Full text data of RPS3
RPS3
[Confidence: high (present in two of the MS resources)]
40S ribosomal protein S3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00011253
IPI00011253 40S ribosomal protein S3 cytosolic small ribosomal subunit, RNA binding ,structural constituent of ribosome,protein biosynthesis soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00011253 40S ribosomal protein S3 cytosolic small ribosomal subunit, RNA binding ,structural constituent of ribosome,protein biosynthesis soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P23396
ID RS3_HUMAN Reviewed; 243 AA.
AC P23396; B2R7N5; J3KN86; Q498B5; Q8NI95;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 2.
DT 22-JAN-2014, entry version 160.
DE RecName: Full=40S ribosomal protein S3;
GN Name=RPS3; ORFNames=OK/SW-cl.26;
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] (ISOFORM 1).
RX PubMed=2129557; DOI=10.1093/nar/18.22.6689;
RA Zhang X.T., Tan Y.M., Tan Y.H.;
RT "Isolation of a cDNA encoding human 40S ribosomal protein s3.";
RL Nucleic Acids Res. 18:6689-6689(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1712897;
RA Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G.,
RA Meisler A.I., Pipas J.M.;
RT "Ribosomal protein genes are overexpressed in colorectal cancer:
RT isolation of a cDNA clone encoding the human S3 ribosomal protein.";
RL Mol. Cell. Biol. 11:3842-3849(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal cortex, Liver, Lymph, Skin, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
RX PubMed=8319909;
RA Tycowski K.T., Shu M.D., Steitz J.A.;
RT "A small nucleolar RNA is processed from an intron of the human gene
RT encoding ribosomal protein S3.";
RL Genes Dev. 7:1176-1190(1993).
RN [10]
RP PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND
RP 202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F.,
RA Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243 (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132;
RP 152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 188-197.
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [17]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [22]
RP IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
RX PubMed=19541769; DOI=10.1261/rna.1578409;
RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E.,
RA Ostareck-Lederer A., Ostareck D.H.;
RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the
RT 3'UTR.";
RL RNA 15:1528-1542(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND MASS 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP STRUCTURE BY NMR OF 17-95.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the KH domain of human ribosomal protein S3.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [30]
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 -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Identified in a HCV IRES-mediated
CC translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and
CC HCV RNA-replicon.
CC -!- INTERACTION:
CC O14920:IKBKB; NbExp=4; IntAct=EBI-351193, EBI-81266;
CC Q15843:NEDD8; NbExp=2; IntAct=EBI-351193, EBI-716247;
CC P19838:NFKB1; NbExp=2; IntAct=EBI-351193, EBI-300010;
CC Q08752:PPID; NbExp=4; IntAct=EBI-351193, EBI-716596;
CC Q04206:RELA; NbExp=6; IntAct=EBI-351193, EBI-73886;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-351193, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23396-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23396-2; Sequence=VSP_046667;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ribosomal protein S3P family.
CC -!- SIMILARITY: Contains 1 KH type-2 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB93471.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rps3/";
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DR EMBL; U14990; AAB60336.1; -; mRNA.
DR EMBL; U14991; AAB60337.1; -; mRNA.
DR EMBL; U14992; AAB60338.1; -; mRNA.
DR EMBL; X55715; CAA39248.1; -; mRNA.
DR EMBL; S42658; AAB19349.2; -; mRNA.
DR EMBL; AB061838; BAB79476.1; -; Genomic_DNA.
DR EMBL; AY791291; AAV40835.1; -; Genomic_DNA.
DR EMBL; AK313051; BAG35882.1; -; mRNA.
DR EMBL; AP000744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74963.1; -; Genomic_DNA.
DR EMBL; BC003137; AAH03137.1; -; mRNA.
DR EMBL; BC003577; AAH03577.1; -; mRNA.
DR EMBL; BC013196; AAH13196.1; -; mRNA.
DR EMBL; BC034149; AAH34149.1; -; mRNA.
DR EMBL; BC071917; AAH71917.1; -; mRNA.
DR EMBL; BC100284; AAI00285.1; -; mRNA.
DR EMBL; L16016; AAA18095.1; -; Genomic_DNA.
DR EMBL; AB062288; BAB93471.1; ALT_INIT; mRNA.
DR PIR; A41247; R3HUS3.
DR RefSeq; NP_000996.2; NM_001005.4.
DR RefSeq; NP_001243731.1; NM_001256802.1.
DR RefSeq; NP_001247435.1; NM_001260506.1.
DR RefSeq; NP_001247436.1; NM_001260507.1.
DR RefSeq; XP_005274220.1; XM_005274163.1.
DR UniGene; Hs.546286; -.
DR UniGene; Hs.740358; -.
DR PDB; 1WH9; NMR; -; A=17-95.
DR PDB; 3J3A; EM; 5.00 A; D=1-243.
DR PDBsum; 1WH9; -.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P23396; -.
DR SMR; P23396; 1-227.
DR IntAct; P23396; 42.
DR MINT; MINT-4999144; -.
DR STRING; 9606.ENSP00000278572; -.
DR PhosphoSite; P23396; -.
DR DMDM; 417719; -.
DR PaxDb; P23396; -.
DR PeptideAtlas; P23396; -.
DR PRIDE; P23396; -.
DR DNASU; 6188; -.
DR Ensembl; ENST00000278572; ENSP00000278572; ENSG00000149273.
DR Ensembl; ENST00000524851; ENSP00000433821; ENSG00000149273.
DR Ensembl; ENST00000527446; ENSP00000436971; ENSG00000149273.
DR Ensembl; ENST00000531188; ENSP00000434643; ENSG00000149273.
DR GeneID; 6188; -.
DR KEGG; hsa:6188; -.
DR UCSC; uc031qcs.1; human.
DR CTD; 6188; -.
DR GeneCards; GC11P075110; -.
DR HGNC; HGNC:10420; RPS3.
DR MIM; 600454; gene.
DR neXtProt; NX_P23396; -.
DR PharmGKB; PA34829; -.
DR eggNOG; COG0092; -.
DR HOGENOM; HOG000210611; -.
DR HOVERGEN; HBG002195; -.
DR InParanoid; P23396; -.
DR KO; K02985; -.
DR OMA; CNDYVET; -.
DR OrthoDB; EOG7F7W9M; -.
DR PhylomeDB; P23396; -.
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 ChiTaRS; RpS3; human.
DR EvolutionaryTrace; P23396; -.
DR GeneWiki; RPS3; -.
DR GenomeRNAi; 6188; -.
DR NextBio; 24029; -.
DR PRO; PR:P23396; -.
DR ArrayExpress; P23396; -.
DR Bgee; P23396; -.
DR CleanEx; HS_RPS3; -.
DR Genevestigator; P23396; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IMP:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; NAS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0045738; P:negative regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
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; NAS:UniProtKB.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_prok-type.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR018280; Ribosomal_S3_CS.
DR InterPro; IPR005703; Ribosomal_S3_euk/arc.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01008; rpsC_E_A; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 243 40S ribosomal protein S3.
FT /FTId=PRO_0000130320.
FT DOMAIN 21 92 KH type-2.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 62 62 N6-acetyllysine.
FT MOD_RES 221 221 Phosphothreonine.
FT MOD_RES 224 224 Phosphoserine.
FT MOD_RES 242 242 Phosphothreonine.
FT CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 85 85 E -> ELKIMVMVTGYPLLPLK (in isoform 2).
FT /FTId=VSP_046667.
FT CONFLICT 8 8 K -> R (in Ref. 2; AAB19349).
FT CONFLICT 104 104 S -> C (in Ref. 1; CAA39248).
FT CONFLICT 233 233 P -> L (in Ref. 1; CAA39248).
FT HELIX 17 28
FT TURN 29 33
FT STRAND 34 41
FT STRAND 46 53
FT HELIX 55 59
FT HELIX 61 63
FT HELIX 64 77
FT STRAND 83 90
SQ SEQUENCE 243 AA; 26688 MW; 6ECBB34A8EE04AAF CRC64;
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG
VLGIKVKIML PWDPTGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV
PTA
//
ID RS3_HUMAN Reviewed; 243 AA.
AC P23396; B2R7N5; J3KN86; Q498B5; Q8NI95;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 2.
DT 22-JAN-2014, entry version 160.
DE RecName: Full=40S ribosomal protein S3;
GN Name=RPS3; ORFNames=OK/SW-cl.26;
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] (ISOFORM 1).
RX PubMed=2129557; DOI=10.1093/nar/18.22.6689;
RA Zhang X.T., Tan Y.M., Tan Y.H.;
RT "Isolation of a cDNA encoding human 40S ribosomal protein s3.";
RL Nucleic Acids Res. 18:6689-6689(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1712897;
RA Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G.,
RA Meisler A.I., Pipas J.M.;
RT "Ribosomal protein genes are overexpressed in colorectal cancer:
RT isolation of a cDNA clone encoding the human S3 ribosomal protein.";
RL Mol. Cell. Biol. 11:3842-3849(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal cortex, Liver, Lymph, Skin, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
RX PubMed=8319909;
RA Tycowski K.T., Shu M.D., Steitz J.A.;
RT "A small nucleolar RNA is processed from an intron of the human gene
RT encoding ribosomal protein S3.";
RL Genes Dev. 7:1176-1190(1993).
RN [10]
RP PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND
RP 202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F.,
RA Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243 (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132;
RP 152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 188-197.
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [17]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [22]
RP IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
RX PubMed=19541769; DOI=10.1261/rna.1578409;
RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E.,
RA Ostareck-Lederer A., Ostareck D.H.;
RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the
RT 3'UTR.";
RL RNA 15:1528-1542(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND MASS 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP STRUCTURE BY NMR OF 17-95.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the KH domain of human ribosomal protein S3.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [30]
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 -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Identified in a HCV IRES-mediated
CC translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and
CC HCV RNA-replicon.
CC -!- INTERACTION:
CC O14920:IKBKB; NbExp=4; IntAct=EBI-351193, EBI-81266;
CC Q15843:NEDD8; NbExp=2; IntAct=EBI-351193, EBI-716247;
CC P19838:NFKB1; NbExp=2; IntAct=EBI-351193, EBI-300010;
CC Q08752:PPID; NbExp=4; IntAct=EBI-351193, EBI-716596;
CC Q04206:RELA; NbExp=6; IntAct=EBI-351193, EBI-73886;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-351193, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23396-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23396-2; Sequence=VSP_046667;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ribosomal protein S3P family.
CC -!- SIMILARITY: Contains 1 KH type-2 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB93471.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rps3/";
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DR EMBL; U14990; AAB60336.1; -; mRNA.
DR EMBL; U14991; AAB60337.1; -; mRNA.
DR EMBL; U14992; AAB60338.1; -; mRNA.
DR EMBL; X55715; CAA39248.1; -; mRNA.
DR EMBL; S42658; AAB19349.2; -; mRNA.
DR EMBL; AB061838; BAB79476.1; -; Genomic_DNA.
DR EMBL; AY791291; AAV40835.1; -; Genomic_DNA.
DR EMBL; AK313051; BAG35882.1; -; mRNA.
DR EMBL; AP000744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74963.1; -; Genomic_DNA.
DR EMBL; BC003137; AAH03137.1; -; mRNA.
DR EMBL; BC003577; AAH03577.1; -; mRNA.
DR EMBL; BC013196; AAH13196.1; -; mRNA.
DR EMBL; BC034149; AAH34149.1; -; mRNA.
DR EMBL; BC071917; AAH71917.1; -; mRNA.
DR EMBL; BC100284; AAI00285.1; -; mRNA.
DR EMBL; L16016; AAA18095.1; -; Genomic_DNA.
DR EMBL; AB062288; BAB93471.1; ALT_INIT; mRNA.
DR PIR; A41247; R3HUS3.
DR RefSeq; NP_000996.2; NM_001005.4.
DR RefSeq; NP_001243731.1; NM_001256802.1.
DR RefSeq; NP_001247435.1; NM_001260506.1.
DR RefSeq; NP_001247436.1; NM_001260507.1.
DR RefSeq; XP_005274220.1; XM_005274163.1.
DR UniGene; Hs.546286; -.
DR UniGene; Hs.740358; -.
DR PDB; 1WH9; NMR; -; A=17-95.
DR PDB; 3J3A; EM; 5.00 A; D=1-243.
DR PDBsum; 1WH9; -.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P23396; -.
DR SMR; P23396; 1-227.
DR IntAct; P23396; 42.
DR MINT; MINT-4999144; -.
DR STRING; 9606.ENSP00000278572; -.
DR PhosphoSite; P23396; -.
DR DMDM; 417719; -.
DR PaxDb; P23396; -.
DR PeptideAtlas; P23396; -.
DR PRIDE; P23396; -.
DR DNASU; 6188; -.
DR Ensembl; ENST00000278572; ENSP00000278572; ENSG00000149273.
DR Ensembl; ENST00000524851; ENSP00000433821; ENSG00000149273.
DR Ensembl; ENST00000527446; ENSP00000436971; ENSG00000149273.
DR Ensembl; ENST00000531188; ENSP00000434643; ENSG00000149273.
DR GeneID; 6188; -.
DR KEGG; hsa:6188; -.
DR UCSC; uc031qcs.1; human.
DR CTD; 6188; -.
DR GeneCards; GC11P075110; -.
DR HGNC; HGNC:10420; RPS3.
DR MIM; 600454; gene.
DR neXtProt; NX_P23396; -.
DR PharmGKB; PA34829; -.
DR eggNOG; COG0092; -.
DR HOGENOM; HOG000210611; -.
DR HOVERGEN; HBG002195; -.
DR InParanoid; P23396; -.
DR KO; K02985; -.
DR OMA; CNDYVET; -.
DR OrthoDB; EOG7F7W9M; -.
DR PhylomeDB; P23396; -.
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 ChiTaRS; RpS3; human.
DR EvolutionaryTrace; P23396; -.
DR GeneWiki; RPS3; -.
DR GenomeRNAi; 6188; -.
DR NextBio; 24029; -.
DR PRO; PR:P23396; -.
DR ArrayExpress; P23396; -.
DR Bgee; P23396; -.
DR CleanEx; HS_RPS3; -.
DR Genevestigator; P23396; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IMP:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; NAS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0045738; P:negative regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
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; NAS:UniProtKB.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_prok-type.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR018280; Ribosomal_S3_CS.
DR InterPro; IPR005703; Ribosomal_S3_euk/arc.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01008; rpsC_E_A; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 243 40S ribosomal protein S3.
FT /FTId=PRO_0000130320.
FT DOMAIN 21 92 KH type-2.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 62 62 N6-acetyllysine.
FT MOD_RES 221 221 Phosphothreonine.
FT MOD_RES 224 224 Phosphoserine.
FT MOD_RES 242 242 Phosphothreonine.
FT CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 85 85 E -> ELKIMVMVTGYPLLPLK (in isoform 2).
FT /FTId=VSP_046667.
FT CONFLICT 8 8 K -> R (in Ref. 2; AAB19349).
FT CONFLICT 104 104 S -> C (in Ref. 1; CAA39248).
FT CONFLICT 233 233 P -> L (in Ref. 1; CAA39248).
FT HELIX 17 28
FT TURN 29 33
FT STRAND 34 41
FT STRAND 46 53
FT HELIX 55 59
FT HELIX 61 63
FT HELIX 64 77
FT STRAND 83 90
SQ SEQUENCE 243 AA; 26688 MW; 6ECBB34A8EE04AAF CRC64;
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG
VLGIKVKIML PWDPTGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV
PTA
//
MIM
600454
*RECORD*
*FIELD* NO
600454
*FIELD* TI
*600454 RIBOSOMAL PROTEIN S3; RPS3
*FIELD* TX
The ribosomal protein S3 has 2 apparently distinct functions: (1) as a
read moreribosomal protein, RPS3 contributes to the domain of the ribosome where
translation is initiated, and (2) as an endonuclease, RPS3 apparently
participates in repair of UV damage. Moreover, the first intron of human
RPS3 transcripts is processed to generate U15A (600455), a small
nucleolar RNA ('snoRNA') (Tycowski et al., 1993). Thus, this is an
example of nested genes or a gene within a gene.
Zhang et al. (1990) isolated a human epithelial cDNA encoding RPS3. The
deduced RPS3 protein has 243 amino acids. Northern blot analysis
indicated that RPS3 is expressed as an approximately 900-bp transcript.
To search for genes whose level of expression changes during
tumorigenesis, Pogue-Geile et al. (1991) screened a cDNA library derived
from a colon adenocarcinoma with cDNAs prepared from the carcinoma and
from adjacent normal mucosa. They isolated cDNAs encoding RPS3. Northern
blot analysis detected a 1-kb RPS3 transcript which was more abundant in
8 of 8 colon adenocarcinomas and 7 of 10 adenomatous polyps relative to
adjacent normal colonic mucosa. The predicted RPS3 protein had no
obvious structural motifs. The human and rat RPS3 coding sequences are
90% identical, and the encoded proteins differ by only 1 amino acid.
By a combination of somatic cell hybrid analysis, fluorescence in situ
hybridization, and YAC/STS content mapping, Polakiewicz et al. (1995)
demonstrated that the RPS3/U15A genes map to the immediate vicinity of
D11S356 and D11S533 on 11q13.3-q13.5. Kenmochi et al. (1998) confirmed
the mapping assignment reported by Polakiewicz et al. (1995).
*FIELD* RF
1. 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.
2. Pogue-Geile, K.; Geiser, J. R.; Shu, M.; Miller, C.; Wool, I. G.;
Meisler, A. I.; Pipas, J. M.: Ribosomal protein genes are overexpressed
in colorectal cancer: isolation of a cDNA clone encoding the human
S3 ribosomal protein. Molec. Cell. Biol. 11: 3842-3849, 1991.
3. Polakiewicz, R. D.; Munroe, D. J.; Jani Sait, S. N.; Tycowski,
K. T.; Nowak, N. J.; Shows, T. B.; Housman, D. E.; Page, D. C.: Mapping
of ribosomal protein S3 and internally nested snoRNA U15A gene to
human chromosome 11q13.3-q13.5. Genomics 25: 577-580, 1995.
4. Tycowski, K. T.; Shu, M. D.; Steitz, J. A.: A small nucleolar
RNA is processed from an intron of the human gene encoding ribosomal
protein S3. Genes Dev. 7: 1176-1190, 1993.
5. Zhang, X. T.; Tan, Y.-M.; Tan, Y. H.: Isolation of a cDNA encoding
human 40S ribosomal protein S3. Nucleic Acids Res. 18: 6689 only,
1990.
*FIELD* CN
Patti M. Sherman - updated: 3/23/1999
*FIELD* CD
Victor A. McKusick: 3/9/1995
*FIELD* ED
carol: 04/01/1999
carol: 3/10/1995
carol: 3/9/1995
*RECORD*
*FIELD* NO
600454
*FIELD* TI
*600454 RIBOSOMAL PROTEIN S3; RPS3
*FIELD* TX
The ribosomal protein S3 has 2 apparently distinct functions: (1) as a
read moreribosomal protein, RPS3 contributes to the domain of the ribosome where
translation is initiated, and (2) as an endonuclease, RPS3 apparently
participates in repair of UV damage. Moreover, the first intron of human
RPS3 transcripts is processed to generate U15A (600455), a small
nucleolar RNA ('snoRNA') (Tycowski et al., 1993). Thus, this is an
example of nested genes or a gene within a gene.
Zhang et al. (1990) isolated a human epithelial cDNA encoding RPS3. The
deduced RPS3 protein has 243 amino acids. Northern blot analysis
indicated that RPS3 is expressed as an approximately 900-bp transcript.
To search for genes whose level of expression changes during
tumorigenesis, Pogue-Geile et al. (1991) screened a cDNA library derived
from a colon adenocarcinoma with cDNAs prepared from the carcinoma and
from adjacent normal mucosa. They isolated cDNAs encoding RPS3. Northern
blot analysis detected a 1-kb RPS3 transcript which was more abundant in
8 of 8 colon adenocarcinomas and 7 of 10 adenomatous polyps relative to
adjacent normal colonic mucosa. The predicted RPS3 protein had no
obvious structural motifs. The human and rat RPS3 coding sequences are
90% identical, and the encoded proteins differ by only 1 amino acid.
By a combination of somatic cell hybrid analysis, fluorescence in situ
hybridization, and YAC/STS content mapping, Polakiewicz et al. (1995)
demonstrated that the RPS3/U15A genes map to the immediate vicinity of
D11S356 and D11S533 on 11q13.3-q13.5. Kenmochi et al. (1998) confirmed
the mapping assignment reported by Polakiewicz et al. (1995).
*FIELD* RF
1. 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.
2. Pogue-Geile, K.; Geiser, J. R.; Shu, M.; Miller, C.; Wool, I. G.;
Meisler, A. I.; Pipas, J. M.: Ribosomal protein genes are overexpressed
in colorectal cancer: isolation of a cDNA clone encoding the human
S3 ribosomal protein. Molec. Cell. Biol. 11: 3842-3849, 1991.
3. Polakiewicz, R. D.; Munroe, D. J.; Jani Sait, S. N.; Tycowski,
K. T.; Nowak, N. J.; Shows, T. B.; Housman, D. E.; Page, D. C.: Mapping
of ribosomal protein S3 and internally nested snoRNA U15A gene to
human chromosome 11q13.3-q13.5. Genomics 25: 577-580, 1995.
4. Tycowski, K. T.; Shu, M. D.; Steitz, J. A.: A small nucleolar
RNA is processed from an intron of the human gene encoding ribosomal
protein S3. Genes Dev. 7: 1176-1190, 1993.
5. Zhang, X. T.; Tan, Y.-M.; Tan, Y. H.: Isolation of a cDNA encoding
human 40S ribosomal protein S3. Nucleic Acids Res. 18: 6689 only,
1990.
*FIELD* CN
Patti M. Sherman - updated: 3/23/1999
*FIELD* CD
Victor A. McKusick: 3/9/1995
*FIELD* ED
carol: 04/01/1999
carol: 3/10/1995
carol: 3/9/1995