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40S ribosomal protein S3 (EC 4.2.99.18) (Small ribosomal subunit protein uS3)

 RS3_HUMAN               Reviewed;         243 AA.
P23396; B2R7N5; J3KN86; Q498B5; Q8NI95;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 2.
30-AUG-2017, entry version 200.
RecName: Full=40S ribosomal protein S3;
EC=4.2.99.18 {ECO:0000269|PubMed:7775413};
AltName: Full=Small ribosomal subunit protein uS3 {ECO:0000303|PubMed:24524803};
Name=RPS3; ORFNames=OK/SW-cl.26;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2129557; DOI=10.1093/nar/18.22.6689;
Zhang X.T., Tan Y.M., Tan Y.H.;
"Isolation of a cDNA encoding human 40S ribosomal protein s3.";
Nucleic Acids Res. 18:6689-6689(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1712897; DOI=10.1128/MCB.11.8.3842;
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.";
Mol. Cell. Biol. 11:3842-3849(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11875025; DOI=10.1101/gr.214202;
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
"The human ribosomal protein genes: sequencing and comparative
analysis of 73 genes.";
Genome Res. 12:379-390(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal cortex, Liver, Lymph, Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
PubMed=8319909; DOI=10.1101/gad.7.7a.1176;
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).
[10]
PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND
202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, and Colon adenocarcinoma;
Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F.,
Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243 (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[12]
PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132;
152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 188-197.
TISSUE=Placenta;
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=7775413; DOI=10.1074/jbc.270.23.13620;
Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.;
"Implication of mammalian ribosomal protein S3 in the processing of
DNA damage.";
J. Biol. Chem. 270:13620-13629(1995).
[15]
FUNCTION, AND INTERACTION WITH APEX1 AND OGG1.
PubMed=15518571; DOI=10.1021/bi049234b;
Hegde V., Wang M., Deutsch W.A.;
"Human ribosomal protein S3 interacts with DNA base excision repair
proteins hAPE/Ref-1 and hOGG1.";
Biochemistry 43:14211-14217(2004).
[16]
FUNCTION.
PubMed=14706345; DOI=10.1016/j.dnarep.2003.10.004;
Hegde V., Wang M., Deutsch W.A.;
"Characterization of human ribosomal protein S3 binding to 7,8-
dihydro-8-oxoguanine and abasic sites by surface plasmon resonance.";
DNA Repair 3:121-126(2004).
[17]
FUNCTION.
PubMed=14988002; DOI=10.1016/S0014-5793(04)00074-2;
Jang C.Y., Lee J.Y., Kim J.;
"RpS3, a DNA repair endonuclease and ribosomal protein, is involved in
apoptosis.";
FEBS Lett. 560:81-85(2004).
[18]
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15707971; DOI=10.1016/j.bbrc.2005.01.045;
Kim S.H., Lee J.Y., Kim J.;
"Characterization of a wide range base-damage-endonuclease activity of
mammalian rpS3.";
Biochem. Biophys. Res. Commun. 328:962-967(2005).
[19]
PHOSPHORYLATION AT THR-42, AND MUTAGENESIS OF THR-42 AND THR-221.
PubMed=15950189; DOI=10.1016/j.bbrc.2005.05.079;
Kim H.D., Lee J.Y., Kim J.;
"Erk phosphorylates threonine 42 residue of ribosomal protein S3.";
Biochem. Biophys. Res. Commun. 333:110-115(2005).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
MUTAGENESIS OF LYS-132.
PubMed=16737853; DOI=10.1016/j.dnarep.2006.04.001;
Hegde V., Wang M., Mian I.S., Spyres L., Deutsch W.A.;
"The high binding affinity of human ribosomal protein S3 to 7,8-
dihydro-8-oxoguanine is abrogated by a single amino acid change.";
DNA Repair 5:810-815(2006).
[22]
INTERACTION WITH HSP90, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=16314389; DOI=10.1091/mbc.E05-08-0713;
Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.;
"Interaction of Hsp90 with ribosomal proteins protects from
ubiquitination and proteasome-dependent degradation.";
Mol. Biol. Cell 17:824-833(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[25]
FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B
P65-P50 COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18045535; DOI=10.1016/j.cell.2007.10.009;
Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L.,
Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A.,
Lenardo M.J.;
"Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that
mediates selective gene regulation.";
Cell 131:927-939(2007).
[26]
FUNCTION.
PubMed=17049931; DOI=10.1016/j.dnarep.2006.09.004;
Hegde V., Yadavilli S., Deutsch W.A.;
"Knockdown of ribosomal protein S3 protects human cells from genotoxic
stress.";
DNA Repair 6:94-99(2007).
[27]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF THR-42.
PubMed=17560175; DOI=10.1016/j.dnarep.2007.04.009;
Yadavilli S., Hegde V., Deutsch W.A.;
"Translocation of human ribosomal protein S3 to sites of DNA damage is
dependant on ERK-mediated phosphorylation following genotoxic
stress.";
DNA Repair 6:1453-1462(2007).
[28]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[29]
FUNCTION.
PubMed=18610840;
Balyeva K.E., Malygin A.A., Karpova G.G., Nevinskii G.A.,
Zharkov D.O.;
"Interactions of human ribosomal protein S3 with undamaged and damaged
DNA.";
Mol. Biol. (Mosk.) 42:314-322(2008).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[31]
FUNCTION, AND INTERACTION WITH UNG.
PubMed=18973764; DOI=10.1016/j.mrfmmm.2008.09.013;
Ko S.I., Park J.H., Park M.J., Kim J., Kang L.W., Han Y.S.;
"Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA
glycosylase (hUNG) and stimulates its glycosylase activity.";
Mutat. Res. 648:54-64(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[34]
INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, AND METHYLATION AT
ARG-64; ARG-65 AND ARG-67.
PubMed=19460357; DOI=10.1016/j.bbrc.2009.05.055;
Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.;
"Arginine methylation of ribosomal protein S3 affects ribosome
assembly.";
Biochem. Biophys. Res. Commun. 385:273-278(2009).
[35]
INTERACTION WITH PRKCD, PHOSPHORYLATION AT SER-6 AND THR-221, AND
MUTAGENESIS OF SER-6; SER-35; THR-42; THR-70; SER-139; SER-149;
THR-195 AND THR-221.
PubMed=19059439; DOI=10.1016/j.bbamcr.2008.10.017;
Kim T.S., Kim H.D., Kim J.;
"PKCdelta-dependent functional switch of rpS3 between translation and
DNA repair.";
Biochim. Biophys. Acta 1793:395-405(2009).
[36]
FUNCTION, INTERACTION WITH MDM2 AND TP53, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19656744; DOI=10.1016/j.dnarep.2009.07.003;
Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A.;
"Ribosomal protein S3: A multi-functional protein that interacts with
both p53 and MDM2 through its KH domain.";
DNA Repair 8:1215-1224(2009).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[38]
INTERACTION WITH E.COLI NLEH1 AND NLEH2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20041225; DOI=10.1371/journal.ppat.1000708;
Gao X., Wan F., Mateo K., Callegari E., Wang D., Deng W., Puente J.,
Li F., Chaussee M.S., Finlay B.B., Lenardo M.J., Hardwidge P.R.;
"Bacterial effector binding to ribosomal protein s3 subverts NF-kappaB
function.";
PLoS Pathog. 5:E1000708-E1000708(2009).
[39]
IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
PubMed=19541769; DOI=10.1261/rna.1578409;
Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E.,
Ostareck-Lederer A., Ostareck D.H.;
"IGF2BP1 enhances HCV IRES-mediated translation initiation via the
3'UTR.";
RNA 15:1528-1542(2009).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[42]
INTERACTION WITH E2F1 AND PKB, PHOSPHORYLATION AT THR-70, AND
MUTAGENESIS OF THR-70.
PubMed=20605787; DOI=10.1074/jbc.M110.131367;
Lee S.B., Kwon I.S., Park J., Lee K.H., Ahn Y., Lee C., Kim J.,
Choi S.Y., Cho S.W., Ahn J.Y.;
"Ribosomal protein S3, a new substrate of Akt, serves as a signal
mediator between neuronal apoptosis and DNA repair.";
J. Biol. Chem. 285:29457-29468(2010).
[43]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20217897; DOI=10.1002/jcb.22537;
Kim H.D., Kim T.S., Joo Y.J., Shin H.S., Kim S.H., Jang C.Y.,
Lee C.E., Kim J.;
"RpS3 translation is repressed by interaction with its own mRNA.";
J. Cell. Biochem. 110:294-303(2010).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[46]
INTERACTION WITH SUMO1 AND UBC9, SUMOYLATION AT LYS-18; LYS-214 AND
LYS-230, AND MUTAGENESIS OF LYS-18; LYS-214 AND LYS-230.
PubMed=21968017; DOI=10.1016/j.bbrc.2011.09.099;
Jang C.Y., Shin H.S., Kim H.D., Kim J.W., Choi S.Y., Kim J.;
"Ribosomal protein S3 is stabilized by sumoylation.";
Biochem. Biophys. Res. Commun. 414:523-527(2011).
[47]
INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
THR-221, AND MUTAGENESIS OF SER-6; THR-42 AND THR-221.
PubMed=21871177; DOI=10.5483/BMBRep.2011.44.8.529;
Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I.,
Kang L.W., Kim T.S., Kim J., Han Y.S.;
"Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M
phase.";
BMB Rep. 44:529-534(2011).
[48]
INTERACTION WITH IKKB AND E.COLI NLEH1, PHOSPHORYLATION AT SER-209,
AND MUTAGENESIS OF SER-209.
PubMed=21399639; DOI=10.1038/ni.2007;
Wan F., Weaver A., Gao X., Bern M., Hardwidge P.R., Lenardo M.J.;
"IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-
kappaB function during infection with Escherichia coli strain
O157:H7.";
Nat. Immunol. 12:335-343(2011).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[50]
FUNCTION, AND INTERACTION WITH TRADD.
PubMed=22510408; DOI=10.1016/j.bbrc.2012.04.020;
Jang C.Y., Kim H.D., Kim J.;
"Ribosomal protein S3 interacts with TRADD to induce apoptosis through
caspase dependent JNK activation.";
Biochem. Biophys. Res. Commun. 421:474-478(2012).
[51]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23131551; DOI=10.1016/j.bbrc.2012.10.093;
Jang C.Y., Kim H.D., Zhang X., Chang J.S., Kim J.;
"Ribosomal protein S3 localizes on the mitotic spindle and functions
as a microtubule associated protein in mitosis.";
Biochem. Biophys. Res. Commun. 429:57-62(2012).
[52]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[53]
FUNCTION, INTERACTION WITH TOM70, AND SUBCELLULAR LOCATION.
PubMed=23911537; DOI=10.1016/j.bbamcr.2013.07.015;
Kim Y., Kim H.D., Kim J.;
"Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in
mitochondrial DNA damage surveillance.";
Biochim. Biophys. Acta 1833:2943-2952(2013).
[54]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-104; THR-220 AND
THR-221, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[55]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[56]
INTERACTION WITH NFKBIA.
PubMed=24457201; DOI=10.1016/j.febslet.2013.12.034;
Stanborough T., Niederhauser J., Koch B., Bergler H., Pertschy B.;
"Ribosomal protein S3 interacts with the NF-kappaB inhibitor
IkappaBalpha.";
FEBS Lett. 588:659-664(2014).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND THR-242, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[58]
INTERACTION WITH HNRPD.
PubMed=24423872; DOI=10.1093/nar/gkt1379;
Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
Hong K.Y., Jang S.K., Kim K.T.;
"AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
translation.";
Nucleic Acids Res. 42:3590-3606(2014).
[59]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[60]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[61]
UBIQUITINATION AT LYS-214.
PubMed=28065601; DOI=10.1016/j.molcel.2016.11.039;
Juszkiewicz S., Hegde R.S.;
"Initiation of quality control during poly(A) translation requires
site-specific ribosome ubiquitination.";
Mol. Cell 0:0-0(2016).
[62]
UBIQUITINATION AT LYS-214.
PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026;
Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A.,
Bennett E.J.;
"ZNF598 and RACK1 regulate mammalian ribosome-associated quality
control function by mediating regulatory 40S ribosomal
ubiquitylation.";
Mol. Cell 0:0-0(2017).
[63]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214 AND LYS-230, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[64]
STRUCTURE BY NMR OF 17-95.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the KH domain of human ribosomal protein S3.";
Submitted (NOV-2004) to the PDB data bank.
[65]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: Involved in translation as a component of the 40S small
ribosomal subunit (PubMed:8706699). Has endonuclease activity and
plays a role in repair of damaged DNA (PubMed:7775413). Cleaves
phosphodiester bonds of DNAs containing altered bases with broad
specificity and cleaves supercoiled DNA more efficiently than
relaxed DNA (PubMed:15707971). Displays high binding affinity for
7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by
reactive oxygen species (ROS) (PubMed:14706345). Has also been
shown to bind with similar affinity to intact and damaged DNA
(PubMed:18610840). Stimulates the N-glycosylase activity of the
base excision protein OGG1 (PubMed:15518571). Enhances the uracil
excision activity of UNG1 (PubMed:18973764). Also stimulates the
cleavage of the phosphodiester backbone by APEX1
(PubMed:18973764). When located in the mitochondrion, reduces
cellular ROS levels and mitochondrial DNA damage
(PubMed:23911537). Has also been shown to negatively regulate DNA
repair in cells exposed to hydrogen peroxide (PubMed:17049931).
Plays a role in regulating transcription as part of the NF-kappa-B
p65-p50 complex where it binds to the RELA/p65 subunit, enhances
binding of the complex to DNA and promotes transcription of target
genes (PubMed:18045535). Represses its own translation by binding
to its cognate mRNA (PubMed:20217897). Binds to and protects
TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744).
Involved in spindle formation and chromosome movement during
mitosis by regulating microtubule polymerization
(PubMed:23131551). Involved in induction of apoptosis through its
role in activation of CASP8 (PubMed:14988002). Induces neuronal
apoptosis by interacting with the E2F1 transcription factor and
acting synergistically with it to up-regulate pro-apoptotic
proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with
TRADD following exposure to UV radiation and induces apoptosis by
caspase-dependent JNK activation (PubMed:22510408).
{ECO:0000269|PubMed:14706345, ECO:0000269|PubMed:14988002,
ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:15707971,
ECO:0000269|PubMed:17049931, ECO:0000269|PubMed:18045535,
ECO:0000269|PubMed:18610840, ECO:0000269|PubMed:18973764,
ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20217897,
ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:22510408,
ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537,
ECO:0000269|PubMed:7775413, ECO:0000269|PubMed:8706699}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000269|PubMed:7775413}.
-!- ENZYME REGULATION: Endonuclease activity is inhibited by MgCl2 on
apurinic/apyrimidinic DNA but not on UV-irradiated DNA.
{ECO:0000269|PubMed:15707971}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is between 8.0 and 9.0 with activity decreasing
sharply below 8.0. {ECO:0000269|PubMed:15707971};
-!- SUBUNIT: Component of the 40S small ribosomal subunit
(PubMed:8706699). Identified in a IGF2BP1-dependent mRNP granule
complex containing untranslated mRNAs (PubMed:17289661). Interacts
with HNRPD (PubMed:24423872). Interacts with PRMT1; the
interaction methylates RPS3 (PubMed:19460357). Interacts with
SUMO1; the interaction sumoylates RPS3 (PubMed:21968017).
Interacts with UBC9 (PubMed:21968017). Interacts with CDK1; the
interaction phosphorylates RPS3 (PubMed:21871177). Interacts with
PRKCD; the interaction phosphorylates RPS3 (PubMed:19059439).
Interacts with PKB/AKT; the interaction phosphorylates RPS3
(PubMed:20605787). Interacts with E2F1; the interaction occurs in
the absence of nerve growth factor and increases transcription of
pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787).
Interacts with the base excision repair proteins APEX1 and OGG1;
interaction with OGG1 increases OGG1 N-glycosylase activity
(PubMed:15518571). Interacts with UNG; the interaction increases
the uracil excision activity of UNG1 (PubMed:18973764). Interacts
with HSP90; the interaction prevents the ubiquitination and
proteasome-dependent degradation of RPS3 and is suppressed by
increased ROS levels (PubMed:16314389). Interacts with TOM70; the
interaction promotes translocation of RPS3 to the mitochondrion
(PubMed:23911537). Interacts (via N-terminus) with RELA (via N-
terminus); the interaction enhances the DNA-binding activity of
the NF-kappa-B p65-p50 complex (PubMed:18045535). Interacts with
NFKBIA; the interaction is direct and may bridge the interaction
between RPS3 and RELA (PubMed:24457201). Interacts with IKKB; the
interaction phosphorylates RPS3 and enhances its translocation to
the nucleus (PubMed:21399639). Interacts (via KH domain) with MDM2
and TP53 (PubMed:19656744). Interacts with TRADD
(PubMed:22510408). Interacts (via N-terminus) with E.coli O157:H7
(strain EDL933) nleH1 and nleH2; the interaction with nleH1
inhibits phosphorylation by IKKB, reduces RPS3 nuclear abundance
and inhibits transcriptional activation by the NF-kappa-B p65-p50
complex (PubMed:20041225, PubMed:21399639). Identified in a HCV
IRES-mediated translation complex, at least composed of EIF3C,
IGF2BP1, RPS3 and HCV RNA-replicon (PubMed:19541769). Interacts
with CRY1 (By similarity). {ECO:0000250|UniProtKB:P62908,
ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:16314389,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18045535,
ECO:0000269|PubMed:18973764, ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:19460357, ECO:0000269|PubMed:19541769,
ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20041225,
ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:21399639,
ECO:0000269|PubMed:21871177, ECO:0000269|PubMed:21968017,
ECO:0000269|PubMed:22510408, ECO:0000269|PubMed:23911537,
ECO:0000269|PubMed:24423872, ECO:0000269|PubMed:24457201,
ECO:0000269|PubMed:8706699, ECO:0000303|PubMed:21399639}.
-!- INTERACTION:
O14920:IKBKB; NbExp=4; IntAct=EBI-351193, EBI-81266;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-351193, EBI-5323863;
Q00987:MDM2; NbExp=8; IntAct=EBI-351193, EBI-389668;
Q15843:NEDD8; NbExp=2; IntAct=EBI-351193, EBI-716247;
P19838:NFKB1; NbExp=4; IntAct=EBI-351193, EBI-300010;
P25963:NFKBIA; NbExp=6; IntAct=EBI-351193, EBI-307386;
Q08752:PPID; NbExp=4; IntAct=EBI-351193, EBI-716596;
Q04206:RELA; NbExp=8; IntAct=EBI-351193, EBI-73886;
P04637:TP53; NbExp=4; IntAct=EBI-351193, EBI-366083;
P63104:YWHAZ; NbExp=2; IntAct=EBI-351193, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16314389,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175,
ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:20217897,
ECO:0000269|PubMed:21871177}. Nucleus
{ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:18045535,
ECO:0000269|PubMed:19460357, ECO:0000269|PubMed:20217897,
ECO:0000269|PubMed:21871177}. Nucleus, nucleolus
{ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:19460357}.
Mitochondrion inner membrane {ECO:0000269|PubMed:23911537};
Peripheral membrane protein {ECO:0000269|PubMed:23911537}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23131551}.
Note=In normal cells, located mainly in the cytoplasm with small
amounts in the nucleus but translocates to the nucleus in cells
undergoing apoptosis (By similarity). Nuclear translocation is
induced by DNA damaging agents such as hydrogen peroxide
(PubMed:17560175). Accumulates in the mitochondrion in response to
increased ROS levels (PubMed:23911537). Localizes to the spindle
during mitosis (PubMed:23131551). Localized in cytoplasmic mRNP
granules containing untranslated mRNAs (PubMed:17289661).
{ECO:0000250|UniProtKB:P62908, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:23131551,
ECO:0000269|PubMed:23911537}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P23396-1; Sequence=Displayed;
Name=2;
IsoId=P23396-2; Sequence=VSP_046667;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- PTM: Methylation by PRMT1 is required for import into the
nucleolus and for ribosome assembly.
{ECO:0000269|PubMed:19460357}.
-!- PTM: Sumoylation by SUMO1 enhances protein stability through
increased resistance to proteolysis. Sumoylation occurs at one or
more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
{ECO:0000269|PubMed:21968017}.
-!- PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M
phase (PubMed:21871177). Phosphorylation by PRKCD occurs on a non-
ribosomal-associated form which results in translocation of RPS3
to the nucleus and enhances its endonuclease activity
(PubMed:19059439). Phosphorylated on Ser-209 by IKKB in response
to activation of the NF-kappa-B p65-p50 complex which enhances the
association of RPS3 with importin-alpha and mediates the nuclear
translocation of RPS3 (PubMed:21399639). Phosphorylation by MAPK
is required for translocation to the nucleus following exposure of
cells to DNA damaging agents such as hydrogen peroxide
(PubMed:17560175). Phosphorylation by PKB/AKT mediates RPS3
nuclear translocation, enhances RPS3 endonuclease activity and
suppresses RPS3-induced neuronal apoptosis (PubMed:20605787).
{ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:21399639,
ECO:0000269|PubMed:21871177}.
-!- PTM: Ubiquitinated (PubMed:16314389). This is prevented by
interaction with HSP90 which stabilizes the protein
(PubMed:16314389). Monoubiquitinated at Lys-214 by ZNF598 when a
ribosome has stalled during translation of poly(A) sequences,
leading to preclude synthesis of a long poly-lysine tail and
initiate the ribosome quality control (RQC) pathway to degrade the
potentially detrimental aberrant nascent polypeptide
(PubMed:28065601, PubMed:28132843). {ECO:0000269|PubMed:16314389,
ECO:0000269|PubMed:28065601, ECO:0000269|PubMed:28132843}.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB93471.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rps3/";
-----------------------------------------------------------------------
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EMBL; U14990; AAB60336.1; -; mRNA.
EMBL; U14991; AAB60337.1; -; mRNA.
EMBL; U14992; AAB60338.1; -; mRNA.
EMBL; X55715; CAA39248.1; -; mRNA.
EMBL; S42658; AAB19349.2; -; mRNA.
EMBL; AB061838; BAB79476.1; -; Genomic_DNA.
EMBL; AY791291; AAV40835.1; -; Genomic_DNA.
EMBL; AK313051; BAG35882.1; -; mRNA.
EMBL; AP000744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74963.1; -; Genomic_DNA.
EMBL; BC003137; AAH03137.1; -; mRNA.
EMBL; BC003577; AAH03577.1; -; mRNA.
EMBL; BC013196; AAH13196.1; -; mRNA.
EMBL; BC034149; AAH34149.1; -; mRNA.
EMBL; BC071917; AAH71917.1; -; mRNA.
EMBL; BC100284; AAI00285.1; -; mRNA.
EMBL; L16016; AAA18095.1; -; Genomic_DNA.
EMBL; AB062288; BAB93471.1; ALT_INIT; mRNA.
CCDS; CCDS58161.1; -. [P23396-2]
CCDS; CCDS8236.1; -. [P23396-1]
PIR; A41247; R3HUS3.
RefSeq; NP_000996.2; NM_001005.4. [P23396-1]
RefSeq; NP_001243731.1; NM_001256802.1. [P23396-1]
RefSeq; NP_001247435.1; NM_001260506.1. [P23396-2]
RefSeq; NP_001247436.1; NM_001260507.1.
UniGene; Hs.546286; -.
UniGene; Hs.740358; -.
PDB; 1WH9; NMR; -; A=17-95.
PDB; 4UG0; EM; -; SD=1-243.
PDB; 4V6X; EM; 5.00 A; AD=1-243.
PDB; 5A2Q; EM; 3.90 A; D=1-243.
PDB; 5AJ0; EM; 3.50 A; BD=1-243.
PDB; 5FLX; EM; 3.90 A; D=1-243.
PDB; 5LKS; EM; 3.60 A; SD=1-243.
PDB; 5T2C; EM; 3.60 A; Aq=1-243.
PDBsum; 1WH9; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
ProteinModelPortal; P23396; -.
SMR; P23396; -.
BioGrid; 112102; 270.
DIP; DIP-33177N; -.
ELM; P23396; -.
IntAct; P23396; 74.
MINT; MINT-4999144; -.
STRING; 9606.ENSP00000433821; -.
iPTMnet; P23396; -.
PhosphoSitePlus; P23396; -.
SwissPalm; P23396; -.
BioMuta; RPS3; -.
DMDM; 417719; -.
EPD; P23396; -.
MaxQB; P23396; -.
PaxDb; P23396; -.
PeptideAtlas; P23396; -.
PRIDE; P23396; -.
DNASU; 6188; -.
Ensembl; ENST00000278572; ENSP00000278572; ENSG00000149273. [P23396-2]
Ensembl; ENST00000524851; ENSP00000433821; ENSG00000149273. [P23396-1]
Ensembl; ENST00000527446; ENSP00000436971; ENSG00000149273. [P23396-1]
Ensembl; ENST00000531188; ENSP00000434643; ENSG00000149273. [P23396-1]
GeneID; 6188; -.
KEGG; hsa:6188; -.
UCSC; uc001owh.5; human. [P23396-1]
CTD; 6188; -.
DisGeNET; 6188; -.
GeneCards; RPS3; -.
HGNC; HGNC:10420; RPS3.
HPA; HPA063339; -.
MIM; 600454; gene.
neXtProt; NX_P23396; -.
OpenTargets; ENSG00000149273; -.
PharmGKB; PA34829; -.
eggNOG; KOG3181; Eukaryota.
eggNOG; COG0092; LUCA.
GeneTree; ENSGT00390000008610; -.
HOGENOM; HOG000210611; -.
HOVERGEN; HBG002195; -.
InParanoid; P23396; -.
KO; K02985; -.
OMA; DHATRHV; -.
OrthoDB; EOG091G0I8D; -.
PhylomeDB; P23396; -.
TreeFam; TF300901; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNOR; P23396; -.
ChiTaRS; RPS3; human.
EvolutionaryTrace; P23396; -.
GeneWiki; RPS3; -.
GenomeRNAi; 6188; -.
PRO; PR:P23396; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149273; -.
CleanEx; HS_RPS3; -.
ExpressionAtlas; P23396; baseline and differential.
Genevisible; P23396; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0071159; C:NF-kappaB complex; IDA:CAFA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0005840; C:ribosome; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
GO; GO:0051536; F:iron-sulfur cluster binding; NAS:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0032357; F:oxidized purine DNA binding; IDA:UniProtKB.
GO; GO:0032358; F:oxidized pyrimidine DNA binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IMP:CAFA.
GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
GO; GO:0032183; F:SUMO binding; IPI:UniProtKB.
GO; GO:0097100; F:supercoiled DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:CAFA.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0045738; P:negative regulation of DNA repair; IMP:UniProtKB.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:CAFA.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:1905053; P:positive regulation of base-excision repair; IDA:UniProtKB.
GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
GO; GO:1902546; P:positive regulation of DNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:CAFA.
GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:CAFA.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0031334; P:positive regulation of protein complex assembly; IMP:CAFA.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:CAFA.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
GO; GO:0061481; P:response to TNF agonist; IDA:UniProtKB.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006412; P:translation; NAS:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
Gene3D; 3.30.300.20; -; 1.
InterPro; IPR015946; KH_dom-like_a/b.
InterPro; IPR004044; KH_dom_type_2.
InterPro; IPR009019; KH_prok-type.
InterPro; IPR001351; Ribosomal_S3_C.
InterPro; IPR018280; Ribosomal_S3_CS.
InterPro; IPR005703; Ribosomal_S3_euk/arc.
Pfam; PF07650; KH_2; 1.
Pfam; PF00189; Ribosomal_S3_C; 1.
SUPFAM; SSF54814; SSF54814; 1.
SUPFAM; SSF54821; SSF54821; 1.
TIGRFAMs; TIGR01008; uS3_euk_arch; 1.
PROSITE; PS50823; KH_TYPE_2; 1.
PROSITE; PS00548; RIBOSOMAL_S3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; DNA damage; DNA repair; DNA-binding;
Isopeptide bond; Lyase; Membrane; Methylation; Mitochondrion;
Mitochondrion inner membrane; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
Transcription; Transcription regulation; Translation regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.10}.
CHAIN 2 243 40S ribosomal protein S3.
/FTId=PRO_0000130320.
DOMAIN 21 92 KH type-2. {ECO:0000255|PROSITE-
ProRule:PRU00118}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.10}.
MOD_RES 6 6 Phosphoserine; by PKC/PRKCD.
{ECO:0000269|PubMed:19059439}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 42 42 Phosphothreonine; by MAPK.
{ECO:0000269|PubMed:15950189}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 64 64 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:19460357}.
MOD_RES 65 65 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:19460357}.
MOD_RES 67 67 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:19460357}.
MOD_RES 70 70 Phosphothreonine; by PKB.
{ECO:0000269|PubMed:20605787}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 132 132 N6-succinyllysine.
{ECO:0000250|UniProtKB:P62908}.
MOD_RES 209 209 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:21399639}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 221 221 Phosphothreonine; by CDK1 and PKC/PRKCD.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:21871177,
ECO:0000269|Ref.12}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:16807684}.
MOD_RES 242 242 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:28065601,
ECO:0000269|PubMed:28132843}.
CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 85 85 E -> ELKIMVMVTGYPLLPLK (in isoform 2).
{ECO:0000305}.
/FTId=VSP_046667.
MUTAGEN 6 6 S->A: No effect on phosphorylation by
CDK1. Greatly reduced phosphorylation by
PRKCD. Abolishes phosphorylation by
PRKCD; when associated with A-221.
{ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:21871177}.
MUTAGEN 18 18 K->R: No effect on sumoylation. Abolishes
sumoylation; when associated with R-214
and R-230. {ECO:0000269|PubMed:21968017}.
MUTAGEN 35 35 S->A: No effect on phosphorylation by
PRKCD. {ECO:0000269|PubMed:19059439}.
MUTAGEN 42 42 T->A: Abolishes phosphorylation by MAPK
and translocation to the nucleus
following exposure of cells to hydrogen
peroxide. No effect on phosphorylation by
CDK1 or PRKCD.
{ECO:0000269|PubMed:15950189,
ECO:0000269|PubMed:17560175,
ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:21871177}.
MUTAGEN 42 42 T->D: Phosphomimetic mutant which is
detected exclusively in the nucleus.
{ECO:0000269|PubMed:17560175}.
MUTAGEN 70 70 T->A: No effect on phosphorylation by
PRKCD. Abolishes phosphorylation by PKB.
{ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:20605787}.
MUTAGEN 70 70 T->D,E,R: Abolishes phosphorylation by
PKB. {ECO:0000269|PubMed:20605787}.
MUTAGEN 132 132 K->A: Does not affect ability to cleave
DNA but abolishes binding to 8-oxoG.
{ECO:0000269|PubMed:16737853}.
MUTAGEN 139 139 S->A: No effect on phosphorylation by
PRKCD. {ECO:0000269|PubMed:19059439}.
MUTAGEN 149 149 S->A: No effect on phosphorylation by
PRKCD. {ECO:0000269|PubMed:19059439}.
MUTAGEN 195 195 T->A: No effect on phosphorylation by
PRKCD. {ECO:0000269|PubMed:19059439}.
MUTAGEN 209 209 S->A: Reduced phosphorylation by IKKB.
{ECO:0000269|PubMed:21399639}.
MUTAGEN 214 214 K->R: No effect on sumoylation. Abolishes
sumoylation; when associated with R-18
and R-230. {ECO:0000269|PubMed:21968017}.
MUTAGEN 221 221 T->A: No effect on phosphorylation by
MAPK. Significantly reduces
phosphorylation by CDK1 and nuclear
accumulation. Greatly reduced
phosphorylation by PRKCD. Abolishes
phosphorylation by PRKCD; when associated
with A-6. {ECO:0000269|PubMed:15950189,
ECO:0000269|PubMed:19059439,
ECO:0000269|PubMed:21871177}.
MUTAGEN 230 230 K->R: No effect on sumoylation. Abolishes
sumoylation; when associated with R-18
and R-214. {ECO:0000269|PubMed:21968017}.
CONFLICT 8 8 K -> R (in Ref. 2; AAB19349).
{ECO:0000305}.
CONFLICT 104 104 S -> C (in Ref. 1; CAA39248).
{ECO:0000305}.
CONFLICT 233 233 P -> L (in Ref. 1; CAA39248).
{ECO:0000305}.
HELIX 17 28 {ECO:0000244|PDB:1WH9}.
TURN 29 33 {ECO:0000244|PDB:1WH9}.
STRAND 34 41 {ECO:0000244|PDB:1WH9}.
STRAND 46 53 {ECO:0000244|PDB:1WH9}.
HELIX 55 59 {ECO:0000244|PDB:1WH9}.
HELIX 61 63 {ECO:0000244|PDB:1WH9}.
HELIX 64 77 {ECO:0000244|PDB:1WH9}.
STRAND 83 90 {ECO:0000244|PDB:1WH9}.
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


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