RS15_YEAST
ID RS15_YEAST Reviewed; 142 AA.
AC Q01855; D6W226;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=40S ribosomal protein S15 {ECO:0000303|PubMed:9559554};
DE AltName: Full=RIG protein;
DE AltName: Full=RP52;
DE AltName: Full=S21;
DE AltName: Full=Small ribosomal subunit protein uS19 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS21;
GN Name=RPS15 {ECO:0000303|PubMed:9559554}; Synonyms=RPS21;
GN OrderedLocusNames=YOL040C;
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 / MRNA].
RX PubMed=1644188; DOI=10.1016/0014-5793(92)80704-k;
RA Takasawa S., Tohgo A., Unno M., Yonekura H., Okamoto H.;
RT "Structural determination of Saccharomyces cerevisiae rig gene and
RT identification of its product as ribosomal protein S21.";
RL FEBS Lett. 307:318-323(1992).
RN [2]
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 [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 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 [6]
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 [7]
RP FUNCTION.
RX PubMed=15167894; DOI=10.1038/sj.emboj.7600252;
RA Leger-Silvestre I., Milkereit P., Ferreira-Cerca S., Saveanu C.,
RA Rousselle J.-C., Choesmel V., Guinefoleau C., Gas N., Gleizes P.-E.;
RT "The ribosomal protein Rps15p is required for nuclear exit of the 40S
RT subunit precursors in yeast.";
RL EMBO J. 23:2336-2347(2004).
RN [8]
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 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 [10]
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 [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-35 AND LYS-64, 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 47-126, 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 OF 47-126, 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 (PubMed:22096102). uS19 is involved in the nuclear export of the
CC small ribosomal subunit precursor. Has a role in the late stage of the
CC assembly of pre-40S particles within the nucleus and controls their
CC export to the cytoplasm (PubMed:15167894).
CC {ECO:0000269|PubMed:15167894, 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:22096102}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS19 family.
CC {ECO:0000305}.
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DR EMBL; D11386; BAA01982.1; -; mRNA.
DR EMBL; D11387; BAA01983.1; -; Genomic_DNA.
DR EMBL; Z74782; CAA99042.1; -; Genomic_DNA.
DR EMBL; AY558426; AAS56752.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10742.1; -; Genomic_DNA.
DR PIR; S24053; S24053.
DR RefSeq; NP_014602.1; NM_001183294.1.
DR PDB; 3J6X; EM; 6.10 A; 15=1-142.
DR PDB; 3J6Y; EM; 6.10 A; 15=1-142.
DR PDB; 3J77; EM; 6.20 A; 15=1-142.
DR PDB; 3J78; EM; 6.30 A; 15=1-142.
DR PDB; 4U3M; X-ray; 3.00 A; C5/c5=2-142.
DR PDB; 4U3N; X-ray; 3.20 A; C5/c5=2-142.
DR PDB; 4U3U; X-ray; 2.90 A; C5/c5=2-142.
DR PDB; 4U4N; X-ray; 3.10 A; C5/c5=2-142.
DR PDB; 4U4O; X-ray; 3.60 A; C5/c5=2-142.
DR PDB; 4U4Q; X-ray; 3.00 A; C5/c5=2-142.
DR PDB; 4U4R; X-ray; 2.80 A; C5/c5=2-142.
DR PDB; 4U4U; X-ray; 3.00 A; C5/c5=2-142.
DR PDB; 4U4Y; X-ray; 3.20 A; C5/c5=2-142.
DR PDB; 4U4Z; X-ray; 3.10 A; C5/c5=2-142.
DR PDB; 4U50; X-ray; 3.20 A; C5/c5=2-142.
DR PDB; 4U51; X-ray; 3.20 A; C5/c5=2-142.
DR PDB; 4U52; X-ray; 3.00 A; C5/c5=2-142.
DR PDB; 4U53; X-ray; 3.30 A; C5/c5=2-142.
DR PDB; 4U55; X-ray; 3.20 A; C5/c5=2-142.
DR PDB; 4U56; X-ray; 3.45 A; C5/c5=2-142.
DR PDB; 4U6F; X-ray; 3.10 A; C5/c5=2-142.
DR PDB; 4V4B; EM; 11.70 A; AS=47-126.
DR PDB; 4V6I; EM; 8.80 A; AR=1-142.
DR PDB; 4V7R; X-ray; 4.00 A; AI/CI=1-142.
DR PDB; 4V88; X-ray; 3.00 A; AP/CP=1-142.
DR PDB; 4V8Y; EM; 4.30 A; AP=1-142.
DR PDB; 4V8Z; EM; 6.60 A; AP=1-142.
DR PDB; 4V92; EM; 3.70 A; P=12-126.
DR PDB; 5DAT; X-ray; 3.15 A; C5/c5=2-138.
DR PDB; 5DC3; X-ray; 3.25 A; C5/c5=2-142.
DR PDB; 5DGE; X-ray; 3.45 A; C5/c5=2-142.
DR PDB; 5DGV; X-ray; 3.10 A; C5/c5=2-142.
DR PDB; 5FCI; X-ray; 3.40 A; C5/c5=2-142.
DR PDB; 5FCJ; X-ray; 3.10 A; C5/c5=2-142.
DR PDB; 5I4L; X-ray; 3.10 A; C5/c5=1-142.
DR PDB; 5JUO; EM; 4.00 A; MB=1-142.
DR PDB; 5JUP; EM; 3.50 A; MB=1-142.
DR PDB; 5JUS; EM; 4.20 A; MB=1-142.
DR PDB; 5JUT; EM; 4.00 A; MB=1-142.
DR PDB; 5JUU; EM; 4.00 A; MB=1-142.
DR PDB; 5LYB; X-ray; 3.25 A; C5=4-134, c5=1-142.
DR PDB; 5M1J; EM; 3.30 A; P2=8-131.
DR PDB; 5MC6; EM; 3.80 A; E=1-142.
DR PDB; 5MEI; X-ray; 3.50 A; Q/c5=2-142.
DR PDB; 5NDG; X-ray; 3.70 A; C5/c5=2-142.
DR PDB; 5NDV; X-ray; 3.30 A; C5/c5=2-142.
DR PDB; 5NDW; X-ray; 3.70 A; C5/c5=2-142.
DR PDB; 5OBM; X-ray; 3.40 A; C5/c5=2-142.
DR PDB; 5ON6; X-ray; 3.10 A; Q/c5=2-142.
DR PDB; 5TBW; X-ray; 3.00 A; Q/c5=4-138.
DR PDB; 5TGA; X-ray; 3.30 A; C5/c5=4-138.
DR PDB; 5TGM; X-ray; 3.50 A; C5/c5=10-134.
DR PDB; 6EML; EM; 3.60 A; E=1-142.
DR PDB; 6FAI; EM; 3.40 A; P=1-142.
DR PDB; 6GQ1; EM; 4.40 A; AF=8-131.
DR PDB; 6GQB; EM; 3.90 A; AF=8-131.
DR PDB; 6GQV; EM; 4.00 A; AF=8-131.
DR PDB; 6HHQ; X-ray; 3.10 A; Q/c5=1-142.
DR PDB; 6I7O; EM; 5.30 A; E/Eb=14-132.
DR PDB; 6Q8Y; EM; 3.10 A; E=8-128.
DR PDB; 6RBD; EM; 3.47 A; P=1-142.
DR PDB; 6RBE; EM; 3.80 A; P=1-142.
DR PDB; 6S47; EM; 3.28 A; BQ=2-142.
DR PDB; 6SNT; EM; 2.80 A; P=1-142.
DR PDB; 6SV4; EM; 3.30 A; E/Eb/Ec=1-142.
DR PDB; 6T4Q; EM; 2.60 A; SP=13-129.
DR PDB; 6T7I; EM; 3.20 A; SP=1-142.
DR PDB; 6T7T; EM; 3.10 A; SP=1-142.
DR PDB; 6T83; EM; 4.00 A; Pb/q=1-142.
DR PDB; 6TB3; EM; 2.80 A; E=13-129.
DR PDB; 6TNU; EM; 3.10 A; E=13-129.
DR PDB; 6WDR; EM; 3.70 A; P=16-142.
DR PDB; 6WOO; EM; 2.90 A; PP=25-127.
DR PDB; 6Y7C; EM; 3.80 A; P=1-142.
DR PDB; 6Z6J; EM; 3.40 A; SP=1-142.
DR PDB; 6Z6K; EM; 3.40 A; SP=1-142.
DR PDB; 6ZCE; EM; 5.30 A; Q=2-142.
DR PDB; 6ZU9; EM; 6.20 A; E=2-142.
DR PDB; 6ZVI; EM; 3.00 A; x=14-132.
DR PDB; 7A1G; EM; 3.00 A; E=13-129.
DR PDB; 7B7D; EM; 3.30 A; E=13-129.
DR PDB; 7NRC; EM; 3.90 A; SE=13-129.
DR PDB; 7NRD; EM; 4.36 A; SE=14-132.
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; 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; 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; Q01855; -.
DR SMR; Q01855; -.
DR BioGRID; 34362; 794.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR IntAct; Q01855; 9.
DR MINT; Q01855; -.
DR STRING; 4932.YOL040C; -.
DR iPTMnet; Q01855; -.
DR MaxQB; Q01855; -.
DR PaxDb; Q01855; -.
DR PRIDE; Q01855; -.
DR TopDownProteomics; Q01855; -.
DR EnsemblFungi; YOL040C_mRNA; YOL040C; YOL040C.
DR GeneID; 854117; -.
DR KEGG; sce:YOL040C; -.
DR SGD; S000005400; RPS15.
DR VEuPathDB; FungiDB:YOL040C; -.
DR eggNOG; KOG0898; Eukaryota.
DR GeneTree; ENSGT00390000000475; -.
DR HOGENOM; CLU_097347_1_0_1; -.
DR InParanoid; Q01855; -.
DR OMA; VIRTHCR; -.
DR BioCyc; YEAST:G3O-33454-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; Q01855; -.
DR PRO; PR:Q01855; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q01855; 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; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; NAS: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 Gene3D; 3.30.860.10; -; 1.
DR HAMAP; MF_00531; Ribosomal_S19; 1.
DR InterPro; IPR020934; Ribosomal_S15/S19_CS.
DR InterPro; IPR002222; Ribosomal_S19.
DR InterPro; IPR023575; Ribosomal_S19_S15_SF.
DR InterPro; IPR005713; Ribosomal_S19A/S15e.
DR PANTHER; PTHR11880; PTHR11880; 1.
DR Pfam; PF00203; Ribosomal_S19; 1.
DR PIRSF; PIRSF002144; Ribosomal_S19; 1.
DR PRINTS; PR00975; RIBOSOMALS19.
DR SUPFAM; SSF54570; SSF54570; 1.
DR TIGRFAMs; TIGR01025; uS19_arch; 1.
DR PROSITE; PS00323; RIBOSOMAL_S19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..142
FT /note="40S ribosomal protein S15"
FT /id="PRO_0000130051"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6FAI"
SQ SEQUENCE 142 AA; 16002 MW; 06B564FD68051CD2 CRC64;
MSQAVNAKKR VFKTHSYRGV DLEKLLEMST EDFVKLAPAR VRRRFARGMT SKPAGFMKKL
RAAKLAAPEN EKPAPVRTHM RNMIIVPEMI GSVVGIYNGK AFNQVEIRPE MLGHYLGEFS
ITYTPVRHGR AGATTSRFIP LK
