ID   RS28A_YEAST             Reviewed;          67 AA.
AC   Q3E7X9; D6W2M5; P02380;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Small ribosomal subunit protein eS28A {ECO:0000303|PubMed:24524803};
DE   AltName: Full=40S ribosomal protein S28-A {ECO:0000303|PubMed:9559554};
DE   AltName: Full=S33;
DE   AltName: Full=YS27;
GN   Name=RPS28A {ECO:0000303|PubMed:9559554}; Synonyms=RPS33, RPS33A;
GN   OrderedLocusNames=YOR167C; ORFNames=O3600;
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=6196722; DOI=10.1093/nar/11.22.7759;
RA   Leer R.J., van Raamsdonk-Duin M.M.C., Schoppink P.J., Cornelissen M.T.E.,
RA   Cohen L.H., Mager W.H., Planta R.J.;
RT   "Yeast ribosomal protein S33 is encoded by an unsplit gene.";
RL   Nucleic Acids Res. 11:7759-7768(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / FY1678;
RX   PubMed=8972579;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA   Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT   "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT   cerevisiae chromosome XV.";
RL   Yeast 12:1563-1573(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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].
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   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   ACETYLATION AT MET-1 BY NATB.
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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   [11]
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   [12]
RP   X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS).
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   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), SUBUNIT, AND 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:22096102}.
CC   -!- PTM: N-terminally acetylated by acetyltransferase NatB.
CC       {ECO:0000269|PubMed:10601260}.
CC   -!- MISCELLANEOUS: Present with 94500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eS28 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family.
CC       {ECO:0000305}.
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DR   EMBL; X00128; CAA24958.1; -; Genomic_DNA.
DR   EMBL; U55021; AAB47414.1; -; Genomic_DNA.
DR   EMBL; Z75075; CAA99373.1; -; Genomic_DNA.
DR   EMBL; AY692746; AAT92765.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10941.1; -; Genomic_DNA.
DR   PIR; A02750; R3BY33.
DR   RefSeq; NP_014810.1; NM_001183586.1.
DR   PDB; 3J6X; EM; 6.10 A; 28=1-67.
DR   PDB; 3J6Y; EM; 6.10 A; 28=1-67.
DR   PDB; 3J77; EM; 6.20 A; 28=1-67.
DR   PDB; 3J78; EM; 6.30 A; 28=1-67.
DR   PDB; 4U3M; X-ray; 3.00 A; D8/d8=2-67.
DR   PDB; 4U3N; X-ray; 3.20 A; D8/d8=2-67.
DR   PDB; 4U3U; X-ray; 2.90 A; D8/d8=2-67.
DR   PDB; 4U4N; X-ray; 3.10 A; D8/d8=2-67.
DR   PDB; 4U4O; X-ray; 3.60 A; D8/d8=2-67.
DR   PDB; 4U4Q; X-ray; 3.00 A; D8/d8=2-67.
DR   PDB; 4U4R; X-ray; 2.80 A; D8/d8=2-67.
DR   PDB; 4U4U; X-ray; 3.00 A; D8/d8=2-67.
DR   PDB; 4U4Y; X-ray; 3.20 A; D8/d8=2-67.
DR   PDB; 4U4Z; X-ray; 3.10 A; D8/d8=2-67.
DR   PDB; 4U50; X-ray; 3.20 A; D8/d8=2-67.
DR   PDB; 4U51; X-ray; 3.20 A; D8/d8=2-67.
DR   PDB; 4U52; X-ray; 3.00 A; D8/d8=2-67.
DR   PDB; 4U53; X-ray; 3.30 A; D8/d8=2-67.
DR   PDB; 4U55; X-ray; 3.20 A; D8/d8=2-67.
DR   PDB; 4U56; X-ray; 3.45 A; D8/d8=2-67.
DR   PDB; 4U6F; X-ray; 3.10 A; D8/d8=2-67.
DR   PDB; 4V6I; EM; 8.80 A; AY=1-67.
DR   PDB; 4V7R; X-ray; 4.00 A; AR/CR=1-67.
DR   PDB; 4V88; X-ray; 3.00 A; Ac/Cc=1-67.
DR   PDB; 4V8Y; EM; 4.30 A; A2=1-67.
DR   PDB; 4V8Z; EM; 6.60 A; A2=1-67.
DR   PDB; 4V92; EM; 3.70 A; c=5-67.
DR   PDB; 5DAT; X-ray; 3.15 A; D8/d8=2-67.
DR   PDB; 5DC3; X-ray; 3.25 A; D8/d8=2-67.
DR   PDB; 5DGE; X-ray; 3.45 A; D8/d8=2-67.
DR   PDB; 5DGF; X-ray; 3.30 A; D8/d8=2-67.
DR   PDB; 5DGV; X-ray; 3.10 A; D8/d8=2-67.
DR   PDB; 5FCI; X-ray; 3.40 A; D8/d8=2-67.
DR   PDB; 5FCJ; X-ray; 3.10 A; D8/d8=2-67.
DR   PDB; 5I4L; X-ray; 3.10 A; D8/d8=5-67.
DR   PDB; 5JPQ; EM; 7.30 A; 1=1-67.
DR   PDB; 5JUO; EM; 4.00 A; ZB=1-67.
DR   PDB; 5JUP; EM; 3.50 A; ZB=1-67.
DR   PDB; 5JUS; EM; 4.20 A; ZB=1-67.
DR   PDB; 5JUT; EM; 4.00 A; ZB=1-67.
DR   PDB; 5JUU; EM; 4.00 A; ZB=1-67.
DR   PDB; 5LYB; X-ray; 3.25 A; D8/d8=5-67.
DR   PDB; 5MEI; X-ray; 3.50 A; d/d8=5-67.
DR   PDB; 5NDG; X-ray; 3.70 A; D8/d8=5-67.
DR   PDB; 5NDV; X-ray; 3.30 A; D8/d8=5-67.
DR   PDB; 5NDW; X-ray; 3.70 A; D8/d8=5-67.
DR   PDB; 5OBM; X-ray; 3.40 A; D8/d8=5-67.
DR   PDB; 5ON6; X-ray; 3.10 A; d/d8=5-67.
DR   PDB; 5TBW; X-ray; 3.00 A; d/d8=5-67.
DR   PDB; 5TGA; X-ray; 3.30 A; D8/d8=5-67.
DR   PDB; 5TGM; X-ray; 3.50 A; D8/d8=5-67.
DR   PDB; 5TZS; EM; 5.10 A; G=1-67.
DR   PDB; 5WLC; EM; 3.80 A; LG=1-67.
DR   PDB; 5WYJ; EM; 8.70 A; Sd=1-67.
DR   PDB; 5WYK; EM; 4.50 A; Sd=1-67.
DR   PDB; 6FAI; EM; 3.40 A; c=1-67.
DR   PDB; 6GQ1; EM; 4.40 A; AS=5-67.
DR   PDB; 6GQB; EM; 3.90 A; AS=5-67.
DR   PDB; 6GQV; EM; 4.00 A; AS=5-67.
DR   PDB; 6HHQ; X-ray; 3.10 A; d/d8=1-67.
DR   PDB; 6I7O; EM; 5.30 A; L/Lb=5-67.
DR   PDB; 6KE6; EM; 3.40 A; Sd=1-67.
DR   PDB; 6LQP; EM; 3.20 A; Sd=1-67.
DR   PDB; 6LQQ; EM; 4.10 A; Sd=1-67.
DR   PDB; 6LQR; EM; 8.60 A; Sd=1-67.
DR   PDB; 6LQS; EM; 3.80 A; Sd=1-67.
DR   PDB; 6LQT; EM; 4.90 A; Sd=1-67.
DR   PDB; 6LQU; EM; 3.70 A; Sd=1-67.
DR   PDB; 6LQV; EM; 4.80 A; Sd=1-67.
DR   PDB; 6Q8Y; EM; 3.10 A; L=5-67.
DR   PDB; 6RBD; EM; 3.47 A; c=1-67.
DR   PDB; 6RBE; EM; 3.80 A; c=1-67.
DR   PDB; 6S47; EM; 3.28 A; Bd=2-67.
DR   PDB; 6T4Q; EM; 2.60 A; Sc=5-67.
DR   PDB; 6TB3; EM; 2.80 A; L=5-67.
DR   PDB; 6TNU; EM; 3.10 A; L=5-67.
DR   PDB; 6WDR; EM; 3.70 A; c=5-67.
DR   PDB; 6WOO; EM; 2.90 A; cc=5-67.
DR   PDB; 6Y7C; EM; 3.80 A; c=1-67.
DR   PDB; 6Z6J; EM; 3.40 A; Sc=1-67.
DR   PDB; 6Z6K; EM; 3.40 A; Sc=1-67.
DR   PDB; 6ZQA; EM; 4.40 A; Dc=1-67.
DR   PDB; 6ZQB; EM; 3.90 A; Dc=1-67.
DR   PDB; 6ZQC; EM; 3.80 A; Dc=1-67.
DR   PDB; 6ZQD; EM; 3.80 A; Dc=1-67.
DR   PDB; 6ZQE; EM; 7.10 A; Dc=1-67.
DR   PDB; 6ZQF; EM; 4.90 A; Dc=1-67.
DR   PDB; 6ZQG; EM; 3.50 A; Dc=1-67.
DR   PDB; 6ZVI; EM; 3.00 A; N=5-67.
DR   PDB; 7A1G; EM; 3.00 A; h=5-67.
DR   PDB; 7AJT; EM; 4.60 A; Dc=1-67.
DR   PDB; 7AJU; EM; 3.80 A; Dc=1-67.
DR   PDB; 7B7D; EM; 3.30 A; L=5-67.
DR   PDB; 7D4I; EM; 4.00 A; Sd=1-67.
DR   PDB; 7D5S; EM; 4.60 A; Sd=1-67.
DR   PDB; 7D5T; EM; 6.00 A; Sd=1-67.
DR   PDB; 7D63; EM; 12.30 A; Sd=1-67.
DR   PDB; 7MPI; EM; 3.05 A; Bc=5-67.
DR   PDB; 7MPJ; EM; 2.70 A; Bc=5-67.
DR   PDB; 7N8B; EM; 3.05 A; Bc=5-67.
DR   PDB; 7NRC; EM; 3.90 A; SL=5-67.
DR   PDB; 7NRD; EM; 4.36 A; SL=5-67.
DR   PDB; 7SUK; EM; 3.99 A; LG=5-67.
DR   PDB; 7ZPQ; EM; 3.47 A; Ac=5-67.
DR   PDB; 7ZRS; EM; 4.80 A; Ac=5-67.
DR   PDB; 7ZUW; EM; 4.30 A; Ac=5-67.
DR   PDB; 7ZUX; EM; 2.50 A; Dc=5-67.
DR   PDB; 7ZW0; EM; 2.40 A; sL=1-67.
DR   PDB; 8BQD; EM; 3.90 A; L=5-67.
DR   PDB; 8BQX; EM; 3.80 A; L=5-67.
DR   PDB; 8C00; EM; 2.90 A; L=1-67.
DR   PDB; 8C01; EM; 2.70 A; L=1-67.
DR   PDB; 8CAH; EM; 3.00 A; h=1-67.
DR   PDB; 8CAS; EM; 3.30 A; i=1-67.
DR   PDB; 8CBJ; EM; 3.80 A; c=1-67.
DR   PDB; 8CCS; EM; 1.97 A; 4=1-67.
DR   PDB; 8CDL; EM; 2.72 A; 4=1-67.
DR   PDB; 8CDR; EM; 2.04 A; 4=1-67.
DR   PDB; 8CEH; EM; 2.05 A; 4=1-67.
DR   PDB; 8CF5; EM; 2.71 A; 4=1-67.
DR   PDB; 8CG8; EM; 2.57 A; 4=1-67.
DR   PDB; 8CGN; EM; 2.28 A; 4=1-67.
DR   PDB; 8CIV; EM; 2.47 A; 4=1-67.
DR   PDB; 8CKU; EM; 3.11 A; 4=1-67.
DR   PDB; 8CMJ; EM; 3.79 A; 4=1-67.
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; 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; 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; 5WLC; -.
DR   PDBsum; 5WYJ; -.
DR   PDBsum; 5WYK; -.
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; 6Q8Y; -.
DR   PDBsum; 6RBD; -.
DR   PDBsum; 6RBE; -.
DR   PDBsum; 6S47; -.
DR   PDBsum; 6T4Q; -.
DR   PDBsum; 6TB3; -.
DR   PDBsum; 6TNU; -.
DR   PDBsum; 6WDR; -.
DR   PDBsum; 6WOO; -.
DR   PDBsum; 6Y7C; -.
DR   PDBsum; 6Z6J; -.
DR   PDBsum; 6Z6K; -.
DR   PDBsum; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 6ZQF; -.
DR   PDBsum; 6ZQG; -.
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; 7MPI; -.
DR   PDBsum; 7MPJ; -.
DR   PDBsum; 7N8B; -.
DR   PDBsum; 7NRC; -.
DR   PDBsum; 7NRD; -.
DR   PDBsum; 7SUK; -.
DR   PDBsum; 7ZPQ; -.
DR   PDBsum; 7ZRS; -.
DR   PDBsum; 7ZUW; -.
DR   PDBsum; 7ZUX; -.
DR   PDBsum; 7ZW0; -.
DR   PDBsum; 8BQD; -.
DR   PDBsum; 8BQX; -.
DR   PDBsum; 8C00; -.
DR   PDBsum; 8C01; -.
DR   PDBsum; 8CAH; -.
DR   PDBsum; 8CAS; -.
DR   PDBsum; 8CBJ; -.
DR   PDBsum; 8CCS; -.
DR   PDBsum; 8CDL; -.
DR   PDBsum; 8CDR; -.
DR   PDBsum; 8CEH; -.
DR   PDBsum; 8CF5; -.
DR   PDBsum; 8CG8; -.
DR   PDBsum; 8CGN; -.
DR   PDBsum; 8CIV; -.
DR   PDBsum; 8CKU; -.
DR   PDBsum; 8CMJ; -.
DR   AlphaFoldDB; Q3E7X9; -.
DR   EMDB; EMD-11608; -.
DR   EMDB; EMD-16563; -.
DR   EMDB; EMD-16591; -.
DR   EMDB; EMD-16594; -.
DR   EMDB; EMD-16609; -.
DR   EMDB; EMD-16616; -.
DR   EMDB; EMD-16634; -.
DR   EMDB; EMD-16648; -.
DR   EMDB; EMD-16684; -.
DR   EMDB; EMD-16702; -.
DR   EMDB; EMD-16729; -.
DR   EMDB; EMD-21859; -.
DR   EMDB; EMD-25441; -.
DR   SMR; Q3E7X9; -.
DR   BioGRID; 34563; 182.
DR   DIP; DIP-29384N; -.
DR   IntAct; Q3E7X9; 7.
DR   STRING; 4932.YOR167C; -.
DR   MoonProt; Q3E7X9; -.
DR   iPTMnet; Q3E7X9; -.
DR   MaxQB; Q3E7X9; -.
DR   PaxDb; 4932-YOR167C; -.
DR   PeptideAtlas; Q3E7X9; -.
DR   TopDownProteomics; Q3E7X9; -.
DR   EnsemblFungi; YOR167C_mRNA; YOR167C; YOR167C.
DR   GeneID; 854338; -.
DR   KEGG; sce:YOR167C; -.
DR   AGR; SGD:S000005693; -.
DR   SGD; S000005693; RPS28A.
DR   VEuPathDB; FungiDB:YOR167C; -.
DR   eggNOG; KOG3502; Eukaryota.
DR   GeneTree; ENSGT00910000144227; -.
DR   HOGENOM; CLU_178987_1_0_1; -.
DR   InParanoid; Q3E7X9; -.
DR   OMA; ETNRSII; -.
DR   OrthoDB; 177850at2759; -.
DR   BioCyc; YEAST:G3O-33683-MONOMER; -.
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-72649; Translation initiation complex formation.
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   BioGRID-ORCS; 854338; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q3E7X9; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q3E7X9; Protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0006407; P:rRNA export from nucleus; IGI:SGD.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd04457; S1_S28E; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00292; Ribosomal_eS28; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000289; Ribosomal_eS28.
DR   InterPro; IPR028626; Ribosomal_eS28_CS.
DR   PANTHER; PTHR10769; 40S RIBOSOMAL PROTEIN S28; 1.
DR   PANTHER; PTHR10769:SF3; 40S RIBOSOMAL PROTEIN S28; 1.
DR   Pfam; PF01200; Ribosomal_S28e; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00961; RIBOSOMAL_S28E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..67
FT                   /note="Small ribosomal subunit protein eS28A"
FT                   /id="PRO_0000136842"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:10601260,
FT                   ECO:0007744|PubMed:22814378"
FT   STRAND          8..20
FT                   /evidence="ECO:0007829|PDB:8C01"
FT   STRAND          25..36
FT                   /evidence="ECO:0007829|PDB:8C01"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:8C01"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:8C01"
SQ   SEQUENCE   67 AA;  7592 MW;  BA145824DEE8A641 CRC64;
     MDNKTPVTLA KVIKVLGRTG SRGGVTQVRV EFLEDTSRTI VRNVKGPVRE NDILVLMESE
     REARRLR
//