RS3_YEAST
ID RS3_YEAST Reviewed; 240 AA.
AC P05750; D6W107;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=40S ribosomal protein S3 {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP13 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein uS3 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS3 {ECO:0000303|PubMed:9559554};
GN Name=RPS3 {ECO:0000303|PubMed:9559554}; Synonyms=SUF14;
GN OrderedLocusNames=YNL178W {ECO:0000312|SGD:S000005122}; ORFNames=N1653;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBY874;
RX PubMed=8670293; DOI=10.1006/bbrc.1996.0905;
RA Finken-Eigen M., Domdey H., Koehrer K.;
RT "The ribosomal protein gene RPS3 is an essential single copy gene of the
RT yeast Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 223:397-403(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=ATCC 204508 / S288c;
RA Okazaki M., Suzuki K., Otaka E.;
RT "Yeast mRNA for ribosomal protein YS3.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Burbee D.G., Armstrong B.C.;
RT "Molecular cloning and analysis of the RPS3 gene of Saccharomyces
RT cerevisiae.";
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP PARTIAL PROTEIN SEQUENCE OF 2-21, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=18782943; DOI=10.1007/bf00341461;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL Mol. Gen. Genet. 195:544-546(1984).
RN [7]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 267:5442-5445(1992).
RN [8]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [9]
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-212, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-129 AND SER-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44; SER-97 AND SER-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND THR-231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP METHYLATION AT ARG-146 BY SFM1, AND MASS SPECTROMETRY.
RX PubMed=22650761; DOI=10.1021/bi300186g;
RA Young B.D., Weiss D.I., Zurita-Lopez C.I., Webb K.J., Clarke S.G.,
RA McBride A.E.;
RT "Identification of methylated proteins in the yeast small ribosomal
RT subunit: a role for SPOUT methyltransferases in protein arginine
RT methylation.";
RL Biochemistry 51:5091-5104(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-132; LYS-141;
RP LYS-151; LYS-200 AND LYS-212, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [19]
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 [20]
RP UBIQUITINATION AT LYS-212, AND MUTAGENESIS OF LYS-212.
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 [21]
RP 3D-STRUCTURE MODELING OF 6-193, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [22]
RP 3D-STRUCTURE MODELING OF 2-193, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [23]
RP STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=20980660; DOI=10.1073/pnas.1009999107;
RA Armache J.P., Jarasch A., Anger A.M., Villa E., Becker T., Bhushan S.,
RA Jossinet F., Habeck M., Dindar G., Franckenberg S., Marquez V., Mielke T.,
RA Thomm M., Berninghausen O., Beatrix B., Soding J., Westhof E., Wilson D.N.,
RA Beckmann R.;
RT "Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome
RT at 5.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19748-19753(2010).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 1-240.
RX PubMed=24021814; DOI=10.1016/j.jmb.2013.08.022;
RA Holzer S., Ban N., Klinge S.;
RT "Crystal structure of the yeast ribosomal protein rpS3 in complex with its
RT chaperone Yar1.";
RL J. Mol. Biol. 425:4154-4160(2013).
RN [27]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 1-240.
RX PubMed=24200810; DOI=10.1126/science.1240585;
RA Fernandez I.S., Bai X.C., Hussain T., Kelley A.C., Lorsch J.R.,
RA Ramakrishnan V., Scheres S.H.;
RT "Molecular architecture of a eukaryotic translational initiation complex.";
RL Science 342:1240585-1240585(2013).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- INTERACTION:
CC P05750; P34078: LTV1; NbExp=2; IntAct=EBI-16140, EBI-10248;
CC P05750; P40160: RIO2; NbExp=2; IntAct=EBI-16140, EBI-29124;
CC P05750; P46683: YAR1; NbExp=2; IntAct=EBI-16140, EBI-20829;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- PTM: Ubiquitinated at 'Lys-212' by HEL2/UBC4.
CC {ECO:0000269|PubMed:28757607}.
CC -!- MASS SPECTROMETRY: Mass=26384.3; Method=Electrospray; Note=The measured
CC mass is that of the monomethylated protein.;
CC Evidence={ECO:0000269|PubMed:22650761};
CC -!- MISCELLANEOUS: Present with 146000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000305}.
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DR EMBL; U34347; AAC49380.1; -; Genomic_DNA.
DR EMBL; D25285; BAA04973.1; -; mRNA.
DR EMBL; L31405; AAA35010.1; -; Genomic_DNA.
DR EMBL; Z71454; CAA96070.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10373.1; -; Genomic_DNA.
DR PIR; S48510; S48510.
DR RefSeq; NP_014221.3; NM_001183016.3.
DR PDB; 3J6X; EM; 6.10 A; S3=1-240.
DR PDB; 3J6Y; EM; 6.10 A; S3=1-240.
DR PDB; 3J77; EM; 6.20 A; S3=1-240.
DR PDB; 3J78; EM; 6.30 A; S3=1-240.
DR PDB; 4BSZ; X-ray; 2.84 A; A=1-240.
DR PDB; 4U3M; X-ray; 3.00 A; S3/s3=2-240.
DR PDB; 4U3N; X-ray; 3.20 A; S3/s3=2-240.
DR PDB; 4U3U; X-ray; 2.90 A; S3/s3=2-240.
DR PDB; 4U4N; X-ray; 3.10 A; S3/s3=2-240.
DR PDB; 4U4O; X-ray; 3.60 A; S3/s3=2-240.
DR PDB; 4U4Q; X-ray; 3.00 A; S3/s3=2-240.
DR PDB; 4U4R; X-ray; 2.80 A; S3/s3=2-240.
DR PDB; 4U4U; X-ray; 3.00 A; S3/s3=2-240.
DR PDB; 4U4Y; X-ray; 3.20 A; S3/s3=2-240.
DR PDB; 4U4Z; X-ray; 3.10 A; S3/s3=2-240.
DR PDB; 4U50; X-ray; 3.20 A; S3/s3=2-240.
DR PDB; 4U51; X-ray; 3.20 A; S3/s3=2-240.
DR PDB; 4U52; X-ray; 3.00 A; S3/s3=2-240.
DR PDB; 4U53; X-ray; 3.30 A; S3/s3=2-240.
DR PDB; 4U55; X-ray; 3.20 A; S3/s3=2-240.
DR PDB; 4U56; X-ray; 3.45 A; S3/s3=2-240.
DR PDB; 4U6F; X-ray; 3.10 A; S3/s3=2-240.
DR PDB; 4V4B; EM; 11.70 A; AC=2-193.
DR PDB; 4V6I; EM; 8.80 A; AB=1-240.
DR PDB; 4V7R; X-ray; 4.00 A; AC/CC=1-240.
DR PDB; 4V88; X-ray; 3.00 A; AD/CD=1-240.
DR PDB; 4V8Y; EM; 4.30 A; AD=1-240.
DR PDB; 4V8Z; EM; 6.60 A; AD=1-240.
DR PDB; 4V92; EM; 3.70 A; D=4-225.
DR PDB; 5DAT; X-ray; 3.15 A; S3/s3=2-240.
DR PDB; 5DC3; X-ray; 3.25 A; S3/s3=2-240.
DR PDB; 5DGE; X-ray; 3.45 A; S3/s3=2-240.
DR PDB; 5DGF; X-ray; 3.30 A; S3/s3=2-240.
DR PDB; 5DGV; X-ray; 3.10 A; S3/s3=2-240.
DR PDB; 5FCI; X-ray; 3.40 A; S3/s3=2-240.
DR PDB; 5FCJ; X-ray; 3.10 A; S3/s3=2-240.
DR PDB; 5I4L; X-ray; 3.10 A; S3/s3=3-225.
DR PDB; 5JUO; EM; 4.00 A; AB=1-240.
DR PDB; 5JUP; EM; 3.50 A; AB=1-240.
DR PDB; 5JUS; EM; 4.20 A; AB=1-240.
DR PDB; 5JUT; EM; 4.00 A; AB=1-240.
DR PDB; 5JUU; EM; 4.00 A; AB=1-240.
DR PDB; 5LYB; X-ray; 3.25 A; S3/s3=3-225.
DR PDB; 5M1J; EM; 3.30 A; D2=3-225.
DR PDB; 5MC6; EM; 3.80 A; A=1-240.
DR PDB; 5MEI; X-ray; 3.50 A; E/s3=3-225.
DR PDB; 5NDG; X-ray; 3.70 A; S3/s3=3-225.
DR PDB; 5NDV; X-ray; 3.30 A; S3/s3=3-225.
DR PDB; 5NDW; X-ray; 3.70 A; S3/s3=3-225.
DR PDB; 5OBM; X-ray; 3.40 A; S3/s3=3-225.
DR PDB; 5ON6; X-ray; 3.10 A; E/s3=3-225.
DR PDB; 5TBW; X-ray; 3.00 A; E/s3=3-225.
DR PDB; 5TGA; X-ray; 3.30 A; S3/s3=3-225.
DR PDB; 5TGM; X-ray; 3.50 A; S3/s3=3-225.
DR PDB; 6FAI; EM; 3.40 A; D=1-240.
DR PDB; 6GQ1; EM; 4.40 A; t=3-225.
DR PDB; 6GQB; EM; 3.90 A; t=3-225.
DR PDB; 6GQV; EM; 4.00 A; t=3-225.
DR PDB; 6HHQ; X-ray; 3.10 A; E/s3=1-240.
DR PDB; 6I7O; EM; 5.30 A; A/Ab=3-225.
DR PDB; 6Q8Y; EM; 3.10 A; A=3-225.
DR PDB; 6RBD; EM; 3.47 A; D=1-240.
DR PDB; 6RBE; EM; 3.80 A; D=1-240.
DR PDB; 6S47; EM; 3.28 A; BE=2-240.
DR PDB; 6SNT; EM; 2.80 A; D=1-240.
DR PDB; 6SV4; EM; 3.30 A; A/Ab/Ac=1-240.
DR PDB; 6T4Q; EM; 2.60 A; SD=4-225.
DR PDB; 6T7I; EM; 3.20 A; SD=1-240.
DR PDB; 6T7T; EM; 3.10 A; SD=1-240.
DR PDB; 6T83; EM; 4.00 A; Db/e=1-240.
DR PDB; 6TB3; EM; 2.80 A; A=4-225.
DR PDB; 6TNU; EM; 3.10 A; A=4-225.
DR PDB; 6WDR; EM; 3.70 A; D=3-225.
DR PDB; 6WOO; EM; 2.90 A; DD=3-225.
DR PDB; 6Z6J; EM; 3.40 A; SD=1-240.
DR PDB; 6Z6K; EM; 3.40 A; SD=1-240.
DR PDB; 6ZCE; EM; 5.30 A; E=1-240.
DR PDB; 6ZU9; EM; 6.20 A; B=1-240.
DR PDB; 6ZVI; EM; 3.00 A; l=3-225.
DR PDB; 7A1G; EM; 3.00 A; A=4-225.
DR PDB; 7B7D; EM; 3.30 A; A=4-225.
DR PDB; 7NRC; EM; 3.90 A; SA=4-225.
DR PDB; 7NRD; EM; 4.36 A; SA=3-225.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4BSZ; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P05750; -.
DR SMR; P05750; -.
DR BioGRID; 35653; 925.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR DIP; DIP-4328N; -.
DR IntAct; P05750; 107.
DR MINT; P05750; -.
DR STRING; 4932.YNL178W; -.
DR CarbonylDB; P05750; -.
DR iPTMnet; P05750; -.
DR UCD-2DPAGE; P05750; -.
DR MaxQB; P05750; -.
DR PaxDb; P05750; -.
DR PRIDE; P05750; -.
DR EnsemblFungi; YNL178W_mRNA; YNL178W; YNL178W.
DR GeneID; 855543; -.
DR KEGG; sce:YNL178W; -.
DR SGD; S000005122; RPS3.
DR VEuPathDB; FungiDB:YNL178W; -.
DR eggNOG; KOG3181; Eukaryota.
DR GeneTree; ENSGT00390000008610; -.
DR HOGENOM; CLU_058591_2_1_1; -.
DR InParanoid; P05750; -.
DR OMA; YIKKCGE; -.
DR BioCyc; YEAST:G3O-33190-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P05750; -.
DR PRO; PR:P05750; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P05750; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:SGD.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:SGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IGI:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
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; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0000269|PubMed:18782943"
FT CHAIN 2..240
FT /note="40S ribosomal protein S3"
FT /id="PRO_0000130332"
FT DOMAIN 21..92
FT /note="KH type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00118"
FT REGION 212..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 146
FT /note="Omega-N-methylarginine; by SFM1"
FT /evidence="ECO:0000269|PubMed:22650761"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28757607,
FT ECO:0007744|PubMed:22106047"
FT MUTAGEN 212
FT /note="K->R: Abolishes ubiquitination by HEL2/UBC4."
FT /evidence="ECO:0000269|PubMed:28757607"
FT CONFLICT 17
FT /note="F -> N (in Ref. 3; AAA35010)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..224
FT /note="KD -> NH (in Ref. 3; AAA35010)"
FT /evidence="ECO:0000305"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:4BSZ"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:4BSZ"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:4BSZ"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4BSZ"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4BSZ"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:4BSZ"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:4BSZ"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4BSZ"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 240 AA; 26503 MW; B85C0DFEB011745F CRC64;
MVALISKKRK LVADGVFYAE LNEFFTRELA EEGYSGVEVR VTPTKTEVII RATRTQDVLG
ENGRRINELT LLVQKRFKYA PGTIVLYAER VQDRGLSAVA QAESMKFKLL NGLAIRRAAY
GVVRYVMESG AKGCEVVVSG KLRAARAKAM KFADGFLIHS GQPVNDFIDT ATRHVLMRQG
VLGIKVKIMR DPAKSRTGPK ALPDAVTIIE PKEEEPILAP SVKDYRPAEE TEAQAEPVEA
