RS3_HUMAN
ID RS3_HUMAN Reviewed; 243 AA.
AC P23396; B2R7N5; J3KN86; Q498B5; Q8NI95;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=40S ribosomal protein S3 {ECO:0000303|PubMed:2129557};
DE EC=4.2.99.18 {ECO:0000269|PubMed:7775413};
DE AltName: Full=Small ribosomal subunit protein uS3 {ECO:0000303|PubMed:24524803};
GN Name=RPS3 {ECO:0000303|PubMed:11875025}; ORFNames=OK/SW-cl.26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (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; DOI=10.1128/mcb.11.8.3842-3849.1991;
RA Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G., Meisler A.I.,
RA Pipas J.M.;
RT "Ribosomal protein genes are overexpressed in colorectal cancer: isolation
RT 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 analysis of
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [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 project:
RT 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; DOI=10.1101/gad.7.7a.1176;
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 IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F., 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-reactive
RT 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; 152-173;
RP 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, AND
RP IDENTIFICATION BY 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., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7775413; DOI=10.1074/jbc.270.23.13620;
RA Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.;
RT "Implication of mammalian ribosomal protein S3 in the processing of DNA
RT damage.";
RL J. Biol. Chem. 270:13620-13629(1995).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
RP FUNCTION, AND INTERACTION WITH APEX1 AND OGG1.
RX PubMed=15518571; DOI=10.1021/bi049234b;
RA Hegde V., Wang M., Deutsch W.A.;
RT "Human ribosomal protein S3 interacts with DNA base excision repair
RT proteins hAPE/Ref-1 and hOGG1.";
RL Biochemistry 43:14211-14217(2004).
RN [17]
RP FUNCTION.
RX PubMed=14706345; DOI=10.1016/j.dnarep.2003.10.004;
RA Hegde V., Wang M., Deutsch W.A.;
RT "Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-
RT oxoguanine and abasic sites by surface plasmon resonance.";
RL DNA Repair 3:121-126(2004).
RN [18]
RP FUNCTION.
RX PubMed=14988002; DOI=10.1016/s0014-5793(04)00074-2;
RA Jang C.Y., Lee J.Y., Kim J.;
RT "RpS3, a DNA repair endonuclease and ribosomal protein, is involved in
RT apoptosis.";
RL FEBS Lett. 560:81-85(2004).
RN [19]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15707971; DOI=10.1016/j.bbrc.2005.01.045;
RA Kim S.H., Lee J.Y., Kim J.;
RT "Characterization of a wide range base-damage-endonuclease activity of
RT mammalian rpS3.";
RL Biochem. Biophys. Res. Commun. 328:962-967(2005).
RN [20]
RP PHOSPHORYLATION AT THR-42, AND MUTAGENESIS OF THR-42 AND THR-221.
RX PubMed=15950189; DOI=10.1016/j.bbrc.2005.05.079;
RA Kim H.D., Lee J.Y., Kim J.;
RT "Erk phosphorylates threonine 42 residue of ribosomal protein S3.";
RL Biochem. Biophys. Res. Commun. 333:110-115(2005).
RN [21]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [22]
RP MUTAGENESIS OF LYS-132.
RX PubMed=16737853; DOI=10.1016/j.dnarep.2006.04.001;
RA Hegde V., Wang M., Mian I.S., Spyres L., Deutsch W.A.;
RT "The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-
RT oxoguanine is abrogated by a single amino acid change.";
RL DNA Repair 5:810-815(2006).
RN [23]
RP INTERACTION WITH HSP90, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=16314389; DOI=10.1091/mbc.e05-08-0713;
RA Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J.;
RT "Interaction of Hsp90 with ribosomal proteins protects from ubiquitination
RT and proteasome-dependent degradation.";
RL Mol. Biol. Cell 17:824-833(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [26]
RP FUNCTION, INTERACTION WITH RELA, IDENTIFICATION IN THE NF-KAPPA-B P65-P50
RP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18045535; DOI=10.1016/j.cell.2007.10.009;
RA Wan F., Anderson D.E., Barnitz R.A., Snow A., Bidere N., Zheng L.,
RA Hegde V., Lam L.T., Staudt L.M., Levens D., Deutsch W.A., Lenardo M.J.;
RT "Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that
RT mediates selective gene regulation.";
RL Cell 131:927-939(2007).
RN [27]
RP FUNCTION.
RX PubMed=17049931; DOI=10.1016/j.dnarep.2006.09.004;
RA Hegde V., Yadavilli S., Deutsch W.A.;
RT "Knockdown of ribosomal protein S3 protects human cells from genotoxic
RT stress.";
RL DNA Repair 6:94-99(2007).
RN [28]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF THR-42.
RX PubMed=17560175; DOI=10.1016/j.dnarep.2007.04.009;
RA Yadavilli S., Hegde V., Deutsch W.A.;
RT "Translocation of human ribosomal protein S3 to sites of DNA damage is
RT dependant on ERK-mediated phosphorylation following genotoxic stress.";
RL DNA Repair 6:1453-1462(2007).
RN [29]
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 [30]
RP FUNCTION.
RX PubMed=18610840;
RA Balyeva K.E., Malygin A.A., Karpova G.G., Nevinskii G.A., Zharkov D.O.;
RT "Interactions of human ribosomal protein S3 with undamaged and damaged
RT DNA.";
RL Mol. Biol. (Mosk.) 42:314-322(2008).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [32]
RP FUNCTION, AND INTERACTION WITH UNG.
RX PubMed=18973764; DOI=10.1016/j.mrfmmm.2008.09.013;
RA Ko S.I., Park J.H., Park M.J., Kim J., Kang L.W., Han Y.S.;
RT "Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase
RT (hUNG) and stimulates its glycosylase activity.";
RL Mutat. Res. 648:54-64(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [35]
RP INTERACTION WITH PRMT1, SUBCELLULAR LOCATION, AND METHYLATION AT ARG-64;
RP ARG-65 AND ARG-67.
RX PubMed=19460357; DOI=10.1016/j.bbrc.2009.05.055;
RA Shin H.S., Jang C.Y., Kim H.D., Kim T.S., Kim S., Kim J.;
RT "Arginine methylation of ribosomal protein S3 affects ribosome assembly.";
RL Biochem. Biophys. Res. Commun. 385:273-278(2009).
RN [36]
RP INTERACTION WITH PRKCD, PHOSPHORYLATION AT SER-6 AND THR-221, AND
RP MUTAGENESIS OF SER-6; SER-35; THR-42; THR-70; SER-139; SER-149; THR-195 AND
RP THR-221.
RX PubMed=19059439; DOI=10.1016/j.bbamcr.2008.10.017;
RA Kim T.S., Kim H.D., Kim J.;
RT "PKCdelta-dependent functional switch of rpS3 between translation and DNA
RT repair.";
RL Biochim. Biophys. Acta 1793:395-405(2009).
RN [37]
RP FUNCTION, INTERACTION WITH MDM2 AND TP53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19656744; DOI=10.1016/j.dnarep.2009.07.003;
RA Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A.;
RT "Ribosomal protein S3: A multi-functional protein that interacts with both
RT p53 and MDM2 through its KH domain.";
RL DNA Repair 8:1215-1224(2009).
RN [38]
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 [39]
RP INTERACTION WITH E.COLI NLEH1 AND NLEH2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20041225; DOI=10.1371/journal.ppat.1000708;
RA Gao X., Wan F., Mateo K., Callegari E., Wang D., Deng W., Puente J., Li F.,
RA Chaussee M.S., Finlay B.B., Lenardo M.J., Hardwidge P.R.;
RT "Bacterial effector binding to ribosomal protein s3 subverts NF-kappaB
RT function.";
RL PLoS Pathog. 5:E1000708-E1000708(2009).
RN [40]
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 3'UTR.";
RL RNA 15:1528-1542(2009).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [43]
RP INTERACTION WITH E2F1 AND PKB, PHOSPHORYLATION AT THR-70, AND MUTAGENESIS
RP OF THR-70.
RX PubMed=20605787; DOI=10.1074/jbc.m110.131367;
RA Lee S.B., Kwon I.S., Park J., Lee K.H., Ahn Y., Lee C., Kim J., Choi S.Y.,
RA Cho S.W., Ahn J.Y.;
RT "Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator
RT between neuronal apoptosis and DNA repair.";
RL J. Biol. Chem. 285:29457-29468(2010).
RN [44]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20217897; DOI=10.1002/jcb.22537;
RA Kim H.D., Kim T.S., Joo Y.J., Shin H.S., Kim S.H., Jang C.Y., Lee C.E.,
RA Kim J.;
RT "RpS3 translation is repressed by interaction with its own mRNA.";
RL J. Cell. Biochem. 110:294-303(2010).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [46]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [47]
RP INTERACTION WITH SUMO1 AND UBC9, SUMOYLATION AT LYS-18; LYS-214 AND
RP LYS-230, AND MUTAGENESIS OF LYS-18; LYS-214 AND LYS-230.
RX PubMed=21968017; DOI=10.1016/j.bbrc.2011.09.099;
RA Jang C.Y., Shin H.S., Kim H.D., Kim J.W., Choi S.Y., Kim J.;
RT "Ribosomal protein S3 is stabilized by sumoylation.";
RL Biochem. Biophys. Res. Commun. 414:523-527(2011).
RN [48]
RP INTERACTION WITH CDK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-221,
RP AND MUTAGENESIS OF SER-6; THR-42 AND THR-221.
RX PubMed=21871177; DOI=10.5483/bmbrep.2011.44.8.529;
RA Yoon I.S., Chung J.H., Hahm S.H., Park M.J., Lee Y.R., Ko S.I., Kang L.W.,
RA Kim T.S., Kim J., Han Y.S.;
RT "Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase.";
RL BMB Rep. 44:529-534(2011).
RN [49]
RP INTERACTION WITH IKKB AND E.COLI NLEH1, PHOSPHORYLATION AT SER-209, AND
RP MUTAGENESIS OF SER-209.
RX PubMed=21399639; DOI=10.1038/ni.2007;
RA Wan F., Weaver A., Gao X., Bern M., Hardwidge P.R., Lenardo M.J.;
RT "IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB
RT function during infection with Escherichia coli strain O157:H7.";
RL Nat. Immunol. 12:335-343(2011).
RN [50]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [51]
RP FUNCTION, AND INTERACTION WITH TRADD.
RX PubMed=22510408; DOI=10.1016/j.bbrc.2012.04.020;
RA Jang C.Y., Kim H.D., Kim J.;
RT "Ribosomal protein S3 interacts with TRADD to induce apoptosis through
RT caspase dependent JNK activation.";
RL Biochem. Biophys. Res. Commun. 421:474-478(2012).
RN [52]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23131551; DOI=10.1016/j.bbrc.2012.10.093;
RA Jang C.Y., Kim H.D., Zhang X., Chang J.S., Kim J.;
RT "Ribosomal protein S3 localizes on the mitotic spindle and functions as a
RT microtubule associated protein in mitosis.";
RL Biochem. Biophys. Res. Commun. 429:57-62(2012).
RN [53]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [54]
RP FUNCTION, INTERACTION WITH TOM70, AND SUBCELLULAR LOCATION.
RX PubMed=23911537; DOI=10.1016/j.bbamcr.2013.07.015;
RA Kim Y., Kim H.D., Kim J.;
RT "Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in
RT mitochondrial DNA damage surveillance.";
RL Biochim. Biophys. Acta 1833:2943-2952(2013).
RN [55]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-104; THR-220 AND
RP THR-221, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [56]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [57]
RP INTERACTION WITH NFKBIA.
RX PubMed=24457201; DOI=10.1016/j.febslet.2013.12.034;
RA Stanborough T., Niederhauser J., Koch B., Bergler H., Pertschy B.;
RT "Ribosomal protein S3 interacts with the NF-kappaB inhibitor
RT IkappaBalpha.";
RL FEBS Lett. 588:659-664(2014).
RN [58]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND THR-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [59]
RP INTERACTION WITH HNRPD.
RX PubMed=24423872; DOI=10.1093/nar/gkt1379;
RA Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
RA Hong K.Y., Jang S.K., Kim K.T.;
RT "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
RT translation.";
RL Nucleic Acids Res. 42:3590-3606(2014).
RN [60]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [61]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [62]
RP UBIQUITINATION AT LYS-214.
RX PubMed=28065601; DOI=10.1016/j.molcel.2016.11.039;
RA Juszkiewicz S., Hegde R.S.;
RT "Initiation of quality control during poly(A) translation requires site-
RT specific ribosome ubiquitination.";
RL Mol. Cell 65:743-750(2016).
RN [63]
RP UBIQUITINATION AT LYS-214.
RX PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026;
RA Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.;
RT "ZNF598 and RACK1 regulate mammalian ribosome-associated quality control
RT function by mediating regulatory 40S ribosomal ubiquitylation.";
RL Mol. Cell 65:751-760(2017).
RN [64]
RP INTERACTION WITH ASCC3.
RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA Inada T.;
RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT control.";
RL Nat. Commun. 8:159-159(2017).
RN [65]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214 AND LYS-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [66]
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 [67]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Involved in translation as a component of the 40S small
CC ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays
CC a role in repair of damaged DNA (PubMed:7775413). Cleaves
CC phosphodiester bonds of DNAs containing altered bases with broad
CC specificity and cleaves supercoiled DNA more efficiently than relaxed
CC DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-
CC 8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen
CC species (ROS) (PubMed:14706345). Has also been shown to bind with
CC similar affinity to intact and damaged DNA (PubMed:18610840).
CC Stimulates the N-glycosylase activity of the base excision protein OGG1
CC (PubMed:15518571). Enhances the uracil excision activity of UNG1
CC (PubMed:18973764). Also stimulates the cleavage of the phosphodiester
CC backbone by APEX1 (PubMed:18973764). When located in the mitochondrion,
CC reduces cellular ROS levels and mitochondrial DNA damage
CC (PubMed:23911537). Has also been shown to negatively regulate DNA
CC repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a
CC role in regulating transcription as part of the NF-kappa-B p65-p50
CC complex where it binds to the RELA/p65 subunit, enhances binding of the
CC complex to DNA and promotes transcription of target genes
CC (PubMed:18045535). Represses its own translation by binding to its
CC cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from
CC MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle
CC formation and chromosome movement during mitosis by regulating
CC microtubule polymerization (PubMed:23131551). Involved in induction of
CC apoptosis through its role in activation of CASP8 (PubMed:14988002).
CC Induces neuronal apoptosis by interacting with the E2F1 transcription
CC factor and acting synergistically with it to up-regulate pro-apoptotic
CC proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with
CC TRADD following exposure to UV radiation and induces apoptosis by
CC caspase-dependent JNK activation (PubMed:22510408).
CC {ECO:0000269|PubMed:14706345, ECO:0000269|PubMed:14988002,
CC ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:15707971,
CC ECO:0000269|PubMed:17049931, ECO:0000269|PubMed:18045535,
CC ECO:0000269|PubMed:18610840, ECO:0000269|PubMed:18973764,
CC ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20217897,
CC ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:22510408,
CC ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537,
CC ECO:0000269|PubMed:7775413, ECO:0000269|PubMed:8706699}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC Evidence={ECO:0000269|PubMed:7775413};
CC -!- ACTIVITY REGULATION: Endonuclease activity is inhibited by MgCl2 on
CC apurinic/apyrimidinic DNA but not on UV-irradiated DNA.
CC {ECO:0000269|PubMed:15707971}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 8.0 and 9.0 with activity decreasing sharply
CC below 8.0. {ECO:0000269|PubMed:15707971};
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit (PubMed:8706699).
CC Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs (PubMed:17289661). Interacts with HNRPD
CC (PubMed:24423872). Interacts with PRMT1; the interaction methylates
CC RPS3 (PubMed:19460357). Interacts with SUMO1; the interaction
CC sumoylates RPS3 (PubMed:21968017). Interacts with UBC9
CC (PubMed:21968017). Interacts with CDK1; the interaction phosphorylates
CC RPS3 (PubMed:21871177). Interacts with PRKCD; the interaction
CC phosphorylates RPS3 (PubMed:19059439). Interacts with PKB/AKT; the
CC interaction phosphorylates RPS3 (PubMed:20605787). Interacts with E2F1;
CC the interaction occurs in the absence of nerve growth factor and
CC increases transcription of pro-apoptotic proteins BCL2L11/BIM and
CC HRK/Dp5 (PubMed:20605787). Interacts with the base excision repair
CC proteins APEX1 and OGG1; interaction with OGG1 increases OGG1 N-
CC glycosylase activity (PubMed:15518571). Interacts with UNG; the
CC interaction increases the uracil excision activity of UNG1
CC (PubMed:18973764). Interacts with HSP90; the interaction prevents the
CC ubiquitination and proteasome-dependent degradation of RPS3 and is
CC suppressed by increased ROS levels (PubMed:16314389). Interacts with
CC TOM70; the interaction promotes translocation of RPS3 to the
CC mitochondrion (PubMed:23911537). Interacts (via N-terminus) with RELA
CC (via N-terminus); the interaction enhances the DNA-binding activity of
CC the NF-kappa-B p65-p50 complex (PubMed:18045535). Interacts with
CC NFKBIA; the interaction is direct and may bridge the interaction
CC between RPS3 and RELA (PubMed:24457201). Interacts with IKKB; the
CC interaction phosphorylates RPS3 and enhances its translocation to the
CC nucleus (PubMed:21399639). Interacts (via KH domain) with MDM2 and TP53
CC (PubMed:19656744). Interacts with TRADD (PubMed:22510408). Interacts
CC (via N-terminus) with E.coli O157:H7 (strain EDL933) nleH1 and nleH2;
CC the interaction with nleH1 inhibits phosphorylation by IKKB, reduces
CC RPS3 nuclear abundance and inhibits transcriptional activation by the
CC NF-kappa-B p65-p50 complex (PubMed:20041225, PubMed:21399639).
CC Interacts with ASCC3 (PubMed:28757607). Identified in a HCV IRES-
CC mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3
CC and HCV RNA-replicon (PubMed:19541769). Interacts with CRY1 (By
CC similarity). {ECO:0000250|UniProtKB:P62908,
CC ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:16314389,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18045535,
CC ECO:0000269|PubMed:18973764, ECO:0000269|PubMed:19059439,
CC ECO:0000269|PubMed:19460357, ECO:0000269|PubMed:19541769,
CC ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20041225,
CC ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:21399639,
CC ECO:0000269|PubMed:21871177, ECO:0000269|PubMed:21968017,
CC ECO:0000269|PubMed:22510408, ECO:0000269|PubMed:23911537,
CC ECO:0000269|PubMed:24423872, ECO:0000269|PubMed:24457201,
CC ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:8706699,
CC ECO:0000303|PubMed:21399639}.
CC -!- INTERACTION:
CC P23396; P42858: HTT; NbExp=3; IntAct=EBI-351193, EBI-466029;
CC P23396; O14920: IKBKB; NbExp=4; IntAct=EBI-351193, EBI-81266;
CC P23396; Q5S007: LRRK2; NbExp=4; IntAct=EBI-351193, EBI-5323863;
CC P23396; Q96GA3: LTV1; NbExp=3; IntAct=EBI-351193, EBI-2558389;
CC P23396; Q00987: MDM2; NbExp=8; IntAct=EBI-351193, EBI-389668;
CC P23396; Q15843: NEDD8; NbExp=3; IntAct=EBI-351193, EBI-716247;
CC P23396; P19838: NFKB1; NbExp=4; IntAct=EBI-351193, EBI-300010;
CC P23396; P25963: NFKBIA; NbExp=6; IntAct=EBI-351193, EBI-307386;
CC P23396; Q08752: PPID; NbExp=4; IntAct=EBI-351193, EBI-716596;
CC P23396; Q04206: RELA; NbExp=8; IntAct=EBI-351193, EBI-73886;
CC P23396; P04637: TP53; NbExp=4; IntAct=EBI-351193, EBI-366083;
CC P23396; P63104: YWHAZ; NbExp=2; IntAct=EBI-351193, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16314389,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175,
CC ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:20217897,
CC ECO:0000269|PubMed:21871177}. Nucleus {ECO:0000269|PubMed:17560175,
CC ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:19460357,
CC ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:21871177}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:19460357}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:23911537}; Peripheral
CC membrane protein {ECO:0000269|PubMed:23911537}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:23131551}. Note=In normal
CC cells, located mainly in the cytoplasm with small amounts in the
CC nucleus but translocates to the nucleus in cells undergoing apoptosis
CC (By similarity). Nuclear translocation is induced by DNA damaging
CC agents such as hydrogen peroxide (PubMed:17560175). Accumulates in the
CC mitochondrion in response to increased ROS levels (PubMed:23911537).
CC Localizes to the spindle during mitosis (PubMed:23131551). Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs
CC (PubMed:17289661). {ECO:0000250|UniProtKB:P62908,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175,
CC ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537}.
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 -!- PTM: Methylation by PRMT1 is required for import into the nucleolus and
CC for ribosome assembly. {ECO:0000269|PubMed:19460357}.
CC -!- PTM: Sumoylation by SUMO1 enhances protein stability through increased
CC resistance to proteolysis. Sumoylation occurs at one or more of the
CC three consensus sites, Lys-18, Lys-214 and Lys-230.
CC {ECO:0000269|PubMed:21968017}.
CC -!- PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase
CC (PubMed:21871177). Phosphorylation by PRKCD occurs on a non-ribosomal-
CC associated form which results in translocation of RPS3 to the nucleus
CC and enhances its endonuclease activity (PubMed:19059439).
CC Phosphorylated on Ser-209 by IKKB in response to activation of the NF-
CC kappa-B p65-p50 complex which enhances the association of RPS3 with
CC importin-alpha and mediates the nuclear translocation of RPS3
CC (PubMed:21399639). Phosphorylation by MAPK is required for
CC translocation to the nucleus following exposure of cells to DNA
CC damaging agents such as hydrogen peroxide (PubMed:17560175).
CC Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation,
CC enhances RPS3 endonuclease activity and suppresses RPS3-induced
CC neuronal apoptosis (PubMed:20605787). {ECO:0000269|PubMed:17560175,
CC ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:20605787,
CC ECO:0000269|PubMed:21399639, ECO:0000269|PubMed:21871177}.
CC -!- PTM: Ubiquitinated (PubMed:16314389). This is prevented by interaction
CC with HSP90 which stabilizes the protein (PubMed:16314389).
CC Monoubiquitinated at Lys-214 by ZNF598 when a ribosome has stalled
CC during translation of poly(A) sequences, leading to preclude synthesis
CC of a long poly-lysine tail and initiate the ribosome quality control
CC (RQC) pathway to degrade the potentially detrimental aberrant nascent
CC polypeptide (PubMed:28065601, PubMed:28132843).
CC {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:28065601,
CC ECO:0000269|PubMed:28132843}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:P62908}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB93471.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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 CCDS; CCDS58161.1; -. [P23396-2]
DR CCDS; CCDS8236.1; -. [P23396-1]
DR PIR; A41247; R3HUS3.
DR RefSeq; NP_000996.2; NM_001005.4. [P23396-1]
DR RefSeq; NP_001243731.1; NM_001256802.1. [P23396-1]
DR RefSeq; NP_001247435.1; NM_001260506.1. [P23396-2]
DR RefSeq; NP_001247436.1; NM_001260507.1.
DR PDB; 1WH9; NMR; -; A=17-95.
DR PDB; 4UG0; EM; -; SD=1-243.
DR PDB; 4V6X; EM; 5.00 A; AD=1-243.
DR PDB; 5A2Q; EM; 3.90 A; D=1-243.
DR PDB; 5AJ0; EM; 3.50 A; BD=1-243.
DR PDB; 5FLX; EM; 3.90 A; D=1-243.
DR PDB; 5LKS; EM; 3.60 A; SD=1-243.
DR PDB; 5OA3; EM; 4.30 A; D=1-243.
DR PDB; 5T2C; EM; 3.60 A; Aq=1-243.
DR PDB; 5VYC; X-ray; 6.00 A; D1/D2/D3/D4/D5/D6=1-243.
DR PDB; 6FEC; EM; 6.30 A; g=1-227.
DR PDB; 6G51; EM; 4.10 A; D=1-243.
DR PDB; 6G53; EM; 4.50 A; D=1-243.
DR PDB; 6G5H; EM; 3.60 A; D=1-243.
DR PDB; 6G5I; EM; 3.50 A; D=1-243.
DR PDB; 6IP5; EM; 3.90 A; 2p=1-243.
DR PDB; 6IP6; EM; 4.50 A; 2p=1-243.
DR PDB; 6IP8; EM; 3.90 A; 2p=1-243.
DR PDB; 6OLE; EM; 3.10 A; SD=2-227.
DR PDB; 6OLF; EM; 3.90 A; SD=2-227.
DR PDB; 6OLG; EM; 3.40 A; BD=2-221.
DR PDB; 6OLI; EM; 3.50 A; SD=2-227.
DR PDB; 6OLZ; EM; 3.90 A; BD=2-221.
DR PDB; 6OM0; EM; 3.10 A; SD=2-227.
DR PDB; 6OM7; EM; 3.70 A; SD=2-227.
DR PDB; 6QZP; EM; 2.90 A; SD=1-227.
DR PDB; 6XA1; EM; 2.80 A; SD=4-227.
DR PDB; 6Y0G; EM; 3.20 A; SD=1-243.
DR PDB; 6Y2L; EM; 3.00 A; SD=1-243.
DR PDB; 6Y57; EM; 3.50 A; SD=1-243.
DR PDB; 6YBS; EM; 3.10 A; Z=1-243.
DR PDB; 6Z6L; EM; 3.00 A; SD=1-243.
DR PDB; 6Z6M; EM; 3.10 A; SD=1-243.
DR PDB; 6Z6N; EM; 2.90 A; SD=1-243.
DR PDB; 6ZLW; EM; 2.60 A; F=1-243.
DR PDB; 6ZM7; EM; 2.70 A; SD=1-243.
DR PDB; 6ZME; EM; 3.00 A; SD=1-243.
DR PDB; 6ZMI; EM; 2.60 A; SD=1-243.
DR PDB; 6ZMO; EM; 3.10 A; SD=1-243.
DR PDB; 6ZMT; EM; 3.00 A; F=1-243.
DR PDB; 6ZMW; EM; 3.70 A; Z=1-243.
DR PDB; 6ZN5; EM; 3.20 A; F=3-227.
DR PDB; 6ZOJ; EM; 2.80 A; D=1-243.
DR PDB; 6ZOL; EM; 2.80 A; D=1-243.
DR PDB; 6ZON; EM; 3.00 A; b=1-243.
DR PDB; 6ZP4; EM; 2.90 A; b=1-243.
DR PDB; 6ZUO; EM; 3.10 A; D=1-243.
DR PDB; 6ZV6; EM; 2.90 A; D=1-243.
DR PDB; 6ZVH; EM; 2.90 A; D=1-227.
DR PDB; 6ZVJ; EM; 3.80 A; b=4-227.
DR PDB; 6ZXD; EM; 3.20 A; D=1-243.
DR PDB; 6ZXE; EM; 3.00 A; D=1-243.
DR PDB; 6ZXF; EM; 3.70 A; D=1-243.
DR PDB; 6ZXG; EM; 2.60 A; D=1-243.
DR PDB; 6ZXH; EM; 2.70 A; D=1-243.
DR PDB; 7A09; EM; 3.50 A; b=1-243.
DR PDB; 7K5I; EM; 2.90 A; D=1-243.
DR PDBsum; 1WH9; -.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P23396; -.
DR BMRB; P23396; -.
DR SMR; P23396; -.
DR BioGRID; 112102; 702.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P23396; -.
DR DIP; DIP-33177N; -.
DR ELM; P23396; -.
DR IntAct; P23396; 140.
DR MINT; P23396; -.
DR STRING; 9606.ENSP00000278572; -.
DR MoonProt; P23396; -.
DR GlyGen; P23396; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P23396; -.
DR MetOSite; P23396; -.
DR PhosphoSitePlus; P23396; -.
DR SwissPalm; P23396; -.
DR BioMuta; RPS3; -.
DR DMDM; 417719; -.
DR EPD; P23396; -.
DR jPOST; P23396; -.
DR MassIVE; P23396; -.
DR MaxQB; P23396; -.
DR PaxDb; P23396; -.
DR PeptideAtlas; P23396; -.
DR PRIDE; P23396; -.
DR ProteomicsDB; 54087; -. [P23396-1]
DR Antibodypedia; 31150; 358 antibodies from 36 providers.
DR DNASU; 6188; -.
DR Ensembl; ENST00000278572.10; ENSP00000278572.6; ENSG00000149273.15. [P23396-2]
DR Ensembl; ENST00000524851.5; ENSP00000433821.1; ENSG00000149273.15. [P23396-1]
DR Ensembl; ENST00000527446.5; ENSP00000436971.1; ENSG00000149273.15. [P23396-1]
DR Ensembl; ENST00000531188.6; ENSP00000434643.1; ENSG00000149273.15. [P23396-1]
DR GeneID; 6188; -.
DR KEGG; hsa:6188; -.
DR MANE-Select; ENST00000531188.6; ENSP00000434643.1; NM_001005.5; NP_000996.2.
DR UCSC; uc001owh.5; human. [P23396-1]
DR CTD; 6188; -.
DR DisGeNET; 6188; -.
DR GeneCards; RPS3; -.
DR HGNC; HGNC:10420; RPS3.
DR HPA; ENSG00000149273; Low tissue specificity.
DR MIM; 600454; gene.
DR neXtProt; NX_P23396; -.
DR OpenTargets; ENSG00000149273; -.
DR PharmGKB; PA34829; -.
DR VEuPathDB; HostDB:ENSG00000149273; -.
DR eggNOG; KOG3181; Eukaryota.
DR GeneTree; ENSGT00390000008610; -.
DR HOGENOM; CLU_058591_2_1_1; -.
DR InParanoid; P23396; -.
DR OMA; YIKKCGE; -.
DR OrthoDB; 1135751at2759; -.
DR PhylomeDB; P23396; -.
DR TreeFam; TF300901; -.
DR PathwayCommons; P23396; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P23396; -.
DR SIGNOR; P23396; -.
DR BioGRID-ORCS; 6188; 789 hits in 1043 CRISPR screens.
DR ChiTaRS; RPS3; human.
DR EvolutionaryTrace; P23396; -.
DR GeneWiki; RPS3; -.
DR GenomeRNAi; 6188; -.
DR Pharos; P23396; Tbio.
DR PRO; PR:P23396; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P23396; protein.
DR Bgee; ENSG00000149273; Expressed in left ovary and 102 other tissues.
DR ExpressionAtlas; P23396; baseline and differential.
DR Genevisible; P23396; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0071159; C:NF-kappaB complex; IDA:CAFA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; NAS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0032357; F:oxidized purine DNA binding; IDA:UniProtKB.
DR GO; GO:0032358; F:oxidized pyrimidine DNA binding; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0097100; F:supercoiled DNA binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:CAFA.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0045738; P:negative regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:CAFA.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:1905053; P:positive regulation of base-excision repair; IDA:UniProtKB.
DR GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
DR GO; GO:1902546; P:positive regulation of DNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:CAFA.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:CAFA.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:CAFA.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:CAFA.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0061481; P:response to TNF agonist; IDA:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; NAS:UniProtKB.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
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 SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01008; uS3_euk_arch; 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; Apoptosis; Cell cycle;
KW Cell division; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW DNA damage; DNA repair; DNA-binding; Isopeptide bond; Lyase; Membrane;
KW Methylation; Mitochondrion; Mitochondrion inner membrane; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..243
FT /note="40S ribosomal protein S3"
FT /id="PRO_0000130320"
FT DOMAIN 21..92
FT /note="KH type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00118"
FT REGION 214..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 6
FT /note="Phosphoserine; by PKC/PRKCD"
FT /evidence="ECO:0000269|PubMed:19059439"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:15950189"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 64
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:19460357"
FT MOD_RES 65
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:19460357"
FT MOD_RES 67
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:19460357"
FT MOD_RES 70
FT /note="Phosphothreonine; by PKB"
FT /evidence="ECO:0000269|PubMed:20605787"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62908"
FT MOD_RES 209
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000269|PubMed:21399639"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphothreonine; by CDK1 and PKC/PRKCD"
FT /evidence="ECO:0000269|PubMed:19059439,
FT ECO:0000269|PubMed:21871177, ECO:0000269|Ref.12,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 85
FT /note="E -> ELKIMVMVTGYPLLPLK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046667"
FT MUTAGEN 6
FT /note="S->A: No effect on phosphorylation by CDK1. Greatly
FT reduced phosphorylation by PRKCD. Abolishes phosphorylation
FT by PRKCD; when associated with A-221."
FT /evidence="ECO:0000269|PubMed:19059439,
FT ECO:0000269|PubMed:21871177"
FT MUTAGEN 18
FT /note="K->R: No effect on sumoylation. Abolishes
FT sumoylation; when associated with R-214 and R-230."
FT /evidence="ECO:0000269|PubMed:21968017"
FT MUTAGEN 35
FT /note="S->A: No effect on phosphorylation by PRKCD."
FT /evidence="ECO:0000269|PubMed:19059439"
FT MUTAGEN 42
FT /note="T->A: Abolishes phosphorylation by MAPK and
FT translocation to the nucleus following exposure of cells to
FT hydrogen peroxide. No effect on phosphorylation by CDK1 or
FT PRKCD."
FT /evidence="ECO:0000269|PubMed:15950189,
FT ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:19059439,
FT ECO:0000269|PubMed:21871177"
FT MUTAGEN 42
FT /note="T->D: Phosphomimetic mutant which is detected
FT exclusively in the nucleus."
FT /evidence="ECO:0000269|PubMed:17560175"
FT MUTAGEN 70
FT /note="T->A: No effect on phosphorylation by PRKCD.
FT Abolishes phosphorylation by PKB."
FT /evidence="ECO:0000269|PubMed:19059439,
FT ECO:0000269|PubMed:20605787"
FT MUTAGEN 70
FT /note="T->D,E,R: Abolishes phosphorylation by PKB."
FT /evidence="ECO:0000269|PubMed:20605787"
FT MUTAGEN 132
FT /note="K->A: Does not affect ability to cleave DNA but
FT abolishes binding to 8-oxoG."
FT /evidence="ECO:0000269|PubMed:16737853"
FT MUTAGEN 139
FT /note="S->A: No effect on phosphorylation by PRKCD."
FT /evidence="ECO:0000269|PubMed:19059439"
FT MUTAGEN 149
FT /note="S->A: No effect on phosphorylation by PRKCD."
FT /evidence="ECO:0000269|PubMed:19059439"
FT MUTAGEN 195
FT /note="T->A: No effect on phosphorylation by PRKCD."
FT /evidence="ECO:0000269|PubMed:19059439"
FT MUTAGEN 209
FT /note="S->A: Reduced phosphorylation by IKKB."
FT /evidence="ECO:0000269|PubMed:21399639"
FT MUTAGEN 214
FT /note="K->R: No effect on sumoylation. Abolishes
FT sumoylation; when associated with R-18 and R-230."
FT /evidence="ECO:0000269|PubMed:21968017"
FT MUTAGEN 221
FT /note="T->A: No effect on phosphorylation by MAPK.
FT Significantly reduces phosphorylation by CDK1 and nuclear
FT accumulation. Greatly reduced phosphorylation by PRKCD.
FT Abolishes phosphorylation by PRKCD; when associated with A-
FT 6."
FT /evidence="ECO:0000269|PubMed:15950189,
FT ECO:0000269|PubMed:19059439, ECO:0000269|PubMed:21871177"
FT MUTAGEN 230
FT /note="K->R: No effect on sumoylation. Abolishes
FT sumoylation; when associated with R-18 and R-214."
FT /evidence="ECO:0000269|PubMed:21968017"
FT CONFLICT 8
FT /note="K -> R (in Ref. 2; AAB19349)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> C (in Ref. 1; CAA39248)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="P -> L (in Ref. 1; CAA39248)"
FT /evidence="ECO:0000305"
FT HELIX 7..29
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 132..146
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6ZLW"
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
