RL32_YEAST
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 03-AUG-2022, entry version 181.
DE RecName: Full=60S ribosomal protein L32 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL32 {ECO:0000303|PubMed:24524803};
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}.
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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; 5FL8; EM; 9.50 A; e=1-130.
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; 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 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; 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; 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; P38061; -.
DR SMR; P38061; -.
DR BioGRID; 32611; 84.
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; P38061; -.
DR PRIDE; P38061; -.
DR TopDownProteomics; P38061; -.
DR EnsemblFungi; YBL092W_mRNA; YBL092W; YBL092W.
DR GeneID; 852185; -.
DR KEGG; sce:YBL092W; -.
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 BioCyc; YEAST:G3O-28980-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; P38061; -.
DR PRO; PR:P38061; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38061; 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 CDD; cd00513; Ribosomal_L32_L32e; 1.
DR InterPro; IPR001515; Ribosomal_L32e.
DR InterPro; IPR018263; Ribosomal_L32e_CS.
DR InterPro; IPR036351; Ribosomal_L32e_sf.
DR PANTHER; PTHR23413; PTHR23413; 1.
DR Pfam; PF01655; Ribosomal_L32e; 1.
DR SMART; SM01393; Ribosomal_L32e; 1.
DR SUPFAM; SSF52042; SSF52042; 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="60S ribosomal protein L32"
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
