ID RL32_YEAST Reviewed; 130 AA. AC P38061; A2TBM1; D6VPR1; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Large ribosomal subunit protein eL32 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L32 {ECO:0000303|PubMed:9559554}; GN Name=RPL32 {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YBL092W; GN ORFNames=YBL0838; 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]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7502586; DOI=10.1002/yea.320111112; RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.; RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces RT cerevisiae chromosome II."; RL Yeast 11:1103-1112(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-76. RC STRAIN=ATCC 201390 / BY4743; RX PubMed=17244705; DOI=10.1073/pnas.0610354104; RA Juneau K., Palm C., Miranda M., Davis R.W.; RT "High-density yeast-tiling array reveals previously undiscovered introns RT and extensive regulation of meiotic splicing."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007). 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 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY RP 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 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 [10] RP 3D-STRUCTURE MODELING OF 14-122, 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 [11] 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 [12] 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 [13] 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 -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 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; X79489; CAA56010.1; -; Genomic_DNA. DR EMBL; Z35853; CAA84914.1; -; Genomic_DNA. DR EMBL; AY558291; AAS56617.1; -; Genomic_DNA. DR EMBL; EF123124; ABM97468.1; -; mRNA. DR EMBL; BK006936; DAA07031.1; -; Genomic_DNA. DR PIR; S45410; S45410. DR RefSeq; NP_009460.1; NM_001178332.1. DR PDB; 3J6X; EM; 6.10 A; 72=1-130. DR PDB; 3J6Y; EM; 6.10 A; 72=1-130. DR PDB; 3J77; EM; 6.20 A; 82=1-130. DR PDB; 3J78; EM; 6.30 A; 82=1-130. DR PDB; 3JCT; EM; 3.08 A; e=1-130. DR PDB; 4U3M; X-ray; 3.00 A; O2/o2=2-130. DR PDB; 4U3N; X-ray; 3.20 A; O2/o2=2-130. DR PDB; 4U3U; X-ray; 2.90 A; O2/o2=2-130. DR PDB; 4U4N; X-ray; 3.10 A; O2/o2=2-130. DR PDB; 4U4O; X-ray; 3.60 A; O2/o2=2-130. DR PDB; 4U4Q; X-ray; 3.00 A; O2/o2=2-130. DR PDB; 4U4R; X-ray; 2.80 A; O2/o2=2-130. DR PDB; 4U4U; X-ray; 3.00 A; O2/o2=2-130. DR PDB; 4U4Y; X-ray; 3.20 A; O2/o2=2-130. DR PDB; 4U4Z; X-ray; 3.10 A; O2/o2=2-130. DR PDB; 4U50; X-ray; 3.20 A; O2/o2=2-130. DR PDB; 4U51; X-ray; 3.20 A; O2/o2=2-130. DR PDB; 4U52; X-ray; 3.00 A; O2/o2=2-130. DR PDB; 4U53; X-ray; 3.30 A; O2/o2=2-130. DR PDB; 4U55; X-ray; 3.20 A; O2/o2=2-130. DR PDB; 4U56; X-ray; 3.45 A; O2/o2=2-130. DR PDB; 4U6F; X-ray; 3.10 A; O2/o2=2-130. DR PDB; 4V4B; EM; 11.70 A; B0=1-130. DR PDB; 4V6I; EM; 8.80 A; Bh=1-130. DR PDB; 4V7F; EM; 8.70 A; d=1-130. DR PDB; 4V7R; X-ray; 4.00 A; Bb/Db=1-130. DR PDB; 4V88; X-ray; 3.00 A; Be/De=1-130. DR PDB; 4V8T; EM; 8.10 A; e=1-130. DR PDB; 4V8Y; EM; 4.30 A; Be=2-130. DR PDB; 4V8Z; EM; 6.60 A; Be=2-130. DR PDB; 4V91; EM; 3.70 A; e=1-130. DR PDB; 5APN; EM; 3.91 A; e=1-130. DR PDB; 5APO; EM; 3.41 A; e=1-130. DR PDB; 5DAT; X-ray; 3.15 A; O2/o2=2-130. DR PDB; 5DC3; X-ray; 3.25 A; O2/o2=2-130. DR PDB; 5DGE; X-ray; 3.45 A; O2/o2=2-130. DR PDB; 5DGF; X-ray; 3.30 A; O2/o2=2-130. DR PDB; 5DGV; X-ray; 3.10 A; O2/o2=2-130. DR PDB; 5FCI; X-ray; 3.40 A; O2/o2=2-130. DR PDB; 5FCJ; X-ray; 3.10 A; O2/o2=2-130. DR PDB; 5GAK; EM; 3.88 A; g=1-130. DR PDB; 5H4P; EM; 3.07 A; e=1-130. DR PDB; 5I4L; X-ray; 3.10 A; O2/o2=2-128. DR PDB; 5JCS; EM; 9.50 A; e=1-130. DR PDB; 5JUO; EM; 4.00 A; JA=1-130. DR PDB; 5JUP; EM; 3.50 A; JA=1-130. DR PDB; 5JUS; EM; 4.20 A; JA=1-130. DR PDB; 5JUT; EM; 4.00 A; JA=1-130. DR PDB; 5JUU; EM; 4.00 A; JA=1-130. DR PDB; 5LYB; X-ray; 3.25 A; O2/o2=2-128. DR PDB; 5M1J; EM; 3.30 A; e5=2-128. DR PDB; 5MC6; EM; 3.80 A; BG=1-130. DR PDB; 5MEI; X-ray; 3.50 A; AF/DG=2-128. DR PDB; 5NDG; X-ray; 3.70 A; O2/o2=2-128. DR PDB; 5NDV; X-ray; 3.30 A; O2/o2=2-128. DR PDB; 5NDW; X-ray; 3.70 A; O2/o2=2-128. DR PDB; 5OBM; X-ray; 3.40 A; O2/o2=2-128. DR PDB; 5ON6; X-ray; 3.10 A; AF/DG=2-128. DR PDB; 5T62; EM; 3.30 A; r=1-130. DR PDB; 5T6R; EM; 4.50 A; r=1-130. DR PDB; 5TBW; X-ray; 3.00 A; AF/DG=2-128. DR PDB; 5TGA; X-ray; 3.30 A; O2/o2=2-128. DR PDB; 5TGM; X-ray; 3.50 A; O2/o2=2-128. DR PDB; 5Z3G; EM; 3.65 A; i=1-130. DR PDB; 6C0F; EM; 3.70 A; e=1-130. DR PDB; 6CB1; EM; 4.60 A; e=1-130. DR PDB; 6ELZ; EM; 3.30 A; e=1-130. DR PDB; 6EM1; EM; 3.60 A; e=1-130. DR PDB; 6EM3; EM; 3.20 A; e=1-130. DR PDB; 6EM4; EM; 4.10 A; e=1-130. DR PDB; 6EM5; EM; 4.30 A; e=1-130. DR PDB; 6FT6; EM; 3.90 A; e=1-130. DR PDB; 6GQ1; EM; 4.40 A; e=2-128. DR PDB; 6GQB; EM; 3.90 A; e=2-128. DR PDB; 6GQV; EM; 4.00 A; e=2-128. DR PDB; 6HD7; EM; 3.40 A; g=1-130. DR PDB; 6HHQ; X-ray; 3.10 A; AF/DG=1-130. DR PDB; 6I7O; EM; 5.30 A; BG/YG=2-128. DR PDB; 6M62; EM; 3.20 A; e=1-130. DR PDB; 6N8J; EM; 3.50 A; e=1-130. DR PDB; 6N8K; EM; 3.60 A; e=1-130. DR PDB; 6N8L; EM; 3.60 A; e=1-130. DR PDB; 6N8M; EM; 3.50 A; r=1-130. DR PDB; 6N8N; EM; 3.80 A; r=1-130. DR PDB; 6N8O; EM; 3.50 A; r=1-130. DR PDB; 6OIG; EM; 3.80 A; e=2-128. DR PDB; 6Q8Y; EM; 3.10 A; BG=2-128. DR PDB; 6QIK; EM; 3.10 A; e=1-130. DR PDB; 6QT0; EM; 3.40 A; e=1-130. DR PDB; 6QTZ; EM; 3.50 A; e=1-130. DR PDB; 6R84; EM; 3.60 A; g=2-128. DR PDB; 6R86; EM; 3.40 A; g=2-128. DR PDB; 6R87; EM; 3.40 A; g=2-128. DR PDB; 6RI5; EM; 3.30 A; e=1-130. DR PDB; 6RZZ; EM; 3.20 A; e=1-130. DR PDB; 6S05; EM; 3.90 A; e=1-130. DR PDB; 6S47; EM; 3.28 A; Ag=2-130. DR PDB; 6SNT; EM; 2.80 A; al=1-130. DR PDB; 6SV4; EM; 3.30 A; BG/YG/ZG=1-130. DR PDB; 6T4Q; EM; 2.60 A; Le=2-128. DR PDB; 6T7I; EM; 3.20 A; Le=1-130. DR PDB; 6T7T; EM; 3.10 A; Le=1-130. DR PDB; 6T83; EM; 4.00 A; P/ey=1-130. DR PDB; 6TB3; EM; 2.80 A; BG=2-128. DR PDB; 6TNU; EM; 3.10 A; BG=2-128. DR PDB; 6WOO; EM; 2.90 A; e=5-126. DR PDB; 6YLG; EM; 3.00 A; e=1-130. DR PDB; 6YLH; EM; 3.10 A; e=1-130. DR PDB; 6YLX; EM; 3.90 A; e=1-130. DR PDB; 6YLY; EM; 3.80 A; e=1-130. DR PDB; 6Z6J; EM; 3.40 A; Le=1-130. DR PDB; 6Z6K; EM; 3.40 A; Le=1-130. DR PDB; 7AZY; EM; 2.88 A; r=1-130. DR PDB; 7B7D; EM; 3.30 A; La=2-128. DR PDB; 7BT6; EM; 3.12 A; e=1-130. DR PDB; 7BTB; EM; 3.22 A; e=1-130. DR PDB; 7MPI; EM; 3.05 A; Ae=2-128. DR PDB; 7MPJ; EM; 2.70 A; Ae=2-128. DR PDB; 7N8B; EM; 3.05 A; Ae=2-128. DR PDB; 7NAC; EM; 3.04 A; e=1-130. DR PDB; 7NRC; EM; 3.90 A; Lg=2-128. DR PDB; 7NRD; EM; 4.36 A; Lg=2-128. DR PDB; 7OF1; EM; 3.10 A; e=1-130. DR PDB; 7OH3; EM; 3.40 A; e=1-130. DR PDB; 7OHP; EM; 3.90 A; e=1-130. DR PDB; 7OHQ; EM; 3.10 A; e=1-130. DR PDB; 7OHR; EM; 4.72 A; e=1-130. DR PDB; 7OHS; EM; 4.38 A; e=1-130. DR PDB; 7OHT; EM; 4.70 A; e=1-130. DR PDB; 7OHU; EM; 3.70 A; e=1-130. DR PDB; 7OHV; EM; 3.90 A; e=1-130. DR PDB; 7OHW; EM; 3.50 A; e=1-130. DR PDB; 7OHX; EM; 3.30 A; e=1-130. DR PDB; 7OHY; EM; 3.90 A; e=1-130. DR PDB; 7R7A; EM; 3.04 A; e=1-130. DR PDB; 7U0H; EM; 2.76 A; e=1-130. DR PDB; 7UG6; EM; 2.90 A; e=1-130. DR PDB; 7UOO; EM; 2.34 A; e=1-130. DR PDB; 7UQB; EM; 2.43 A; e=1-130. DR PDB; 7UQZ; EM; 2.44 A; e=1-130. DR PDB; 7V08; EM; 2.36 A; e=1-130. DR PDB; 7Z34; EM; 3.80 A; e=1-130. DR PDB; 7ZPQ; EM; 3.47 A; Bd=2-128. DR PDB; 7ZRS; EM; 4.80 A; Bd=2-128. DR PDB; 7ZS5; EM; 3.20 A; Bf=2-128. DR PDB; 7ZUW; EM; 4.30 A; Bd=2-128. DR PDB; 7ZUX; EM; 2.50 A; Ed=2-128. DR PDB; 7ZW0; EM; 2.40 A; Lh=1-130. DR PDB; 8AAF; EM; 2.50 A; R=1-130. DR PDB; 8AGT; EM; 2.60 A; R=1-130. DR PDB; 8AGU; EM; 2.70 A; R=1-130. DR PDB; 8AGV; EM; 2.60 A; R=1-130. DR PDB; 8AGW; EM; 2.60 A; R=1-130. DR PDB; 8AGX; EM; 2.40 A; R=1-130. DR PDB; 8AGZ; EM; 2.60 A; R=1-130. DR PDB; 8BIP; EM; 3.10 A; Le=2-128. DR PDB; 8BJQ; EM; 3.80 A; Le=2-128. DR PDB; 8BQD; EM; 3.90 A; BG=2-128. DR PDB; 8BQX; EM; 3.80 A; BG=2-128. DR PDB; 8CCS; EM; 1.97 A; Q=1-130. DR PDB; 8CDL; EM; 2.72 A; Q=1-130. DR PDB; 8CDR; EM; 2.04 A; Q=1-130. DR PDB; 8CEH; EM; 2.05 A; Q=1-130. DR PDB; 8CF5; EM; 2.71 A; Q=1-130. DR PDB; 8CG8; EM; 2.57 A; Q=1-130. DR PDB; 8CGN; EM; 2.28 A; Q=1-130. DR PDB; 8CIV; EM; 2.47 A; Q=1-130. DR PDB; 8CKU; EM; 3.11 A; Q=1-130. DR PDB; 8CMJ; EM; 3.79 A; Q=1-130. DR PDB; 8E5T; EM; 4.00 A; e=1-130. DR PDB; 8HFR; EM; 2.64 A; eH=1-130. 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; 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; 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; 8HFR; -. DR AlphaFoldDB; P38061; -. DR EMDB; EMD-11951; -. DR EMDB; EMD-12904; -. 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-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-21859; -. DR EMDB; EMD-26485; -. DR EMDB; EMD-34725; -. DR EMDB; EMD-6878; -. DR EMDB; EMD-7324; -. DR SMR; P38061; -. DR BioGRID; 32611; 172. DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit. DR DIP; DIP-5176N; -. DR IntAct; P38061; 15. DR MINT; P38061; -. DR STRING; 4932.YBL092W; -. DR CarbonylDB; P38061; -. DR iPTMnet; P38061; -. DR MaxQB; P38061; -. DR PaxDb; 4932-YBL092W; -. DR PeptideAtlas; P38061; -. DR TopDownProteomics; P38061; -. DR EnsemblFungi; YBL092W_mRNA; YBL092W; YBL092W. DR GeneID; 852185; -. DR KEGG; sce:YBL092W; -. DR AGR; SGD:S000000188; -. DR SGD; S000000188; RPL32. DR VEuPathDB; FungiDB:YBL092W; -. DR eggNOG; KOG0878; Eukaryota. DR GeneTree; ENSGT00940000171258; -. DR HOGENOM; CLU_071479_4_0_1; -. DR InParanoid; P38061; -. DR OMA; HPSGYEE; -. DR OrthoDB; 5473460at2759; -. DR BioCyc; YEAST:G3O-28980-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; 852185; 8 hits in 10 CRISPR screens. DR EvolutionaryTrace; P38061; -. DR PRO; PR:P38061; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38061; Protein. DR GO; GO:0005737; C:cytoplasm; NAS: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; NAS:ComplexPortal. DR CDD; cd00513; Ribosomal_L32_L32e; 1. DR InterPro; IPR001515; Ribosomal_eL32. DR InterPro; IPR018263; Ribosomal_eL32_CS. DR InterPro; IPR036351; Ribosomal_eL32_sf. DR PANTHER; PTHR23413:SF1; 60S RIBOSOMAL PROTEIN L32; 1. DR PANTHER; PTHR23413; 60S RIBOSOMAL PROTEIN L32 AND DNA-DIRECTED RNA POLYMERASE II, SUBUNIT N; 1. DR Pfam; PF01655; Ribosomal_L32e; 1. DR SMART; SM01393; Ribosomal_L32e; 1. DR SUPFAM; SSF52042; Ribosomal protein L32e; 1. DR PROSITE; PS00580; RIBOSOMAL_L32E; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10601260" FT CHAIN 2..130 FT /note="Large ribosomal subunit protein eL32" FT /id="PRO_0000131145" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT TURN 20..24 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:6EM3" FT TURN 41..45 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:6EM3" FT TURN 83..86 FT /evidence="ECO:0007829|PDB:6EM3" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:6EM3" FT HELIX 102..115 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:6EM3" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:6EM3" SQ SEQUENCE 130 AA; 14771 MW; 5C5EDD87D6841976 CRC64; MASLPHPKIV KKHTKKFKRH HSDRYHRVAE NWRKQKGIDS VVRRRFRGNI SQPKIGYGSN KKTKFLSPSG HKTFLVANVK DLETLTMHTK TYAAEIAHNI SAKNRVVILA RAKALGIKVT NPKGRLALEA //