RL6A_YEAST
ID RL6A_YEAST Reviewed; 176 AA.
AC Q02326; D6VZA0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=60S ribosomal protein L6-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L17;
DE AltName: Full=Large ribosomal subunit protein eL6-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP18;
DE AltName: Full=YL16;
GN Name=RPL6A {ECO:0000303|PubMed:9559554}; Synonyms=RPL17A, YL16A;
GN OrderedLocusNames=YML073C;
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].
RX PubMed=1390890; DOI=10.1016/0167-4781(92)90011-n;
RA Hashimoto T., Suzuki K., Mizuta K., Otaka E.;
RT "Yeast ribosomal proteins: XIV. Complete nucleotide sequences of the two
RT genes encoding Saccharomyces cerevisiae YL16.";
RL Biochim. Biophys. Acta 1132:195-198(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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, AND ACETYLATION AT SER-2 BY NATA.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP 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 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 [10]
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 [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:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: Present with 37100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL6 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 family.
CC {ECO:0000305}.
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DR EMBL; D10225; BAA01077.1; -; Genomic_DNA.
DR EMBL; Z46373; CAA86505.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09824.1; -; Genomic_DNA.
DR PIR; S28944; S28944.
DR RefSeq; NP_013638.1; NM_001182432.1.
DR PDB; 3J6X; EM; 6.10 A; L6=1-176.
DR PDB; 3J6Y; EM; 6.10 A; L6=1-176.
DR PDB; 3J77; EM; 6.20 A; L6=1-176.
DR PDB; 3J78; EM; 6.30 A; L6=1-176.
DR PDB; 3JBS; EM; 2.90 A; A=1-176.
DR PDB; 3JCT; EM; 3.08 A; E=1-176.
DR PDB; 4U3M; X-ray; 3.00 A; L6/l6=2-176.
DR PDB; 4U3N; X-ray; 3.20 A; L6/l6=2-176.
DR PDB; 4U3U; X-ray; 2.90 A; L6/l6=2-176.
DR PDB; 4U4N; X-ray; 3.10 A; L6/l6=2-176.
DR PDB; 4U4O; X-ray; 3.60 A; L6/l6=2-176.
DR PDB; 4U4Q; X-ray; 3.00 A; L6/l6=2-176.
DR PDB; 4U4R; X-ray; 2.80 A; L6/l6=2-176.
DR PDB; 4U4U; X-ray; 3.00 A; L6/l6=2-176.
DR PDB; 4U4Y; X-ray; 3.20 A; L6/l6=2-176.
DR PDB; 4U4Z; X-ray; 3.10 A; L6/l6=2-176.
DR PDB; 4U50; X-ray; 3.20 A; L6/l6=2-176.
DR PDB; 4U51; X-ray; 3.20 A; L6/l6=2-176.
DR PDB; 4U52; X-ray; 3.00 A; L6/l6=2-176.
DR PDB; 4U53; X-ray; 3.30 A; L6/l6=2-176.
DR PDB; 4U55; X-ray; 3.20 A; L6/l6=2-176.
DR PDB; 4U56; X-ray; 3.45 A; L6/l6=2-176.
DR PDB; 4U6F; X-ray; 3.10 A; L6/l6=2-176.
DR PDB; 4V6I; EM; 8.80 A; BG=1-176.
DR PDB; 4V7F; EM; 8.70 A; G=1-176.
DR PDB; 4V7R; X-ray; 4.00 A; BF/DF=1-176.
DR PDB; 4V88; X-ray; 3.00 A; BE/DE=1-176.
DR PDB; 4V8T; EM; 8.10 A; E=1-176.
DR PDB; 4V8Y; EM; 4.30 A; BE=2-176.
DR PDB; 4V8Z; EM; 6.60 A; BE=2-176.
DR PDB; 4V91; EM; 3.70 A; E=1-176.
DR PDB; 5APN; EM; 3.91 A; E=1-176.
DR PDB; 5DAT; X-ray; 3.15 A; L6/l6=2-176.
DR PDB; 5DC3; X-ray; 3.25 A; L6/l6=2-176.
DR PDB; 5DGE; X-ray; 3.45 A; L6/l6=2-176.
DR PDB; 5DGF; X-ray; 3.30 A; L6/l6=2-176.
DR PDB; 5DGV; X-ray; 3.10 A; L6/l6=2-176.
DR PDB; 5FCI; X-ray; 3.40 A; L6/l6=2-176.
DR PDB; 5FCJ; X-ray; 3.10 A; L6/l6=2-176.
DR PDB; 5FL8; EM; 9.50 A; E=1-176.
DR PDB; 5GAK; EM; 3.88 A; I=1-176.
DR PDB; 5H4P; EM; 3.07 A; E=1-176.
DR PDB; 5I4L; X-ray; 3.10 A; L6/l6=1-176.
DR PDB; 5JCS; EM; 9.50 A; E=1-176.
DR PDB; 5JUO; EM; 4.00 A; J=1-176.
DR PDB; 5JUP; EM; 3.50 A; J=1-176.
DR PDB; 5JUS; EM; 4.20 A; J=1-176.
DR PDB; 5JUT; EM; 4.00 A; J=1-176.
DR PDB; 5JUU; EM; 4.00 A; J=1-176.
DR PDB; 5LYB; X-ray; 3.25 A; L6/l6=2-176.
DR PDB; 5M1J; EM; 3.30 A; E5=2-176.
DR PDB; 5MC6; EM; 3.80 A; BM=1-176.
DR PDB; 5MEI; X-ray; 3.50 A; CH/n=2-176.
DR PDB; 5NDG; X-ray; 3.70 A; L6/l6=1-176.
DR PDB; 5NDV; X-ray; 3.30 A; L6/l6=1-176.
DR PDB; 5NDW; X-ray; 3.70 A; L6/l6=1-176.
DR PDB; 5OBM; X-ray; 3.40 A; L6/l6=1-176.
DR PDB; 5ON6; X-ray; 3.10 A; CH/n=2-176.
DR PDB; 5T62; EM; 3.30 A; H=1-176.
DR PDB; 5T6R; EM; 4.50 A; H=1-176.
DR PDB; 5TBW; X-ray; 3.00 A; CH/n=2-176.
DR PDB; 5TGA; X-ray; 3.30 A; L6/l6=2-176.
DR PDB; 5TGM; X-ray; 3.50 A; L6/l6=2-176.
DR PDB; 5Z3G; EM; 3.65 A; I=1-176.
DR PDB; 6C0F; EM; 3.70 A; E=1-176.
DR PDB; 6CB1; EM; 4.60 A; E=1-176.
DR PDB; 6ELZ; EM; 3.30 A; E=1-176.
DR PDB; 6EM1; EM; 3.60 A; E=1-176.
DR PDB; 6EM3; EM; 3.20 A; E=1-176.
DR PDB; 6EM4; EM; 4.10 A; E=1-176.
DR PDB; 6EM5; EM; 4.30 A; E=1-176.
DR PDB; 6FT6; EM; 3.90 A; E=1-176.
DR PDB; 6GQ1; EM; 4.40 A; E=2-176.
DR PDB; 6GQB; EM; 3.90 A; E=2-176.
DR PDB; 6GQV; EM; 4.00 A; E=2-176.
DR PDB; 6HD7; EM; 3.40 A; I=1-176.
DR PDB; 6HHQ; X-ray; 3.10 A; CH/n=1-176.
DR PDB; 6I7O; EM; 5.30 A; BM/YM=1-176.
DR PDB; 6M62; EM; 3.20 A; E=1-176.
DR PDB; 6N8J; EM; 3.50 A; E=1-176.
DR PDB; 6N8K; EM; 3.60 A; E=1-176.
DR PDB; 6N8L; EM; 3.60 A; E=1-176.
DR PDB; 6N8M; EM; 3.50 A; H=1-176.
DR PDB; 6N8N; EM; 3.80 A; H=1-176.
DR PDB; 6N8O; EM; 3.50 A; H=1-176.
DR PDB; 6OIG; EM; 3.80 A; E=2-176.
DR PDB; 6Q8Y; EM; 3.10 A; BM=2-176.
DR PDB; 6QIK; EM; 3.10 A; G=1-176.
DR PDB; 6QT0; EM; 3.40 A; G=1-176.
DR PDB; 6QTZ; EM; 3.50 A; G=1-176.
DR PDB; 6R84; EM; 3.60 A; I=2-176.
DR PDB; 6R86; EM; 3.40 A; I=2-176.
DR PDB; 6R87; EM; 3.40 A; I=2-176.
DR PDB; 6RI5; EM; 3.30 A; G=1-176.
DR PDB; 6RZZ; EM; 3.20 A; G=1-176.
DR PDB; 6S05; EM; 3.90 A; G=1-176.
DR PDB; 6S47; EM; 3.28 A; AH=2-176.
DR PDB; 6SV4; EM; 3.30 A; BM/YM/ZM=1-176.
DR PDB; 6T83; EM; 4.00 A; Ey/Ha=1-176.
DR PDB; 6WOO; EM; 2.90 A; E=2-176.
DR PDB; 6XIQ; EM; 4.20 A; E=1-176.
DR PDB; 6XIR; EM; 3.20 A; E=1-176.
DR PDB; 6YLG; EM; 3.00 A; E=1-176.
DR PDB; 6YLH; EM; 3.10 A; E=1-176.
DR PDB; 6YLX; EM; 3.90 A; E=1-176.
DR PDB; 6YLY; EM; 3.80 A; E=1-176.
DR PDB; 6Z6J; EM; 3.40 A; LE=1-176.
DR PDB; 6Z6K; EM; 3.40 A; LE=1-176.
DR PDB; 7AZY; EM; 2.88 A; A=1-176.
DR PDB; 7BT6; EM; 3.12 A; E=1-176.
DR PDB; 7BTB; EM; 3.22 A; E=1-176.
DR PDB; 7OF1; EM; 3.10 A; E=1-176.
DR PDB; 7OH3; EM; 3.40 A; E=1-176.
DR PDB; 7OHP; EM; 3.90 A; E=1-176.
DR PDB; 7OHQ; EM; 3.10 A; E=1-176.
DR PDB; 7OHR; EM; 4.72 A; E=1-176.
DR PDB; 7OHS; EM; 4.38 A; E=1-176.
DR PDB; 7OHT; EM; 4.70 A; E=1-176.
DR PDB; 7OHU; EM; 3.70 A; E=1-176.
DR PDB; 7OHV; EM; 3.90 A; E=1-176.
DR PDB; 7OHW; EM; 3.50 A; E=1-176.
DR PDB; 7OHX; EM; 3.30 A; E=1-176.
DR PDB; 7OHY; EM; 3.90 A; E=1-176.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JBS; -.
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; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
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; 6SV4; -.
DR PDBsum; 6T83; -.
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; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; Q02326; -.
DR SMR; Q02326; -.
DR BioGRID; 35068; 193.
DR IntAct; Q02326; 39.
DR MINT; Q02326; -.
DR STRING; 4932.YML073C; -.
DR CarbonylDB; Q02326; -.
DR iPTMnet; Q02326; -.
DR MaxQB; Q02326; -.
DR PaxDb; Q02326; -.
DR PRIDE; Q02326; -.
DR EnsemblFungi; YML073C_mRNA; YML073C; YML073C.
DR GeneID; 854902; -.
DR KEGG; sce:YML073C; -.
DR SGD; S000004538; RPL6A.
DR VEuPathDB; FungiDB:YML073C; -.
DR eggNOG; KOG1694; Eukaryota.
DR GeneTree; ENSGT00390000003682; -.
DR HOGENOM; CLU_066767_2_1_1; -.
DR InParanoid; Q02326; -.
DR OMA; GPYEVNG; -.
DR BioCyc; YEAST:G3O-32667-MON; -.
DR PRO; PR:Q02326; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02326; 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 GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR CDD; cd13156; KOW_RPL6; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR000915; 60S_ribosomal_L6E.
DR InterPro; IPR041997; KOW_RPL6.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR10715; PTHR10715; 1.
DR Pfam; PF01159; Ribosomal_L6e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01170; RIBOSOMAL_L6E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..176
FT /note="60S ribosomal protein L6-A"
FT /id="PRO_0000171017"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P05739"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3JBS"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3JBS"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3JBS"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3JBS"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3JBS"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3JBS"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3JBS"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3JBS"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:3JBS"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:3JBS"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3JBS"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:3JBS"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:3JBS"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3JBS"
SQ SEQUENCE 176 AA; 19962 MW; 2E0AB1810D3AE121 CRC64;
MSAQKAPKWY PSEDVAALKK TRKAARPQKL RASLVPGTVL ILLAGRFRGK RVVYLKHLED
NTLLISGPFK VNGVPLRRVN ARYVIATSTK VSVEGVNVEK FNVEYFAKEK LTKKEKKEAN
LFPEQQNKEI KAERVEDQKV VDKALIAEIK KTPLLKQYLS ASFSLKNGDK PHMLKF
