Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

40S ribosomal protein S18

Gene

RPS18

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

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

  • poly(A) RNA binding Source: UniProtKB
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

Complete GO annotation...

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 Componentsi: Chromosome 6, Unplaced

Organism-specific databases

HGNCiHGNC:10401. RPS18.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: GO_Central
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • ribosome Source: UniProtKB
  • small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34801.

Polymorphism and mutation databases

BioMutaiRPS18.
DMDMi50403625.

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.
ExpressionAtlasiP62269. baseline.
GenevestigatoriP62269.

Organism-specific databases

HPAiHPA050159.
HPA055007.

Interactioni

Protein-protein interaction databases

BioGridi112136. 101 interactions.
IntActiP62269. 34 interactions.
MINTiMINT-1151113.
STRINGi9606.ENSP00000403175.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AS1-152[»]
ProteinModelPortaliP62269.
SMRiP62269. Positions 6-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S13P family.Curated

Phylogenomic databases

eggNOGiCOG0099.
GeneTreeiENSGT00390000012691.
HOGENOMiHOG000039877.
HOVERGENiHBG000200.
InParanoidiP62269.
KOiK02964.
OMAiIRAYRGI.
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

        10         20         30         40         50
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI
60 70 80 90 100
DLTKRAGELT EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA
110 120 130 140 150
NGLDNKLRED LERLKKIRAH RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK

KK
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:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AS1-152[»]
ProteinModelPortaliP62269.
SMRiP62269. Positions 6-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112136. 101 interactions.
IntActiP62269. 34 interactions.
MINTiMINT-1151113.
STRINGi9606.ENSP00000403175.

PTM databases

PhosphoSiteiP62269.

Polymorphism and mutation databases

BioMutaiRPS18.
DMDMi50403625.

Proteomic databases

MaxQBiP62269.
PaxDbiP62269.
PeptideAtlasiP62269.
PRIDEiP62269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6222.
GeneCardsiGC06P033240.
GC06Pj33161.
GC06Pk33217.
GC06Pm33410.
GC06Pn33168.
HGNCiHGNC:10401. RPS18.
HPAiHPA050159.
HPA055007.
MIMi180473. gene.
neXtProtiNX_P62269.
PharmGKBiPA34801.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0099.
GeneTreeiENSGT00390000012691.
HOGENOMiHOG000039877.
HOVERGENiHBG000200.
InParanoidiP62269.
KOiK02964.
OMAiIRAYRGI.
PhylomeDBiP62269.
TreeFamiTF317649.

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.

Miscellaneous databases

ChiTaRSiRPS18. human.
GeneWikiiRPS18.
GenomeRNAii6222.
NextBioi24155.
PROiP62269.
SOURCEiSearch...

Gene expression databases

BgeeiP62269.
CleanExiHS_RPS18.
ExpressionAtlasiP62269. baseline.
GenevestigatoriP62269.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. 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: May 27, 2015
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 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.