RS2_YEAST
ID RS2_YEAST Reviewed; 254 AA.
AC P25443; D6VU25;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=40S ribosomal protein S2 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Omnipotent suppressor protein SUP44;
DE AltName: Full=RP12;
DE AltName: Full=S4;
DE AltName: Full=Small ribosomal subunit protein uS5 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS5;
GN Name=RPS2 {ECO:0000303|PubMed:9559554}; Synonyms=RPS4, SUP38, SUP44;
GN OrderedLocusNames=YGL123W; ORFNames=G2893;
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].
RX PubMed=2247072; DOI=10.1128/mcb.10.12.6544-6553.1990;
RA All-Robyn J.A., Brown N., Otaka E., Liebman S.W.;
RT "Sequence and functional similarity between a yeast ribosomal protein and
RT the Escherichia coli S5 ram protein.";
RL Mol. Cell. Biol. 10:6544-6553(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896269;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1047::aid-yea991>3.0.co;2-n;
RA Tizon B., Rodriguez-Torres A.M., Rodriguez-Belmonte E., Cadahia J.L.,
RA Cerdan E.;
RT "Identification of a putative methylenetetrahydrofolate reductase by
RT sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII.";
RL Yeast 12:1047-1051(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT SER-2.
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 [7]
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 [8]
RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
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 [9]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [10]
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 [11]
RP METHYLATION BY HMT1.
RX PubMed=20035717; DOI=10.1016/j.bbrc.2009.12.112;
RA Lipson R.S., Webb K.J., Clarke S.G.;
RT "Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal
RT protein Rps2 in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 391:1658-1662(2010).
RN [12]
RP METHYLATION AT ARG-11.
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [15]
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 [16]
RP METHYLATION AT ARG-11 AND ARG-17.
RX PubMed=26081071; DOI=10.1002/pmic.201500075;
RA Yagoub D., Hart-Smith G., Moecking J., Erce M.A., Wilkins M.R.;
RT "Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively
RT methylated and are substrates of the arginine methyltransferase Hmt1p.";
RL Proteomics 15:3209-3218(2015).
RN [17]
RP 3D-STRUCTURE MODELING OF 75-223.
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 [18]
RP 3D-STRUCTURE MODELING OF 75-223, 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 [19]
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 [20]
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 [21]
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 [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 1-254.
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 (PubMed:22096102). uS5 is important for the assembly and
CC function of the 40S ribosomal subunit. Mutations in this protein
CC affects the control of translational fidelity. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly
CC (PubMed:15590835). {ECO:0000269|PubMed:15590835,
CC 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 Interacts with snoRNA U3. Interacts with MPP10. Component of the
CC ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3 (PubMed:15590835).
CC {ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15590835}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; M59375; AAA63576.1; -; Genomic_DNA.
DR EMBL; X94106; CAA63835.1; -; Genomic_DNA.
DR EMBL; Z72645; CAA96831.1; -; Genomic_DNA.
DR EMBL; AY557815; AAS56141.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07986.1; -; Genomic_DNA.
DR PIR; A36363; R3BYS2.
DR RefSeq; NP_011392.1; NM_001180988.1.
DR PDB; 3J6X; EM; 6.10 A; S2=1-254.
DR PDB; 3J6Y; EM; 6.10 A; S2=1-254.
DR PDB; 3J77; EM; 6.20 A; S2=1-254.
DR PDB; 3J78; EM; 6.30 A; S2=1-254.
DR PDB; 4U3M; X-ray; 3.00 A; S2/s2=2-254.
DR PDB; 4U3N; X-ray; 3.20 A; S2/s2=2-254.
DR PDB; 4U3U; X-ray; 2.90 A; S2/s2=2-254.
DR PDB; 4U4N; X-ray; 3.10 A; S2/s2=2-254.
DR PDB; 4U4O; X-ray; 3.60 A; S2/s2=2-254.
DR PDB; 4U4Q; X-ray; 3.00 A; S2/s2=2-254.
DR PDB; 4U4R; X-ray; 2.80 A; S2/s2=2-254.
DR PDB; 4U4U; X-ray; 3.00 A; S2/s2=2-254.
DR PDB; 4U4Y; X-ray; 3.20 A; S2/s2=2-254.
DR PDB; 4U4Z; X-ray; 3.10 A; S2/s2=2-254.
DR PDB; 4U50; X-ray; 3.20 A; S2/s2=2-254.
DR PDB; 4U51; X-ray; 3.20 A; S2/s2=2-254.
DR PDB; 4U52; X-ray; 3.00 A; S2/s2=2-254.
DR PDB; 4U53; X-ray; 3.30 A; S2/s2=2-254.
DR PDB; 4U55; X-ray; 3.20 A; S2/s2=2-254.
DR PDB; 4U56; X-ray; 3.45 A; S2/s2=2-254.
DR PDB; 4U6F; X-ray; 3.10 A; S2/s2=2-254.
DR PDB; 4V4B; EM; 11.70 A; AE=75-223.
DR PDB; 4V6I; EM; 8.80 A; AE=1-254.
DR PDB; 4V7R; X-ray; 4.00 A; AB/CB=1-254.
DR PDB; 4V88; X-ray; 3.00 A; AC/CC=1-254.
DR PDB; 4V8Y; EM; 4.30 A; AC=1-254.
DR PDB; 4V8Z; EM; 6.60 A; AC=1-254.
DR PDB; 4V92; EM; 3.70 A; C=34-249.
DR PDB; 5DAT; X-ray; 3.15 A; S2/s2=2-254.
DR PDB; 5DC3; X-ray; 3.25 A; S2/s2=2-254.
DR PDB; 5DGE; X-ray; 3.45 A; S2/s2=2-254.
DR PDB; 5DGF; X-ray; 3.30 A; S2/s2=2-254.
DR PDB; 5DGV; X-ray; 3.10 A; S2/s2=2-254.
DR PDB; 5FCI; X-ray; 3.40 A; S2/s2=2-254.
DR PDB; 5FCJ; X-ray; 3.10 A; S2/s2=2-254.
DR PDB; 5I4L; X-ray; 3.10 A; S2/s2=34-250.
DR PDB; 5JUO; EM; 4.00 A; ZA=1-254.
DR PDB; 5JUP; EM; 3.50 A; ZA=1-254.
DR PDB; 5JUS; EM; 4.20 A; ZA=1-254.
DR PDB; 5JUT; EM; 4.00 A; ZA=1-254.
DR PDB; 5JUU; EM; 4.00 A; ZA=1-254.
DR PDB; 5LL6; EM; 3.90 A; R=1-254.
DR PDB; 5LYB; X-ray; 3.25 A; S2/s2=34-250.
DR PDB; 5M1J; EM; 3.30 A; C2=34-250.
DR PDB; 5MC6; EM; 3.80 A; R=1-254.
DR PDB; 5MEI; X-ray; 3.50 A; D/s2=34-250.
DR PDB; 5NDG; X-ray; 3.70 A; S2/s2=34-250.
DR PDB; 5NDV; X-ray; 3.30 A; S2/s2=34-250.
DR PDB; 5NDW; X-ray; 3.70 A; S2/s2=34-250.
DR PDB; 5OBM; X-ray; 3.40 A; S2/s2=34-250.
DR PDB; 5ON6; X-ray; 3.10 A; D/s2=34-250.
DR PDB; 5TBW; X-ray; 3.00 A; D/s2=34-250.
DR PDB; 5TGA; X-ray; 3.30 A; S2/s2=34-250.
DR PDB; 5TGM; X-ray; 3.50 A; S2/s2=34-250.
DR PDB; 6EML; EM; 3.60 A; R=1-254.
DR PDB; 6FAI; EM; 3.40 A; C=1-254.
DR PDB; 6GQ1; EM; 4.40 A; s=34-250.
DR PDB; 6GQB; EM; 3.90 A; s=34-250.
DR PDB; 6GQV; EM; 4.00 A; s=34-250.
DR PDB; 6HHQ; X-ray; 3.10 A; D/s2=1-254.
DR PDB; 6I7O; EM; 5.30 A; R/Rb=34-250.
DR PDB; 6Q8Y; EM; 3.10 A; R=35-254.
DR PDB; 6RBD; EM; 3.47 A; C=1-254.
DR PDB; 6RBE; EM; 3.80 A; C=1-254.
DR PDB; 6S47; EM; 3.28 A; BD=2-254.
DR PDB; 6SNT; EM; 2.80 A; C=1-254.
DR PDB; 6SV4; EM; 3.30 A; R/Rb/Rc=1-254.
DR PDB; 6T4Q; EM; 2.60 A; SC=34-249.
DR PDB; 6T7I; EM; 3.20 A; SC=1-254.
DR PDB; 6T7T; EM; 3.10 A; SC=1-254.
DR PDB; 6T83; EM; 4.00 A; Cb/d=1-254.
DR PDB; 6TB3; EM; 2.80 A; R=34-249.
DR PDB; 6TNU; EM; 3.10 A; R=34-249.
DR PDB; 6WDR; EM; 3.70 A; C=34-250.
DR PDB; 6WOO; EM; 2.90 A; CC=34-250.
DR PDB; 6Y7C; EM; 3.80 A; C=1-254.
DR PDB; 6Z6J; EM; 3.40 A; SC=1-254.
DR PDB; 6Z6K; EM; 3.40 A; SC=1-254.
DR PDB; 6ZCE; EM; 5.30 A; D=1-254.
DR PDB; 6ZU9; EM; 6.20 A; R=1-254.
DR PDB; 6ZVI; EM; 3.00 A; k=34-250.
DR PDB; 7A1G; EM; 3.00 A; R=34-249.
DR PDB; 7B7D; EM; 3.30 A; R=34-249.
DR PDB; 7NRC; EM; 3.90 A; SR=34-249.
DR PDB; 7NRD; EM; 4.36 A; SR=34-250.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
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; 5LL6; -.
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; 6EML; -.
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; 6Y7C; -.
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; P25443; -.
DR SMR; P25443; -.
DR BioGRID; 33128; 894.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR IntAct; P25443; 15.
DR MINT; P25443; -.
DR STRING; 4932.YGL123W; -.
DR CarbonylDB; P25443; -.
DR iPTMnet; P25443; -.
DR MaxQB; P25443; -.
DR PaxDb; P25443; -.
DR PRIDE; P25443; -.
DR EnsemblFungi; YGL123W_mRNA; YGL123W; YGL123W.
DR GeneID; 852754; -.
DR KEGG; sce:YGL123W; -.
DR SGD; S000003091; RPS2.
DR VEuPathDB; FungiDB:YGL123W; -.
DR eggNOG; KOG0877; Eukaryota.
DR GeneTree; ENSGT00940000153095; -.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; P25443; -.
DR OMA; DLKNWVP; -.
DR BioCyc; YEAST:G3O-30620-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; P25443; -.
DR PRO; PR:P25443; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P25443; protein.
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:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis; rRNA processing;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT CHAIN 2..254
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131684"
FT DOMAIN 76..139
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT MOD_RES 11
FT /note="Asymmetric dimethylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:20035717,
FT ECO:0000269|PubMed:22650761, ECO:0000269|PubMed:26081071"
FT MOD_RES 11
FT /note="Omega-N-methylarginine; by HMT1; alternate"
FT /evidence="ECO:0000269|PubMed:20035717,
FT ECO:0000269|PubMed:22650761, ECO:0000269|PubMed:26081071"
FT MOD_RES 17
FT /note="Omega-N-methylarginine; by HMT1"
FT /evidence="ECO:0000269|PubMed:26081071"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 77..89
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 91..105
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 107..120
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6RBD"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 254 AA; 27450 MW; 5EFDA4C7DE7BDFFB CRC64;
MSAPEAQQQK RGGFGGRNRG RPNRRGPRNT EEKGWVPVTK LGRLVKAGKI TTIEEIFLHS
LPVKEFQIID TLLPGLQDEV MNIKPVQKQT RAGQRTRFKA VVVVGDSNGH VGLGIKTAKE
VAGAIRAGII IAKLSVIPIR RGYWGTNLGQ PHSLATKTTG KCGSVTVRLI PAPRGSGIVA
SPAVKKLLQL AGVEDVYTQS NGKTRTLENT LKAAFVAIGN TYGFLTPNLW AEQPLPVSPL
DIYSDEASAQ KKRF
