RL21A_YEAST
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 03-AUG-2022, entry version 184.
DE RecName: Full=60S ribosomal protein L21-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL21-A {ECO:0000303|PubMed:24524803};
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}.
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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; 5FL8; EM; 9.50 A; T=1-160.
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; 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 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; 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; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHT; -.
DR AlphaFoldDB; Q02753; -.
DR SMR; Q02753; -.
DR BioGRID; 32888; 114.
DR IntAct; Q02753; 11.
DR MINT; Q02753; -.
DR STRING; 4932.YBR191W; -.
DR iPTMnet; Q02753; -.
DR MaxQB; Q02753; -.
DR PaxDb; Q02753; -.
DR PRIDE; Q02753; -.
DR EnsemblFungi; YBR191W_mRNA; YBR191W; YBR191W.
DR GeneID; 852489; -.
DR KEGG; sce:YBR191W; -.
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; IIYNVTP; -.
DR BioCyc; YEAST:G3O-29133-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 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; 2.30.30.70; -; 1.
DR InterPro; IPR036948; Ribosomal_L21_sf.
DR InterPro; IPR001147; Ribosomal_L21e.
DR InterPro; IPR018259; Ribosomal_L21e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR20981; PTHR20981; 1.
DR Pfam; PF01157; Ribosomal_L21e; 1.
DR SUPFAM; SSF50104; SSF50104; 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="60S ribosomal protein L21-A"
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
