RL18A_YEAST
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 03-AUG-2022, entry version 90.
DE RecName: Full=60S ribosomal protein L18-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL18-A {ECO:0000303|PubMed:24524803};
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=20419.431; 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}.
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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; 5FL8; EM; 9.50 A; Q=1-186.
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; 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 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; 5FL8; -.
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; 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 AlphaFoldDB; P0CX49; -.
DR SMR; P0CX49; -.
DR BioGRID; 34281; 120.
DR BioGRID; 35537; 131.
DR IntAct; P0CX49; 5.
DR MINT; P0CX49; -.
DR STRING; 4932.YNL301C; -.
DR iPTMnet; P0CX49; -.
DR MaxQB; P0CX49; -.
DR PaxDb; P0CX49; -.
DR PRIDE; 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 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; MSKIHRP; -.
DR BioCyc; YEAST:G3O-33516-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-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 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 InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR021132; Ribosomal_L18/L18-A/B/e_CS.
DR InterPro; IPR000039; Ribosomal_L18e.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR PANTHER; PTHR10934; PTHR10934; 1.
DR Pfam; PF17135; Ribosomal_L18; 1.
DR SUPFAM; SSF52080; SSF52080; 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="60S ribosomal protein L18-A"
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
