RL39_YEAST
ID RL39_YEAST Reviewed; 51 AA.
AC P04650; D6VW02;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=60S ribosomal protein L39 {ECO:0000303|PubMed:9559554};
DE AltName: Full=L46;
DE AltName: Full=Large ribosomal subunit protein eL39 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL40;
GN Name=RPL39 {ECO:0000303|PubMed:9559554}; Synonyms=RPL46, SPB2;
GN OrderedLocusNames=YJL189W; ORFNames=J0360;
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=4000930; DOI=10.1093/nar/13.3.701;
RA Leer R.J., van Raamsdonk-Duin M.M.C., Kraakman P., Mager W.H., Planta R.J.;
RT "The genes for yeast ribosomal proteins S24 and L46 are adjacent and
RT divergently transcribed.";
RL Nucleic Acids Res. 13:701-709(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 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.
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 INTERACTION WITH YIH1.
RX PubMed=22404850; DOI=10.1111/j.1742-4658.2012.08553.x;
RA Waller T., Lee S.J., Sattlegger E.;
RT "Evidence that Yih1 resides in a complex with ribosomes.";
RL FEBS J. 279:1761-1776(2012).
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 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 [10]
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). eL39
CC interacts with YIH1 (PubMed:22404850). {ECO:0000269|PubMed:22096102,
CC ECO:0000269|PubMed:22404850, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family.
CC {ECO:0000305}.
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DR EMBL; X01963; CAA25999.1; -; Genomic_DNA.
DR EMBL; Z49464; CAA89483.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08618.1; -; Genomic_DNA.
DR PIR; B23082; R6BY46.
DR RefSeq; NP_012346.1; NM_001181622.1.
DR PDB; 2WW9; EM; 8.60 A; O=1-51.
DR PDB; 2WWA; EM; 8.90 A; O=1-51.
DR PDB; 2WWB; EM; 6.48 A; O=1-51.
DR PDB; 3J6X; EM; 6.10 A; 79=1-51.
DR PDB; 3J6Y; EM; 6.10 A; 79=1-51.
DR PDB; 3J77; EM; 6.20 A; 89=1-51.
DR PDB; 3J78; EM; 6.30 A; 89=1-51.
DR PDB; 3JCT; EM; 3.08 A; l=1-51.
DR PDB; 4U3M; X-ray; 3.00 A; O9/o9=2-51.
DR PDB; 4U3N; X-ray; 3.20 A; O9/o9=2-51.
DR PDB; 4U3U; X-ray; 2.90 A; O9/o9=2-51.
DR PDB; 4U4N; X-ray; 3.10 A; O9/o9=2-51.
DR PDB; 4U4O; X-ray; 3.60 A; O9/o9=2-51.
DR PDB; 4U4Q; X-ray; 3.00 A; O9/o9=2-51.
DR PDB; 4U4R; X-ray; 2.80 A; O9/o9=2-51.
DR PDB; 4U4U; X-ray; 3.00 A; O9/o9=2-51.
DR PDB; 4U4Y; X-ray; 3.20 A; O9/o9=2-51.
DR PDB; 4U4Z; X-ray; 3.10 A; O9/o9=2-51.
DR PDB; 4U50; X-ray; 3.20 A; O9/o9=2-51.
DR PDB; 4U51; X-ray; 3.20 A; O9/o9=2-51.
DR PDB; 4U52; X-ray; 3.00 A; O9/o9=2-51.
DR PDB; 4U53; X-ray; 3.30 A; O9/o9=2-51.
DR PDB; 4U55; X-ray; 3.20 A; O9/o9=2-51.
DR PDB; 4U56; X-ray; 3.45 A; O9/o9=2-51.
DR PDB; 4U6F; X-ray; 3.10 A; O9/o9=2-51.
DR PDB; 4V6I; EM; 8.80 A; Bo=1-51.
DR PDB; 4V7F; EM; 8.70 A; j=1-51.
DR PDB; 4V7R; X-ray; 4.00 A; Be/De=1-51.
DR PDB; 4V88; X-ray; 3.00 A; Bl/Dl=1-51.
DR PDB; 4V8T; EM; 8.10 A; l=1-51.
DR PDB; 4V8Y; EM; 4.30 A; Bl=2-51.
DR PDB; 4V8Z; EM; 6.60 A; Bl=2-51.
DR PDB; 4V91; EM; 3.70 A; l=1-51.
DR PDB; 5APN; EM; 3.91 A; l=1-51.
DR PDB; 5APO; EM; 3.41 A; l=1-51.
DR PDB; 5DAT; X-ray; 3.15 A; O9/o9=2-51.
DR PDB; 5DC3; X-ray; 3.25 A; O9/o9=2-51.
DR PDB; 5DGE; X-ray; 3.45 A; O9/o9=2-51.
DR PDB; 5DGF; X-ray; 3.30 A; O9/o9=2-51.
DR PDB; 5DGV; X-ray; 3.10 A; O9/o9=2-51.
DR PDB; 5FCI; X-ray; 3.40 A; O9/o9=2-51.
DR PDB; 5FCJ; X-ray; 3.10 A; O9/o9=2-51.
DR PDB; 5FL8; EM; 9.50 A; l=1-51.
DR PDB; 5GAK; EM; 3.88 A; n=1-51.
DR PDB; 5H4P; EM; 3.07 A; l=1-51.
DR PDB; 5I4L; X-ray; 3.10 A; O9/o9=2-51.
DR PDB; 5IT7; EM; 3.60 A; ll=2-50.
DR PDB; 5JCS; EM; 9.50 A; l=1-51.
DR PDB; 5JUO; EM; 4.00 A; QA=1-51.
DR PDB; 5JUP; EM; 3.50 A; QA=1-51.
DR PDB; 5JUS; EM; 4.20 A; QA=1-51.
DR PDB; 5JUT; EM; 4.00 A; QA=1-51.
DR PDB; 5JUU; EM; 4.00 A; QA=1-51.
DR PDB; 5LYB; X-ray; 3.25 A; O9/o9=2-51.
DR PDB; 5M1J; EM; 3.30 A; l5=2-51.
DR PDB; 5MC6; EM; 3.80 A; AL=1-51.
DR PDB; 5MEI; X-ray; 3.50 A; AM/DN=2-51.
DR PDB; 5NDG; X-ray; 3.70 A; O9/o9=2-51.
DR PDB; 5NDV; X-ray; 3.30 A; O9/o9=2-51.
DR PDB; 5NDW; X-ray; 3.70 A; O9/o9=2-51.
DR PDB; 5OBM; X-ray; 3.40 A; O9/o9=2-51.
DR PDB; 5ON6; X-ray; 3.10 A; AM/DN=2-51.
DR PDB; 5T62; EM; 3.30 A; y=1-51.
DR PDB; 5T6R; EM; 4.50 A; y=1-51.
DR PDB; 5TBW; X-ray; 3.00 A; AM/DN=2-51.
DR PDB; 5TGA; X-ray; 3.30 A; O9/o9=2-51.
DR PDB; 5TGM; X-ray; 3.50 A; O9/o9=2-51.
DR PDB; 6FT6; EM; 3.90 A; l=1-51.
DR PDB; 6GQ1; EM; 4.40 A; l=2-51.
DR PDB; 6GQB; EM; 3.90 A; l=2-51.
DR PDB; 6GQV; EM; 4.00 A; l=2-51.
DR PDB; 6HD7; EM; 3.40 A; n=1-51.
DR PDB; 6HHQ; X-ray; 3.10 A; AM/DN=1-51.
DR PDB; 6I7O; EM; 5.30 A; AL/XL=2-51.
DR PDB; 6M62; EM; 3.20 A; l=1-51.
DR PDB; 6N8J; EM; 3.50 A; l=1-51.
DR PDB; 6N8K; EM; 3.60 A; l=1-51.
DR PDB; 6N8L; EM; 3.60 A; l=1-51.
DR PDB; 6N8M; EM; 3.50 A; y=1-51.
DR PDB; 6N8N; EM; 3.80 A; y=1-51.
DR PDB; 6N8O; EM; 3.50 A; y=1-51.
DR PDB; 6OIG; EM; 3.80 A; l=2-51.
DR PDB; 6Q8Y; EM; 3.10 A; AL=2-51.
DR PDB; 6QIK; EM; 3.10 A; k=1-51.
DR PDB; 6QT0; EM; 3.40 A; k=1-51.
DR PDB; 6QTZ; EM; 3.50 A; k=1-51.
DR PDB; 6R84; EM; 3.60 A; n=2-51.
DR PDB; 6R86; EM; 3.40 A; n=2-51.
DR PDB; 6R87; EM; 3.40 A; n=2-51.
DR PDB; 6RI5; EM; 3.30 A; k=1-51.
DR PDB; 6RZZ; EM; 3.20 A; k=1-51.
DR PDB; 6S05; EM; 3.90 A; k=1-51.
DR PDB; 6S47; EM; 3.28 A; An=2-51.
DR PDB; 6SNT; EM; 2.80 A; ae=1-51.
DR PDB; 6SV4; EM; 3.30 A; AL/XL/zL=1-51.
DR PDB; 6T4Q; EM; 2.60 A; Ll=2-51.
DR PDB; 6T7I; EM; 3.20 A; Ll=1-51.
DR PDB; 6T7T; EM; 3.10 A; Ll=1-51.
DR PDB; 6T83; EM; 4.00 A; W/lb=1-51.
DR PDB; 6TB3; EM; 2.80 A; AL=2-51.
DR PDB; 6TNU; EM; 3.10 A; AL=2-51.
DR PDB; 6WOO; EM; 2.90 A; l=2-50.
DR PDB; 6XIQ; EM; 4.20 A; l=1-51.
DR PDB; 6XIR; EM; 3.20 A; l=1-51.
DR PDB; 6YLG; EM; 3.00 A; l=1-51.
DR PDB; 6YLH; EM; 3.10 A; l=1-51.
DR PDB; 6YLX; EM; 3.90 A; l=1-51.
DR PDB; 6YLY; EM; 3.80 A; l=1-51.
DR PDB; 6Z6J; EM; 3.40 A; Ll=1-51.
DR PDB; 6Z6K; EM; 3.40 A; Ll=1-51.
DR PDB; 7AZY; EM; 2.88 A; M=1-51.
DR PDB; 7B7D; EM; 3.30 A; Lh=2-51.
DR PDB; 7NRC; EM; 3.90 A; Ln=2-51.
DR PDB; 7NRD; EM; 4.36 A; Ln=2-51.
DR PDB; 7OF1; EM; 3.10 A; l=1-51.
DR PDB; 7OH3; EM; 3.40 A; l=1-51.
DR PDB; 7OHQ; EM; 3.10 A; l=1-51.
DR PDBsum; 2WW9; -.
DR PDBsum; 2WWA; -.
DR PDBsum; 2WWB; -.
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; 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; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5IT7; -.
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; 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; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR AlphaFoldDB; P04650; -.
DR SMR; P04650; -.
DR BioGRID; 33574; 48.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-4522N; -.
DR IntAct; P04650; 12.
DR MINT; P04650; -.
DR STRING; 4932.YJL189W; -.
DR PaxDb; P04650; -.
DR PRIDE; P04650; -.
DR TopDownProteomics; P04650; -.
DR EnsemblFungi; YJL189W_mRNA; YJL189W; YJL189W.
DR GeneID; 853250; -.
DR KEGG; sce:YJL189W; -.
DR SGD; S000003725; RPL39.
DR VEuPathDB; FungiDB:YJL189W; -.
DR eggNOG; KOG0002; Eukaryota.
DR GeneTree; ENSGT00940000175753; -.
DR HOGENOM; CLU_181948_3_0_1; -.
DR InParanoid; P04650; -.
DR BioCyc; YEAST:G3O-31621-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; P04650; -.
DR PRO; PR:P04650; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P04650; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR Gene3D; 1.10.1620.10; -; 1.
DR HAMAP; MF_00629; Ribosomal_L39e; 1.
DR InterPro; IPR000077; Ribosomal_L39.
DR InterPro; IPR020083; Ribosomal_L39_CS.
DR InterPro; IPR023626; Ribosomal_L39e_dom_sf.
DR Pfam; PF00832; Ribosomal_L39; 1.
DR SUPFAM; SSF48662; SSF48662; 1.
DR PROSITE; PS00051; RIBOSOMAL_L39E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..51
FT /note="60S ribosomal protein L39"
FT /id="PRO_0000127044"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 51 AA; 6342 MW; FE518D8B3949C163 CRC64;
MAAQKSFRIK QKMAKAKKQN RPLPQWIRLR TNNTIRYNAK RRNWRRTKMN I
