RL28_YEAST
ID RL28_YEAST Reviewed; 149 AA.
AC P02406; D6VU43;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=60S ribosomal protein L28 {ECO:0000303|PubMed:9559554};
DE AltName: Full=L27a;
DE AltName: Full=L29;
DE AltName: Full=Large ribosomal subunit protein uL15 {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP44;
DE AltName: Full=RP62;
DE AltName: Full=YL24;
GN Name=RPL28 {ECO:0000303|PubMed:9559554}; Synonyms=CYH2;
GN OrderedLocusNames=YGL103W;
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 GLU-38.
RX PubMed=6304624; DOI=10.1093/nar/11.10.3123;
RA Kaufer N.F., Fried H.M., Schwindinger W.F., Jasin M., Warner J.R.;
RT "Cycloheximide resistance in yeast: the gene and its protein.";
RL Nucleic Acids Res. 11:3123-3135(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=3553182; DOI=10.1016/s0021-9258(18)45630-x;
RA Schwindinger W.F., Warner J.R.;
RT "Transcriptional elements of the yeast ribosomal protein gene CYH2.";
RL J. Biol. Chem. 262:5690-5695(1987).
RN [6]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=2104804; DOI=10.1002/j.1460-2075.1990.tb08084.x;
RA Underwood M.R., Fried H.M.;
RT "Characterization of nuclear localizing sequences derived from yeast
RT ribosomal protein L29.";
RL EMBO J. 9:91-99(1990).
RN [7]
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 [8]
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96, AND IDENTIFICATION BY MASS
RP 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 3D-STRUCTURE MODELING OF 6-148, 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 [12]
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 [13]
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 [14]
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; X01573; CAA25729.1; -; Genomic_DNA.
DR EMBL; Z72625; CAA96808.1; -; Genomic_DNA.
DR EMBL; M19490; AAA35002.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08004.1; -; Genomic_DNA.
DR PIR; A02782; R6BY29.
DR RefSeq; NP_011412.1; NM_001180968.1.
DR PDB; 3J6X; EM; 6.10 A; 68=1-149.
DR PDB; 3J6Y; EM; 6.10 A; 68=1-149.
DR PDB; 3J77; EM; 6.20 A; 78=1-149.
DR PDB; 3J78; EM; 6.30 A; 78=1-149.
DR PDB; 3JCT; EM; 3.08 A; a=1-149.
DR PDB; 4U3M; X-ray; 3.00 A; N8/n8=2-149.
DR PDB; 4U3N; X-ray; 3.20 A; N8/n8=2-149.
DR PDB; 4U3U; X-ray; 2.90 A; N8/n8=2-149.
DR PDB; 4U4N; X-ray; 3.10 A; N8/n8=2-149.
DR PDB; 4U4O; X-ray; 3.60 A; N8/n8=2-149.
DR PDB; 4U4Q; X-ray; 3.00 A; N8/n8=2-149.
DR PDB; 4U4R; X-ray; 2.80 A; N8/n8=2-149.
DR PDB; 4U4U; X-ray; 3.00 A; N8/n8=2-149.
DR PDB; 4U4Y; X-ray; 3.20 A; N8/n8=2-149.
DR PDB; 4U4Z; X-ray; 3.10 A; N8/n8=2-149.
DR PDB; 4U50; X-ray; 3.20 A; N8/n8=2-149.
DR PDB; 4U51; X-ray; 3.20 A; N8/n8=2-149.
DR PDB; 4U52; X-ray; 3.00 A; N8/n8=2-149.
DR PDB; 4U53; X-ray; 3.30 A; N8/n8=2-149.
DR PDB; 4U55; X-ray; 3.20 A; N8/n8=2-149.
DR PDB; 4U56; X-ray; 3.45 A; N8/n8=2-149.
DR PDB; 4U6F; X-ray; 3.10 A; N8/n8=2-149.
DR PDB; 4V4B; EM; 11.70 A; BV=2-149.
DR PDB; 4V6I; EM; 8.80 A; BO=1-149.
DR PDB; 4V7F; EM; 8.70 A; N=1-149.
DR PDB; 4V7R; X-ray; 4.00 A; BY/DY=1-149.
DR PDB; 4V88; X-ray; 3.00 A; Ba/Da=1-149.
DR PDB; 4V8T; EM; 8.10 A; a=1-149.
DR PDB; 4V8Y; EM; 4.30 A; Ba=2-149.
DR PDB; 4V8Z; EM; 6.60 A; Ba=2-149.
DR PDB; 4V91; EM; 3.70 A; a=1-149.
DR PDB; 5APN; EM; 3.91 A; a=1-149.
DR PDB; 5APO; EM; 3.41 A; a=1-149.
DR PDB; 5DAT; X-ray; 3.15 A; N8/n8=2-149.
DR PDB; 5DC3; X-ray; 3.25 A; N8/n8=2-149.
DR PDB; 5DGE; X-ray; 3.45 A; N8/n8=2-149.
DR PDB; 5DGF; X-ray; 3.30 A; N8/n8=2-149.
DR PDB; 5DGV; X-ray; 3.10 A; N8/n8=2-149.
DR PDB; 5FCI; X-ray; 3.40 A; N8/n8=2-149.
DR PDB; 5FCJ; X-ray; 3.10 A; N8/n8=2-149.
DR PDB; 5FL8; EM; 9.50 A; a=1-149.
DR PDB; 5GAK; EM; 3.88 A; c=1-149.
DR PDB; 5H4P; EM; 3.07 A; a=1-149.
DR PDB; 5I4L; X-ray; 3.10 A; N8/n8=2-149.
DR PDB; 5JCS; EM; 9.50 A; a=1-149.
DR PDB; 5JUO; EM; 4.00 A; FA=1-149.
DR PDB; 5JUP; EM; 3.50 A; FA=1-149.
DR PDB; 5JUS; EM; 4.20 A; FA=1-149.
DR PDB; 5JUT; EM; 4.00 A; FA=1-149.
DR PDB; 5JUU; EM; 4.00 A; FA=1-149.
DR PDB; 5LYB; X-ray; 3.25 A; N8/n8=2-149.
DR PDB; 5M1J; EM; 3.30 A; a5=2-149.
DR PDB; 5MC6; EM; 3.80 A; AR=1-149.
DR PDB; 5MEI; X-ray; 3.50 A; AB/DC=2-149.
DR PDB; 5NDG; X-ray; 3.70 A; N8/n8=2-149.
DR PDB; 5NDV; X-ray; 3.30 A; N8/n8=2-149.
DR PDB; 5NDW; X-ray; 3.70 A; N8/n8=2-149.
DR PDB; 5OBM; X-ray; 3.40 A; N8/n8=2-149.
DR PDB; 5ON6; X-ray; 3.10 A; AB/DC=2-149.
DR PDB; 5T62; EM; 3.30 A; n=1-149.
DR PDB; 5T6R; EM; 4.50 A; n=1-149.
DR PDB; 5TBW; X-ray; 3.00 A; AB/DC=2-149.
DR PDB; 5TGA; X-ray; 3.30 A; N8/n8=2-149.
DR PDB; 5TGM; X-ray; 3.50 A; N8/n8=2-149.
DR PDB; 6ELZ; EM; 3.30 A; a=1-149.
DR PDB; 6FT6; EM; 3.90 A; a=1-149.
DR PDB; 6GQ1; EM; 4.40 A; a=2-149.
DR PDB; 6GQB; EM; 3.90 A; a=2-149.
DR PDB; 6GQV; EM; 4.00 A; a=2-149.
DR PDB; 6HD7; EM; 3.40 A; c=1-149.
DR PDB; 6HHQ; X-ray; 3.10 A; AB/DC=1-149.
DR PDB; 6I7O; EM; 5.30 A; AR/XR=2-149.
DR PDB; 6M62; EM; 3.20 A; a=1-149.
DR PDB; 6N8J; EM; 3.50 A; a=1-149.
DR PDB; 6N8K; EM; 3.60 A; a=1-149.
DR PDB; 6N8L; EM; 3.60 A; a=1-149.
DR PDB; 6N8M; EM; 3.50 A; n=1-149.
DR PDB; 6N8N; EM; 3.80 A; n=1-149.
DR PDB; 6N8O; EM; 3.50 A; n=1-149.
DR PDB; 6OIG; EM; 3.80 A; a=2-149.
DR PDB; 6Q8Y; EM; 3.10 A; AR=2-149.
DR PDB; 6QIK; EM; 3.10 A; N=1-149.
DR PDB; 6QT0; EM; 3.40 A; N=1-149.
DR PDB; 6QTZ; EM; 3.50 A; N=1-149.
DR PDB; 6R84; EM; 3.60 A; c=2-149.
DR PDB; 6R86; EM; 3.40 A; c=2-149.
DR PDB; 6R87; EM; 3.40 A; c=2-149.
DR PDB; 6RI5; EM; 3.30 A; N=1-149.
DR PDB; 6RZZ; EM; 3.20 A; N=1-149.
DR PDB; 6S05; EM; 3.90 A; N=1-149.
DR PDB; 6S47; EM; 3.28 A; Ac=2-149.
DR PDB; 6SNT; EM; 2.80 A; ap=1-149.
DR PDB; 6SV4; EM; 3.30 A; AR/XR/zR=1-149.
DR PDB; 6T4Q; EM; 2.60 A; La=2-149.
DR PDB; 6T7I; EM; 3.20 A; La=1-149.
DR PDB; 6T7T; EM; 3.10 A; La=1-149.
DR PDB; 6T83; EM; 4.00 A; L/ay=1-149.
DR PDB; 6TB3; EM; 2.80 A; AR=2-149.
DR PDB; 6TNU; EM; 3.10 A; AR=2-149.
DR PDB; 6WOO; EM; 2.90 A; a=2-148.
DR PDB; 6XIQ; EM; 4.20 A; a=1-149.
DR PDB; 6XIR; EM; 3.20 A; a=1-149.
DR PDB; 6YLG; EM; 3.00 A; a=1-149.
DR PDB; 6YLH; EM; 3.10 A; a=1-149.
DR PDB; 6YLX; EM; 3.90 A; a=1-149.
DR PDB; 6YLY; EM; 3.80 A; a=1-149.
DR PDB; 6Z6J; EM; 3.40 A; La=1-149.
DR PDB; 6Z6K; EM; 3.40 A; La=1-149.
DR PDB; 7AZY; EM; 2.88 A; S=1-149.
DR PDB; 7B7D; EM; 3.30 A; LW=2-149.
DR PDB; 7BT6; EM; 3.12 A; a=1-149.
DR PDB; 7BTB; EM; 3.22 A; a=1-149.
DR PDB; 7NRC; EM; 3.90 A; Lc=2-149.
DR PDB; 7NRD; EM; 4.36 A; Lc=2-149.
DR PDB; 7OF1; EM; 3.10 A; a=1-149.
DR PDB; 7OH3; EM; 3.40 A; a=1-149.
DR PDB; 7OHQ; EM; 3.10 A; a=1-149.
DR PDB; 7OHV; EM; 3.90 A; a=1-149.
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; 6ELZ; -.
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; 7OHQ; -.
DR PDBsum; 7OHV; -.
DR AlphaFoldDB; P02406; -.
DR SMR; P02406; -.
DR BioGRID; 33147; 315.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR ELM; P02406; -.
DR IntAct; P02406; 36.
DR MINT; P02406; -.
DR STRING; 4932.YGL103W; -.
DR CarbonylDB; P02406; -.
DR iPTMnet; P02406; -.
DR MaxQB; P02406; -.
DR PaxDb; P02406; -.
DR PRIDE; P02406; -.
DR EnsemblFungi; YGL103W_mRNA; YGL103W; YGL103W.
DR GeneID; 852775; -.
DR KEGG; sce:YGL103W; -.
DR SGD; S000003071; RPL28.
DR VEuPathDB; FungiDB:YGL103W; -.
DR eggNOG; KOG1742; Eukaryota.
DR GeneTree; ENSGT00390000005534; -.
DR HOGENOM; CLU_109163_1_0_1; -.
DR InParanoid; P02406; -.
DR OMA; WGRVGQH; -.
DR BioCyc; YEAST:G3O-30602-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; P02406; -.
DR PRO; PR:P02406; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P02406; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IMP:SGD.
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 HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..149
FT /note="60S ribosomal protein L28"
FT /id="PRO_0000104904"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..13
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:2104804"
FT MOTIF 24..30
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:2104804"
FT COMPBIAS 1..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 38
FT /note="Q -> E (confers resistance to cycloheximide, an
FT inhibitor of polypeptide elongation)"
FT /evidence="ECO:0000269|PubMed:6304624"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 33..41
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 149 AA; 16722 MW; B34C325C01E14ACB CRC64;
MPSRFTKTRK HRGHVSAGKG RIGKHRKHPG GRGMAGGQHH HRINMDKYHP GYFGKVGMRY
FHKQQAHFWK PVLNLDKLWT LIPEDKRDQY LKSASKETAP VIDTLAAGYG KILGKGRIPN
VPVIVKARFV SKLAEEKIRA AGGVVELIA
