RS16A_YEAST
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 03-AUG-2022, entry version 91.
DE RecName: Full=40S ribosomal protein S16-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP61R;
DE AltName: Full=Small ribosomal subunit protein uS9-A {ECO:0000303|PubMed:24524803};
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}.
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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; 7NRC; EM; 3.90 A; SF=3-143.
DR PDB; 7NRD; EM; 4.36 A; SF=3-143.
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; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX51; -.
DR SMR; P0CX51; -.
DR BioGRID; 31978; 285.
DR BioGRID; 35319; 316.
DR IntAct; P0CX51; 7.
DR MINT; P0CX51; -.
DR STRING; 4932.YDL083C; -.
DR CarbonylDB; P0CX51; -.
DR iPTMnet; P0CX51; -.
DR MaxQB; P0CX51; -.
DR PaxDb; P0CX51; -.
DR PRIDE; 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 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; FMGQAEA; -.
DR BioCyc; YEAST:G3O-32835-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; 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:0015935; C: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:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 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="40S ribosomal protein S16-A"
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..13
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 16..26
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:6ZVI"
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
