RL44A_YEAST
ID RL44A_YEAST Reviewed; 106 AA.
AC P0CX27; D3DL90; P02405;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=60S ribosomal protein L42-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L41;
DE AltName: Full=Large ribosomal subunit protein eL42-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL27;
DE AltName: Full=YP44;
GN Name=RPL42A {ECO:0000303|PubMed:9559554}; Synonyms=RPL41A, SCL41A;
GN OrderedLocusNames=YNL162W; ORFNames=N1722;
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], AND VARIANT GLN-56.
RX PubMed=1729213; DOI=10.1128/jb.174.1.254-262.1992;
RA Kawai S., Murao S., Mochizuki M., Shibuya I., Yano K., Takagi M.;
RT "Drastic alteration of cycloheximide sensitivity by substitution of one
RT amino acid in the L41 ribosomal protein of yeasts.";
RL J. Bacteriol. 174:254-262(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 PROTEIN SEQUENCE OF 2-106.
RX PubMed=365584; DOI=10.1016/0014-5793(78)80447-5;
RA Itoh T., Wittmann-Liebold B.;
RT "The primary structure of protein 44 from the large subunit of yeast
RT ribosomes.";
RL FEBS Lett. 96:399-402(1978).
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 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 [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 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 [10]
RP METHYLATION AT LYS-40 AND LYS-55, AND MASS SPECTROMETRY.
RX PubMed=18957409; DOI=10.1074/jbc.m806006200;
RA Webb K.J., Laganowsky A., Whitelegge J.P., Clarke S.G.;
RT "Identification of two SET domain proteins required for methylation of
RT lysine residues in yeast ribosomal protein Rpl42ab.";
RL J. Biol. Chem. 283:35561-35568(2008).
RN [11]
RP METHYLATION AT LYS-40.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [12]
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 [13]
RP METHYLATION AT LYS-40 BY RKM3, AND METHYLATION AT LYS-55 BY RKM4.
RX PubMed=24517342; DOI=10.1021/pr401251k;
RA Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.;
RT "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights
RT into non-histone protein lysine methyltransferase activity.";
RL J. Proteome Res. 13:1744-1756(2014).
RN [14]
RP 3D-STRUCTURE MODELING OF 2-92, 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 [15]
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 [16]
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 [17]
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 -!- PTM: In wild-type cells, 78% of L42 is monomethylated at both Lys-40
CC and Lys-55, and 22% are a mixture of species with either residue
CC monomethylated. {ECO:0000269|PubMed:24517342}.
CC -!- MASS SPECTROMETRY: Mass=12100.729; Method=Electrospray;
CC Note=Monoisotopic mass with 2 methylation modifications.;
CC Evidence={ECO:0000269|PubMed:11983894};
CC -!- MASS SPECTROMETRY: Mass=12100.71; Method=Electrospray;
CC Note=Monoisotopic mass with N6-methyl-Lys-40 and N6-methyl-Lys-55.;
CC Evidence={ECO:0000269|PubMed:18957409};
CC -!- MASS SPECTROMETRY: Mass=12108.0; Method=Electrospray; Note=With N6-
CC methyl-Lys-40 and N6-methyl-Lys-55.;
CC Evidence={ECO:0000269|PubMed:18957409};
CC -!- MISCELLANEOUS: Present with 13600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL42 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA96049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D10578; BAA01435.1; -; Genomic_DNA.
DR EMBL; X92517; CAA63277.1; -; Genomic_DNA.
DR EMBL; Z71438; CAA96049.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006947; DAA10387.1; -; Genomic_DNA.
DR PIR; S63114; S63114.
DR RefSeq; NP_012010.1; NM_001179271.1.
DR RefSeq; NP_014237.2; NM_001183000.1.
DR PDB; 3J6X; EM; 6.10 A; 82=1-106.
DR PDB; 3J6Y; EM; 6.10 A; 82=1-106.
DR PDB; 3J77; EM; 6.20 A; 92=1-106.
DR PDB; 3J78; EM; 6.30 A; 92=1-106.
DR PDB; 4U3M; X-ray; 3.00 A; Q2/q2=2-106.
DR PDB; 4U3N; X-ray; 3.20 A; Q2/q2=2-106.
DR PDB; 4U3U; X-ray; 2.90 A; Q2/q2=2-106.
DR PDB; 4U4N; X-ray; 3.10 A; Q2/q2=2-106.
DR PDB; 4U4O; X-ray; 3.60 A; Q2/q2=2-106.
DR PDB; 4U4Q; X-ray; 3.00 A; Q2/q2=2-106.
DR PDB; 4U4R; X-ray; 2.80 A; Q2/q2=2-106.
DR PDB; 4U4U; X-ray; 3.00 A; Q2/q2=2-106.
DR PDB; 4U4Y; X-ray; 3.20 A; Q2/q2=2-106.
DR PDB; 4U4Z; X-ray; 3.10 A; Q2/q2=2-106.
DR PDB; 4U50; X-ray; 3.20 A; Q2/q2=2-106.
DR PDB; 4U51; X-ray; 3.20 A; Q2/q2=2-106.
DR PDB; 4U52; X-ray; 3.00 A; Q2/q2=2-106.
DR PDB; 4U53; X-ray; 3.30 A; Q2/q2=2-106.
DR PDB; 4U55; X-ray; 3.20 A; Q2/q2=2-106.
DR PDB; 4U56; X-ray; 3.45 A; Q2/q2=2-106.
DR PDB; 4U6F; X-ray; 3.10 A; Q2/q2=2-106.
DR PDB; 4V4B; EM; 11.70 A; BZ=2-106.
DR PDB; 4V6I; EM; 8.80 A; Br=1-106.
DR PDB; 4V7R; X-ray; 4.00 A; Bf/Df=1-106.
DR PDB; 4V88; X-ray; 3.00 A; Bo/Do=1-106.
DR PDB; 4V8T; EM; 8.10 A; o=1-106.
DR PDB; 4V8Y; EM; 4.30 A; Bo=2-106.
DR PDB; 4V8Z; EM; 6.60 A; Bo=2-106.
DR PDB; 4V91; EM; 3.70 A; o=1-106.
DR PDB; 5APN; EM; 3.91 A; o=1-106.
DR PDB; 5APO; EM; 3.41 A; o=1-106.
DR PDB; 5DAT; X-ray; 3.15 A; Q2/q2=2-106.
DR PDB; 5DC3; X-ray; 3.25 A; Q2/q2=2-106.
DR PDB; 5DGE; X-ray; 3.45 A; Q2/q2=2-106.
DR PDB; 5DGF; X-ray; 3.30 A; Q2/q2=2-106.
DR PDB; 5DGV; X-ray; 3.10 A; Q2/q2=2-106.
DR PDB; 5FCI; X-ray; 3.40 A; Q2/q2=2-106.
DR PDB; 5FCJ; X-ray; 3.10 A; Q2/q2=2-106.
DR PDB; 5GAK; EM; 3.88 A; C=1-106.
DR PDB; 5H4P; EM; 3.07 A; o=1-106.
DR PDB; 5I4L; X-ray; 3.10 A; Q2/q2=2-106.
DR PDB; 5JUO; EM; 4.00 A; TA=1-106.
DR PDB; 5JUP; EM; 3.50 A; TA=1-106.
DR PDB; 5JUS; EM; 4.20 A; TA=1-106.
DR PDB; 5JUT; EM; 4.00 A; TA=1-106.
DR PDB; 5JUU; EM; 4.00 A; TA=1-106.
DR PDB; 5LYB; X-ray; 3.25 A; Q2/q2=2-106.
DR PDB; 5MC6; EM; 3.80 A; AP=1-106.
DR PDB; 5MEI; X-ray; 3.50 A; AP/DQ=2-106.
DR PDB; 5NDG; X-ray; 3.70 A; Q2/q2=2-106.
DR PDB; 5NDV; X-ray; 3.30 A; Q2/q2=2-106.
DR PDB; 5NDW; X-ray; 3.70 A; Q2/q2=2-106.
DR PDB; 5OBM; X-ray; 3.40 A; Q2/q2=2-106.
DR PDB; 5ON6; X-ray; 3.10 A; AP/DQ=2-106.
DR PDB; 5T62; EM; 3.30 A; Q=1-106.
DR PDB; 5T6R; EM; 4.50 A; Q=1-106.
DR PDB; 5TBW; X-ray; 3.00 A; AP/DQ=2-106.
DR PDB; 5TGA; X-ray; 3.30 A; Q2/q2=2-106.
DR PDB; 5TGM; X-ray; 3.50 A; Q2/q2=2-106.
DR PDB; 6GQ1; EM; 4.40 A; o=2-106.
DR PDB; 6GQB; EM; 3.90 A; o=2-106.
DR PDB; 6GQV; EM; 4.00 A; o=2-106.
DR PDB; 6HD7; EM; 3.40 A; C=1-106.
DR PDB; 6HHQ; X-ray; 3.10 A; AP/DQ=1-106.
DR PDB; 6I7O; EM; 5.30 A; AP/XP=2-106.
DR PDB; 6N8J; EM; 3.50 A; q=1-106.
DR PDB; 6N8K; EM; 3.60 A; q=1-106.
DR PDB; 6N8L; EM; 3.60 A; q=1-106.
DR PDB; 6N8M; EM; 3.50 A; Q=1-106.
DR PDB; 6N8N; EM; 3.80 A; Q=1-106.
DR PDB; 6N8O; EM; 3.50 A; Q=1-106.
DR PDB; 6OIG; EM; 3.80 A; o=2-106.
DR PDB; 6Q8Y; EM; 3.10 A; AP=2-106.
DR PDB; 6QIK; EM; 3.10 A; l=1-106.
DR PDB; 6QT0; EM; 3.40 A; l=1-106.
DR PDB; 6QTZ; EM; 3.50 A; l=1-106.
DR PDB; 6R84; EM; 3.60 A; C=2-106.
DR PDB; 6R86; EM; 3.40 A; C=2-106.
DR PDB; 6R87; EM; 3.40 A; C=2-106.
DR PDB; 6RI5; EM; 3.30 A; l=1-106.
DR PDB; 6RZZ; EM; 3.20 A; l=1-106.
DR PDB; 6S05; EM; 3.90 A; l=1-106.
DR PDB; 6S47; EM; 3.28 A; Aq=2-106.
DR PDB; 6SNT; EM; 2.80 A; ab=1-106.
DR PDB; 6SV4; EM; 3.30 A; AP/XP/zP=1-106.
DR PDB; 6T4Q; EM; 2.60 A; Lo=2-104.
DR PDB; 6T7I; EM; 3.20 A; Lo=1-106.
DR PDB; 6T7T; EM; 3.10 A; Lo=1-106.
DR PDB; 6T83; EM; 4.00 A; Z/ob=1-106.
DR PDB; 6TB3; EM; 2.80 A; AP=2-104.
DR PDB; 6TNU; EM; 3.10 A; AP=2-104.
DR PDB; 6WOO; EM; 2.90 A; o=2-102.
DR PDB; 6XIQ; EM; 4.20 A; o=1-106.
DR PDB; 6XIR; EM; 3.20 A; o=1-106.
DR PDB; 6Z6J; EM; 3.40 A; Lo=1-106.
DR PDB; 6Z6K; EM; 3.40 A; Lo=1-106.
DR PDB; 7AZY; EM; 2.88 A; Q=1-106.
DR PDB; 7B7D; EM; 3.30 A; Lk=2-104.
DR PDB; 7NRC; EM; 3.90 A; Lq=2-104.
DR PDB; 7NRD; EM; 4.36 A; Lq=2-104.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
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; 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; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
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; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
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; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX27; -.
DR SMR; P0CX27; -.
DR BioGRID; 35667; 67.
DR BioGRID; 36574; 34.
DR IntAct; P0CX27; 5.
DR MINT; P0CX27; -.
DR STRING; 4932.YHR141C; -.
DR iPTMnet; P0CX27; -.
DR MaxQB; P0CX27; -.
DR PaxDb; P0CX27; -.
DR PRIDE; P0CX27; -.
DR EnsemblFungi; YHR141C_mRNA; YHR141C; YHR141C.
DR EnsemblFungi; YNL162W_mRNA; YNL162W; YNL162W.
DR GeneID; 855560; -.
DR GeneID; 856544; -.
DR KEGG; sce:YHR141C; -.
DR KEGG; sce:YNL162W; -.
DR SGD; S000005106; RPL42A.
DR VEuPathDB; FungiDB:YHR141C; -.
DR VEuPathDB; FungiDB:YNL162W; -.
DR eggNOG; KOG3464; Eukaryota.
DR HOGENOM; CLU_114645_2_1_1; -.
DR InParanoid; P0CX27; -.
DR OMA; CKKHTIH; -.
DR BioCyc; YEAST:G3O-33178-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; P0CX27; -.
DR PRO; PR:P0CX27; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P0CX27; protein.
DR ExpressionAtlas; P0CX27; 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:0003735; F:structural constituent of ribosome; IC:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0046898; P:response to cycloheximide; IEA:UniProtKB-KW.
DR InterPro; IPR000552; Ribosomal_L44e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR10369; PTHR10369; 1.
DR Pfam; PF00935; Ribosomal_L44; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01172; RIBOSOMAL_L44E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cycloheximide resistance; Cytoplasm;
KW Direct protein sequencing; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:365584"
FT CHAIN 2..106
FT /note="60S ribosomal protein L42-A"
FT /id="PRO_0000149147"
FT MOD_RES 40
FT /note="N6-methyllysine; by RKM3"
FT /evidence="ECO:0000269|PubMed:18957409,
FT ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342"
FT MOD_RES 55
FT /note="N6-methyllysine; by RKM4"
FT /evidence="ECO:0000269|PubMed:18957409,
FT ECO:0000269|PubMed:24517342"
FT VARIANT 56
FT /note="P -> Q (confers resistance to cycloheximide, an
FT inhibitor of polypeptide elongation)"
FT /evidence="ECO:0000269|PubMed:1729213"
FT CONFLICT 40..41
FT /note="KR -> RK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..89
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 106 AA; 12212 MW; 730CA11F2CF7F2B4 CRC64;
MVNVPKTRKT YCKGKTCRKH TQHKVTQYKA GKASLFAQGK RRYDRKQSGF GGQTKPVFHK
KAKTTKKVVL RLECVKCKTR AQLTLKRCKH FELGGEKKQK GQALQF
