P62269 (RS18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S18

Alternative name(s):
Ke-3
Short name=Ke3

Gene names

Name:	RPS18
Synonyms:	D6S218E

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane 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 translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB
Molecular_function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 152	151	40S ribosomal protein S18 HAMAP-Rule MF_01315		PRO_0000132212
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.5
	Modified residue	94	1	N6-acetyllysine Ref.7
	Modified residue	106	1	N6-acetyllysine Ref.7
Experimental info
	Sequence conflict	55	1	R → S AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P62269 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4DAF0662C3F37F22	FASTA	152	17,719
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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]	"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, MASS SPECTROMETRY.
[8]	"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].
+	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.
IPI	IPI00013296.
PIR	S30393.
RefSeq	NP_072045.1. NM_022551.2.
UniGene	Hs.448854. Hs.627414.
3D structure databases
ProteinModelPortal	P62269.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62269. 23 interactions.
MINT	MINT-1151113.
STRING	9606.ENSP00000403175.
PTM databases
PhosphoSite	P62269.
Polymorphism databases
DMDM	50403625.
Proteomic databases
PaxDb	P62269.
PeptideAtlas	P62269.
PRIDE	P62269.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000211372; ENSP00000211372; ENSG00000096150. ENST00000434122; ENSP00000403175; ENSG00000226225. ENST00000439602; ENSP00000393241; ENSG00000231500. ENST00000454021; ENSP00000416110; ENSG00000235650. ENST00000457341; ENSP00000412583; ENSG00000223367.
GeneID	6222.
KEGG	hsa:6222.
UCSC	uc003odp.1. human.
Organism-specific databases
CTD	6222.
GeneCards	GC06P033240.
HGNC	HGNC:10401. RPS18.
HPA	HPA050159.
MIM	180473. gene.
neXtProt	NX_P62269.
PharmGKB	PA34801.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0099.
HOGENOM	HOG000039877.
HOVERGEN	HBG000200.
InParanoid	P62269.
KO	K02964.
OMA	FQHILRI.
OrthoDB	EOG4KSPM2.
PhylomeDB	P62269.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P62269.
Bgee	P62269.
CleanEx	HS_RPS18.
Genevestigator	P62269.
GermOnline	ENSG00000182498. Homo sapiens.
Family and domain databases
HAMAP	MF_01315. Ribosomal_S13/S18.
InterPro	IPR001892. Ribosomal_S13. IPR010979. Ribosomal_S13-like_H2TH. IPR018269. Ribosomal_S13_CS. [Graphical view]
PANTHER	PTHR10871. PTHR10871. 1 hit.
Pfam	PF00416. Ribosomal_S13. 1 hit. [Graphical view]
PIRSF	PIRSF002134. Ribosomal_S13. 1 hit.
SUPFAM	SSF46946. Ribosomal_H2TH. 1 hit.
PROSITE	PS00646. RIBOSOMAL_S13_1. 1 hit. PS50159. RIBOSOMAL_S13_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	6222.
NextBio	24155.
SOURCE	Search...

Entry information

Entry name

RS18_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.