 .
    ENST00000439602 ; ENSP00000393241 ; ENSG00000231500 .
    ENST00000454021 ; ENSP00000416110 ; ENSG00000235650 .
    ENST00000457341 ; ENSP00000412583 ; ENSG00000223367 .
    GeneIDi 6222.
    KEGGi hsa:6222.
    UCSCi uc003odp.1. human.

    Organism-specific databases

    CTDi 6222.
    GeneCardsi GC06P033240.
    GC06Pj33161.
    GC06Pk33217.
    GC06Pm33410.
    GC06Pn33168.
    HGNCi HGNC:10401. RPS18.
    HPAi HPA050159.
    MIMi 180473. gene.
    neXtProti NX_P62269.
    PharmGKBi PA34801.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0099.
    HOGENOMi HOG000039877.
    HOVERGENi HBG000200.
    InParanoidi P62269.
    KOi K02964.
    OMAi QHILRVM.
    PhylomeDBi P62269.
    TreeFami TF317649.

    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

    GeneWikii RPS18.
    GenomeRNAii 6222.
    NextBioi 24155.
    PROi P62269.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62269.
    CleanExi HS_RPS18.
    Genevestigatori P62269.

    Family and domain databases

    Gene3Di 4.10.910.10. 1 hit.
    HAMAPi MF_01315. Ribosomal_S13_S18.
    InterProi IPR027437. 30s_Rbsml_prot_S13_C.
    IPR001892. Ribosomal_S13.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR018269. Ribosomal_S13_CS.
    [Graphical view ]
    Pfami PF00416. Ribosomal_S13. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002134. Ribosomal_S13. 1 hit.
    SUPFAMi SSF46946. SSF46946. 1 hit.
    PROSITEi PS00646. RIBOSOMAL_S13_1. 1 hit.
    PS50159. RIBOSOMAL_S13_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human homolog of ribosomal protein S18."
      Chassin D., Bellet D., Koman A.
      Nucleic Acids Res. 21:745-745(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 Brain.
    5. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-23; 25-34; 40-75; 79-86; 95-113 AND 125-130, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    6. "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 55-69.
      Tissue: Placenta.
    7. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-94 AND LYS-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRS18_HUMAN
    AccessioniPrimary (citable) accession number: P62269
    Secondary accession number(s): P25232, Q5SUJ3, Q6IPF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 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 6
      Human chromosome 6: 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