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P62269 (RS18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S18
Alternative name(s):
Ke-3
Short name=Ke3
Gene names
Name:RPS18
Synonyms:D6S218E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA By similarity. HAMAP-Rule MF_01315

Subcellular location

Cytoplasm HAMAP-Rule MF_01315.

Sequence similarities

Belongs to the ribosomal protein S13P family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

ribosome biogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

translation

Inferred by curator PubMed 15883184Ref.6. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay PubMed 21630459PubMed 22720776. Source: UniProt

ribosome

Non-traceable author statement Ref.1. Source: UniProtKB

small ribosomal subunit

Inferred from direct assay PubMed 15883184. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 15215140S ribosomal protein S18 HAMAP-Rule MF_01315
PRO_0000132212

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.7 Ref.10
Modified residue941N6-acetyllysine Ref.8
Modified residue1061N6-acetyllysine Ref.8

Experimental info

Sequence conflict551R → S AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
P62269 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4DAF0662C3F37F22

FASTA15217,719
        10         20         30         40         50         60 
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT 

        70         80         90        100        110        120 
EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH 

       130        140        150 
RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4771.1.
PIRS30393.
RefSeqNP_072045.1. NM_022551.2.
UniGeneHs.448854.
Hs.627414.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00S1-152[»]
ProteinModelPortalP62269.
SMRP62269. Positions 6-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112136. 121 interactions.
IntActP62269. 31 interactions.
MINTMINT-1151113.
STRING9606.ENSP00000403175.

PTM databases

PhosphoSiteP62269.

Polymorphism databases

DMDM50403625.

Proteomic databases

MaxQBP62269.
PaxDbP62269.
PeptideAtlasP62269.
PRIDEP62269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000211372; ENSP00000211372; ENSG00000096150.
ENST00000434122; ENSP00000403175; ENSG00000226225.
ENST00000439602; ENSP00000393241; ENSG00000231500.
ENST00000454021; ENSP00000416110; ENSG00000235650.
ENST00000457341; ENSP00000412583; ENSG00000223367.
GeneID6222.
KEGGhsa:6222.
UCSCuc003odp.1. human.

Organism-specific databases

CTD6222.
GeneCardsGC06P033240.
GC06Pj33161.
GC06Pk33217.
GC06Pm33410.
GC06Pn33168.
HGNCHGNC:10401. RPS18.
HPAHPA050159.
MIM180473. gene.
neXtProtNX_P62269.
PharmGKBPA34801.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0099.
HOGENOMHOG000039877.
HOVERGENHBG000200.
InParanoidP62269.
KOK02964.
OMAQHILRVM.
PhylomeDBP62269.
TreeFamTF317649.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP62269.
CleanExHS_RPS18.
GenevestigatorP62269.

Family and domain databases

Gene3D4.10.910.10. 1 hit.
HAMAPMF_01315. Ribosomal_S13_S18.
InterProIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMSSF46946. SSF46946. 1 hit.
PROSITEPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPS18.
GenomeRNAi6222.
NextBio24155.
PROP62269.
SOURCESearch...

Entry information

Entry nameRS18_HUMAN
AccessionPrimary (citable) accession number: P62269
Secondary accession number(s): P25232, Q5SUJ3, Q6IPF8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM