RL22A_YEAST
ID RL22A_YEAST Reviewed; 121 AA.
AC P05749; D6VY63;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=60S ribosomal protein L22-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L1c;
DE AltName: Full=Large ribosomal subunit protein eL22-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP4;
DE AltName: Full=YL31;
GN Name=RPL22A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YLR061W;
GN ORFNames=L2168;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 PROTEIN SEQUENCE OF 2-52.
RX PubMed=6814480; DOI=10.1021/bi00262a005;
RA Otaka E., Higo K., Osawa S.;
RT "Isolation of seventeen proteins and amino-terminal amino acid sequences of
RT eight proteins from cytoplasmic ribosomes of yeast.";
RL Biochemistry 21:4545-4550(1982).
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 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 [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 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 [11]
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: Present with 60400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL22 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL22 family.
CC {ECO:0000305}.
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DR EMBL; X94607; CAA64308.1; -; Genomic_DNA.
DR EMBL; Z73233; CAA97592.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09379.1; -; Genomic_DNA.
DR PIR; S61635; S61635.
DR RefSeq; NP_013162.1; NM_001181948.1.
DR PDB; 3J6X; EM; 6.10 A; 62=1-121.
DR PDB; 3J6Y; EM; 6.10 A; 62=1-121.
DR PDB; 3J77; EM; 6.20 A; 72=1-121.
DR PDB; 3J78; EM; 6.30 A; 72=1-121.
DR PDB; 3JCT; EM; 3.08 A; U=1-121.
DR PDB; 4U3M; X-ray; 3.00 A; N2/n2=2-121.
DR PDB; 4U3N; X-ray; 3.20 A; N2/n2=2-121.
DR PDB; 4U3U; X-ray; 2.90 A; N2/n2=2-121.
DR PDB; 4U4N; X-ray; 3.10 A; N2/n2=2-121.
DR PDB; 4U4O; X-ray; 3.60 A; N2/n2=2-121.
DR PDB; 4U4Q; X-ray; 3.00 A; N2/n2=2-121.
DR PDB; 4U4R; X-ray; 2.80 A; N2/n2=2-121.
DR PDB; 4U4U; X-ray; 3.00 A; N2/n2=2-121.
DR PDB; 4U4Y; X-ray; 3.20 A; N2/n2=2-121.
DR PDB; 4U4Z; X-ray; 3.10 A; N2/n2=2-121.
DR PDB; 4U50; X-ray; 3.20 A; N2/n2=2-121.
DR PDB; 4U51; X-ray; 3.20 A; N2/n2=2-121.
DR PDB; 4U52; X-ray; 3.00 A; N2/n2=2-121.
DR PDB; 4U53; X-ray; 3.30 A; N2/n2=2-121.
DR PDB; 4U55; X-ray; 3.20 A; N2/n2=2-121.
DR PDB; 4U56; X-ray; 3.45 A; N2/n2=2-121.
DR PDB; 4U6F; X-ray; 3.10 A; N2/n2=2-121.
DR PDB; 4V6I; EM; 8.80 A; BW=1-121.
DR PDB; 4V7F; EM; 8.70 A; V=1-121.
DR PDB; 4V88; X-ray; 3.00 A; BU/DU=1-121.
DR PDB; 4V8T; EM; 8.10 A; U=1-121.
DR PDB; 4V8Y; EM; 4.30 A; BU=2-121.
DR PDB; 4V8Z; EM; 6.60 A; BU=2-121.
DR PDB; 4V91; EM; 3.70 A; U=1-121.
DR PDB; 5APN; EM; 3.91 A; U=1-121.
DR PDB; 5APO; EM; 3.41 A; U=1-121.
DR PDB; 5DAT; X-ray; 3.15 A; N2/n2=2-121.
DR PDB; 5DC3; X-ray; 3.25 A; N2/n2=2-121.
DR PDB; 5DGE; X-ray; 3.45 A; N2/n2=2-121.
DR PDB; 5DGF; X-ray; 3.30 A; N2/n2=2-121.
DR PDB; 5DGV; X-ray; 3.10 A; N2/n2=2-121.
DR PDB; 5FCI; X-ray; 3.40 A; N2/n2=2-121.
DR PDB; 5FCJ; X-ray; 3.10 A; N2/n2=2-121.
DR PDB; 5FL8; EM; 9.50 A; U=1-121.
DR PDB; 5GAK; EM; 3.88 A; W=1-121.
DR PDB; 5H4P; EM; 3.07 A; U=1-121.
DR PDB; 5I4L; X-ray; 3.10 A; N2/n2=9-108.
DR PDB; 5JCS; EM; 9.50 A; U=1-121.
DR PDB; 5JUO; EM; 4.00 A; Z=1-121.
DR PDB; 5JUP; EM; 3.50 A; Z=1-121.
DR PDB; 5JUS; EM; 4.20 A; Z=1-121.
DR PDB; 5JUT; EM; 4.00 A; Z=1-121.
DR PDB; 5JUU; EM; 4.00 A; Z=1-121.
DR PDB; 5LYB; X-ray; 3.25 A; N2/n2=9-108.
DR PDB; 5M1J; EM; 3.30 A; U5=9-108.
DR PDB; 5MC6; EM; 3.80 A; BL=1-121.
DR PDB; 5MEI; X-ray; 3.50 A; 5/CW=9-108.
DR PDB; 5NDG; X-ray; 3.70 A; N2/n2=11-108.
DR PDB; 5NDV; X-ray; 3.30 A; N2/n2=10-108.
DR PDB; 5NDW; X-ray; 3.70 A; N2/n2=9-108.
DR PDB; 5OBM; X-ray; 3.40 A; N2/n2=9-108.
DR PDB; 5ON6; X-ray; 3.10 A; 5/CW=9-108.
DR PDB; 5T62; EM; 3.30 A; h=1-121.
DR PDB; 5T6R; EM; 4.50 A; h=1-121.
DR PDB; 5TBW; X-ray; 3.00 A; 5/CW=9-108.
DR PDB; 5TGA; X-ray; 3.30 A; N2/n2=9-108.
DR PDB; 5TGM; X-ray; 3.50 A; N2/n2=9-108.
DR PDB; 6ELZ; EM; 3.30 A; U=1-121.
DR PDB; 6EM5; EM; 4.30 A; U=1-121.
DR PDB; 6FT6; EM; 3.90 A; U=1-121.
DR PDB; 6GQ1; EM; 4.40 A; U=9-108.
DR PDB; 6GQB; EM; 3.90 A; U=9-108.
DR PDB; 6GQV; EM; 4.00 A; U=9-108.
DR PDB; 6HD7; EM; 3.40 A; W=1-121.
DR PDB; 6HHQ; X-ray; 3.10 A; 5/CW=1-121.
DR PDB; 6I7O; EM; 5.30 A; BL/YL=11-108.
DR PDB; 6M62; EM; 3.20 A; U=1-121.
DR PDB; 6N8J; EM; 3.50 A; U=1-121.
DR PDB; 6N8K; EM; 3.60 A; U=1-121.
DR PDB; 6N8L; EM; 3.60 A; U=1-121.
DR PDB; 6N8M; EM; 3.50 A; h=1-121.
DR PDB; 6N8N; EM; 3.80 A; h=1-121.
DR PDB; 6N8O; EM; 3.50 A; h=1-121.
DR PDB; 6OIG; EM; 3.80 A; U=9-108.
DR PDB; 6Q8Y; EM; 3.10 A; BL=9-108.
DR PDB; 6QIK; EM; 3.10 A; V=1-121.
DR PDB; 6QT0; EM; 3.40 A; V=1-121.
DR PDB; 6QTZ; EM; 3.50 A; V=1-121.
DR PDB; 6R84; EM; 3.60 A; W=9-108.
DR PDB; 6R86; EM; 3.40 A; W=9-108.
DR PDB; 6R87; EM; 3.40 A; W=9-108.
DR PDB; 6RI5; EM; 3.30 A; V=1-121.
DR PDB; 6RZZ; EM; 3.20 A; V=1-121.
DR PDB; 6S05; EM; 3.90 A; V=1-121.
DR PDB; 6S47; EM; 3.28 A; AW=2-121.
DR PDB; 6SNT; EM; 2.80 A; au=1-121.
DR PDB; 6SV4; EM; 3.30 A; BL/YL/ZL=1-121.
DR PDB; 6T4Q; EM; 2.60 A; LU=9-108.
DR PDB; 6T7I; EM; 3.20 A; LU=1-121.
DR PDB; 6T7T; EM; 3.10 A; LU=1-121.
DR PDB; 6T83; EM; 4.00 A; F/Uy=1-121.
DR PDB; 6TB3; EM; 2.80 A; BL=9-108.
DR PDB; 6TNU; EM; 3.10 A; BL=9-108.
DR PDB; 6WOO; EM; 2.90 A; U=9-108.
DR PDB; 6XIQ; EM; 4.20 A; U=1-121.
DR PDB; 6XIR; EM; 3.20 A; U=1-121.
DR PDB; 6YLG; EM; 3.00 A; U=1-121.
DR PDB; 6YLH; EM; 3.10 A; U=1-121.
DR PDB; 6YLX; EM; 3.90 A; U=1-121.
DR PDB; 6YLY; EM; 3.80 A; U=1-121.
DR PDB; 6Z6J; EM; 3.40 A; LU=1-121.
DR PDB; 6Z6K; EM; 3.40 A; LU=1-121.
DR PDB; 7AZY; EM; 2.88 A; w=1-121.
DR PDB; 7B7D; EM; 3.30 A; Lq=9-108.
DR PDB; 7BT6; EM; 3.12 A; U=1-121.
DR PDB; 7BTB; EM; 3.22 A; U=1-121.
DR PDB; 7NRC; EM; 3.90 A; LW=9-108.
DR PDB; 7NRD; EM; 4.36 A; LW=9-108.
DR PDB; 7OF1; EM; 3.10 A; U=1-121.
DR PDB; 7OH3; EM; 3.40 A; U=1-121.
DR PDB; 7OHQ; EM; 3.10 A; U=1-121.
DR PDB; 7OHR; EM; 4.72 A; U=1-121.
DR PDB; 7OHV; EM; 3.90 A; U=1-121.
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; 4V6I; -.
DR PDBsum; 4V7F; -.
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; 7OHR; -.
DR PDBsum; 7OHV; -.
DR AlphaFoldDB; P05749; -.
DR SMR; P05749; -.
DR BioGRID; 31336; 430.
DR IntAct; P05749; 9.
DR MINT; P05749; -.
DR STRING; 4932.YLR061W; -.
DR iPTMnet; P05749; -.
DR MaxQB; P05749; -.
DR PaxDb; P05749; -.
DR PRIDE; P05749; -.
DR TopDownProteomics; P05749; -.
DR EnsemblFungi; YLR061W_mRNA; YLR061W; YLR061W.
DR GeneID; 850750; -.
DR KEGG; sce:YLR061W; -.
DR SGD; S000004051; RPL22A.
DR VEuPathDB; FungiDB:YLR061W; -.
DR eggNOG; KOG3434; Eukaryota.
DR GeneTree; ENSGT00940000169435; -.
DR HOGENOM; CLU_105624_0_0_1; -.
DR InParanoid; P05749; -.
DR BioCyc; YEAST:G3O-32215-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:P05749; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P05749; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR Gene3D; 3.30.1360.210; -; 1.
DR InterPro; IPR002671; Ribosomal_L22e.
DR InterPro; IPR038526; Ribosomal_L22e_sf.
DR PANTHER; PTHR10064; PTHR10064; 1.
DR Pfam; PF01776; Ribosomal_L22e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:6814480"
FT CHAIN 2..121
FT /note="60S ribosomal protein L22-A"
FT /id="PRO_0000215514"
FT CONFLICT 49
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4U3U"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 49..53
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 121 AA; 13693 MW; AFF542E484A52069 CRC64;
MAPNTSRKQK IAKTFTVDVS SPTENGVFDP ASYAKYLIDH IKVEGAVGNL GNAVTVTEDG
TVVTVVSTAK FSGKYLKYLT KKYLKKNQLR DWIRFVSTKT NEYRLAFYQV TPEEDEEEDE
E
