ID RL18A_YEAST Reviewed; 186 AA. AC P0CX49; D6W0P3; P07279; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Large ribosomal subunit protein eL18A {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L18-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=RP28; GN Name=RPL18A {ECO:0000303|PubMed:9559554}; Synonyms=RP28A; GN OrderedLocusNames=YOL120C; 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=6387623; DOI=10.1093/nar/12.19.7345; RA Molenaar C.M.T., Woudt L.P., Jansen A.E.M., Mager W.H., Planta R.J., RA Donovan D.M., Pearson N.J.; RT "Structure and organization of two linked ribosomal protein genes in RT yeast."; RL Nucleic Acids Res. 12:7345-7358(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8896268; RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1041::aid-yea989>3.0.co;2-i; RA Lafuente M.J., Gamo F.-J., Gancedo C.; RT "DNA sequence analysis of a 10 624 bp fragment of the left arm of RT chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein, RT a mitochondrial protein, two ribosomal proteins and two new open reading RT frames."; RL Yeast 12:1041-1045(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 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 MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=11983894; DOI=10.1073/pnas.082119899; RA Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A., RA Shen Y., Zhao R., Smith R.D.; RT "Direct mass spectrometric analysis of intact proteins of the yeast large RT ribosomal subunit using capillary LC/FTICR."; RL Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002). RN [7] 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 [8] RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18086883; DOI=10.1128/mcb.01035-07; RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., RA Pemberton L.F.; RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and RT function."; RL Mol. Cell. Biol. 28:1313-1325(2008). RN [9] RP IDENTIFICATION BY MASS 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 [10] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY RP 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 [11] RP METHYLATION AT LYS-50. RX PubMed=22522802; DOI=10.1002/pmic.201100570; RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.; RT "Methylation of translation-associated proteins in Saccharomyces RT cerevisiae: Identification of methylated lysines and their RT methyltransferases."; RL Proteomics 12:960-972(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 22-141, 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 22-141, 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 STRUCTURE BY ELECTRON MICROSCOPY (8.80 ANGSTROMS). RX PubMed=20980660; DOI=10.1073/pnas.1009999107; RA Armache J.P., Jarasch A., Anger A.M., Villa E., Becker T., Bhushan S., RA Jossinet F., Habeck M., Dindar G., Franckenberg S., Marquez V., Mielke T., RA Thomm M., Berninghausen O., Beatrix B., Soding J., Westhof E., Wilson D.N., RA Beckmann R.; RT "Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome RT at 5.5-A resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 107:19748-19753(2010). RN [16] RP X-RAY CRYSTALLOGRAPHY (4.0 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 [17] RP X-RAY CRYSTALLOGRAPHY (3.0 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 large ribosomal subunit (LSU). 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). eL18 CC interacts with NAP1 (PubMed:18086883). {ECO:0000269|PubMed:18086883, CC ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. CC -!- MASS SPECTROMETRY: Mass=20419.432; Method=Electrospray; CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:11983894}; CC -!- MISCELLANEOUS: There are 2 genes for eL18 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 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; X01099; CAA25573.1; -; Genomic_DNA. DR EMBL; X02635; CAA26481.1; -; Genomic_DNA. DR EMBL; X95258; CAA64550.1; -; Genomic_DNA. DR EMBL; Z74862; CAA99139.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10664.1; -; Genomic_DNA. DR PIR; S05867; R5BY8E. DR RefSeq; NP_014098.1; NM_001183139.1. DR RefSeq; NP_014521.1; NM_001183374.1. DR PDB; 3J6X; EM; 6.10 A; 58=1-186. DR PDB; 3J6Y; EM; 6.10 A; 58=1-186. DR PDB; 3J77; EM; 6.20 A; 68=1-186. DR PDB; 3J78; EM; 6.30 A; 68=1-186. DR PDB; 3JCT; EM; 3.08 A; Q=1-186. DR PDB; 4U3M; X-ray; 3.00 A; M8/m8=2-186. DR PDB; 4U3N; X-ray; 3.20 A; M8/m8=2-186. DR PDB; 4U3U; X-ray; 2.90 A; M8/m8=2-186. DR PDB; 4U4N; X-ray; 3.10 A; M8/m8=2-186. DR PDB; 4U4O; X-ray; 3.60 A; M8/m8=2-186. DR PDB; 4U4Q; X-ray; 3.00 A; M8/m8=2-186. DR PDB; 4U4R; X-ray; 2.80 A; M8/m8=2-186. DR PDB; 4U4U; X-ray; 3.00 A; M8/m8=2-186. DR PDB; 4U4Y; X-ray; 3.20 A; M8/m8=2-186. DR PDB; 4U4Z; X-ray; 3.10 A; M8/m8=2-186. DR PDB; 4U50; X-ray; 3.20 A; M8/m8=2-186. DR PDB; 4U51; X-ray; 3.20 A; M8/m8=2-186. DR PDB; 4U52; X-ray; 3.00 A; M8/m8=2-186. DR PDB; 4U53; X-ray; 3.30 A; M8/m8=2-186. DR PDB; 4U55; X-ray; 3.20 A; M8/m8=2-186. DR PDB; 4U56; X-ray; 3.45 A; M8/m8=2-186. DR PDB; 4U6F; X-ray; 3.10 A; M8/m8=2-186. DR PDB; 4V4B; EM; 11.70 A; BO=22-141. DR PDB; 4V6I; EM; 8.80 A; BR=1-186. DR PDB; 4V7F; EM; 8.70 A; Q=1-186. DR PDB; 4V7R; X-ray; 4.00 A; BR/DR=1-186. DR PDB; 4V88; X-ray; 3.00 A; BQ/DQ=1-186. DR PDB; 4V8Y; EM; 4.30 A; BQ=2-186. DR PDB; 4V8Z; EM; 6.60 A; BQ=2-186. DR PDB; 4V91; EM; 3.70 A; Q=1-186. DR PDB; 5APN; EM; 3.91 A; Q=1-186. DR PDB; 5APO; EM; 3.41 A; Q=1-186. DR PDB; 5DAT; X-ray; 3.15 A; M8/m8=2-186. DR PDB; 5DC3; X-ray; 3.25 A; M8/m8=2-186. DR PDB; 5DGE; X-ray; 3.45 A; M8/m8=2-186. DR PDB; 5DGF; X-ray; 3.30 A; M8/m8=2-186. DR PDB; 5DGV; X-ray; 3.10 A; M8/m8=2-186. DR PDB; 5FCI; X-ray; 3.40 A; M8/m8=2-186. DR PDB; 5FCJ; X-ray; 3.10 A; M8/m8=2-186. DR PDB; 5GAK; EM; 3.88 A; S=1-186. DR PDB; 5H4P; EM; 3.07 A; Q=1-186. DR PDB; 5I4L; X-ray; 3.10 A; M8/m8=2-186. DR PDB; 5JCS; EM; 9.50 A; Q=1-186. DR PDB; 5JUO; EM; 4.00 A; V=1-186. DR PDB; 5JUP; EM; 3.50 A; V=1-186. DR PDB; 5JUS; EM; 4.20 A; V=1-186. DR PDB; 5JUT; EM; 4.00 A; V=1-186. DR PDB; 5JUU; EM; 4.00 A; V=1-186. DR PDB; 5LYB; X-ray; 3.25 A; M8/m8=2-186. DR PDB; 5M1J; EM; 3.30 A; Q5=2-186. DR PDB; 5MC6; EM; 3.80 A; BB=1-186. DR PDB; 5MEI; X-ray; 3.50 A; CS/y=2-186. DR PDB; 5NDG; X-ray; 3.70 A; M8/m8=2-186. DR PDB; 5NDV; X-ray; 3.30 A; M8/m8=2-186. DR PDB; 5NDW; X-ray; 3.70 A; M8/m8=2-186. DR PDB; 5OBM; X-ray; 3.40 A; M8/m8=2-186. DR PDB; 5ON6; X-ray; 3.10 A; CS/y=2-186. DR PDB; 5T62; EM; 3.30 A; d=1-186. DR PDB; 5T6R; EM; 4.50 A; d=1-186. DR PDB; 5TBW; X-ray; 3.00 A; CS/y=2-186. DR PDB; 5TGA; X-ray; 3.30 A; M8/m8=2-186. DR PDB; 5TGM; X-ray; 3.50 A; M8/m8=2-186. DR PDB; 5Z3G; EM; 3.65 A; U=1-186. DR PDB; 6C0F; EM; 3.70 A; Q=1-186. DR PDB; 6CB1; EM; 4.60 A; Q=1-186. DR PDB; 6ELZ; EM; 3.30 A; Q=1-186. DR PDB; 6EM1; EM; 3.60 A; Q=1-186. DR PDB; 6EM3; EM; 3.20 A; Q=1-186. DR PDB; 6EM4; EM; 4.10 A; Q=1-186. DR PDB; 6EM5; EM; 4.30 A; Q=1-186. DR PDB; 6FT6; EM; 3.90 A; Q=1-186. DR PDB; 6GQ1; EM; 4.40 A; Q=2-186. DR PDB; 6GQB; EM; 3.90 A; Q=2-186. DR PDB; 6GQV; EM; 4.00 A; Q=2-186. DR PDB; 6HD7; EM; 3.40 A; S=1-186. DR PDB; 6HHQ; X-ray; 3.10 A; CS/y=1-186. DR PDB; 6I7O; EM; 5.30 A; BB/YB=2-186. DR PDB; 6M62; EM; 3.20 A; Q=1-186. DR PDB; 6N8J; EM; 3.50 A; Q=1-186. DR PDB; 6N8K; EM; 3.60 A; Q=1-186. DR PDB; 6N8L; EM; 3.60 A; Q=1-186. DR PDB; 6N8M; EM; 3.50 A; d=1-186. DR PDB; 6N8N; EM; 3.80 A; d=1-186. DR PDB; 6N8O; EM; 3.50 A; d=1-186. DR PDB; 6OIG; EM; 3.80 A; Q=2-186. DR PDB; 6Q8Y; EM; 3.10 A; BB=2-186. DR PDB; 6QIK; EM; 3.10 A; Q=1-186. DR PDB; 6QT0; EM; 3.40 A; Q=1-186. DR PDB; 6QTZ; EM; 3.50 A; Q=1-186. DR PDB; 6R84; EM; 3.60 A; S=2-186. DR PDB; 6R86; EM; 3.40 A; S=2-186. DR PDB; 6R87; EM; 3.40 A; S=2-186. DR PDB; 6RI5; EM; 3.30 A; Q=1-186. DR PDB; 6RZZ; EM; 3.20 A; Q=1-186. DR PDB; 6S05; EM; 3.90 A; Q=1-186. DR PDB; 6S47; EM; 3.28 A; AS=2-186. DR PDB; 6SNT; EM; 2.80 A; w=1-186. DR PDB; 6SV4; EM; 3.30 A; BB/YB/ZB=1-186. DR PDB; 6T4Q; EM; 2.60 A; LQ=2-186. DR PDB; 6T7I; EM; 3.20 A; LQ=1-186. DR PDB; 6T7T; EM; 3.10 A; LQ=1-186. DR PDB; 6T83; EM; 4.00 A; B/Qy=1-186. DR PDB; 6TB3; EM; 2.80 A; BB=2-186. DR PDB; 6TNU; EM; 3.10 A; BB=2-186. DR PDB; 6WOO; EM; 2.90 A; Q=3-186. DR PDB; 6XIQ; EM; 4.20 A; Q=1-186. DR PDB; 6XIR; EM; 3.20 A; Q=1-186. DR PDB; 6YLG; EM; 3.00 A; Q=1-186. DR PDB; 6YLH; EM; 3.10 A; Q=1-186. DR PDB; 6YLX; EM; 3.90 A; Q=1-186. DR PDB; 6YLY; EM; 3.80 A; Q=1-186. DR PDB; 6Z6J; EM; 3.40 A; LQ=1-186. DR PDB; 6Z6K; EM; 3.40 A; LQ=1-186. DR PDB; 7AZY; EM; 2.88 A; m=1-186. DR PDB; 7B7D; EM; 3.30 A; Lm=2-186. DR PDB; 7BT6; EM; 3.12 A; Q=1-186. DR PDB; 7BTB; EM; 3.22 A; Q=1-186. DR PDB; 7MPI; EM; 3.05 A; AQ=2-186. DR PDB; 7MPJ; EM; 2.70 A; AQ=2-186. DR PDB; 7N8B; EM; 3.05 A; AQ=2-186. DR PDB; 7NAC; EM; 3.04 A; Q=1-186. DR PDB; 7NRC; EM; 3.90 A; LS=2-186. DR PDB; 7NRD; EM; 4.36 A; LS=2-186. DR PDB; 7OF1; EM; 3.10 A; Q=1-186. DR PDB; 7OH3; EM; 3.40 A; Q=1-186. DR PDB; 7OHP; EM; 3.90 A; Q=1-186. DR PDB; 7OHQ; EM; 3.10 A; Q=1-186. DR PDB; 7OHR; EM; 4.72 A; Q=1-186. DR PDB; 7OHS; EM; 4.38 A; Q=1-186. DR PDB; 7OHT; EM; 4.70 A; Q=1-186. DR PDB; 7OHU; EM; 3.70 A; Q=1-186. DR PDB; 7OHV; EM; 3.90 A; Q=1-186. DR PDB; 7OHW; EM; 3.50 A; Q=1-186. DR PDB; 7OHX; EM; 3.30 A; Q=1-186. DR PDB; 7OHY; EM; 3.90 A; Q=1-186. DR PDB; 7R7A; EM; 3.04 A; Q=1-186. DR PDB; 7TOO; EM; 2.70 A; AL18=1-186. DR PDB; 7TOP; EM; 2.40 A; AL18=1-186. DR PDB; 7U0H; EM; 2.76 A; Q=1-186. DR PDB; 7UG6; EM; 2.90 A; Q=1-186. DR PDB; 7UOO; EM; 2.34 A; Q=1-186. DR PDB; 7UQB; EM; 2.43 A; Q=1-186. DR PDB; 7UQZ; EM; 2.44 A; Q=1-186. DR PDB; 7V08; EM; 2.36 A; Q=1-186. DR PDB; 7Z34; EM; 3.80 A; Q=1-186. DR PDB; 7ZPQ; EM; 3.47 A; BP=2-186. DR PDB; 7ZRS; EM; 4.80 A; BP=2-186. DR PDB; 7ZS5; EM; 3.20 A; BR=2-186. DR PDB; 7ZUW; EM; 4.30 A; BP=2-186. DR PDB; 7ZUX; EM; 2.50 A; EP=2-186. DR PDB; 7ZW0; EM; 2.40 A; LT=1-186. DR PDB; 8AAF; EM; 2.50 A; D=1-186. DR PDB; 8AGT; EM; 2.60 A; D=1-186. DR PDB; 8AGU; EM; 2.70 A; D=1-186. DR PDB; 8AGV; EM; 2.60 A; D=1-186. DR PDB; 8AGW; EM; 2.60 A; D=1-186. DR PDB; 8AGX; EM; 2.40 A; D=1-186. DR PDB; 8AGZ; EM; 2.60 A; D=1-186. DR PDB; 8BIP; EM; 3.10 A; LQ=2-186. DR PDB; 8BJQ; EM; 3.80 A; LQ=2-186. DR PDB; 8BQD; EM; 3.90 A; BB=2-186. DR PDB; 8BQX; EM; 3.80 A; BB=2-186. DR PDB; 8CCS; EM; 1.97 A; C=1-186. DR PDB; 8CDL; EM; 2.72 A; C=1-186. DR PDB; 8CDR; EM; 2.04 A; C=1-186. DR PDB; 8CEH; EM; 2.05 A; C=1-186. DR PDB; 8CF5; EM; 2.71 A; C=1-186. DR PDB; 8CG8; EM; 2.57 A; C=1-186. DR PDB; 8CGN; EM; 2.28 A; C=1-186. DR PDB; 8CIV; EM; 2.47 A; C=1-186. DR PDB; 8CKU; EM; 3.11 A; C=1-186. DR PDB; 8CMJ; EM; 3.79 A; C=1-186. DR PDB; 8E5T; EM; 4.00 A; Q=1-186. DR PDB; 8EUB; EM; 2.52 A; AQ=1-186. DR PDB; 8EVP; EM; 2.38 A; AQ=1-186. DR PDB; 8EVQ; EM; 2.72 A; AQ=1-186. DR PDB; 8EVR; EM; 2.87 A; AQ=1-186. DR PDB; 8EVS; EM; 2.62 A; AQ=1-186. DR PDB; 8EVT; EM; 2.20 A; AQ=1-186. DR PDB; 8EWB; EM; 2.87 A; AQ=1-186. DR PDB; 8EWC; EM; 2.45 A; AQ=1-186. DR PDB; 8HFR; EM; 2.64 A; Qk=1-186. DR PDBsum; 3J6X; -. DR PDBsum; 3J6Y; -. DR PDBsum; 3J77; -. DR PDBsum; 3J78; -. DR PDBsum; 3JCT; -. 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; 4V7F; -. DR PDBsum; 4V7R; -. DR PDBsum; 4V88; -. DR PDBsum; 4V8Y; -. DR PDBsum; 4V8Z; -. DR PDBsum; 4V91; -. DR PDBsum; 5APN; -. DR PDBsum; 5APO; -. DR PDBsum; 5DAT; -. DR PDBsum; 5DC3; -. DR PDBsum; 5DGE; -. DR PDBsum; 5DGF; -. DR PDBsum; 5DGV; -. DR PDBsum; 5FCI; -. DR PDBsum; 5FCJ; -. DR PDBsum; 5GAK; -. DR PDBsum; 5H4P; -. DR PDBsum; 5I4L; -. DR PDBsum; 5JCS; -. 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; 5T62; -. DR PDBsum; 5T6R; -. DR PDBsum; 5TBW; -. DR PDBsum; 5TGA; -. DR PDBsum; 5TGM; -. DR PDBsum; 5Z3G; -. DR PDBsum; 6C0F; -. DR PDBsum; 6CB1; -. DR PDBsum; 6ELZ; -. DR PDBsum; 6EM1; -. DR PDBsum; 6EM3; -. DR PDBsum; 6EM4; -. DR PDBsum; 6EM5; -. DR PDBsum; 6FT6; -. DR PDBsum; 6GQ1; -. DR PDBsum; 6GQB; -. DR PDBsum; 6GQV; -. DR PDBsum; 6HD7; -. DR PDBsum; 6HHQ; -. DR PDBsum; 6I7O; -. DR PDBsum; 6M62; -. DR PDBsum; 6N8J; -. DR PDBsum; 6N8K; -. DR PDBsum; 6N8L; -. DR PDBsum; 6N8M; -. DR PDBsum; 6N8N; -. DR PDBsum; 6N8O; -. DR PDBsum; 6OIG; -. DR PDBsum; 6Q8Y; -. DR PDBsum; 6QIK; -. DR PDBsum; 6QT0; -. DR PDBsum; 6QTZ; -. DR PDBsum; 6R84; -. DR PDBsum; 6R86; -. DR PDBsum; 6R87; -. DR PDBsum; 6RI5; -. DR PDBsum; 6RZZ; -. DR PDBsum; 6S05; -. 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; 6WOO; -. DR PDBsum; 6XIQ; -. DR PDBsum; 6XIR; -. DR PDBsum; 6YLG; -. DR PDBsum; 6YLH; -. DR PDBsum; 6YLX; -. DR PDBsum; 6YLY; -. DR PDBsum; 6Z6J; -. DR PDBsum; 6Z6K; -. DR PDBsum; 7AZY; -. DR PDBsum; 7B7D; -. DR PDBsum; 7BT6; -. DR PDBsum; 7BTB; -. DR PDBsum; 7MPI; -. DR PDBsum; 7MPJ; -. DR PDBsum; 7N8B; -. DR PDBsum; 7NAC; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7OF1; -. DR PDBsum; 7OH3; -. DR PDBsum; 7OHP; -. DR PDBsum; 7OHQ; -. DR PDBsum; 7OHR; -. DR PDBsum; 7OHS; -. DR PDBsum; 7OHT; -. DR PDBsum; 7OHU; -. DR PDBsum; 7OHV; -. DR PDBsum; 7OHW; -. DR PDBsum; 7OHX; -. DR PDBsum; 7OHY; -. DR PDBsum; 7R7A; -. DR PDBsum; 7TOO; -. DR PDBsum; 7TOP; -. DR PDBsum; 7U0H; -. DR PDBsum; 7UG6; -. DR PDBsum; 7UOO; -. DR PDBsum; 7UQB; -. DR PDBsum; 7UQZ; -. DR PDBsum; 7V08; -. DR PDBsum; 7Z34; -. DR PDBsum; 7ZPQ; -. DR PDBsum; 7ZRS; -. DR PDBsum; 7ZS5; -. DR PDBsum; 7ZUW; -. DR PDBsum; 7ZUX; -. DR PDBsum; 7ZW0; -. DR PDBsum; 8AAF; -. DR PDBsum; 8AGT; -. DR PDBsum; 8AGU; -. DR PDBsum; 8AGV; -. DR PDBsum; 8AGW; -. DR PDBsum; 8AGX; -. DR PDBsum; 8AGZ; -. DR PDBsum; 8BIP; -. DR PDBsum; 8BJQ; -. DR PDBsum; 8BQD; -. DR PDBsum; 8BQX; -. 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; 8E5T; -. 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 PDBsum; 8HFR; -. DR AlphaFoldDB; P0CX49; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0202; -. DR EMDB; EMD-0369; -. DR EMDB; EMD-0370; -. DR EMDB; EMD-0371; -. DR EMDB; EMD-0372; -. DR EMDB; EMD-0373; -. DR EMDB; EMD-0374; -. DR EMDB; EMD-10068; -. DR EMDB; EMD-10071; -. 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-10838; -. DR EMDB; EMD-10839; -. DR EMDB; EMD-10841; -. DR EMDB; EMD-10842; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11951; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-12866; -. DR EMDB; EMD-12892; -. DR EMDB; EMD-12904; -. DR EMDB; EMD-12905; -. DR EMDB; EMD-12906; -. DR EMDB; EMD-12907; -. DR EMDB; EMD-12908; -. DR EMDB; EMD-12909; -. DR EMDB; EMD-12910; -. DR EMDB; EMD-12911; -. DR EMDB; EMD-12912; -. DR EMDB; EMD-12913; -. DR EMDB; EMD-14471; -. 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-20077; -. 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-24269; -. DR EMDB; EMD-24296; -. DR EMDB; EMD-26033; -. DR EMDB; EMD-26034; -. 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-30108; -. DR EMDB; EMD-30170; -. DR EMDB; EMD-30174; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-4302; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4560; -. DR EMDB; EMD-4630; -. DR EMDB; EMD-4636; -. DR EMDB; EMD-4751; -. DR EMDB; EMD-4752; -. DR EMDB; EMD-4753; -. DR EMDB; EMD-4884; -. DR EMDB; EMD-6878; -. DR EMDB; EMD-7324; -. DR EMDB; EMD-7445; -. DR EMDB; EMD-8362; -. DR EMDB; EMD-8368; -. DR SMR; P0CX49; -. DR BioGRID; 34281; 164. DR BioGRID; 35537; 191. DR IntAct; P0CX49; 5. DR MINT; P0CX49; -. DR STRING; 4932.YNL301C; -. DR iPTMnet; P0CX49; -. DR MaxQB; P0CX49; -. DR PaxDb; 4932-YNL301C; -. DR PeptideAtlas; P0CX49; -. DR EnsemblFungi; YNL301C_mRNA; YNL301C; YNL301C. DR EnsemblFungi; YOL120C_mRNA; YOL120C; YOL120C. DR GeneID; 854029; -. DR GeneID; 855415; -. DR KEGG; sce:YNL301C; -. DR KEGG; sce:YOL120C; -. DR AGR; SGD:S000005480; -. DR SGD; S000005480; RPL18A. DR VEuPathDB; FungiDB:YNL301C; -. DR VEuPathDB; FungiDB:YOL120C; -. DR eggNOG; KOG1714; Eukaryota. DR HOGENOM; CLU_080024_0_1_1; -. DR InParanoid; P0CX49; -. DR OMA; DHTTKQH; -. DR OrthoDB; 1122253at2759; -. DR BioCyc; YEAST:G3O-33516-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-72689; Formation of a pool of free 40S subunits. 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; 854029; 2 hits in 10 CRISPR screens. DR BioGRID-ORCS; 855415; 6 hits in 10 CRISPR screens. DR EvolutionaryTrace; P0CX49; -. DR PRO; PR:P0CX49; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P0CX49; Protein. DR ExpressionAtlas; P0CX49; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD. 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; IC:SGD. DR Gene3D; 3.100.10.10; -; 1. DR InterPro; IPR000039; Ribosomal_eL18. DR InterPro; IPR021132; Ribosomal_eL18/eL18-A/B/_CS. DR InterPro; IPR021131; Ribosomal_uL15/eL18. DR InterPro; IPR036227; Ribosomal_uL15/eL18_sf. DR PANTHER; PTHR10934; 60S RIBOSOMAL PROTEIN L18; 1. DR PANTHER; PTHR10934:SF2; 60S RIBOSOMAL PROTEIN L18; 1. DR Pfam; PF17135; Ribosomal_L18; 1. DR SUPFAM; SSF52080; Ribosomal proteins L15p and L18e; 1. DR PROSITE; PS01106; RIBOSOMAL_L18E; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Methylation; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11983894" FT CHAIN 2..186 FT /note="Large ribosomal subunit protein eL18A" FT /id="PRO_0000132784" FT MOD_RES 50 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:22522802" FT CROSSLNK 116 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT HELIX 24..39 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 43..52 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 64..70 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 80..88 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 108..117 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 124..130 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:6EM3" SQ SEQUENCE 186 AA; 20563 MW; D097B187F369EACD CRC64; MGIDHTSKQH KRSGHRTAPK SDNVYLKLLV KLYTFLARRT DAPFNKVVLK ALFLSKINRP PVSVSRIARA LKQEGAANKT VVVVGTVTDD ARIFEFPKTT VAALRFTAGA RAKIVKAGGE CITLDQLAVR APKGQNTLIL RGPRNSREAV RHFGMGPHKG KAPRILSTGR KFERARGRRR SKGFKV //