ID RL2A_YEAST Reviewed; 254 AA. AC P0CX45; D6VTR2; P05736; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Large ribosomal subunit protein uL2A {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L2-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=L5; DE AltName: Full=RP8; DE AltName: Full=YL6; GN Name=RPL2A {ECO:0000303|PubMed:9559554}; Synonyms=RPL5B; GN OrderedLocusNames=YFR031C-A; ORFNames=YFR031BC; 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 204660 / DBY746; RX PubMed=7753035; DOI=10.1007/bf00705656; RA Moore J., Jacobs H.T., Kaiser K.; RT "Characterisation of Saccharomyces cerevisiae genes encoding ribosomal RT protein YL6."; RL Mol. Gen. Genet. 247:247-254(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=8686381; RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a; RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M., RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H., RA Hanaoka F., Murakami Y.; RT "Fifteen open reading frames in a 30.8 kb region of the right arm of RT chromosome VI from Saccharomyces cerevisiae."; RL Yeast 12:177-190(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). RN [4] 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 [5] RP PARTIAL PROTEIN SEQUENCE OF 2-41, AND CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=18782943; DOI=10.1007/bf00341461; RA Otaka E., Higo K., Itoh T.; RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence RT characterization of twenty-four proteins from cytoplasmic ribosomes."; RL Mol. Gen. Genet. 195:544-546(1984). RN [6] RP PROTEIN SEQUENCE OF 2-21. RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8; RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.; RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces RT cerevisiae."; RL J. Biol. Chem. 267:5442-5445(1992). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-254. RX PubMed=7698648; DOI=10.1101/gad.9.5.587; RA Strunnikov A.V., Hogan E., Koshland D.; RT "SMC2, a Saccharomyces cerevisiae gene essential for chromosome segregation RT and condensation, defines a subgroup within the SMC family."; RL Genes Dev. 9:587-599(1995). RN [8] 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 [9] RP MASS SPECTROMETRY. RX PubMed=11983894; DOI=10.1073/pnas.082119899; RA Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A., RA Shen Y., Zhao R., Smith R.D.; RT "Direct mass spectrometric analysis of intact proteins of the yeast large RT ribosomal subunit using capillary LC/FTICR."; RL Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-159; SER-160 AND RP SER-249, AND IDENTIFICATION BY 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [13] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-93; LYS-119 AND RP LYS-145, AND 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 [14] 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 [15] RP 3D-STRUCTURE MODELING OF 2-245, 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 [16] 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 [17] 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 [18] 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 -!- MASS SPECTROMETRY: Mass=27277.348; Method=Electrospray; Note=Average CC mass.; Evidence={ECO:0000269|PubMed:11983894}; CC -!- MISCELLANEOUS: There are 2 genes for uL2 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 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; U17359; AAA92283.1; -; Genomic_DNA. DR EMBL; D50617; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U05820; AAA17418.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12472.1; -; Genomic_DNA. DR PIR; S50243; S50243. DR RefSeq; NP_012246.1; NM_001179368.1. DR RefSeq; NP_116688.3; NM_001180030.3. DR PDB; 3J6X; EM; 6.10 A; L2=1-254. DR PDB; 3J6Y; EM; 6.10 A; L2=1-254. DR PDB; 3J77; EM; 6.20 A; L2=1-254. DR PDB; 3J78; EM; 6.30 A; L2=1-254. DR PDB; 3JCT; EM; 3.08 A; A=1-254. DR PDB; 4U3M; X-ray; 3.00 A; L2/l2=2-254. DR PDB; 4U3N; X-ray; 3.20 A; L2/l2=2-254. DR PDB; 4U3U; X-ray; 2.90 A; L2/l2=2-254. DR PDB; 4U4N; X-ray; 3.10 A; L2/l2=2-254. DR PDB; 4U4O; X-ray; 3.60 A; L2/l2=2-254. DR PDB; 4U4Q; X-ray; 3.00 A; L2/l2=2-254. DR PDB; 4U4R; X-ray; 2.80 A; L2/l2=2-254. DR PDB; 4U4U; X-ray; 3.00 A; L2/l2=2-254. DR PDB; 4U4Y; X-ray; 3.20 A; L2/l2=2-254. DR PDB; 4U4Z; X-ray; 3.10 A; L2/l2=2-254. DR PDB; 4U50; X-ray; 3.20 A; L2/l2=2-254. DR PDB; 4U51; X-ray; 3.20 A; L2/l2=2-254. DR PDB; 4U52; X-ray; 3.00 A; L2/l2=2-254. DR PDB; 4U53; X-ray; 3.30 A; L2/l2=2-254. DR PDB; 4U55; X-ray; 3.20 A; L2/l2=2-254. DR PDB; 4U56; X-ray; 3.45 A; L2/l2=2-254. DR PDB; 4U6F; X-ray; 3.10 A; L2/l2=2-254. DR PDB; 4V4B; EM; 11.70 A; BB=2-254. DR PDB; 4V6I; EM; 8.80 A; BB=1-254. DR PDB; 4V7F; EM; 8.70 A; B=1-254. DR PDB; 4V7R; X-ray; 4.00 A; BB/DB=1-254. DR PDB; 4V88; X-ray; 3.00 A; BA/DA=1-254. DR PDB; 4V91; EM; 3.70 A; A=1-254. DR PDB; 5APN; EM; 3.91 A; A=1-254. DR PDB; 5APO; EM; 3.41 A; A=1-254. DR PDB; 5DAT; X-ray; 3.15 A; L2/l2=2-254. DR PDB; 5DC3; X-ray; 3.25 A; L2/l2=2-254. DR PDB; 5DGE; X-ray; 3.45 A; L2/l2=2-254. DR PDB; 5DGF; X-ray; 3.30 A; L2/l2=2-254. DR PDB; 5DGV; X-ray; 3.10 A; L2/l2=2-254. DR PDB; 5FCI; X-ray; 3.40 A; L2/l2=2-254. DR PDB; 5FCJ; X-ray; 3.10 A; L2/l2=2-254. DR PDB; 5GAK; EM; 3.88 A; E=1-254. DR PDB; 5H4P; EM; 3.07 A; A=2-247. DR PDB; 5I4L; X-ray; 3.10 A; L2/l2=2-253. DR PDB; 5JCS; EM; 9.50 A; A=1-254. DR PDB; 5JUO; EM; 4.00 A; F=1-254. DR PDB; 5JUP; EM; 3.50 A; F=1-254. DR PDB; 5JUS; EM; 4.20 A; F=1-254. DR PDB; 5JUT; EM; 4.00 A; F=1-254. DR PDB; 5JUU; EM; 4.00 A; F=1-254. DR PDB; 5LYB; X-ray; 3.25 A; L2/l2=2-253. DR PDB; 5M1J; EM; 3.30 A; A5=2-253. DR PDB; 5MC6; EM; 3.80 A; AW=1-254. DR PDB; 5MEI; X-ray; 3.50 A; CD/j=2-253. DR PDB; 5NDG; X-ray; 3.70 A; L2/l2=2-253. DR PDB; 5NDV; X-ray; 3.30 A; L2/l2=2-249. DR PDB; 5NDW; X-ray; 3.70 A; L2/l2=2-253. DR PDB; 5OBM; X-ray; 3.40 A; L2/l2=2-253. DR PDB; 5ON6; X-ray; 3.10 A; CD/j=2-253. DR PDB; 5T62; EM; 3.30 A; D=1-254. DR PDB; 5T6R; EM; 4.50 A; D=1-254. DR PDB; 5TBW; X-ray; 3.00 A; CD/j=2-253. DR PDB; 5TGA; X-ray; 3.30 A; L2/l2=2-253. DR PDB; 5TGM; X-ray; 3.50 A; L2/l2=2-253. DR PDB; 6FT6; EM; 3.90 A; A=1-254. DR PDB; 6GQ1; EM; 4.40 A; A=2-253. DR PDB; 6GQB; EM; 3.90 A; A=2-253. DR PDB; 6GQV; EM; 4.00 A; A=2-253. DR PDB; 6HD7; EM; 3.40 A; E=1-254. DR PDB; 6HHQ; X-ray; 3.10 A; CD/j=1-254. DR PDB; 6I7O; EM; 5.30 A; AW/XW=2-253. DR PDB; 6M62; EM; 3.20 A; A=1-254. DR PDB; 6N8J; EM; 3.50 A; A=1-254. DR PDB; 6N8K; EM; 3.60 A; A=1-254. DR PDB; 6N8L; EM; 3.60 A; A=1-254. DR PDB; 6N8M; EM; 3.50 A; D=1-254. DR PDB; 6N8N; EM; 3.80 A; D=1-254. DR PDB; 6N8O; EM; 3.50 A; D=1-254. DR PDB; 6OIG; EM; 3.80 A; A=2-253. DR PDB; 6Q8Y; EM; 3.10 A; AW=2-253. DR PDB; 6QIK; EM; 3.10 A; B=1-254. DR PDB; 6QT0; EM; 3.40 A; B=1-254. DR PDB; 6QTZ; EM; 3.50 A; B=1-254. DR PDB; 6R84; EM; 3.60 A; E=2-253. DR PDB; 6R86; EM; 3.40 A; E=2-253. DR PDB; 6R87; EM; 3.40 A; E=2-253. DR PDB; 6RI5; EM; 3.30 A; B=1-254. DR PDB; 6RZZ; EM; 3.20 A; B=1-254. DR PDB; 6S05; EM; 3.90 A; B=1-254. DR PDB; 6S47; EM; 3.28 A; AD=2-253. DR PDB; 6SNT; EM; 2.80 A; h=1-254. DR PDB; 6SV4; EM; 3.30 A; AW/XW/zW=1-254. DR PDB; 6T4Q; EM; 2.60 A; LA=2-252. DR PDB; 6T7I; EM; 3.20 A; LA=1-254. DR PDB; 6T7T; EM; 3.10 A; LA=1-254. DR PDB; 6T83; EM; 4.00 A; Ay/Da=1-254. DR PDB; 6TB3; EM; 2.80 A; AW=2-252. DR PDB; 6TNU; EM; 3.10 A; AW=2-252. DR PDB; 6WOO; EM; 2.90 A; A=2-250. DR PDB; 6XIQ; EM; 4.20 A; A=1-254. DR PDB; 6XIR; EM; 3.20 A; A=1-254. DR PDB; 6YLG; EM; 3.00 A; A=1-254. DR PDB; 6YLH; EM; 3.10 A; A=1-254. DR PDB; 6YLY; EM; 3.80 A; A=1-254. DR PDB; 6Z6J; EM; 3.40 A; LA=1-254. DR PDB; 6Z6K; EM; 3.40 A; LA=1-254. DR PDB; 7AZY; EM; 2.88 A; x=1-254. DR PDB; 7B7D; EM; 3.30 A; LD=2-252. DR PDB; 7BT6; EM; 3.12 A; A=1-254. DR PDB; 7BTB; EM; 3.22 A; A=1-254. DR PDB; 7MPI; EM; 3.05 A; AA=2-248. DR PDB; 7MPJ; EM; 2.70 A; AA=2-248. DR PDB; 7N8B; EM; 3.05 A; AA=2-248. DR PDB; 7NRC; EM; 3.90 A; LD=2-252. DR PDB; 7NRD; EM; 4.36 A; LD=2-252. DR PDB; 7OF1; EM; 3.10 A; A=1-254. DR PDB; 7OH3; EM; 3.40 A; A=1-254. DR PDB; 7OHQ; EM; 3.10 A; A=1-254. DR PDB; 7TOO; EM; 2.70 A; AL02=1-254. DR PDB; 7TOP; EM; 2.40 A; AL02=1-254. DR PDB; 7U0H; EM; 2.76 A; A=1-254. DR PDB; 7UG6; EM; 2.90 A; A=1-254. DR PDB; 7UOO; EM; 2.34 A; A=1-254. DR PDB; 7UQB; EM; 2.43 A; A=1-254. DR PDB; 7UQZ; EM; 2.44 A; A=1-254. DR PDB; 7V08; EM; 2.36 A; A=1-254. DR PDB; 7Z34; EM; 3.80 A; A=1-254. DR PDB; 7ZPQ; EM; 3.47 A; BA=2-252. DR PDB; 7ZRS; EM; 4.80 A; BA=2-252. DR PDB; 7ZS5; EM; 3.20 A; BC=2-253. DR PDB; 7ZUW; EM; 4.30 A; BA=2-252. DR PDB; 7ZUX; EM; 2.50 A; EA=2-252. DR PDB; 7ZW0; EM; 2.40 A; LE=1-254. DR PDB; 8AAF; EM; 2.50 A; j=1-254. DR PDB; 8AGT; EM; 2.60 A; j=1-254. DR PDB; 8AGU; EM; 2.70 A; j=1-254. DR PDB; 8AGV; EM; 2.60 A; j=1-254. DR PDB; 8AGW; EM; 2.60 A; j=1-254. DR PDB; 8AGX; EM; 2.40 A; j=1-254. DR PDB; 8AGZ; EM; 2.60 A; j=1-254. DR PDB; 8BIP; EM; 3.10 A; LA=2-252. DR PDB; 8BJQ; EM; 3.80 A; LA=2-252. DR PDB; 8BQD; EM; 3.90 A; AW=2-252. DR PDB; 8BQX; EM; 3.80 A; AW=2-252. DR PDB; 8CCS; EM; 1.97 A; EE=1-254. DR PDB; 8CDL; EM; 2.72 A; EE=1-254. DR PDB; 8CDR; EM; 2.04 A; EE=1-254. DR PDB; 8CEH; EM; 2.05 A; EE=1-254. DR PDB; 8CF5; EM; 2.71 A; EE=1-254. DR PDB; 8CG8; EM; 2.57 A; EE=1-254. DR PDB; 8CGN; EM; 2.28 A; EE=1-254. DR PDB; 8CIV; EM; 2.47 A; EE=1-254. DR PDB; 8CKU; EM; 3.11 A; EE=1-254. DR PDB; 8CMJ; EM; 3.79 A; EE=1-254. DR PDB; 8EUB; EM; 2.52 A; AA=1-254. DR PDB; 8EVP; EM; 2.38 A; AA=1-254. DR PDB; 8EVQ; EM; 2.72 A; AA=1-254. DR PDB; 8EVR; EM; 2.87 A; AA=1-254. DR PDB; 8EVS; EM; 2.62 A; AA=1-254. DR PDB; 8EVT; EM; 2.20 A; AA=1-254. DR PDB; 8EWB; EM; 2.87 A; AA=1-254. DR PDB; 8EWC; EM; 2.45 A; AA=1-254. DR PDB; 8HFR; EM; 2.64 A; B4=1-254. 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; 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; 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; 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; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7OF1; -. DR PDBsum; 7OH3; -. DR PDBsum; 7OHQ; -. 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; P0CX45; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0202; -. DR EMDB; EMD-0369; -. DR EMDB; EMD-0370; -. DR EMDB; EMD-0371; -. DR EMDB; EMD-0372; -. DR EMDB; EMD-0373; -. DR EMDB; EMD-0374; -. DR EMDB; EMD-10068; -. DR EMDB; EMD-10071; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-10838; -. DR EMDB; EMD-10839; -. DR EMDB; EMD-10842; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11951; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-12866; -. DR EMDB; EMD-12892; -. DR EMDB; EMD-12905; -. DR EMDB; EMD-14471; -. DR EMDB; EMD-14990; -. 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-20077; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-22196; -. DR EMDB; EMD-22198; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-26033; -. DR EMDB; EMD-26034; -. 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-30108; -. DR EMDB; EMD-30170; -. DR EMDB; EMD-30174; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-4302; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4560; -. DR EMDB; EMD-4630; -. DR EMDB; EMD-4636; -. DR EMDB; EMD-4751; -. DR EMDB; EMD-4752; -. DR EMDB; EMD-4753; -. DR EMDB; EMD-4884; -. DR EMDB; EMD-8362; -. DR EMDB; EMD-8368; -. DR SMR; P0CX45; -. DR BioGRID; 31187; 461. DR BioGRID; 34970; 72. DR IntAct; P0CX45; 5. DR MINT; P0CX45; -. DR STRING; 4932.YFR031C-A; -. DR MoonProt; P0CX45; -. DR CarbonylDB; P0CX45; -. DR iPTMnet; P0CX45; -. DR MaxQB; P0CX45; -. DR PaxDb; 4932-YFR031C-A; -. DR PeptideAtlas; P0CX45; -. DR TopDownProteomics; P0CX45; -. DR EnsemblFungi; YFR031C-A_mRNA; YFR031C-A; YFR031C-A. DR EnsemblFungi; YIL018W_mRNA; YIL018W; YIL018W. DR GeneID; 850590; -. DR GeneID; 854794; -. DR KEGG; sce:YFR031C-A; -. DR KEGG; sce:YIL018W; -. DR AGR; SGD:S000002104; -. DR SGD; S000002104; RPL2A. DR VEuPathDB; FungiDB:YFR031C-A; -. DR VEuPathDB; FungiDB:YIL018W; -. DR eggNOG; KOG2309; Eukaryota. DR HOGENOM; CLU_036235_0_3_1; -. DR InParanoid; P0CX45; -. DR OMA; HPYKFKM; -. DR OrthoDB; 1086454at2759; -. DR BioCyc; YEAST:G3O-30501-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; 850590; 7 hits in 10 CRISPR screens. DR BioGRID-ORCS; 854794; 9 hits in 10 CRISPR screens. DR EvolutionaryTrace; P0CX45; -. DR PRO; PR:P0CX45; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P0CX45; Protein. DR ExpressionAtlas; P0CX45; baseline and differential. 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:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 4.10.950.10; Ribosomal protein L2, domain 3; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR002171; Ribosomal_uL2. DR InterPro; IPR022669; Ribosomal_uL2_C. DR InterPro; IPR022671; Ribosomal_uL2_CS. DR InterPro; IPR014726; Ribosomal_uL2_dom3. DR InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR PANTHER; PTHR13691:SF16; 60S RIBOSOMAL PROTEIN L8; 1. DR PANTHER; PTHR13691; RIBOSOMAL PROTEIN L2; 1. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR PIRSF; PIRSF002158; Ribosomal_L2; 1. DR SMART; SM01383; Ribosomal_L2; 1. DR SMART; SM01382; Ribosomal_L2_C; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1544921, FT ECO:0000269|PubMed:18782943" FT CHAIN 2..254 FT /note="Large ribosomal subunit protein uL2A" FT /id="PRO_0000129761" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT CROSSLNK 46 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 93 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 119 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 145 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 10..12 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:4U4U" FT HELIX 34..38 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 58..64 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 68..77 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 112..116 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:4U56" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 141..144 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 145..149 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:4U4Q" FT STRAND 155..159 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:4U4U" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 182..190 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:4U3U" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:4U3U" FT TURN 214..217 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:4U4R" SQ SEQUENCE 254 AA; 27408 MW; 5159A980574DF05A CRC64; MGRVIRNQRK GAGSIFTSHT RLRQGAAKLR TLDYAERHGY IRGIVKQIVH DSGRGAPLAK VVFRDPYKYR LREEIFIANE GVHTGQFIYA GKKASLNVGN VLPLGSVPEG TIVSNVEEKP GDRGALARAS GNYVIIIGHN PDENKTRVRL PSGAKKVISS DARGVIGVIA GGGRVDKPLL KAGRAFHKYR LKRNSWPKTR GVAMNPVDHP HGGGNHQHIG KASTISRGAV SGQKAGLIAA RRTGLLRGSQ KTQD //