ID RS16A_YEAST Reviewed; 143 AA. AC P0CX51; D6VRR6; P26787; P40213; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Small ribosomal subunit protein uS9A {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S16-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=RP61R; GN Name=RPS16A {ECO:0000303|PubMed:9559554}; Synonyms=RP61R; GN OrderedLocusNames=YMR143W; ORFNames=YM9375.12; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] 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 [3] RP PRELIMINARY PROTEIN SEQUENCE OF 2-26, 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 [4] 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 [5] 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 [6] 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 [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; THR-70 AND SER-76, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY RP 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 [11] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-47 AND LYS-59, 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 [12] 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 [13] RP 3D-STRUCTURE MODELING OF 5-143, 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 [14] RP 3D-STRUCTURE MODELING, 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 [15] 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 [16] 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:22096102}. CC -!- MISCELLANEOUS: Present with 33800 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: There are 2 genes for uS9 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z47071; CAA87357.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10039.1; -; Genomic_DNA. DR PIR; S67619; S67619. DR RefSeq; NP_010200.1; NM_001180142.1. DR RefSeq; NP_013863.2; NM_001182645.1. DR PDB; 3J6X; EM; 6.10 A; 16=1-143. DR PDB; 3J6Y; EM; 6.10 A; 16=1-143. DR PDB; 3J77; EM; 6.20 A; 16=1-143. DR PDB; 3J78; EM; 6.30 A; 16=1-143. DR PDB; 4U3M; X-ray; 3.00 A; C6/c6=2-143. DR PDB; 4U3N; X-ray; 3.20 A; C6/c6=2-143. DR PDB; 4U3U; X-ray; 2.90 A; C6/c6=2-143. DR PDB; 4U4N; X-ray; 3.10 A; C6/c6=2-143. DR PDB; 4U4O; X-ray; 3.60 A; C6/c6=2-143. DR PDB; 4U4Q; X-ray; 3.00 A; C6/c6=2-143. DR PDB; 4U4R; X-ray; 2.80 A; C6/c6=2-143. DR PDB; 4U4U; X-ray; 3.00 A; C6/c6=2-143. DR PDB; 4U4Y; X-ray; 3.20 A; C6/c6=2-143. DR PDB; 4U4Z; X-ray; 3.10 A; C6/c6=2-143. DR PDB; 4U50; X-ray; 3.20 A; C6/c6=2-143. DR PDB; 4U51; X-ray; 3.20 A; C6/c6=2-143. DR PDB; 4U52; X-ray; 3.00 A; C6/c6=2-143. DR PDB; 4U53; X-ray; 3.30 A; C6/c6=2-143. DR PDB; 4U55; X-ray; 3.20 A; C6/c6=2-143. DR PDB; 4U56; X-ray; 3.45 A; C6/c6=2-143. DR PDB; 4U6F; X-ray; 3.10 A; C6/c6=2-143. DR PDB; 4V4B; EM; 11.70 A; AI=2-143. DR PDB; 4V6I; EM; 8.80 A; AI=1-143. DR PDB; 4V7R; X-ray; 4.00 A; AJ/CJ=1-143. DR PDB; 4V88; X-ray; 3.00 A; AQ/CQ=1-143. DR PDB; 4V8Y; EM; 4.30 A; AQ=1-143. DR PDB; 4V8Z; EM; 6.60 A; AQ=1-143. DR PDB; 4V92; EM; 3.70 A; Q=3-142. DR PDB; 5DAT; X-ray; 3.15 A; C6/c6=2-143. DR PDB; 5DC3; X-ray; 3.25 A; C6/c6=2-143. DR PDB; 5DGE; X-ray; 3.45 A; C6/c6=2-143. DR PDB; 5DGF; X-ray; 3.30 A; C6/c6=2-143. DR PDB; 5DGV; X-ray; 3.10 A; C6/c6=2-143. DR PDB; 5FCI; X-ray; 3.40 A; C6/c6=2-143. DR PDB; 5FCJ; X-ray; 3.10 A; C6/c6=2-143. DR PDB; 5I4L; X-ray; 3.10 A; C6/c6=2-143. DR PDB; 5JPQ; EM; 7.30 A; x=1-143. DR PDB; 5JUO; EM; 4.00 A; NB=1-143. DR PDB; 5JUP; EM; 3.50 A; NB=1-143. DR PDB; 5JUS; EM; 4.20 A; NB=1-143. DR PDB; 5JUT; EM; 4.00 A; NB=1-143. DR PDB; 5JUU; EM; 4.00 A; NB=1-143. DR PDB; 5LYB; X-ray; 3.25 A; C6/c6=2-143. DR PDB; 5M1J; EM; 3.30 A; Q2=3-143. DR PDB; 5MC6; EM; 3.80 A; F=1-143. DR PDB; 5MEI; X-ray; 3.50 A; R/c6=2-143. DR PDB; 5NDG; X-ray; 3.70 A; C6/c6=3-143. DR PDB; 5NDV; X-ray; 3.30 A; C6/c6=2-143. DR PDB; 5NDW; X-ray; 3.70 A; C6/c6=3-143. DR PDB; 5OBM; X-ray; 3.40 A; C6/c6=2-143. DR PDB; 5ON6; X-ray; 3.10 A; R/c6=2-143. DR PDB; 5TBW; X-ray; 3.00 A; R/c6=2-143. DR PDB; 5TGA; X-ray; 3.30 A; C6/c6=2-143. DR PDB; 5TGM; X-ray; 3.50 A; C6/c6=2-143. DR PDB; 5TZS; EM; 5.10 A; C=1-143. DR PDB; 5WLC; EM; 3.80 A; LC=1-143. DR PDB; 5WYJ; EM; 8.70 A; SR=1-143. DR PDB; 5WYK; EM; 4.50 A; SR=1-143. DR PDB; 6EML; EM; 3.60 A; F=1-143. DR PDB; 6FAI; EM; 3.40 A; Q=1-143. DR PDB; 6GQ1; EM; 4.40 A; AG=3-143. DR PDB; 6GQB; EM; 3.90 A; AG=3-143. DR PDB; 6GQV; EM; 4.00 A; AG=3-143. DR PDB; 6HHQ; X-ray; 3.10 A; R/c6=1-143. DR PDB; 6I7O; EM; 5.30 A; F/Fb=3-143. DR PDB; 6KE6; EM; 3.40 A; SR=1-143. DR PDB; 6LQP; EM; 3.20 A; SR=1-143. DR PDB; 6LQQ; EM; 4.10 A; SR=1-143. DR PDB; 6LQR; EM; 8.60 A; SR=1-143. DR PDB; 6LQS; EM; 3.80 A; SR=1-143. DR PDB; 6LQT; EM; 4.90 A; SR=1-143. DR PDB; 6LQU; EM; 3.70 A; SR=1-143. DR PDB; 6LQV; EM; 4.80 A; SR=1-143. DR PDB; 6Q8Y; EM; 3.10 A; F=3-143. DR PDB; 6RBD; EM; 3.47 A; Q=1-143. DR PDB; 6RBE; EM; 3.80 A; Q=1-143. DR PDB; 6S47; EM; 3.28 A; BR=2-143. DR PDB; 6SNT; EM; 2.80 A; Q=1-143. DR PDB; 6SV4; EM; 3.30 A; F/Fb/Fc=1-143. DR PDB; 6T4Q; EM; 2.60 A; SQ=3-143. DR PDB; 6T7I; EM; 3.20 A; SQ=1-143. DR PDB; 6T7T; EM; 3.10 A; SQ=1-143. DR PDB; 6T83; EM; 4.00 A; Qb/r=1-143. DR PDB; 6TB3; EM; 2.80 A; F=3-143. DR PDB; 6TNU; EM; 3.10 A; F=3-143. DR PDB; 6WDR; EM; 3.70 A; Q=3-129. DR PDB; 6WOO; EM; 2.90 A; QQ=3-143. DR PDB; 6XIQ; EM; 4.20 A; AG=1-143. DR PDB; 6XIR; EM; 3.20 A; AG=1-143. DR PDB; 6Y7C; EM; 3.80 A; Q=1-143. DR PDB; 6Z6J; EM; 3.40 A; SQ=1-143. DR PDB; 6Z6K; EM; 3.40 A; SQ=1-143. DR PDB; 6ZCE; EM; 5.30 A; R=1-143. DR PDB; 6ZQA; EM; 4.40 A; DQ=1-143. DR PDB; 6ZQB; EM; 3.90 A; DQ=1-143. DR PDB; 6ZQC; EM; 3.80 A; DQ=1-143. DR PDB; 6ZQD; EM; 3.80 A; DQ=1-143. DR PDB; 6ZQE; EM; 7.10 A; DQ=1-143. DR PDB; 6ZQF; EM; 4.90 A; DQ=1-143. DR PDB; 6ZQG; EM; 3.50 A; DQ=1-143. DR PDB; 6ZU9; EM; 6.20 A; H=1-143. DR PDB; 6ZVI; EM; 3.00 A; y=3-143. DR PDB; 7A1G; EM; 3.00 A; F=3-143. DR PDB; 7AJT; EM; 4.60 A; DQ=1-143. DR PDB; 7AJU; EM; 3.80 A; DQ=1-143. DR PDB; 7B7D; EM; 3.30 A; F=3-143. DR PDB; 7D4I; EM; 4.00 A; SR=1-143. DR PDB; 7D5S; EM; 4.60 A; SR=1-143. DR PDB; 7D5T; EM; 6.00 A; SR=1-143. DR PDB; 7D63; EM; 12.30 A; SR=1-143. DR PDB; 7MPI; EM; 3.05 A; BQ=3-143. DR PDB; 7MPJ; EM; 2.70 A; BQ=3-143. DR PDB; 7N8B; EM; 3.05 A; BQ=3-143. DR PDB; 7NRC; EM; 3.90 A; SF=3-143. DR PDB; 7NRD; EM; 4.36 A; SF=3-143. DR PDB; 7SUK; EM; 3.99 A; LC=3-127. DR PDB; 7ZPQ; EM; 3.47 A; AQ=3-143. DR PDB; 7ZRS; EM; 4.80 A; AQ=3-143. DR PDB; 7ZUW; EM; 4.30 A; AQ=3-143. DR PDB; 7ZUX; EM; 2.50 A; DQ=3-143. DR PDB; 7ZW0; EM; 2.40 A; sF=1-143. DR PDB; 8BQD; EM; 3.90 A; F=3-143. DR PDB; 8BQX; EM; 3.80 A; F=3-143. DR PDB; 8C00; EM; 2.90 A; F=1-143. DR PDB; 8C01; EM; 2.70 A; F=1-143. DR PDB; 8CAH; EM; 3.00 A; F=1-143. DR PDB; 8CAS; EM; 3.30 A; H=1-143. DR PDB; 8CBJ; EM; 3.80 A; Q=1-143. DR PDB; 8CCS; EM; 1.97 A; s=1-143. DR PDB; 8CDL; EM; 2.72 A; s=1-143. DR PDB; 8CDR; EM; 2.04 A; s=1-143. DR PDB; 8CEH; EM; 2.05 A; s=1-143. DR PDB; 8CF5; EM; 2.71 A; s=1-143. DR PDB; 8CG8; EM; 2.57 A; s=1-143. DR PDB; 8CGN; EM; 2.28 A; s=1-143. DR PDB; 8CIV; EM; 2.47 A; s=1-143. DR PDB; 8CKU; EM; 3.11 A; s=1-143. DR PDB; 8CMJ; EM; 3.79 A; s=1-143. DR PDB; 8EUB; EM; 2.52 A; BQ=1-143. DR PDB; 8EVP; EM; 2.38 A; BQ=1-143. DR PDB; 8EVQ; EM; 2.72 A; BQ=1-143. DR PDB; 8EVR; EM; 2.87 A; BQ=1-143. DR PDB; 8EVS; EM; 2.62 A; BQ=1-143. DR PDB; 8EVT; EM; 2.20 A; BQ=1-143. DR PDB; 8EWB; EM; 2.87 A; BQ=1-143. DR PDB; 8EWC; EM; 2.45 A; BQ=1-143. 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; 5WLC; -. 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; 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; 6XIQ; -. DR PDBsum; 6XIR; -. DR PDBsum; 6Y7C; -. DR PDBsum; 6Z6J; -. DR PDBsum; 6Z6K; -. DR PDBsum; 6ZCE; -. DR PDBsum; 6ZQA; -. DR PDBsum; 6ZQB; -. DR PDBsum; 6ZQC; -. DR PDBsum; 6ZQD; -. 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; 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 PDBsum; 8EUB; -. DR PDBsum; 8EVP; -. DR PDBsum; 8EVQ; -. DR PDBsum; 8EVR; -. DR PDBsum; 8EVS; -. DR PDBsum; 8EVT; -. DR PDBsum; 8EWB; -. DR PDBsum; 8EWC; -. DR AlphaFoldDB; P0CX51; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0949; -. DR EMDB; EMD-0950; -. DR EMDB; EMD-0951; -. DR EMDB; EMD-0952; -. DR EMDB; EMD-0953; -. DR EMDB; EMD-0954; -. DR EMDB; EMD-0955; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-10713; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11160; -. DR EMDB; EMD-11357; -. DR EMDB; EMD-11358; -. DR EMDB; EMD-11359; -. DR EMDB; EMD-11360; -. DR EMDB; EMD-11361; -. DR EMDB; EMD-11362; -. DR EMDB; EMD-11363; -. DR EMDB; EMD-11439; -. DR EMDB; EMD-11457; -. DR EMDB; EMD-11608; -. DR EMDB; EMD-11807; -. DR EMDB; EMD-11808; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-14990; -. 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-21644; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-22196; -. DR EMDB; EMD-22198; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-25441; -. DR EMDB; EMD-28610; -. DR EMDB; EMD-28632; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28636; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-28643; -. DR EMDB; EMD-30574; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-30585; -. DR EMDB; EMD-30588; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-4214; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4792; -. DR EMDB; EMD-4793; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-9964; -. DR SMR; P0CX51; -. DR BioGRID; 31978; 290. DR BioGRID; 35319; 363. DR IntAct; P0CX51; 7. DR MINT; P0CX51; -. DR STRING; 4932.YDL083C; -. DR CarbonylDB; P0CX51; -. DR iPTMnet; P0CX51; -. DR MaxQB; P0CX51; -. DR PaxDb; 4932-YDL083C; -. DR PeptideAtlas; P0CX51; -. DR TopDownProteomics; P0CX51; -. DR EnsemblFungi; YDL083C_mRNA; YDL083C; YDL083C. DR EnsemblFungi; YMR143W_mRNA; YMR143W; YMR143W. DR GeneID; 851476; -. DR GeneID; 855174; -. DR KEGG; sce:YDL083C; -. DR KEGG; sce:YMR143W; -. DR AGR; SGD:S000004751; -. DR SGD; S000004751; RPS16A. DR VEuPathDB; FungiDB:YDL083C; -. DR VEuPathDB; FungiDB:YMR143W; -. DR eggNOG; KOG1753; Eukaryota. DR HOGENOM; CLU_046483_4_0_1; -. DR InParanoid; P0CX51; -. DR OMA; WPIEMAR; -. DR OrthoDB; 22228at2759; -. DR BioCyc; YEAST:G3O-32835-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; 851476; 4 hits in 10 CRISPR screens. DR BioGRID-ORCS; 855174; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; P0CX51; -. DR PRO; PR:P0CX51; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P0CX51; Protein. DR ExpressionAtlas; P0CX51; baseline and differential. DR GO; GO:0030686; C:90S preribosome; HDA:SGD. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD. DR GO; GO:0006412; P:translation; IEA:InterPro. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR000754; Ribosomal_uS9. DR InterPro; IPR020574; Ribosomal_uS9_CS. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR PANTHER; PTHR21569:SF16; 40S RIBOSOMAL PROTEIN S16; 1. DR PANTHER; PTHR21569; RIBOSOMAL PROTEIN S9; 1. DR Pfam; PF00380; Ribosomal_S9; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00360; RIBOSOMAL_S9; 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..143 FT /note="Small ribosomal subunit protein uS9A" FT /id="PRO_0000111503" FT REGION 123..143 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" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 70 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT CROSSLNK 30 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 47 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 59 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT STRAND 6..15 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 17..26 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 46..53 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 76..96 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 99..112 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:6ZVI" SQ SEQUENCE 143 AA; 15847 MW; 46360374CD9730CC CRC64; MSAVPSVQTF GKKKSATAVA HVKAGKGLIK VNGSPITLVE PEILRFKVYE PLLLVGLDKF SNIDIRVRVT GGGHVSQVYA IRQAIAKGLV AYHQKYVDEQ SKNELKKAFT SYDRTLLIAD SRRPEPKKFG GKGARSRFQK SYR //