ID RL21A_YEAST Reviewed; 160 AA. AC Q02753; D6VQI5; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Large ribosomal subunit protein eL21A {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L21-A {ECO:0000303|PubMed:9559554}; GN Name=RPL21A {ECO:0000303|PubMed:9559554}; Synonyms=URP1; GN OrderedLocusNames=YBR191W; ORFNames=YBR1401; 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=8428379; DOI=10.1007/bf00336743; RA Jank B., Waldherr M., Schweyen R.J.; RT "Yeast single copy gene URP1 is a homolog of rat ribosomal protein gene RT L21."; RL Curr. Genet. 23:15-18(1993). 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] OF 1-39. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7871891; DOI=10.1002/yea.320101116; RA Demolis N., Jacquet M., Mallet L.; RT "A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes RT encoding ribosomal proteins and six putative new genes, one of which RT encodes a putative transcriptional factor."; RL Yeast 10:1511-1525(1994). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-160. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8346681; DOI=10.1002/yea.320090611; RA Demolis N., Mallet L., Bussereau F., Jacquet M.; RT "RIM2, MSI1 and PGI1 are located within an 8 kb segment of Saccharomyces RT cerevisiae chromosome II, which also contains the putative ribosomal gene RT L21 and a new putative essential gene with a leucine zipper motif."; RL Yeast 9:645-659(1993). 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). 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 4-100, 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 OF 2-100, 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:14562095, CC ECO:0000269|PubMed:22096102}. CC -!- MISCELLANEOUS: There are 2 genes for eL21 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 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; M86408; AAA35202.1; -; Genomic_DNA. DR EMBL; Z36059; CAA85153.1; -; Genomic_DNA. DR EMBL; Z21487; CAA79677.1; -; Genomic_DNA. DR EMBL; U02073; AAB60284.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07305.1; -; Genomic_DNA. DR PIR; S28921; S28921. DR RefSeq; NP_009750.1; NM_001178539.1. DR PDB; 3J6X; EM; 6.10 A; 61=1-160. DR PDB; 3J6Y; EM; 6.10 A; 61=1-160. DR PDB; 3J77; EM; 6.20 A; 71=1-160. DR PDB; 3J78; EM; 6.30 A; 71=1-160. DR PDB; 3JCT; EM; 3.08 A; T=1-160. DR PDB; 4U3M; X-ray; 3.00 A; N1/n1=2-160. DR PDB; 4U3N; X-ray; 3.20 A; N1/n1=2-160. DR PDB; 4U3U; X-ray; 2.90 A; N1/n1=2-160. DR PDB; 4U4N; X-ray; 3.10 A; N1/n1=2-160. DR PDB; 4U4O; X-ray; 3.60 A; N1/n1=2-160. DR PDB; 4U4Q; X-ray; 3.00 A; N1/n1=2-160. DR PDB; 4U4R; X-ray; 2.80 A; N1/n1=2-160. DR PDB; 4U4U; X-ray; 3.00 A; N1/n1=2-160. DR PDB; 4U4Y; X-ray; 3.20 A; N1/n1=2-160. DR PDB; 4U4Z; X-ray; 3.10 A; N1/n1=2-160. DR PDB; 4U50; X-ray; 3.20 A; N1/n1=2-160. DR PDB; 4U51; X-ray; 3.20 A; N1/n1=2-160. DR PDB; 4U52; X-ray; 3.00 A; N1/n1=2-160. DR PDB; 4U53; X-ray; 3.30 A; N1/n1=2-160. DR PDB; 4U55; X-ray; 3.20 A; N1/n1=2-160. DR PDB; 4U56; X-ray; 3.45 A; N1/n1=2-160. DR PDB; 4U6F; X-ray; 3.10 A; N1/n1=2-160. DR PDB; 4V4B; EM; 11.70 A; BQ=1-100. DR PDB; 4V6I; EM; 8.80 A; BU=1-160. DR PDB; 4V7F; EM; 8.70 A; T=1-160. DR PDB; 4V7R; X-ray; 4.00 A; BT/DT=1-160. DR PDB; 4V88; X-ray; 3.00 A; BT/DT=1-160. DR PDB; 4V8T; EM; 8.10 A; T=1-160. DR PDB; 4V8Y; EM; 4.30 A; BT=2-160. DR PDB; 4V8Z; EM; 6.60 A; BT=2-160. DR PDB; 4V91; EM; 3.70 A; T=1-160. DR PDB; 5APN; EM; 3.91 A; T=1-160. DR PDB; 5APO; EM; 3.41 A; T=1-160. DR PDB; 5DAT; X-ray; 3.15 A; N1/n1=2-160. DR PDB; 5DC3; X-ray; 3.25 A; N1/n1=2-160. DR PDB; 5DGE; X-ray; 3.45 A; N1/n1=2-160. DR PDB; 5DGF; X-ray; 3.30 A; N1/n1=2-160. DR PDB; 5DGV; X-ray; 3.10 A; N1/n1=2-160. DR PDB; 5FCI; X-ray; 3.40 A; N1/n1=2-160. DR PDB; 5FCJ; X-ray; 3.10 A; N1/n1=2-160. DR PDB; 5GAK; EM; 3.88 A; V=1-160. DR PDB; 5H4P; EM; 3.07 A; T=1-160. DR PDB; 5I4L; X-ray; 3.10 A; N1/n1=2-160. DR PDB; 5JCS; EM; 9.50 A; T=1-160. DR PDB; 5JUO; EM; 4.00 A; Y=1-160. DR PDB; 5JUP; EM; 3.50 A; Y=1-160. DR PDB; 5JUS; EM; 4.20 A; Y=1-160. DR PDB; 5JUT; EM; 4.00 A; Y=1-160. DR PDB; 5JUU; EM; 4.00 A; Y=1-160. DR PDB; 5LYB; X-ray; 3.25 A; N1/n1=2-160. DR PDB; 5M1J; EM; 3.30 A; T5=2-160. DR PDB; 5MC6; EM; 3.80 A; BJ=1-160. DR PDB; 5MEI; X-ray; 3.50 A; 2/CV=2-160. DR PDB; 5NDG; X-ray; 3.70 A; N1/n1=2-160. DR PDB; 5NDV; X-ray; 3.30 A; N1/n1=2-160. DR PDB; 5NDW; X-ray; 3.70 A; N1/n1=2-160. DR PDB; 5OBM; X-ray; 3.40 A; N1/n1=2-160. DR PDB; 5ON6; X-ray; 3.10 A; 2/CV=2-160. DR PDB; 5T62; EM; 3.30 A; g=1-160. DR PDB; 5T6R; EM; 4.50 A; g=1-160. DR PDB; 5TBW; X-ray; 3.00 A; 2/CV=2-160. DR PDB; 5TGA; X-ray; 3.30 A; N1/n1=2-160. DR PDB; 5TGM; X-ray; 3.50 A; N1/n1=2-160. DR PDB; 6ELZ; EM; 3.30 A; T=1-160. DR PDB; 6EM5; EM; 4.30 A; T=1-160. DR PDB; 6FT6; EM; 3.90 A; T=1-160. DR PDB; 6GQ1; EM; 4.40 A; T=2-160. DR PDB; 6GQB; EM; 3.90 A; T=2-160. DR PDB; 6GQV; EM; 4.00 A; T=2-160. DR PDB; 6HD7; EM; 3.40 A; V=1-160. DR PDB; 6HHQ; X-ray; 3.10 A; 2/CV=1-160. DR PDB; 6I7O; EM; 5.30 A; BJ/YJ=2-160. DR PDB; 6M62; EM; 3.20 A; T=1-160. DR PDB; 6N8J; EM; 3.50 A; T=1-160. DR PDB; 6N8K; EM; 3.60 A; T=1-160. DR PDB; 6N8L; EM; 3.60 A; T=1-160. DR PDB; 6N8M; EM; 3.50 A; g=1-160. DR PDB; 6N8N; EM; 3.80 A; g=1-160. DR PDB; 6N8O; EM; 3.50 A; g=1-160. DR PDB; 6OIG; EM; 3.80 A; T=2-160. DR PDB; 6Q8Y; EM; 3.10 A; BJ=2-160. DR PDB; 6QIK; EM; 3.10 A; T=1-160. DR PDB; 6QT0; EM; 3.40 A; T=1-160. DR PDB; 6QTZ; EM; 3.50 A; T=1-160. DR PDB; 6R84; EM; 3.60 A; V=2-160. DR PDB; 6R86; EM; 3.40 A; V=2-160. DR PDB; 6R87; EM; 3.40 A; V=2-160. DR PDB; 6RI5; EM; 3.30 A; T=1-160. DR PDB; 6RZZ; EM; 3.20 A; T=1-160. DR PDB; 6S05; EM; 3.90 A; T=1-160. DR PDB; 6S47; EM; 3.28 A; AV=2-160. DR PDB; 6SNT; EM; 2.80 A; z=1-160. DR PDB; 6SV4; EM; 3.30 A; BJ/YJ/ZJ=1-160. DR PDB; 6T4Q; EM; 2.60 A; LT=2-160. DR PDB; 6T7I; EM; 3.20 A; LT=1-160. DR PDB; 6T7T; EM; 3.10 A; LT=1-160. DR PDB; 6T83; EM; 4.00 A; E/Ty=1-160. DR PDB; 6TB3; EM; 2.80 A; BJ=2-160. DR PDB; 6TNU; EM; 3.10 A; BJ=2-160. DR PDB; 6WOO; EM; 2.90 A; T=2-159. DR PDB; 6XIQ; EM; 4.20 A; T=1-160. DR PDB; 6XIR; EM; 3.20 A; T=1-160. DR PDB; 6YLG; EM; 3.00 A; T=1-160. DR PDB; 6YLH; EM; 3.10 A; T=1-160. DR PDB; 6YLX; EM; 3.90 A; T=1-160. DR PDB; 6YLY; EM; 3.80 A; T=1-160. DR PDB; 6Z6J; EM; 3.40 A; LT=1-160. DR PDB; 6Z6K; EM; 3.40 A; LT=1-160. DR PDB; 7AZY; EM; 2.88 A; u=1-160. DR PDB; 7B7D; EM; 3.30 A; Lp=2-160. DR PDB; 7BT6; EM; 3.12 A; T=1-160. DR PDB; 7BTB; EM; 3.22 A; T=1-160. DR PDB; 7MPI; EM; 3.05 A; AT=2-160. DR PDB; 7MPJ; EM; 2.70 A; AT=2-160. DR PDB; 7N8B; EM; 3.05 A; AT=2-160. DR PDB; 7NAC; EM; 3.04 A; T=1-160. DR PDB; 7NRC; EM; 3.90 A; LV=2-160. DR PDB; 7NRD; EM; 4.36 A; LV=2-160. DR PDB; 7OF1; EM; 3.10 A; T=1-160. DR PDB; 7OH3; EM; 3.40 A; T=1-160. DR PDB; 7OHQ; EM; 3.10 A; T=1-160. DR PDB; 7OHT; EM; 4.70 A; T=1-160. DR PDB; 7R7A; EM; 3.04 A; T=1-160. DR PDB; 7TOO; EM; 2.70 A; AL21=1-160. DR PDB; 7TOP; EM; 2.40 A; AL21=1-160. DR PDB; 7U0H; EM; 2.76 A; T=1-160. DR PDB; 7UG6; EM; 2.90 A; T=1-160. DR PDB; 7UOO; EM; 2.34 A; T=1-160. DR PDB; 7UQB; EM; 2.43 A; T=1-160. DR PDB; 7UQZ; EM; 2.44 A; T=1-160. DR PDB; 7V08; EM; 2.36 A; T=1-160. DR PDB; 7Z34; EM; 3.80 A; T=1-160. DR PDB; 7ZPQ; EM; 3.47 A; BS=2-160. DR PDB; 7ZRS; EM; 4.80 A; BS=2-160. DR PDB; 7ZS5; EM; 3.20 A; BU=2-160. DR PDB; 7ZUW; EM; 4.30 A; BS=2-160. DR PDB; 7ZUX; EM; 2.50 A; ES=2-160. DR PDB; 7ZW0; EM; 2.40 A; LW=1-160. DR PDB; 8AAF; EM; 2.50 A; G=1-160. DR PDB; 8AGT; EM; 2.60 A; G=1-160. DR PDB; 8AGU; EM; 2.70 A; G=1-160. DR PDB; 8AGV; EM; 2.60 A; G=1-160. DR PDB; 8AGW; EM; 2.60 A; G=1-160. DR PDB; 8AGX; EM; 2.40 A; G=1-160. DR PDB; 8AGZ; EM; 2.60 A; G=1-160. DR PDB; 8BIP; EM; 3.10 A; LT=2-160. DR PDB; 8BJQ; EM; 3.80 A; LT=2-160. DR PDB; 8BQD; EM; 3.90 A; BJ=2-160. DR PDB; 8BQX; EM; 3.80 A; BJ=2-160. DR PDB; 8CCS; EM; 1.97 A; F=1-160. DR PDB; 8CDL; EM; 2.72 A; F=1-160. DR PDB; 8CDR; EM; 2.04 A; F=1-160. DR PDB; 8CEH; EM; 2.05 A; F=1-160. DR PDB; 8CF5; EM; 2.71 A; F=1-160. DR PDB; 8CG8; EM; 2.57 A; F=1-160. DR PDB; 8CGN; EM; 2.28 A; F=1-160. DR PDB; 8CIV; EM; 2.47 A; F=1-160. DR PDB; 8CKU; EM; 3.11 A; F=1-160. DR PDB; 8CMJ; EM; 3.79 A; F=1-160. DR PDB; 8EUB; EM; 2.52 A; AT=1-160. DR PDB; 8EVP; EM; 2.38 A; AT=1-160. DR PDB; 8EVQ; EM; 2.72 A; AT=1-160. DR PDB; 8EVR; EM; 2.87 A; AT=1-160. DR PDB; 8EVS; EM; 2.62 A; AT=1-160. DR PDB; 8EVT; EM; 2.20 A; AT=1-160. DR PDB; 8EWB; EM; 2.87 A; AT=1-160. DR PDB; 8EWC; EM; 2.45 A; AT=1-160. DR PDB; 8HFR; EM; 2.64 A; Tl=1-160. 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; 6ELZ; -. 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; 7OHQ; -. DR PDBsum; 7OHT; -. DR PDBsum; 7R7A; -. 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; 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; Q02753; -. DR EMDB; EMD-10068; -. DR EMDB; EMD-10071; -. 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-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-34725; -. DR EMDB; EMD-4560; -. DR EMDB; EMD-4630; -. DR EMDB; EMD-4636; -. DR EMDB; EMD-4884; -. DR SMR; Q02753; -. DR BioGRID; 32888; 231. DR IntAct; Q02753; 11. DR MINT; Q02753; -. DR STRING; 4932.YBR191W; -. DR iPTMnet; Q02753; -. DR MaxQB; Q02753; -. DR PaxDb; 4932-YBR191W; -. DR PeptideAtlas; Q02753; -. DR EnsemblFungi; YBR191W_mRNA; YBR191W; YBR191W. DR GeneID; 852489; -. DR KEGG; sce:YBR191W; -. DR AGR; SGD:S000000395; -. DR SGD; S000000395; RPL21A. DR VEuPathDB; FungiDB:YBR191W; -. DR eggNOG; KOG1732; Eukaryota. DR GeneTree; ENSGT00950000182922; -. DR HOGENOM; CLU_103610_0_1_1; -. DR InParanoid; Q02753; -. DR OMA; INYGDYV; -. DR OrthoDB; 148212at2759; -. DR BioCyc; YEAST:G3O-29133-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; 852489; 9 hits in 10 CRISPR screens. DR ChiTaRS; RPL21A; yeast. DR EvolutionaryTrace; Q02753; -. DR PRO; PR:Q02753; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; Q02753; Protein. 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; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD. DR Gene3D; 6.10.250.3260; -; 1. DR Gene3D; 2.30.30.70; Ribosomal protein L21; 1. DR InterPro; IPR001147; Ribosomal_eL21. DR InterPro; IPR018259; Ribosomal_eL21_CS. DR InterPro; IPR036948; Ribosomal_eL21_sf. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR PANTHER; PTHR20981; 60S RIBOSOMAL PROTEIN L21; 1. DR PANTHER; PTHR20981:SF6; 60S RIBOSOMAL PROTEIN L21; 1. DR Pfam; PF01157; Ribosomal_L21e; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS01171; RIBOSOMAL_L21E; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10601260" FT CHAIN 2..160 FT /note="Large ribosomal subunit protein eL21A" FT /id="PRO_0000149682" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q12672" FT TURN 7..10 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 69..80 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 83..92 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:4U3M" FT HELIX 103..120 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:4U4R" SQ SEQUENCE 160 AA; 18242 MW; 45286521C8473A72 CRC64; MGKSHGYRSR TRYMFQRDFR KHGAVHLSTY LKVYKVGDIV DIKANGSIQK GMPHKFYQGK TGVVYNVTKS SVGVIINKMV GNRYLEKRLN LRVEHIKHSK CRQEFLERVK ANAAKRAEAK AQGVAVQLKR QPAQPRESRI VSTEGNVPQT LAPVPYETFI //