RL20A_YEAST
ID RL20A_YEAST Reviewed; 172 AA.
AC P0CX23; A1YV95; A1YV96; D6W068; P0C2I0; P0C2I1; P47913;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=60S ribosomal protein L20-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L18a;
DE AltName: Full=Large ribosomal subunit protein eL20-A {ECO:0000303|PubMed:24524803};
GN Name=RPL20A {ECO:0000303|PubMed:9559554}; Synonyms=RPL18A, RPL18A2;
GN OrderedLocusNames=YMR242C; ORFNames=YM9408.04C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-105.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17351133; DOI=10.1101/gr.6049107;
RA Zhang Z., Hesselberth J.R., Fields S.;
RT "Genome-wide identification of spliced introns using a tiling microarray.";
RL Genome Res. 17:503-509(2007).
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 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 [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION OF INTRON.
RX PubMed=17101987; DOI=10.1073/pnas.0605645103;
RA Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S.,
RA Ito T.;
RT "A large-scale full-length cDNA analysis to explore the budding yeast
RT transcriptome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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 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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-131 AND LYS-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [11]
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 [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). eL20 forms multiple interactions with
CC RNA and proteins in the central protuberance, connecting components of
CC core functional centers that are locatzed far apart (PubMed:9559554,
CC PubMed:22096102). {ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: Present with 54300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL20 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL20 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88652.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z48756; CAA88652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF138821; ABL89189.1; -; mRNA.
DR EMBL; BK006946; DAA10142.1; -; Genomic_DNA.
DR PIR; S56056; S56056.
DR RefSeq; NP_013969.3; NM_001182749.1.
DR RefSeq; NP_014957.2; NM_001183732.1.
DR PDB; 3J6X; EM; 6.10 A; 60=1-172.
DR PDB; 3J6Y; EM; 6.10 A; 60=1-172.
DR PDB; 3J77; EM; 6.20 A; 70=1-172.
DR PDB; 3J78; EM; 6.30 A; 70=1-172.
DR PDB; 3JCT; EM; 3.08 A; S=1-172.
DR PDB; 4U3M; X-ray; 3.00 A; N0/n0=1-172.
DR PDB; 4U3N; X-ray; 3.20 A; N0/n0=1-172.
DR PDB; 4U3U; X-ray; 2.90 A; N0/n0=1-172.
DR PDB; 4U4N; X-ray; 3.10 A; N0/n0=1-172.
DR PDB; 4U4O; X-ray; 3.60 A; N0/n0=1-172.
DR PDB; 4U4Q; X-ray; 3.00 A; N0/n0=1-172.
DR PDB; 4U4R; X-ray; 2.80 A; N0/n0=1-172.
DR PDB; 4U4U; X-ray; 3.00 A; N0/n0=1-172.
DR PDB; 4U4Y; X-ray; 3.20 A; N0/n0=1-172.
DR PDB; 4U4Z; X-ray; 3.10 A; N0/n0=1-172.
DR PDB; 4U50; X-ray; 3.20 A; N0/n0=1-172.
DR PDB; 4U51; X-ray; 3.20 A; N0/n0=1-172.
DR PDB; 4U52; X-ray; 3.00 A; N0/n0=1-172.
DR PDB; 4U53; X-ray; 3.30 A; N0/n0=1-172.
DR PDB; 4U55; X-ray; 3.20 A; N0/n0=1-172.
DR PDB; 4U56; X-ray; 3.45 A; N0/n0=1-172.
DR PDB; 4U6F; X-ray; 3.10 A; N0/n0=1-172.
DR PDB; 4V7F; EM; 8.70 A; S=1-172.
DR PDB; 4V88; X-ray; 3.00 A; BS/DS=1-172.
DR PDB; 4V8T; EM; 8.10 A; S=1-172.
DR PDB; 4V91; EM; 3.70 A; S=1-172.
DR PDB; 5APN; EM; 3.91 A; S=1-172.
DR PDB; 5APO; EM; 3.41 A; S=1-172.
DR PDB; 5DAT; X-ray; 3.15 A; N0/n0=1-172.
DR PDB; 5DC3; X-ray; 3.25 A; N0/n0=1-172.
DR PDB; 5DGE; X-ray; 3.45 A; N0/n0=1-172.
DR PDB; 5DGF; X-ray; 3.30 A; N0/n0=1-172.
DR PDB; 5DGV; X-ray; 3.10 A; N0/n0=1-172.
DR PDB; 5FCI; X-ray; 3.40 A; N0/n0=1-172.
DR PDB; 5FCJ; X-ray; 3.10 A; N0/n0=1-172.
DR PDB; 5FL8; EM; 9.50 A; S=1-172.
DR PDB; 5GAK; EM; 3.88 A; U=1-172.
DR PDB; 5H4P; EM; 3.07 A; S=1-172.
DR PDB; 5I4L; X-ray; 3.10 A; N0/n0=1-172.
DR PDB; 5JCS; EM; 9.50 A; S=1-172.
DR PDB; 5JUO; EM; 4.00 A; X=1-172.
DR PDB; 5JUP; EM; 3.50 A; X=1-172.
DR PDB; 5JUS; EM; 4.20 A; X=1-172.
DR PDB; 5JUT; EM; 4.00 A; X=1-172.
DR PDB; 5JUU; EM; 4.00 A; X=1-172.
DR PDB; 5LYB; X-ray; 3.25 A; N0/n0=1-172.
DR PDB; 5M1J; EM; 3.30 A; S5=1-172.
DR PDB; 5MC6; EM; 3.80 A; BH=1-172.
DR PDB; 5MEI; X-ray; 3.50 A; 0/CU=1-172.
DR PDB; 5NDG; X-ray; 3.70 A; N0/n0=1-172.
DR PDB; 5NDV; X-ray; 3.30 A; N0/n0=1-172.
DR PDB; 5NDW; X-ray; 3.70 A; N0/n0=1-172.
DR PDB; 5OBM; X-ray; 3.40 A; N0/n0=1-172.
DR PDB; 5ON6; X-ray; 3.10 A; 0/CU=1-172.
DR PDB; 5T62; EM; 3.30 A; f=1-172.
DR PDB; 5T6R; EM; 4.50 A; f=1-172.
DR PDB; 5TBW; X-ray; 3.00 A; 0/CU=1-172.
DR PDB; 5TGA; X-ray; 3.30 A; N0/n0=1-172.
DR PDB; 5TGM; X-ray; 3.50 A; N0/n0=1-172.
DR PDB; 5Z3G; EM; 3.65 A; W=1-172.
DR PDB; 6C0F; EM; 3.70 A; S=1-172.
DR PDB; 6CB1; EM; 4.60 A; S=1-172.
DR PDB; 6ELZ; EM; 3.30 A; S=1-172.
DR PDB; 6EM1; EM; 3.60 A; S=1-172.
DR PDB; 6EM3; EM; 3.20 A; S=1-172.
DR PDB; 6EM4; EM; 4.10 A; S=1-172.
DR PDB; 6EM5; EM; 4.30 A; S=1-172.
DR PDB; 6FT6; EM; 3.90 A; S=1-172.
DR PDB; 6GQ1; EM; 4.40 A; S=1-172.
DR PDB; 6GQB; EM; 3.90 A; S=1-172.
DR PDB; 6GQV; EM; 4.00 A; S=1-172.
DR PDB; 6HD7; EM; 3.40 A; U=1-172.
DR PDB; 6HHQ; X-ray; 3.10 A; 0/CU=1-172.
DR PDB; 6I7O; EM; 5.30 A; BH/YH=1-172.
DR PDB; 6M62; EM; 3.20 A; S=1-172.
DR PDB; 6N8J; EM; 3.50 A; S=1-172.
DR PDB; 6N8K; EM; 3.60 A; S=1-172.
DR PDB; 6N8L; EM; 3.60 A; S=1-172.
DR PDB; 6N8M; EM; 3.50 A; f=1-172.
DR PDB; 6N8N; EM; 3.80 A; f=1-172.
DR PDB; 6N8O; EM; 3.50 A; f=1-172.
DR PDB; 6OIG; EM; 3.80 A; S=1-172.
DR PDB; 6Q8Y; EM; 3.10 A; BH=1-172.
DR PDB; 6QIK; EM; 3.10 A; S=1-172.
DR PDB; 6QT0; EM; 3.40 A; S=1-172.
DR PDB; 6QTZ; EM; 3.50 A; S=1-172.
DR PDB; 6R84; EM; 3.60 A; U=1-172.
DR PDB; 6R86; EM; 3.40 A; U=1-172.
DR PDB; 6R87; EM; 3.40 A; U=1-172.
DR PDB; 6RI5; EM; 3.30 A; S=1-172.
DR PDB; 6RZZ; EM; 3.20 A; S=1-172.
DR PDB; 6S05; EM; 3.90 A; S=1-172.
DR PDB; 6S47; EM; 3.28 A; AU=1-172.
DR PDB; 6SNT; EM; 2.80 A; y=1-172.
DR PDB; 6SV4; EM; 3.30 A; BH/YH/ZH=1-172.
DR PDB; 6T4Q; EM; 2.60 A; LS=2-172.
DR PDB; 6T7I; EM; 3.20 A; LS=1-172.
DR PDB; 6T7T; EM; 3.10 A; LS=1-172.
DR PDB; 6T83; EM; 4.00 A; D/Sy=1-172.
DR PDB; 6TB3; EM; 2.80 A; BH=2-172.
DR PDB; 6TNU; EM; 3.10 A; BH=2-172.
DR PDB; 6WOO; EM; 2.90 A; S=4-172.
DR PDB; 6XIQ; EM; 4.20 A; S=1-172.
DR PDB; 6XIR; EM; 3.20 A; S=1-172.
DR PDB; 6YLG; EM; 3.00 A; S=1-172.
DR PDB; 6YLH; EM; 3.10 A; S=1-172.
DR PDB; 6YLX; EM; 3.90 A; S=1-172.
DR PDB; 6YLY; EM; 3.80 A; S=1-172.
DR PDB; 6Z6J; EM; 3.40 A; LS=1-172.
DR PDB; 6Z6K; EM; 3.40 A; LS=1-172.
DR PDB; 7AZY; EM; 2.88 A; s=1-172.
DR PDB; 7B7D; EM; 3.30 A; Lo=2-172.
DR PDB; 7BT6; EM; 3.12 A; S=1-172.
DR PDB; 7BTB; EM; 3.22 A; S=1-172.
DR PDB; 7NRC; EM; 3.90 A; LU=2-172.
DR PDB; 7NRD; EM; 4.36 A; LU=2-172.
DR PDB; 7OF1; EM; 3.10 A; S=1-172.
DR PDB; 7OH3; EM; 3.40 A; S=1-172.
DR PDB; 7OHP; EM; 3.90 A; S=1-172.
DR PDB; 7OHQ; EM; 3.10 A; S=1-172.
DR PDB; 7OHR; EM; 4.72 A; S=1-172.
DR PDB; 7OHS; EM; 4.38 A; S=1-172.
DR PDB; 7OHT; EM; 4.70 A; S=1-172.
DR PDB; 7OHU; EM; 3.70 A; S=1-172.
DR PDB; 7OHV; EM; 3.90 A; S=1-172.
DR PDB; 7OHW; EM; 3.50 A; S=1-172.
DR PDB; 7OHX; EM; 3.30 A; S=1-172.
DR PDB; 7OHY; EM; 3.90 A; S=1-172.
DR PDB; 7RR5; EM; 3.23 A; LS=1-172.
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; 4V7F; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
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; 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; 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; 7RR5; -.
DR AlphaFoldDB; P0CX23; -.
DR SMR; P0CX23; -.
DR BioGRID; 34700; 205.
DR BioGRID; 35421; 192.
DR IntAct; P0CX23; 5.
DR MINT; P0CX23; -.
DR STRING; 4932.YMR242C; -.
DR CarbonylDB; P0CX23; -.
DR iPTMnet; P0CX23; -.
DR MaxQB; P0CX23; -.
DR PaxDb; P0CX23; -.
DR PRIDE; P0CX23; -.
DR TopDownProteomics; P0CX23; -.
DR GeneID; 854489; -.
DR GeneID; 855283; -.
DR KEGG; sce:YMR242C; -.
DR KEGG; sce:YOR312C; -.
DR SGD; S000004855; RPL20A.
DR VEuPathDB; FungiDB:YMR242C; -.
DR VEuPathDB; FungiDB:YOR312C; -.
DR eggNOG; KOG0829; Eukaryota.
DR HOGENOM; CLU_080773_1_1_1; -.
DR InParanoid; P0CX23; -.
DR OMA; RFWYFMK; -.
DR BioCyc; YEAST:G3O-32922-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 PRO; PR:P0CX23; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P0CX23; 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; IC:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR HAMAP; MF_00273; Ribosomal_L18Ae; 1.
DR InterPro; IPR028877; 50S_L18Ae/Ribosomal_L18a/L20.
DR InterPro; IPR023573; Ribosomal_L18a//L18Ae/LX.
DR InterPro; IPR021138; Ribosomal_L18a/L20_eukaryotes.
DR PANTHER; PTHR10052; PTHR10052; 1.
DR Pfam; PF01775; Ribosomal_L18A; 1.
DR PIRSF; PIRSF002190; Ribosomal_L18a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..172
FT /note="60S ribosomal protein L20-A"
FT /id="PRO_0000278969"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 172 AA; 20437 MW; 28D470F11A48A43A CRC64;
MAHFKEYQVI GRRLPTESVP EPKLFRMRIF ASNEVIAKSR YWYFLQKLHK VKKASGEIVS
INQINEAHPT KVKNFGVWVR YDSRSGTHNM YKEIRDVSRV AAVETLYQDM AARHRARFRS
IHILKVAEIE KTADVKRQYV KQFLTKDLKF PLPHRVQKST KTFSYKRPST FY
