RS18_HUMAN
ID RS18_HUMAN Reviewed; 152 AA.
AC P62269; P25232; Q5SUJ3; Q6IPF8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=40S ribosomal protein S18;
DE AltName: Full=Ke-3;
DE Short=Ke3;
DE AltName: Full=Small ribosomal subunit protein uS13 {ECO:0000303|PubMed:24524803};
GN Name=RPS18; Synonyms=D6S218E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8441687; DOI=10.1093/nar/21.3.745;
RA Chassin D., Bellet D., Koman A.;
RT "The human homolog of ribosomal protein S18.";
RL Nucleic Acids Res. 21:745-745(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-23; 25-34; 40-75; 79-86; 95-113 AND 125-130, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (NOV-2006) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 55-69.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-94 AND LYS-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Located at the top of the head of the 40S subunit, it
CC contacts several helices of the 18S rRNA. {ECO:0000250}.
CC -!- INTERACTION:
CC P62269; Q5S007: LRRK2; NbExp=3; IntAct=EBI-352451, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000305}.
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DR EMBL; X69150; CAB56794.1; -; mRNA.
DR EMBL; AL031228; CAA20231.1; -; Genomic_DNA.
DR EMBL; AL662827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03695.1; -; Genomic_DNA.
DR EMBL; BC101786; AAI01787.1; -; mRNA.
DR EMBL; BC101788; AAI01789.1; -; mRNA.
DR EMBL; BC106063; AAI06064.1; -; mRNA.
DR CCDS; CCDS4771.1; -.
DR PIR; S30393; S30393.
DR RefSeq; NP_072045.1; NM_022551.2.
DR PDB; 4UG0; EM; -; SS=1-152.
DR PDB; 4V6X; EM; 5.00 A; AS=1-152.
DR PDB; 5A2Q; EM; 3.90 A; S=1-152.
DR PDB; 5AJ0; EM; 3.50 A; BS=1-152.
DR PDB; 5FLX; EM; 3.90 A; S=1-152.
DR PDB; 5LKS; EM; 3.60 A; SS=1-152.
DR PDB; 5OA3; EM; 4.30 A; S=1-152.
DR PDB; 5T2C; EM; 3.60 A; A0=1-152.
DR PDB; 5VYC; X-ray; 6.00 A; S1/S2/S3/S4/S5/S6=1-152.
DR PDB; 6FEC; EM; 6.30 A; L=6-142.
DR PDB; 6G18; EM; 3.60 A; S=1-152.
DR PDB; 6G4S; EM; 4.00 A; S=1-152.
DR PDB; 6G4W; EM; 4.50 A; S=1-152.
DR PDB; 6G51; EM; 4.10 A; S=1-152.
DR PDB; 6G53; EM; 4.50 A; S=1-152.
DR PDB; 6G5H; EM; 3.60 A; S=1-152.
DR PDB; 6G5I; EM; 3.50 A; S=1-152.
DR PDB; 6IP5; EM; 3.90 A; 2z=1-152.
DR PDB; 6IP6; EM; 4.50 A; 2z=1-152.
DR PDB; 6IP8; EM; 3.90 A; 2z=1-152.
DR PDB; 6OLE; EM; 3.10 A; SS=1-145.
DR PDB; 6OLF; EM; 3.90 A; SS=1-145.
DR PDB; 6OLG; EM; 3.40 A; BS=4-142.
DR PDB; 6OLI; EM; 3.50 A; SS=1-145.
DR PDB; 6OLZ; EM; 3.90 A; BS=4-142.
DR PDB; 6OM0; EM; 3.10 A; SS=1-145.
DR PDB; 6OM7; EM; 3.70 A; SS=1-145.
DR PDB; 6QZP; EM; 2.90 A; SS=1-145.
DR PDB; 6XA1; EM; 2.80 A; SS=3-145.
DR PDB; 6Y0G; EM; 3.20 A; SS=1-152.
DR PDB; 6Y2L; EM; 3.00 A; SS=1-152.
DR PDB; 6Y57; EM; 3.50 A; SS=1-152.
DR PDB; 6YBS; EM; 3.10 A; f=1-152.
DR PDB; 6Z6L; EM; 3.00 A; SS=1-152.
DR PDB; 6Z6M; EM; 3.10 A; SS=1-152.
DR PDB; 6Z6N; EM; 2.90 A; SS=1-152.
DR PDB; 6ZLW; EM; 2.60 A; T=1-152.
DR PDB; 6ZM7; EM; 2.70 A; SS=1-152.
DR PDB; 6ZME; EM; 3.00 A; SS=1-152.
DR PDB; 6ZMI; EM; 2.60 A; SS=1-152.
DR PDB; 6ZMO; EM; 3.10 A; SS=1-152.
DR PDB; 6ZMT; EM; 3.00 A; T=1-152.
DR PDB; 6ZMW; EM; 3.70 A; f=1-152.
DR PDB; 6ZN5; EM; 3.20 A; T=3-145.
DR PDB; 6ZOJ; EM; 2.80 A; S=1-152.
DR PDB; 6ZOL; EM; 2.80 A; S=1-152.
DR PDB; 6ZON; EM; 3.00 A; k=1-152.
DR PDB; 6ZP4; EM; 2.90 A; k=1-152.
DR PDB; 6ZUO; EM; 3.10 A; S=1-152.
DR PDB; 6ZV6; EM; 2.90 A; S=1-152.
DR PDB; 6ZVH; EM; 2.90 A; S=1-145.
DR PDB; 6ZVJ; EM; 3.80 A; k=3-142.
DR PDB; 6ZXD; EM; 3.20 A; S=1-152.
DR PDB; 6ZXE; EM; 3.00 A; S=1-152.
DR PDB; 6ZXF; EM; 3.70 A; S=1-152.
DR PDB; 6ZXG; EM; 2.60 A; S=1-152.
DR PDB; 6ZXH; EM; 2.70 A; S=1-152.
DR PDB; 7A09; EM; 3.50 A; k=1-152.
DR PDB; 7K5I; EM; 2.90 A; S=1-152.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P62269; -.
DR SMR; P62269; -.
DR BioGRID; 112136; 313.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62269; -.
DR DIP; DIP-32892N; -.
DR IntAct; P62269; 87.
DR MINT; P62269; -.
DR STRING; 9606.ENSP00000393241; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; P62269; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62269; -.
DR MetOSite; P62269; -.
DR PhosphoSitePlus; P62269; -.
DR SwissPalm; P62269; -.
DR BioMuta; RPS18; -.
DR DMDM; 50403625; -.
DR EPD; P62269; -.
DR jPOST; P62269; -.
DR MassIVE; P62269; -.
DR MaxQB; P62269; -.
DR PaxDb; P62269; -.
DR PeptideAtlas; P62269; -.
DR PRIDE; P62269; -.
DR ProteomicsDB; 57381; -.
DR TopDownProteomics; P62269; -.
DR Antibodypedia; 53237; 188 antibodies from 26 providers.
DR DNASU; 6222; -.
DR Ensembl; ENST00000211372.9; ENSP00000211372.5; ENSG00000096150.9.
DR Ensembl; ENST00000434122.2; ENSP00000403175.2; ENSG00000226225.6.
DR Ensembl; ENST00000439602.7; ENSP00000393241.2; ENSG00000231500.7.
DR Ensembl; ENST00000454021.6; ENSP00000416110.2; ENSG00000235650.6.
DR Ensembl; ENST00000457341.6; ENSP00000412583.2; ENSG00000223367.6.
DR GeneID; 6222; -.
DR KEGG; hsa:6222; -.
DR MANE-Select; ENST00000439602.7; ENSP00000393241.2; NM_022551.3; NP_072045.1.
DR UCSC; uc003odp.2; human.
DR CTD; 6222; -.
DR DisGeNET; 6222; -.
DR GeneCards; RPS18; -.
DR HGNC; HGNC:10401; RPS18.
DR HPA; ENSG00000231500; Low tissue specificity.
DR MIM; 180473; gene.
DR neXtProt; NX_P62269; -.
DR OpenTargets; ENSG00000231500; -.
DR PharmGKB; PA34801; -.
DR VEuPathDB; HostDB:ENSG00000231500; -.
DR eggNOG; KOG3311; Eukaryota.
DR GeneTree; ENSGT00390000012691; -.
DR HOGENOM; CLU_103849_0_1_1; -.
DR InParanoid; P62269; -.
DR OMA; IRAYRGI; -.
DR OrthoDB; 1343043at2759; -.
DR PhylomeDB; P62269; -.
DR TreeFam; TF317649; -.
DR PathwayCommons; P62269; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62269; -.
DR SIGNOR; P62269; -.
DR BioGRID-ORCS; 6222; 820 hits in 1050 CRISPR screens.
DR ChiTaRS; RPS18; human.
DR GeneWiki; RPS18; -.
DR GenomeRNAi; 6222; -.
DR Pharos; P62269; Tbio.
DR PRO; PR:P62269; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P62269; protein.
DR Bgee; ENSG00000096150; Expressed in material anatomical entity and 45 other tissues.
DR ExpressionAtlas; P62269; baseline and differential.
DR Genevisible; P62269; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR Gene3D; 4.10.910.10; -; 1.
DR HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR InterPro; IPR001892; Ribosomal_S13.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR018269; Ribosomal_S13_CS.
DR Pfam; PF00416; Ribosomal_S13; 1.
DR PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..152
FT /note="40S ribosomal protein S18"
FT /id="PRO_0000132212"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 106
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 55
FT /note="R -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:6ZN5"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6ZMT"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 152 AA; 17719 MW; 4DAF0662C3F37F22 CRC64;
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT
EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH
RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK
