ID RL15A_YEAST Reviewed; 204 AA. AC P05748; D6VY31; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 199. DE RecName: Full=Large ribosomal subunit protein eL15A {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L15-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=L13; DE AltName: Full=RP15R; DE AltName: Full=YL10; DE AltName: Full=YP18; GN Name=RPL15A {ECO:0000303|PubMed:9559554}; GN Synonyms=RPL10A, RPL13A, YL10A; OrderedLocusNames=YLR029C; 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]. RA Tomiyoshi A., Suzuki K., Otaka E.; RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(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 PROTEIN SEQUENCE OF 2-44. RX PubMed=6814480; DOI=10.1021/bi00262a005; RA Otaka E., Higo K., Osawa S.; RT "Isolation of seventeen proteins and amino-terminal amino acid sequences of RT eight proteins from cytoplasmic ribosomes of yeast."; RL Biochemistry 21:4545-4550(1982). RN [5] RP PROTEIN SEQUENCE OF 2-9. 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 [6] 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 [7] 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 [8] 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 [9] RP 3D-STRUCTURE MODELING OF 3-196, 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 [10] 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 [11] RP X-RAY CRYSTALLOGRAPHY (4.0 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 [12] RP X-RAY CRYSTALLOGRAPHY (3.0 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 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). CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. CC -!- MISCELLANEOUS: There are 2 genes for eL15 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 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; D14675; BAA03506.1; -; Genomic_DNA. DR EMBL; Z73201; CAA97553.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09347.1; -; Genomic_DNA. DR PIR; S48502; S48502. DR RefSeq; NP_013129.1; NM_001181916.1. DR PDB; 3J6X; EM; 6.10 A; 55=1-204. DR PDB; 3J6Y; EM; 6.10 A; 55=1-204. DR PDB; 3J77; EM; 6.20 A; 65=1-204. DR PDB; 3J78; EM; 6.30 A; 65=1-204. DR PDB; 3JCT; EM; 3.08 A; N=1-204. DR PDB; 4U3M; X-ray; 3.00 A; M5/m5=2-204. DR PDB; 4U3N; X-ray; 3.20 A; M5/m5=2-204. DR PDB; 4U3U; X-ray; 2.90 A; M5/m5=2-204. DR PDB; 4U4N; X-ray; 3.10 A; M5/m5=2-204. DR PDB; 4U4O; X-ray; 3.60 A; M5/m5=2-204. DR PDB; 4U4Q; X-ray; 3.00 A; M5/m5=2-204. DR PDB; 4U4R; X-ray; 2.80 A; M5/m5=2-204. DR PDB; 4U4U; X-ray; 3.00 A; M5/m5=2-204. DR PDB; 4U4Y; X-ray; 3.20 A; M5/m5=2-204. DR PDB; 4U4Z; X-ray; 3.10 A; M5/m5=2-204. DR PDB; 4U50; X-ray; 3.20 A; M5/m5=2-204. DR PDB; 4U51; X-ray; 3.20 A; M5/m5=2-204. DR PDB; 4U52; X-ray; 3.00 A; M5/m5=2-204. DR PDB; 4U53; X-ray; 3.30 A; M5/m5=2-204. DR PDB; 4U55; X-ray; 3.20 A; M5/m5=2-204. DR PDB; 4U56; X-ray; 3.45 A; M5/m5=2-204. DR PDB; 4U6F; X-ray; 3.10 A; M5/m5=2-204. DR PDB; 4V4B; EM; 11.70 A; BL=2-204. DR PDB; 4V6I; EM; 8.80 A; BP=1-204. DR PDB; 4V7F; EM; 8.70 A; O=1-204. DR PDB; 4V7R; X-ray; 4.00 A; BO/DO=1-204. DR PDB; 4V88; X-ray; 3.00 A; BN/DN=1-204. DR PDB; 4V8T; EM; 8.10 A; N=1-204. DR PDB; 4V8Y; EM; 4.30 A; BN=2-204. DR PDB; 4V8Z; EM; 6.60 A; BN=2-204. DR PDB; 4V91; EM; 3.70 A; N=1-204. DR PDB; 5APN; EM; 3.91 A; N=1-204. DR PDB; 5APO; EM; 3.41 A; N=1-204. DR PDB; 5DAT; X-ray; 3.15 A; M5=2-204, m5=2-204. DR PDB; 5DC3; X-ray; 3.25 A; M5/m5=2-204. DR PDB; 5DGE; X-ray; 3.45 A; M5/m5=2-204. DR PDB; 5DGF; X-ray; 3.30 A; M5/m5=2-204. DR PDB; 5DGV; X-ray; 3.10 A; M5/m5=2-204. DR PDB; 5FCI; X-ray; 3.40 A; M5/m5=2-204. DR PDB; 5FCJ; X-ray; 3.10 A; M5/m5=2-204. DR PDB; 5GAK; EM; 3.88 A; P=1-204. DR PDB; 5H4P; EM; 3.07 A; N=1-204. DR PDB; 5I4L; X-ray; 3.10 A; M5/m5=2-204. DR PDB; 5JCS; EM; 9.50 A; N=1-204. DR PDB; 5JUO; EM; 4.00 A; S=1-204. DR PDB; 5JUP; EM; 3.50 A; S=1-204. DR PDB; 5JUS; EM; 4.20 A; S=1-204. DR PDB; 5JUT; EM; 4.00 A; S=1-204. DR PDB; 5JUU; EM; 4.00 A; S=1-204. DR PDB; 5LYB; X-ray; 3.25 A; M5/m5=2-204. DR PDB; 5M1J; EM; 3.30 A; N5=2-204. DR PDB; 5MC6; EM; 3.80 A; AQ=1-204. DR PDB; 5MEI; X-ray; 3.50 A; CP/v=2-204. DR PDB; 5NDG; X-ray; 3.70 A; M5/m5=2-204. DR PDB; 5NDV; X-ray; 3.30 A; M5/m5=2-204. DR PDB; 5NDW; X-ray; 3.70 A; M5/m5=2-204. DR PDB; 5OBM; X-ray; 3.40 A; M5/m5=2-204. DR PDB; 5ON6; X-ray; 3.10 A; CP/v=2-204. DR PDB; 5T62; EM; 3.30 A; a=1-204. DR PDB; 5T6R; EM; 4.50 A; a=1-204. DR PDB; 5TBW; X-ray; 3.00 A; CP/v=2-204. DR PDB; 5TGA; X-ray; 3.30 A; M5/m5=2-204. DR PDB; 5TGM; X-ray; 3.50 A; M5/m5=2-204. DR PDB; 5Z3G; EM; 3.65 A; R=1-204. DR PDB; 6C0F; EM; 3.70 A; N=1-204. DR PDB; 6CB1; EM; 4.60 A; N=1-204. DR PDB; 6ELZ; EM; 3.30 A; N=1-204. DR PDB; 6EM1; EM; 3.60 A; N=1-204. DR PDB; 6EM3; EM; 3.20 A; N=1-204. DR PDB; 6EM4; EM; 4.10 A; N=1-204. DR PDB; 6EM5; EM; 4.30 A; N=1-204. DR PDB; 6FT6; EM; 3.90 A; N=1-204. DR PDB; 6GQ1; EM; 4.40 A; N=2-204. DR PDB; 6GQB; EM; 3.90 A; N=2-204. DR PDB; 6GQV; EM; 4.00 A; N=2-204. DR PDB; 6HD7; EM; 3.40 A; P=1-204. DR PDB; 6HHQ; X-ray; 3.10 A; CP/v=1-204. DR PDB; 6I7O; EM; 5.30 A; AQ/XQ=2-204. DR PDB; 6M62; EM; 3.20 A; N=1-204. DR PDB; 6N8J; EM; 3.50 A; N=1-204. DR PDB; 6N8K; EM; 3.60 A; N=1-204. DR PDB; 6N8L; EM; 3.60 A; N=1-204. DR PDB; 6N8M; EM; 3.50 A; a=1-204. DR PDB; 6N8N; EM; 3.80 A; a=1-204. DR PDB; 6N8O; EM; 3.50 A; a=1-204. DR PDB; 6OIG; EM; 3.80 A; N=2-204. DR PDB; 6Q8Y; EM; 3.10 A; AQ=2-204. DR PDB; 6QIK; EM; 3.10 A; O=1-204. DR PDB; 6QT0; EM; 3.40 A; O=1-204. DR PDB; 6QTZ; EM; 3.50 A; O=1-204. DR PDB; 6R84; EM; 3.60 A; p=2-204. DR PDB; 6R86; EM; 3.40 A; p=2-204. DR PDB; 6R87; EM; 3.40 A; p=2-204. DR PDB; 6RI5; EM; 3.30 A; O=1-204. DR PDB; 6RZZ; EM; 3.20 A; O=1-204. DR PDB; 6S05; EM; 3.90 A; O=1-204. DR PDB; 6S47; EM; 3.28 A; AP=2-204. DR PDB; 6SNT; EM; 2.80 A; t=1-204. DR PDB; 6SV4; EM; 3.30 A; AQ/XQ/zQ=1-204. DR PDB; 6T4Q; EM; 2.60 A; LN=2-204. DR PDB; 6T7I; EM; 3.20 A; LN=1-204. DR PDB; 6T7T; EM; 3.10 A; LN=1-204. DR PDB; 6T83; EM; 4.00 A; Ny/Pa=1-204. DR PDB; 6TB3; EM; 2.80 A; AQ=2-204. DR PDB; 6TNU; EM; 3.10 A; AQ=2-204. DR PDB; 6WOO; EM; 2.90 A; N=2-203. DR PDB; 6XIQ; EM; 4.20 A; N=1-204. DR PDB; 6XIR; EM; 3.20 A; N=1-204. DR PDB; 6YLG; EM; 3.00 A; N=1-204. DR PDB; 6YLH; EM; 3.10 A; N=1-204. DR PDB; 6YLX; EM; 3.90 A; N=1-204. DR PDB; 6YLY; EM; 3.80 A; N=1-204. DR PDB; 6Z6J; EM; 3.40 A; LN=1-204. DR PDB; 6Z6K; EM; 3.40 A; LN=1-204. DR PDB; 7AZY; EM; 2.88 A; R=1-204. DR PDB; 7B7D; EM; 3.30 A; LP=2-204. DR PDB; 7BT6; EM; 3.12 A; N=1-204. DR PDB; 7BTB; EM; 3.22 A; N=1-204. DR PDB; 7MPI; EM; 3.05 A; AN=2-204. DR PDB; 7MPJ; EM; 2.70 A; AN=2-204. DR PDB; 7N8B; EM; 3.05 A; AN=2-204. DR PDB; 7NAC; EM; 3.04 A; N=1-204. DR PDB; 7NRC; EM; 3.90 A; LP=2-204. DR PDB; 7NRD; EM; 4.36 A; LP=2-204. DR PDB; 7OF1; EM; 3.10 A; N=1-204. DR PDB; 7OH3; EM; 3.40 A; N=1-204. DR PDB; 7OHP; EM; 3.90 A; N=1-204. DR PDB; 7OHQ; EM; 3.10 A; N=1-204. DR PDB; 7OHR; EM; 4.72 A; N=1-204. DR PDB; 7OHS; EM; 4.38 A; N=1-204. DR PDB; 7OHU; EM; 3.70 A; N=1-204. DR PDB; 7OHV; EM; 3.90 A; N=1-204. DR PDB; 7OHW; EM; 3.50 A; N=1-204. DR PDB; 7OHX; EM; 3.30 A; N=1-204. DR PDB; 7OHY; EM; 3.90 A; N=1-204. DR PDB; 7OSA; X-ray; 3.00 A; eL15=1-204. DR PDB; 7OSM; X-ray; 3.00 A; eL15=1-204. DR PDB; 7R6K; EM; 3.17 A; N=1-204. DR PDB; 7R6Q; EM; 2.98 A; N=1-204. DR PDB; 7R7A; EM; 3.04 A; N=1-204. DR PDB; 7RR5; EM; 3.23 A; LN=1-204. DR PDB; 7TOO; EM; 2.70 A; AL15=1-204. DR PDB; 7TOP; EM; 2.40 A; AL15=1-204. DR PDB; 7U0H; EM; 2.76 A; N=1-204. DR PDB; 7UG6; EM; 2.90 A; N=1-204. DR PDB; 7UOO; EM; 2.34 A; N=1-204. DR PDB; 7UQB; EM; 2.43 A; N=1-204. DR PDB; 7UQZ; EM; 2.44 A; N=2-204. DR PDB; 7V08; EM; 2.36 A; N=1-204. DR PDB; 7Z34; EM; 3.80 A; N=1-204. DR PDB; 7ZPQ; EM; 3.47 A; BM=2-204. DR PDB; 7ZRS; EM; 4.80 A; BM=2-204. DR PDB; 7ZS5; EM; 3.20 A; BO=2-204. DR PDB; 7ZUW; EM; 4.30 A; BM=2-204. DR PDB; 7ZUX; EM; 2.50 A; EM=2-204. DR PDB; 7ZW0; EM; 2.40 A; LQ=1-204. DR PDB; 8AAF; EM; 2.50 A; A=1-204. DR PDB; 8AGT; EM; 2.60 A; A=1-204. DR PDB; 8AGU; EM; 2.70 A; A=1-204. DR PDB; 8AGV; EM; 2.60 A; A=1-204. DR PDB; 8AGW; EM; 2.60 A; A=1-204. DR PDB; 8AGX; EM; 2.40 A; A=1-204. DR PDB; 8AGZ; EM; 2.60 A; A=1-204. DR PDB; 8BIP; EM; 3.10 A; LN=2-204. DR PDB; 8BJQ; EM; 3.80 A; LN=2-204. DR PDB; 8BQD; EM; 3.90 A; AQ=2-204. DR PDB; 8BQX; EM; 3.80 A; AQ=2-204. DR PDB; 8CCS; EM; 1.97 A; QQ=1-204. DR PDB; 8CDL; EM; 2.72 A; QQ=1-204. DR PDB; 8CDR; EM; 2.04 A; QQ=1-204. DR PDB; 8CEH; EM; 2.05 A; QQ=1-204. DR PDB; 8CF5; EM; 2.71 A; QQ=1-204. DR PDB; 8CG8; EM; 2.57 A; QQ=1-204. DR PDB; 8CGN; EM; 2.28 A; QQ=1-204. DR PDB; 8CIV; EM; 2.47 A; QQ=1-204. DR PDB; 8CKU; EM; 3.11 A; QQ=1-204. DR PDB; 8CMJ; EM; 3.79 A; QQ=1-204. DR PDB; 8E5T; EM; 4.00 A; N=1-204. DR PDB; 8EUB; EM; 2.52 A; AN=1-204. DR PDB; 8EVP; EM; 2.38 A; AN=1-204. DR PDB; 8EVQ; EM; 2.72 A; AN=1-204. DR PDB; 8EVR; EM; 2.87 A; AN=1-204. DR PDB; 8EVS; EM; 2.62 A; AN=1-204. DR PDB; 8EVT; EM; 2.20 A; AN=1-204. DR PDB; 8EWB; EM; 2.87 A; AN=1-204. DR PDB; 8EWC; EM; 2.45 A; AN=1-204. DR PDB; 8HFR; EM; 2.64 A; No=1-204. 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; 4V8T; -. 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; 7OHU; -. DR PDBsum; 7OHV; -. DR PDBsum; 7OHW; -. DR PDBsum; 7OHX; -. DR PDBsum; 7OHY; -. DR PDBsum; 7OSA; -. DR PDBsum; 7OSM; -. DR PDBsum; 7R6K; -. DR PDBsum; 7R6Q; -. DR PDBsum; 7R7A; -. DR PDBsum; 7RR5; -. 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; P05748; -. 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-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-24280; -. DR EMDB; EMD-24286; -. DR EMDB; EMD-24296; -. DR EMDB; EMD-24652; -. DR EMDB; EMD-26033; -. DR EMDB; EMD-26034; -. DR EMDB; EMD-26485; -. 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-34725; -. 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; P05748; -. DR BioGRID; 31303; 362. DR IntAct; P05748; 27. DR MINT; P05748; -. DR STRING; 4932.YLR029C; -. DR iPTMnet; P05748; -. DR MaxQB; P05748; -. DR PaxDb; 4932-YLR029C; -. DR PeptideAtlas; P05748; -. DR EnsemblFungi; YLR029C_mRNA; YLR029C; YLR029C. DR GeneID; 850716; -. DR KEGG; sce:YLR029C; -. DR AGR; SGD:S000004019; -. DR SGD; S000004019; RPL15A. DR VEuPathDB; FungiDB:YLR029C; -. DR eggNOG; KOG1678; Eukaryota. DR GeneTree; ENSGT00910000144184; -. DR HOGENOM; CLU_080796_0_0_1; -. DR InParanoid; P05748; -. DR OMA; YIRDAWK; -. DR OrthoDB; 819949at2759; -. DR BioCyc; YEAST:G3O-32188-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; 850716; 8 hits in 10 CRISPR screens. DR EvolutionaryTrace; P05748; -. DR PRO; PR:P05748; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P05748; Protein. 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; IDA:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD. DR Gene3D; 3.40.1120.10; Ribosomal protein l15e; 1. DR InterPro; IPR024794; Rbsml_eL15_core_dom_sf. DR InterPro; IPR000439; Ribosomal_eL15. DR InterPro; IPR020925; Ribosomal_eL15_CS. DR InterPro; IPR012678; Ribosomal_uL23/eL15/eS24_sf. DR PANTHER; PTHR11847; RIBOSOMAL PROTEIN L15; 1. DR PANTHER; PTHR11847:SF4; RIBOSOMAL PROTEIN L15; 1. DR Pfam; PF00827; Ribosomal_L15e; 1. DR SMART; SM01384; Ribosomal_L15e; 1. DR SUPFAM; SSF54189; Ribosomal proteins S24e, L23 and L15e; 1. DR PROSITE; PS01194; RIBOSOMAL_L15E; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1544921, FT ECO:0000269|PubMed:6814480" FT CHAIN 2..204 FT /note="Large ribosomal subunit protein eL15A" FT /id="PRO_0000127566" FT REGION 164..185 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 28 FT /note="W -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 4..11 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:7R6K" FT HELIX 17..31 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 45..51 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 59..67 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:7R6K" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 113..123 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 125..135 FT /evidence="ECO:0007829|PDB:7R6Q" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 140..143 FT /evidence="ECO:0007829|PDB:7R6Q" FT TURN 146..152 FT /evidence="ECO:0007829|PDB:7R6Q" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:6EM3" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:7R6K" FT HELIX 166..172 FT /evidence="ECO:0007829|PDB:7R6K" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 187..194 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:6EM3" SQ SEQUENCE 204 AA; 24422 MW; 3913F9E4AB9ECA2C CRC64; MGAYKYLEEL QRKKQSDVLR FLQRVRVWEY RQKNVIHRAA RPTRPDKARR LGYKAKQGFV IYRVRVRRGN RKRPVPKGAT YGKPTNQGVN ELKYQRSLRA TAEERVGRRA ANLRVLNSYW VNQDSTYKYF EVILVDPQHK AIRRDARYNW ICDPVHKHRE ARGLTATGKK SRGINKGHKF NNTKAGRRKT WKRQNTLSLW RYRK //