RS5_YEAST
ID RS5_YEAST Reviewed; 225 AA.
AC P26783; D6VWU2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=40S ribosomal protein S5 {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP14;
DE AltName: Full=S2;
DE AltName: Full=Small ribosomal subunit protein uS7 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS8;
GN Name=RPS5 {ECO:0000303|PubMed:9559554}; Synonyms=RPS2;
GN OrderedLocusNames=YJR123W; ORFNames=J2045;
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=8524651; DOI=10.1093/nar/23.22.4616;
RA Ignatovich O., Cooper M., Kulesza H.M., Beggs J.D.;
RT "Cloning and characterisation of the gene encoding the ribosomal protein S5
RT (also known as rp14, S2, YS8) of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 23:4616-4619(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-21, AND ACETYLATION AT SER-2 BY NATA.
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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, AND IDENTIFICATION BY
RP 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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-45 AND LYS-203, AND
RP IDENTIFICATION BY MASS 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 [10]
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 [11]
RP 3D-STRUCTURE MODELING OF 76-225, 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 [12]
RP 3D-STRUCTURE MODELING OF 76-225, 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 [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 76-225.
RX PubMed=17115051; DOI=10.1038/nsmb1177;
RA Schueler M., Connell S.R., Lescoute A., Giesebrecht J., Dabrowski M.,
RA Schroeer B., Mielke T., Penczek P.A., Westhof E., Spahn C.M.T.;
RT "Structure of the ribosome-bound cricket paralysis virus IRES RNA.";
RL Nat. Struct. Mol. Biol. 13:1092-1096(2006).
RN [14]
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 [15]
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).
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 P26783; P48524: BUL1; NbExp=3; IntAct=EBI-16150, EBI-3881;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
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 uS7 family.
CC {ECO:0000305}.
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DR EMBL; X89368; CAA61550.1; -; Genomic_DNA.
DR EMBL; Z49623; CAA89654.1; -; Genomic_DNA.
DR EMBL; AY692868; AAT92887.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08908.1; -; Genomic_DNA.
DR PIR; S55720; S55720.
DR RefSeq; NP_012657.1; NM_001181781.1.
DR PDB; 2NOQ; EM; 7.30 A; F=76-225.
DR PDB; 3J6X; EM; 6.10 A; S5=1-225.
DR PDB; 3J6Y; EM; 6.10 A; S5=1-225.
DR PDB; 3J77; EM; 6.20 A; S5=1-225.
DR PDB; 3J78; EM; 6.30 A; S5=1-225.
DR PDB; 4U3M; X-ray; 3.00 A; S5/s5=2-225.
DR PDB; 4U3N; X-ray; 3.20 A; S5/s5=2-225.
DR PDB; 4U3U; X-ray; 2.90 A; S5/s5=2-225.
DR PDB; 4U4N; X-ray; 3.10 A; S5/s5=2-225.
DR PDB; 4U4O; X-ray; 3.60 A; S5/s5=2-225.
DR PDB; 4U4Q; X-ray; 3.00 A; S5/s5=2-225.
DR PDB; 4U4R; X-ray; 2.80 A; S5/s5=2-225.
DR PDB; 4U4U; X-ray; 3.00 A; S5/s5=2-225.
DR PDB; 4U4Y; X-ray; 3.20 A; S5/s5=2-225.
DR PDB; 4U4Z; X-ray; 3.10 A; S5/s5=2-225.
DR PDB; 4U50; X-ray; 3.20 A; S5/s5=2-225.
DR PDB; 4U51; X-ray; 3.20 A; S5/s5=2-225.
DR PDB; 4U52; X-ray; 3.00 A; S5/s5=2-225.
DR PDB; 4U53; X-ray; 3.30 A; S5/s5=2-225.
DR PDB; 4U55; X-ray; 3.20 A; S5/s5=2-225.
DR PDB; 4U56; X-ray; 3.45 A; S5/s5=2-225.
DR PDB; 4U6F; X-ray; 3.10 A; S5/s5=2-225.
DR PDB; 4V4B; EM; 11.70 A; AG=76-225.
DR PDB; 4V6I; EM; 8.80 A; AF=1-225.
DR PDB; 4V7R; X-ray; 4.00 A; AD/CD=1-225.
DR PDB; 4V88; X-ray; 3.00 A; AF/CF=1-225.
DR PDB; 4V8Y; EM; 4.30 A; AF=1-225.
DR PDB; 4V8Z; EM; 6.60 A; AF=1-225.
DR PDB; 4V92; EM; 3.70 A; F=20-225.
DR PDB; 5DAT; X-ray; 3.15 A; S5/s5=2-225.
DR PDB; 5DC3; X-ray; 3.25 A; S5/s5=2-225.
DR PDB; 5DGE; X-ray; 3.45 A; S5/s5=2-225.
DR PDB; 5DGF; X-ray; 3.30 A; S5/s5=2-225.
DR PDB; 5DGV; X-ray; 3.10 A; S5/s5=2-225.
DR PDB; 5FCI; X-ray; 3.40 A; S5/s5=2-225.
DR PDB; 5FCJ; X-ray; 3.10 A; S5/s5=2-225.
DR PDB; 5I4L; X-ray; 3.10 A; S5/s5=20-225.
DR PDB; 5JPQ; EM; 7.30 A; q=1-225.
DR PDB; 5JUO; EM; 4.00 A; CB=1-225.
DR PDB; 5JUP; EM; 3.50 A; CB=1-225.
DR PDB; 5JUS; EM; 4.20 A; CB=1-225.
DR PDB; 5JUT; EM; 4.00 A; CB=1-225.
DR PDB; 5JUU; EM; 4.00 A; CB=1-225.
DR PDB; 5LYB; X-ray; 3.25 A; S5/s5=20-225.
DR PDB; 5M1J; EM; 3.30 A; F2=20-225.
DR PDB; 5MC6; EM; 3.80 A; B=1-225.
DR PDB; 5MEI; X-ray; 3.50 A; G/s5=20-225.
DR PDB; 5NDG; X-ray; 3.70 A; S5/s5=20-225.
DR PDB; 5NDV; X-ray; 3.30 A; S5/s5=20-225.
DR PDB; 5NDW; X-ray; 3.70 A; S5/s5=20-225.
DR PDB; 5OBM; X-ray; 3.40 A; S5/s5=20-225.
DR PDB; 5ON6; X-ray; 3.10 A; G/s5=20-225.
DR PDB; 5TBW; X-ray; 3.00 A; G/s5=20-225.
DR PDB; 5TGA; X-ray; 3.30 A; S5/s5=20-225.
DR PDB; 5TGM; X-ray; 3.50 A; S5/s5=20-225.
DR PDB; 5TZS; EM; 5.10 A; 6=1-225.
DR PDB; 5WYJ; EM; 8.70 A; SG=1-225.
DR PDB; 5WYK; EM; 4.50 A; SG=1-225.
DR PDB; 6EML; EM; 3.60 A; B=1-225.
DR PDB; 6FAI; EM; 3.40 A; F=1-225.
DR PDB; 6GQ1; EM; 4.40 A; v=20-225.
DR PDB; 6GQB; EM; 3.90 A; v=20-225.
DR PDB; 6GQV; EM; 4.00 A; v=20-225.
DR PDB; 6HHQ; X-ray; 3.10 A; G/s5=1-225.
DR PDB; 6I7O; EM; 5.30 A; B/Bb=20-225.
DR PDB; 6KE6; EM; 3.40 A; SG=1-225.
DR PDB; 6LQP; EM; 3.20 A; SG=1-225.
DR PDB; 6LQQ; EM; 4.10 A; SG=1-225.
DR PDB; 6LQR; EM; 8.60 A; SG=1-225.
DR PDB; 6LQS; EM; 3.80 A; SG=1-225.
DR PDB; 6LQT; EM; 4.90 A; SG=1-225.
DR PDB; 6LQU; EM; 3.70 A; SG=1-225.
DR PDB; 6LQV; EM; 4.80 A; SG=1-225.
DR PDB; 6RBD; EM; 3.47 A; F=1-225.
DR PDB; 6RBE; EM; 3.80 A; F=1-225.
DR PDB; 6SNT; EM; 2.80 A; F=1-225.
DR PDB; 6WDR; EM; 3.70 A; F=20-225.
DR PDB; 6Y7C; EM; 3.80 A; F=1-225.
DR PDB; 6Z6J; EM; 3.40 A; SF=1-225.
DR PDB; 6ZCE; EM; 5.30 A; G=1-225.
DR PDB; 6ZQA; EM; 4.40 A; DF=1-225.
DR PDB; 6ZQB; EM; 3.90 A; DF=1-225.
DR PDB; 6ZQC; EM; 3.80 A; DF=1-225.
DR PDB; 6ZQE; EM; 7.10 A; DF=1-225.
DR PDB; 6ZQF; EM; 4.90 A; DF=1-225.
DR PDB; 6ZQG; EM; 3.50 A; DF=1-225.
DR PDB; 6ZU9; EM; 6.20 A; C=1-225.
DR PDB; 6ZVI; EM; 3.00 A; n=20-225.
DR PDB; 7A1G; EM; 3.00 A; B=20-225.
DR PDB; 7AJT; EM; 4.60 A; DF=1-225.
DR PDB; 7AJU; EM; 3.80 A; DF=1-225.
DR PDB; 7B7D; EM; 3.30 A; B=20-225.
DR PDB; 7D4I; EM; 4.00 A; SG=1-225.
DR PDB; 7D5S; EM; 4.60 A; SG=1-225.
DR PDB; 7D5T; EM; 6.00 A; SG=1-225.
DR PDB; 7D63; EM; 12.30 A; SG=1-225.
DR PDB; 7NRC; EM; 3.90 A; SB=20-225.
DR PDB; 7NRD; EM; 4.36 A; SB=20-225.
DR PDBsum; 2NOQ; -.
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; 5JPQ; -.
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; 5TZS; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P26783; -.
DR SMR; P26783; -.
DR BioGRID; 33879; 152.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR DIP; DIP-5092N; -.
DR IntAct; P26783; 73.
DR MINT; P26783; -.
DR STRING; 4932.YJR123W; -.
DR CarbonylDB; P26783; -.
DR iPTMnet; P26783; -.
DR UCD-2DPAGE; P26783; -.
DR MaxQB; P26783; -.
DR PaxDb; P26783; -.
DR PRIDE; P26783; -.
DR EnsemblFungi; YJR123W_mRNA; YJR123W; YJR123W.
DR GeneID; 853587; -.
DR KEGG; sce:YJR123W; -.
DR SGD; S000003884; RPS5.
DR VEuPathDB; FungiDB:YJR123W; -.
DR eggNOG; KOG3291; Eukaryota.
DR GeneTree; ENSGT00390000010806; -.
DR HOGENOM; CLU_063975_0_0_1; -.
DR InParanoid; P26783; -.
DR OMA; KMNIVER; -.
DR BioCyc; YEAST:G3O-31744-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; P26783; -.
DR PRO; PR:P26783; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P26783; 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:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006450; P:regulation of translational fidelity; ISA:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd14867; uS7_Eukaryote; 1.
DR Gene3D; 1.10.455.10; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01028; uS7_euk_arch; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921"
FT CHAIN 2..225
FT /note="40S ribosomal protein S5"
FT /id="PRO_0000124540"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 21
FT /note="T -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 164..182
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 225 AA; 25039 MW; CD3F743B56CB1127 CRC64;
MSDTEAPVEV QEDFEVVEEF TPVVLATPIP EEVQQAQTEI KLFNKWSFEE VEVKDASLVD
YVQVRQPIFV AHTAGRYANK RFRKAQCPII ERLTNSLMMN GRNNGKKLKA VRIIKHTLDI
INVLTDQNPI QVVVDAITNT GPREDTTRVG GGGAARRQAV DVSPLRRVNQ AIALLTIGAR
EAAFRNIKTI AETLAEELIN AAKGSSTSYA IKKKDELERV AKSNR
