RL15A_YEAST
ID RL15A_YEAST Reviewed; 204 AA.
AC P05748; D6VY31;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=60S ribosomal protein L15-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L13;
DE AltName: Full=Large ribosomal subunit protein eL15-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP15R;
DE AltName: Full=YL10;
DE AltName: Full=YP18;
GN Name=RPL15A {ECO:0000303|PubMed:9559554}; Synonyms=RPL10A, RPL13A, YL10A;
GN OrderedLocusNames=YLR029C;
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].
RA Tomiyoshi A., Suzuki K., Otaka E.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-44.
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 [5]
RP PROTEIN SEQUENCE OF 2-9.
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 [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 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 [8]
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 [9]
RP 3D-STRUCTURE MODELING OF 3-196, 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 [10]
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 [11]
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 [12]
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:22096102}.
CC -!- MISCELLANEOUS: There are 2 genes for eL15 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family.
CC {ECO:0000305}.
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DR EMBL; D14675; BAA03506.1; -; Genomic_DNA.
DR EMBL; Z73201; CAA97553.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09347.1; -; Genomic_DNA.
DR PIR; S48502; S48502.
DR RefSeq; NP_013129.1; NM_001181916.1.
DR PDB; 3J6X; EM; 6.10 A; 55=1-204.
DR PDB; 3J6Y; EM; 6.10 A; 55=1-204.
DR PDB; 3J77; EM; 6.20 A; 65=1-204.
DR PDB; 3J78; EM; 6.30 A; 65=1-204.
DR PDB; 3JCT; EM; 3.08 A; N=1-204.
DR PDB; 4U3M; X-ray; 3.00 A; M5/m5=2-204.
DR PDB; 4U3N; X-ray; 3.20 A; M5/m5=2-204.
DR PDB; 4U3U; X-ray; 2.90 A; M5/m5=2-204.
DR PDB; 4U4N; X-ray; 3.10 A; M5/m5=2-204.
DR PDB; 4U4O; X-ray; 3.60 A; M5/m5=2-204.
DR PDB; 4U4Q; X-ray; 3.00 A; M5/m5=2-204.
DR PDB; 4U4R; X-ray; 2.80 A; M5/m5=2-204.
DR PDB; 4U4U; X-ray; 3.00 A; M5/m5=2-204.
DR PDB; 4U4Y; X-ray; 3.20 A; M5/m5=2-204.
DR PDB; 4U4Z; X-ray; 3.10 A; M5/m5=2-204.
DR PDB; 4U50; X-ray; 3.20 A; M5/m5=2-204.
DR PDB; 4U51; X-ray; 3.20 A; M5/m5=2-204.
DR PDB; 4U52; X-ray; 3.00 A; M5/m5=2-204.
DR PDB; 4U53; X-ray; 3.30 A; M5/m5=2-204.
DR PDB; 4U55; X-ray; 3.20 A; M5/m5=2-204.
DR PDB; 4U56; X-ray; 3.45 A; M5/m5=2-204.
DR PDB; 4U6F; X-ray; 3.10 A; M5/m5=2-204.
DR PDB; 4V4B; EM; 11.70 A; BL=2-204.
DR PDB; 4V6I; EM; 8.80 A; BP=1-204.
DR PDB; 4V7F; EM; 8.70 A; O=1-204.
DR PDB; 4V7R; X-ray; 4.00 A; BO/DO=1-204.
DR PDB; 4V88; X-ray; 3.00 A; BN/DN=1-204.
DR PDB; 4V8T; EM; 8.10 A; N=1-204.
DR PDB; 4V8Y; EM; 4.30 A; BN=2-204.
DR PDB; 4V8Z; EM; 6.60 A; BN=2-204.
DR PDB; 4V91; EM; 3.70 A; N=1-204.
DR PDB; 5APN; EM; 3.91 A; N=1-204.
DR PDB; 5APO; EM; 3.41 A; N=1-204.
DR PDB; 5DAT; X-ray; 3.15 A; M5=2-204, m5=2-204.
DR PDB; 5DC3; X-ray; 3.25 A; M5/m5=2-204.
DR PDB; 5DGE; X-ray; 3.45 A; M5/m5=2-204.
DR PDB; 5DGF; X-ray; 3.30 A; M5/m5=2-204.
DR PDB; 5DGV; X-ray; 3.10 A; M5/m5=2-204.
DR PDB; 5FCI; X-ray; 3.40 A; M5/m5=2-204.
DR PDB; 5FCJ; X-ray; 3.10 A; M5/m5=2-204.
DR PDB; 5FL8; EM; 9.50 A; N=1-204.
DR PDB; 5GAK; EM; 3.88 A; P=1-204.
DR PDB; 5H4P; EM; 3.07 A; N=1-204.
DR PDB; 5I4L; X-ray; 3.10 A; M5/m5=2-204.
DR PDB; 5JCS; EM; 9.50 A; N=1-204.
DR PDB; 5JUO; EM; 4.00 A; S=1-204.
DR PDB; 5JUP; EM; 3.50 A; S=1-204.
DR PDB; 5JUS; EM; 4.20 A; S=1-204.
DR PDB; 5JUT; EM; 4.00 A; S=1-204.
DR PDB; 5JUU; EM; 4.00 A; S=1-204.
DR PDB; 5LYB; X-ray; 3.25 A; M5/m5=2-204.
DR PDB; 5M1J; EM; 3.30 A; N5=2-204.
DR PDB; 5MC6; EM; 3.80 A; AQ=1-204.
DR PDB; 5MEI; X-ray; 3.50 A; CP/v=2-204.
DR PDB; 5NDG; X-ray; 3.70 A; M5/m5=2-204.
DR PDB; 5NDV; X-ray; 3.30 A; M5/m5=2-204.
DR PDB; 5NDW; X-ray; 3.70 A; M5/m5=2-204.
DR PDB; 5OBM; X-ray; 3.40 A; M5/m5=2-204.
DR PDB; 5ON6; X-ray; 3.10 A; CP/v=2-204.
DR PDB; 5T62; EM; 3.30 A; a=1-204.
DR PDB; 5T6R; EM; 4.50 A; a=1-204.
DR PDB; 5TBW; X-ray; 3.00 A; CP/v=2-204.
DR PDB; 5TGA; X-ray; 3.30 A; M5/m5=2-204.
DR PDB; 5TGM; X-ray; 3.50 A; M5/m5=2-204.
DR PDB; 5Z3G; EM; 3.65 A; R=1-204.
DR PDB; 6C0F; EM; 3.70 A; N=1-204.
DR PDB; 6CB1; EM; 4.60 A; N=1-204.
DR PDB; 6ELZ; EM; 3.30 A; N=1-204.
DR PDB; 6EM1; EM; 3.60 A; N=1-204.
DR PDB; 6EM3; EM; 3.20 A; N=1-204.
DR PDB; 6EM4; EM; 4.10 A; N=1-204.
DR PDB; 6EM5; EM; 4.30 A; N=1-204.
DR PDB; 6FT6; EM; 3.90 A; N=1-204.
DR PDB; 6GQ1; EM; 4.40 A; N=2-204.
DR PDB; 6GQB; EM; 3.90 A; N=2-204.
DR PDB; 6GQV; EM; 4.00 A; N=2-204.
DR PDB; 6HD7; EM; 3.40 A; P=1-204.
DR PDB; 6HHQ; X-ray; 3.10 A; CP/v=1-204.
DR PDB; 6I7O; EM; 5.30 A; AQ/XQ=2-204.
DR PDB; 6M62; EM; 3.20 A; N=1-204.
DR PDB; 6N8J; EM; 3.50 A; N=1-204.
DR PDB; 6N8K; EM; 3.60 A; N=1-204.
DR PDB; 6N8L; EM; 3.60 A; N=1-204.
DR PDB; 6N8M; EM; 3.50 A; a=1-204.
DR PDB; 6N8N; EM; 3.80 A; a=1-204.
DR PDB; 6N8O; EM; 3.50 A; a=1-204.
DR PDB; 6OIG; EM; 3.80 A; N=2-204.
DR PDB; 6Q8Y; EM; 3.10 A; AQ=2-204.
DR PDB; 6QIK; EM; 3.10 A; O=1-204.
DR PDB; 6QT0; EM; 3.40 A; O=1-204.
DR PDB; 6QTZ; EM; 3.50 A; O=1-204.
DR PDB; 6R84; EM; 3.60 A; p=2-204.
DR PDB; 6R86; EM; 3.40 A; p=2-204.
DR PDB; 6R87; EM; 3.40 A; p=2-204.
DR PDB; 6RI5; EM; 3.30 A; O=1-204.
DR PDB; 6RZZ; EM; 3.20 A; O=1-204.
DR PDB; 6S05; EM; 3.90 A; O=1-204.
DR PDB; 6S47; EM; 3.28 A; AP=2-204.
DR PDB; 6SNT; EM; 2.80 A; t=1-204.
DR PDB; 6SV4; EM; 3.30 A; AQ/XQ/zQ=1-204.
DR PDB; 6T4Q; EM; 2.60 A; LN=2-204.
DR PDB; 6T7I; EM; 3.20 A; LN=1-204.
DR PDB; 6T7T; EM; 3.10 A; LN=1-204.
DR PDB; 6T83; EM; 4.00 A; Ny/Pa=1-204.
DR PDB; 6TB3; EM; 2.80 A; AQ=2-204.
DR PDB; 6TNU; EM; 3.10 A; AQ=2-204.
DR PDB; 6WOO; EM; 2.90 A; N=2-203.
DR PDB; 6XIQ; EM; 4.20 A; N=1-204.
DR PDB; 6XIR; EM; 3.20 A; N=1-204.
DR PDB; 6YLG; EM; 3.00 A; N=1-204.
DR PDB; 6YLH; EM; 3.10 A; N=1-204.
DR PDB; 6YLX; EM; 3.90 A; N=1-204.
DR PDB; 6YLY; EM; 3.80 A; N=1-204.
DR PDB; 6Z6J; EM; 3.40 A; LN=1-204.
DR PDB; 6Z6K; EM; 3.40 A; LN=1-204.
DR PDB; 7AZY; EM; 2.88 A; R=1-204.
DR PDB; 7B7D; EM; 3.30 A; LP=2-204.
DR PDB; 7BT6; EM; 3.12 A; N=1-204.
DR PDB; 7BTB; EM; 3.22 A; N=1-204.
DR PDB; 7NRC; EM; 3.90 A; LP=2-204.
DR PDB; 7NRD; EM; 4.36 A; LP=2-204.
DR PDB; 7OF1; EM; 3.10 A; N=1-204.
DR PDB; 7OH3; EM; 3.40 A; N=1-204.
DR PDB; 7OHP; EM; 3.90 A; N=1-204.
DR PDB; 7OHQ; EM; 3.10 A; N=1-204.
DR PDB; 7OHR; EM; 4.72 A; N=1-204.
DR PDB; 7OHS; EM; 4.38 A; N=1-204.
DR PDB; 7OHU; EM; 3.70 A; N=1-204.
DR PDB; 7OHV; EM; 3.90 A; N=1-204.
DR PDB; 7OHW; EM; 3.50 A; N=1-204.
DR PDB; 7OHX; EM; 3.30 A; N=1-204.
DR PDB; 7OHY; EM; 3.90 A; N=1-204.
DR PDB; 7OSA; X-ray; 3.00 A; eL15=1-204.
DR PDB; 7OSM; X-ray; 3.00 A; eL15=1-204.
DR PDB; 7RR5; EM; 3.23 A; LN=1-204.
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; 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; 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; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR PDBsum; 7OSA; -.
DR PDBsum; 7OSM; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P05748; -.
DR SMR; P05748; -.
DR BioGRID; 31303; 279.
DR IntAct; P05748; 27.
DR MINT; P05748; -.
DR STRING; 4932.YLR029C; -.
DR iPTMnet; P05748; -.
DR MaxQB; P05748; -.
DR PaxDb; P05748; -.
DR PRIDE; P05748; -.
DR EnsemblFungi; YLR029C_mRNA; YLR029C; YLR029C.
DR GeneID; 850716; -.
DR KEGG; sce:YLR029C; -.
DR SGD; S000004019; RPL15A.
DR VEuPathDB; FungiDB:YLR029C; -.
DR eggNOG; KOG1678; Eukaryota.
DR GeneTree; ENSGT00910000144184; -.
DR HOGENOM; CLU_080796_0_0_1; -.
DR InParanoid; P05748; -.
DR OMA; KYMQELY; -.
DR BioCyc; YEAST:G3O-32188-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; P05748; -.
DR PRO; PR:P05748; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P05748; 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; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR Gene3D; 3.40.1120.10; -; 1.
DR InterPro; IPR024794; Rbsml_L15e_core_dom_sf.
DR InterPro; IPR000439; Ribosomal_L15e.
DR InterPro; IPR020925; Ribosomal_L15e_CS.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR PANTHER; PTHR11847; PTHR11847; 1.
DR Pfam; PF00827; Ribosomal_L15e; 1.
DR SMART; SM01384; Ribosomal_L15e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS01194; RIBOSOMAL_L15E; 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:1544921,
FT ECO:0000269|PubMed:6814480"
FT CHAIN 2..204
FT /note="60S ribosomal protein L15-A"
FT /id="PRO_0000127566"
FT REGION 164..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 28
FT /note="W -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 204 AA; 24422 MW; 3913F9E4AB9ECA2C CRC64;
MGAYKYLEEL QRKKQSDVLR FLQRVRVWEY RQKNVIHRAA RPTRPDKARR LGYKAKQGFV
IYRVRVRRGN RKRPVPKGAT YGKPTNQGVN ELKYQRSLRA TAEERVGRRA ANLRVLNSYW
VNQDSTYKYF EVILVDPQHK AIRRDARYNW ICDPVHKHRE ARGLTATGKK SRGINKGHKF
NNTKAGRRKT WKRQNTLSLW RYRK
