Full text data of RPS18
RPS18
(D6S218E)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
40S ribosomal protein S18 (Ke-3; Ke3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S18 (Ke-3; Ke3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62269
ID RS18_HUMAN Reviewed; 152 AA.
AC P62269; P25232; Q5SUJ3; Q6IPF8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=40S ribosomal protein S18;
DE AltName: Full=Ke-3;
DE Short=Ke3;
GN Name=RPS18; Synonyms=D6S218E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND 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.,
RA Egorov T.A., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-106, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [9]
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.,
RA Buerckstuemmer T., 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 [10]
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ribosomal protein S13P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X69150; CAB56794.1; -; mRNA.
DR EMBL; AL031228; CAA20231.1; -; Genomic_DNA.
DR EMBL; AL662827; CAI17530.1; -; Genomic_DNA.
DR EMBL; AL713971; CAI17530.1; JOINED; Genomic_DNA.
DR EMBL; AL713971; CAI17656.1; -; Genomic_DNA.
DR EMBL; AL662827; CAI17656.1; JOINED; Genomic_DNA.
DR EMBL; AL645940; CAI18076.1; -; Genomic_DNA.
DR EMBL; AL662820; CAI18076.1; JOINED; Genomic_DNA.
DR EMBL; AL662820; CAI18127.1; -; Genomic_DNA.
DR EMBL; AL645940; CAI18127.1; JOINED; Genomic_DNA.
DR EMBL; AL844527; CAI41848.1; -; Genomic_DNA.
DR EMBL; CR759817; CAQ08021.1; -; Genomic_DNA.
DR EMBL; CR759786; CAQ08251.1; -; 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 PIR; S30393; S30393.
DR RefSeq; NP_072045.1; NM_022551.2.
DR UniGene; Hs.448854; -.
DR UniGene; Hs.627414; -.
DR PDB; 3J3A; EM; 5.00 A; S=1-152.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62269; -.
DR SMR; P62269; 6-142.
DR IntAct; P62269; 30.
DR MINT; MINT-1151113; -.
DR STRING; 9606.ENSP00000403175; -.
DR PhosphoSite; P62269; -.
DR DMDM; 50403625; -.
DR PaxDb; P62269; -.
DR PeptideAtlas; P62269; -.
DR PRIDE; P62269; -.
DR Ensembl; ENST00000211372; ENSP00000211372; ENSG00000096150.
DR Ensembl; ENST00000434122; ENSP00000403175; ENSG00000226225.
DR Ensembl; ENST00000439602; ENSP00000393241; ENSG00000231500.
DR Ensembl; ENST00000454021; ENSP00000416110; ENSG00000235650.
DR Ensembl; ENST00000457341; ENSP00000412583; ENSG00000223367.
DR GeneID; 6222; -.
DR KEGG; hsa:6222; -.
DR UCSC; uc003odp.1; human.
DR CTD; 6222; -.
DR GeneCards; GC06P033240; -.
DR GeneCards; GC06Pj33161; -.
DR GeneCards; GC06Pk33217; -.
DR GeneCards; GC06Pm33410; -.
DR GeneCards; GC06Pn33168; -.
DR HGNC; HGNC:10401; RPS18.
DR HPA; HPA050159; -.
DR MIM; 180473; gene.
DR neXtProt; NX_P62269; -.
DR PharmGKB; PA34801; -.
DR eggNOG; COG0099; -.
DR HOGENOM; HOG000039877; -.
DR HOVERGEN; HBG000200; -.
DR InParanoid; P62269; -.
DR KO; K02964; -.
DR OMA; IRAYRGI; -.
DR PhylomeDB; P62269; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPS18; -.
DR GenomeRNAi; 6222; -.
DR NextBio; 24155; -.
DR PRO; PR:P62269; -.
DR ArrayExpress; P62269; -.
DR Bgee; P62269; -.
DR CleanEx; HS_RPS18; -.
DR Genevestigator; P62269; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:RefGenome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:RefGenome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 152 40S ribosomal protein S18.
FT /FTId=PRO_0000132212.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 94 94 N6-acetyllysine.
FT MOD_RES 106 106 N6-acetyllysine.
FT CONFLICT 55 55 R -> S (in Ref. 6; AA sequence).
SQ SEQUENCE 152 AA; 17719 MW; 4DAF0662C3F37F22 CRC64;
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT
EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH
RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK
//
ID RS18_HUMAN Reviewed; 152 AA.
AC P62269; P25232; Q5SUJ3; Q6IPF8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=40S ribosomal protein S18;
DE AltName: Full=Ke-3;
DE Short=Ke3;
GN Name=RPS18; Synonyms=D6S218E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND 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.,
RA Egorov T.A., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-106, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [9]
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.,
RA Buerckstuemmer T., 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 [10]
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ribosomal protein S13P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X69150; CAB56794.1; -; mRNA.
DR EMBL; AL031228; CAA20231.1; -; Genomic_DNA.
DR EMBL; AL662827; CAI17530.1; -; Genomic_DNA.
DR EMBL; AL713971; CAI17530.1; JOINED; Genomic_DNA.
DR EMBL; AL713971; CAI17656.1; -; Genomic_DNA.
DR EMBL; AL662827; CAI17656.1; JOINED; Genomic_DNA.
DR EMBL; AL645940; CAI18076.1; -; Genomic_DNA.
DR EMBL; AL662820; CAI18076.1; JOINED; Genomic_DNA.
DR EMBL; AL662820; CAI18127.1; -; Genomic_DNA.
DR EMBL; AL645940; CAI18127.1; JOINED; Genomic_DNA.
DR EMBL; AL844527; CAI41848.1; -; Genomic_DNA.
DR EMBL; CR759817; CAQ08021.1; -; Genomic_DNA.
DR EMBL; CR759786; CAQ08251.1; -; 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 PIR; S30393; S30393.
DR RefSeq; NP_072045.1; NM_022551.2.
DR UniGene; Hs.448854; -.
DR UniGene; Hs.627414; -.
DR PDB; 3J3A; EM; 5.00 A; S=1-152.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P62269; -.
DR SMR; P62269; 6-142.
DR IntAct; P62269; 30.
DR MINT; MINT-1151113; -.
DR STRING; 9606.ENSP00000403175; -.
DR PhosphoSite; P62269; -.
DR DMDM; 50403625; -.
DR PaxDb; P62269; -.
DR PeptideAtlas; P62269; -.
DR PRIDE; P62269; -.
DR Ensembl; ENST00000211372; ENSP00000211372; ENSG00000096150.
DR Ensembl; ENST00000434122; ENSP00000403175; ENSG00000226225.
DR Ensembl; ENST00000439602; ENSP00000393241; ENSG00000231500.
DR Ensembl; ENST00000454021; ENSP00000416110; ENSG00000235650.
DR Ensembl; ENST00000457341; ENSP00000412583; ENSG00000223367.
DR GeneID; 6222; -.
DR KEGG; hsa:6222; -.
DR UCSC; uc003odp.1; human.
DR CTD; 6222; -.
DR GeneCards; GC06P033240; -.
DR GeneCards; GC06Pj33161; -.
DR GeneCards; GC06Pk33217; -.
DR GeneCards; GC06Pm33410; -.
DR GeneCards; GC06Pn33168; -.
DR HGNC; HGNC:10401; RPS18.
DR HPA; HPA050159; -.
DR MIM; 180473; gene.
DR neXtProt; NX_P62269; -.
DR PharmGKB; PA34801; -.
DR eggNOG; COG0099; -.
DR HOGENOM; HOG000039877; -.
DR HOVERGEN; HBG000200; -.
DR InParanoid; P62269; -.
DR KO; K02964; -.
DR OMA; IRAYRGI; -.
DR PhylomeDB; P62269; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPS18; -.
DR GenomeRNAi; 6222; -.
DR NextBio; 24155; -.
DR PRO; PR:P62269; -.
DR ArrayExpress; P62269; -.
DR Bgee; P62269; -.
DR CleanEx; HS_RPS18; -.
DR Genevestigator; P62269; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:RefGenome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:RefGenome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 152 40S ribosomal protein S18.
FT /FTId=PRO_0000132212.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 94 94 N6-acetyllysine.
FT MOD_RES 106 106 N6-acetyllysine.
FT CONFLICT 55 55 R -> S (in Ref. 6; AA sequence).
SQ SEQUENCE 152 AA; 17719 MW; 4DAF0662C3F37F22 CRC64;
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT
EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH
RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK
//
MIM
180473
*RECORD*
*FIELD* NO
180473
*FIELD* TI
*180473 RIBOSOMAL PROTEIN S18; RPS18
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
In a search for new genes preferentially expressed in cytotrophoblasts
of first-trimester human placenta, Chassin et al. (1993) made a
subtracted cDNA library and found clones with an open reading frame
showing a sequence that predicted a protein with 100% amino acid
homology to the mouse ke3 gene product. The Ke3 gene in the mouse is
located in the major histocompatibility complex. The deduced RPS18
protein has 152 amino acids (SWISS-PROT SWISSPROT P25232).
In their GenBank submission (GENBANK X69150), Chassin et al. (1993)
noted that the RPS18 gene maps to 6p21.3. Kenmochi et al. (1998) mapped
the RPS18 gene to 6p using somatic cell hybrid and radiation hybrid
mapping analyses.
*FIELD* RF
1. Chassin, D.; Bellet, D.; Koman, A.: The human homolog of ribosomal
protein S18. Nucleic Acids Res. 21: 745 only, 1993.
2. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
*FIELD* CN
Patti M. Sherman - updated: 3/30/1999
*FIELD* CD
Victor A. McKusick: 9/15/1993
*FIELD* ED
carol: 03/31/1999
psherman: 3/30/1999
carol: 9/15/1993
*RECORD*
*FIELD* NO
180473
*FIELD* TI
*180473 RIBOSOMAL PROTEIN S18; RPS18
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins.
In a search for new genes preferentially expressed in cytotrophoblasts
of first-trimester human placenta, Chassin et al. (1993) made a
subtracted cDNA library and found clones with an open reading frame
showing a sequence that predicted a protein with 100% amino acid
homology to the mouse ke3 gene product. The Ke3 gene in the mouse is
located in the major histocompatibility complex. The deduced RPS18
protein has 152 amino acids (SWISS-PROT SWISSPROT P25232).
In their GenBank submission (GENBANK X69150), Chassin et al. (1993)
noted that the RPS18 gene maps to 6p21.3. Kenmochi et al. (1998) mapped
the RPS18 gene to 6p using somatic cell hybrid and radiation hybrid
mapping analyses.
*FIELD* RF
1. Chassin, D.; Bellet, D.; Koman, A.: The human homolog of ribosomal
protein S18. Nucleic Acids Res. 21: 745 only, 1993.
2. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
*FIELD* CN
Patti M. Sherman - updated: 3/30/1999
*FIELD* CD
Victor A. McKusick: 9/15/1993
*FIELD* ED
carol: 03/31/1999
psherman: 3/30/1999
carol: 9/15/1993