RL2A_YEAST
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 03-AUG-2022, entry version 95.
DE RecName: Full=60S ribosomal protein L2-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L5;
DE AltName: Full=Large ribosomal subunit protein uL2-A {ECO:0000303|PubMed:24524803};
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=27277.347; 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}.
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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; 5FL8; EM; 9.50 A; A=1-254.
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; 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 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; 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; 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; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR AlphaFoldDB; P0CX45; -.
DR SMR; P0CX45; -.
DR BioGRID; 31187; 388.
DR BioGRID; 34970; 66.
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; P0CX45; -.
DR PRIDE; 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 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 BioCyc; YEAST:G3O-30501-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 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; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 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; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 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="60S ribosomal protein L2-A"
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
