RL16A_YEAST
ID RL16A_YEAST Reviewed; 199 AA.
AC P26784; D6VVF4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=60S ribosomal protein L16-A {ECO:0000303|PubMed:14562095};
DE AltName: Full=L13a;
DE AltName: Full=L21;
DE AltName: Full=Large ribosomal subunit protein uL13-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP22;
DE AltName: Full=YL15;
GN Name=RPL16A {ECO:0000303|PubMed:14562095}; Synonyms=RPL13, RPL21A;
GN OrderedLocusNames=YIL133C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-26, AND ACETYLATION AT SER-2 BY NATA.
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 [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 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 [6]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-177, AND IDENTIFICATION BY
RP 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 [9]
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 [10]
RP 3D-STRUCTURE MODELING OF 2-147, 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 [11]
RP 3D-STRUCTURE MODELING OF 2-147, 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 [12]
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 [13]
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:1544921}.
CC -!- MISCELLANEOUS: Present with 43300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uL13 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000305}.
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DR EMBL; Z38059; CAA86145.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08420.1; -; Genomic_DNA.
DR PIR; S48401; S48401.
DR RefSeq; NP_012133.1; NM_001179481.1.
DR PDB; 3J6X; EM; 6.10 A; 56=1-199.
DR PDB; 3J6Y; EM; 6.10 A; 56=1-199.
DR PDB; 3J77; EM; 6.20 A; 66=1-199.
DR PDB; 3J78; EM; 6.30 A; 66=1-199.
DR PDB; 3JCT; EM; 3.08 A; O=1-199.
DR PDB; 4U3M; X-ray; 3.00 A; M6/m6=2-199.
DR PDB; 4U3N; X-ray; 3.20 A; M6/m6=2-199.
DR PDB; 4U3U; X-ray; 2.90 A; M6/m6=2-199.
DR PDB; 4U4N; X-ray; 3.10 A; M6/m6=2-199.
DR PDB; 4U4O; X-ray; 3.60 A; M6/m6=2-199.
DR PDB; 4U4Q; X-ray; 3.00 A; M6/m6=2-199.
DR PDB; 4U4R; X-ray; 2.80 A; M6/m6=2-199.
DR PDB; 4U4U; X-ray; 3.00 A; M6/m6=2-199.
DR PDB; 4U4Y; X-ray; 3.20 A; M6/m6=2-199.
DR PDB; 4U4Z; X-ray; 3.10 A; M6/m6=2-199.
DR PDB; 4U50; X-ray; 3.20 A; M6/m6=2-199.
DR PDB; 4U51; X-ray; 3.20 A; M6/m6=2-199.
DR PDB; 4U52; X-ray; 3.00 A; M6/m6=2-199.
DR PDB; 4U53; X-ray; 3.30 A; M6/m6=2-199.
DR PDB; 4U55; X-ray; 3.20 A; M6/m6=2-199.
DR PDB; 4U56; X-ray; 3.45 A; M6/m6=2-199.
DR PDB; 4U6F; X-ray; 3.10 A; M6/m6=2-199.
DR PDB; 4V4B; EM; 11.70 A; BM=2-147.
DR PDB; 4V6I; EM; 8.80 A; BK=1-199.
DR PDB; 4V7F; EM; 8.70 A; J=1-199.
DR PDB; 4V7R; X-ray; 4.00 A; BP/DP=1-199.
DR PDB; 4V88; X-ray; 3.00 A; BO/DO=1-199.
DR PDB; 4V8T; EM; 8.10 A; O=1-199.
DR PDB; 4V8Y; EM; 4.30 A; BO=2-199.
DR PDB; 4V8Z; EM; 6.60 A; BO=2-199.
DR PDB; 4V91; EM; 3.70 A; O=1-199.
DR PDB; 5APN; EM; 3.91 A; O=1-199.
DR PDB; 5APO; EM; 3.41 A; O=1-199.
DR PDB; 5DAT; X-ray; 3.15 A; M6/m6=2-199.
DR PDB; 5DC3; X-ray; 3.25 A; M6/m6=2-199.
DR PDB; 5DGE; X-ray; 3.45 A; M6/m6=2-199.
DR PDB; 5DGF; X-ray; 3.30 A; M6/m6=2-199.
DR PDB; 5DGV; X-ray; 3.10 A; M6/m6=2-199.
DR PDB; 5FCI; X-ray; 3.40 A; M6/m6=2-199.
DR PDB; 5FCJ; X-ray; 3.10 A; M6/m6=2-199.
DR PDB; 5FL8; EM; 9.50 A; O=1-199.
DR PDB; 5GAK; EM; 3.88 A; Q=1-199.
DR PDB; 5H4P; EM; 3.07 A; O=1-199.
DR PDB; 5I4L; X-ray; 3.10 A; M6/m6=3-199.
DR PDB; 5JCS; EM; 9.50 A; O=1-199.
DR PDB; 5JUO; EM; 4.00 A; T=1-199.
DR PDB; 5JUP; EM; 3.50 A; T=1-199.
DR PDB; 5JUS; EM; 4.20 A; T=1-199.
DR PDB; 5JUT; EM; 4.00 A; T=1-199.
DR PDB; 5JUU; EM; 4.00 A; T=1-199.
DR PDB; 5LYB; X-ray; 3.25 A; M6/m6=3-199.
DR PDB; 5M1J; EM; 3.30 A; K5=3-199.
DR PDB; 5MC6; EM; 3.80 A; AU=1-199.
DR PDB; 5MEI; X-ray; 3.50 A; CQ/w=3-199.
DR PDB; 5NDG; X-ray; 3.70 A; M6/m6=3-199.
DR PDB; 5NDV; X-ray; 3.30 A; M6/m6=3-199.
DR PDB; 5NDW; X-ray; 3.70 A; M6/m6=3-199.
DR PDB; 5OBM; X-ray; 3.40 A; M6/m6=3-199.
DR PDB; 5ON6; X-ray; 3.10 A; CQ/w=3-199.
DR PDB; 5T62; EM; 3.30 A; b=1-199.
DR PDB; 5T6R; EM; 4.50 A; b=1-199.
DR PDB; 5TBW; X-ray; 3.00 A; CQ/w=3-199.
DR PDB; 5TGA; X-ray; 3.30 A; M6/m6=3-199.
DR PDB; 5TGM; X-ray; 3.50 A; M6/m6=3-199.
DR PDB; 5Z3G; EM; 3.65 A; S=1-199.
DR PDB; 6C0F; EM; 3.70 A; O=1-199.
DR PDB; 6CB1; EM; 4.60 A; O=1-199.
DR PDB; 6ELZ; EM; 3.30 A; O=1-199.
DR PDB; 6EM1; EM; 3.60 A; O=1-199.
DR PDB; 6EM3; EM; 3.20 A; O=1-199.
DR PDB; 6EM4; EM; 4.10 A; O=1-199.
DR PDB; 6EM5; EM; 4.30 A; O=1-199.
DR PDB; 6FT6; EM; 3.90 A; O=1-199.
DR PDB; 6GQ1; EM; 4.40 A; O=3-199.
DR PDB; 6GQB; EM; 3.90 A; O=3-199.
DR PDB; 6GQV; EM; 4.00 A; O=3-199.
DR PDB; 6HD7; EM; 3.40 A; Q=1-199.
DR PDB; 6HHQ; X-ray; 3.10 A; CQ/w=1-199.
DR PDB; 6I7O; EM; 5.30 A; AU/XU=3-199.
DR PDB; 6M62; EM; 3.20 A; O=1-199.
DR PDB; 6N8J; EM; 3.50 A; O=1-199.
DR PDB; 6N8K; EM; 3.60 A; O=1-199.
DR PDB; 6N8L; EM; 3.60 A; O=1-199.
DR PDB; 6N8M; EM; 3.50 A; b=1-199.
DR PDB; 6N8N; EM; 3.80 A; b=1-199.
DR PDB; 6N8O; EM; 3.50 A; b=1-199.
DR PDB; 6OIG; EM; 3.80 A; O=3-199.
DR PDB; 6Q8Y; EM; 3.10 A; AU=3-199.
DR PDB; 6R84; EM; 3.60 A; Q=3-199.
DR PDB; 6R86; EM; 3.40 A; Q=3-199.
DR PDB; 6R87; EM; 3.40 A; Q=3-199.
DR PDB; 6S47; EM; 3.28 A; AQ=2-199.
DR PDB; 6SNT; EM; 2.80 A; u=1-199.
DR PDB; 6SV4; EM; 3.30 A; AU/XU/zU=1-199.
DR PDB; 6T4Q; EM; 2.60 A; LO=3-199.
DR PDB; 6T7I; EM; 3.20 A; LO=1-199.
DR PDB; 6T7T; EM; 3.10 A; LO=1-199.
DR PDB; 6T83; EM; 4.00 A; Oy/Qa=1-199.
DR PDB; 6TB3; EM; 2.80 A; AU=3-199.
DR PDB; 6TNU; EM; 3.10 A; AU=3-199.
DR PDB; 6WOO; EM; 2.90 A; O=3-199.
DR PDB; 6XIQ; EM; 4.20 A; O=1-199.
DR PDB; 6XIR; EM; 3.20 A; O=1-199.
DR PDB; 6YLG; EM; 3.00 A; O=1-199.
DR PDB; 6YLH; EM; 3.10 A; O=1-199.
DR PDB; 6YLX; EM; 3.90 A; O=1-199.
DR PDB; 6YLY; EM; 3.80 A; O=1-199.
DR PDB; 6Z6J; EM; 3.40 A; LO=1-199.
DR PDB; 6Z6K; EM; 3.40 A; LO=1-199.
DR PDB; 7AZY; EM; 2.88 A; V=1-199.
DR PDB; 7B7D; EM; 3.30 A; LQ=3-199.
DR PDB; 7BT6; EM; 3.12 A; O=1-199.
DR PDB; 7BTB; EM; 3.22 A; O=1-199.
DR PDB; 7NRC; EM; 3.90 A; LQ=3-199.
DR PDB; 7NRD; EM; 4.36 A; LQ=3-199.
DR PDB; 7OF1; EM; 3.10 A; O=1-199.
DR PDB; 7OH3; EM; 3.40 A; O=1-199.
DR PDB; 7OHP; EM; 3.90 A; O=1-199.
DR PDB; 7OHQ; EM; 3.10 A; O=1-199.
DR PDB; 7OHR; EM; 4.72 A; O=1-199.
DR PDB; 7OHS; EM; 4.38 A; O=1-199.
DR PDB; 7OHT; EM; 4.70 A; O=1-199.
DR PDB; 7OHU; EM; 3.70 A; O=1-199.
DR PDB; 7OHV; EM; 3.90 A; O=1-199.
DR PDB; 7OHW; EM; 3.50 A; O=1-199.
DR PDB; 7OHX; EM; 3.30 A; O=1-199.
DR PDB; 7OHY; EM; 3.90 A; O=1-199.
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; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
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; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; P26784; -.
DR SMR; P26784; -.
DR BioGRID; 34858; 376.
DR IntAct; P26784; 42.
DR MINT; P26784; -.
DR STRING; 4932.YIL133C; -.
DR CarbonylDB; P26784; -.
DR iPTMnet; P26784; -.
DR MaxQB; P26784; -.
DR PaxDb; P26784; -.
DR PRIDE; P26784; -.
DR EnsemblFungi; YIL133C_mRNA; YIL133C; YIL133C.
DR GeneID; 854673; -.
DR KEGG; sce:YIL133C; -.
DR SGD; S000001395; RPL16A.
DR VEuPathDB; FungiDB:YIL133C; -.
DR eggNOG; KOG3204; Eukaryota.
DR GeneTree; ENSGT00390000010799; -.
DR HOGENOM; CLU_076922_0_0_1; -.
DR InParanoid; P26784; -.
DR OMA; RGPFHHR; -.
DR BioCyc; YEAST:G3O-31384-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 ChiTaRS; RPL16A; yeast.
DR EvolutionaryTrace; P26784; -.
DR PRO; PR:P26784; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P26784; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR CDD; cd00392; Ribosomal_L13; 1.
DR Gene3D; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR005755; Ribosomal_L13_euk/arc.
DR InterPro; IPR036899; Ribosomal_L13_sf.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR PANTHER; PTHR11545:SF3; PTHR11545:SF3; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01077; L13_A_E; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1544921"
FT CHAIN 2..199
FT /note="60S ribosomal protein L16-A"
FT /id="PRO_0000133791"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1544921"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 14
FT /note="H -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="S -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 110..114
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 150..185
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 199 AA; 22201 MW; DAB11B0D4A91EF0B CRC64;
MSVEPVVVID GKGHLVGRLA SVVAKQLLNG QKIVVVRAEE LNISGEFFRN KLKYHDFLRK
ATAFNKTRGP FHFRAPSRIF YKALRGMVSH KTARGKAALE RLKVFEGIPP PYDKKKRVVV
PQALRVLRLK PGRKYTTLGK LSTSVGWKYE DVVAKLEAKR KVSSAEYYAK KRAFTKKVAS
ANATAAESDV AKQLAALGY
