RL24A_YEAST
ID RL24A_YEAST Reviewed; 155 AA.
AC P04449; A2TBN7; D6VUA7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=60S ribosomal protein L24-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L30;
DE AltName: Full=Large ribosomal subunit protein eL24-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP29;
DE AltName: Full=YL21;
GN Name=RPL24A {ECO:0000303|PubMed:9559554}; Synonyms=RP29, RPL30A;
GN OrderedLocusNames=YGL031C;
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=6086628; DOI=10.1016/s0021-9258(17)47288-7;
RA Mitra G., Warner J.R.;
RT "A yeast ribosomal protein gene whose intron is in the 5' leader.";
RL J. Biol. Chem. 259:9218-9224(1984).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [5]
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 [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 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 [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 4-56, 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 1-56, 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 -!- MISCELLANEOUS: Present with 247000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL24 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K02650; AAA35004.1; -; Genomic_DNA.
DR EMBL; Z72553; CAA96732.1; -; Genomic_DNA.
DR EMBL; EF123140; ABM97484.1; -; mRNA.
DR EMBL; BK006941; DAA08068.1; -; Genomic_DNA.
DR PIR; A02783; R6BYT9.
DR RefSeq; NP_011484.1; NM_001180896.1.
DR PDB; 2X7N; EM; 11.80 A; D=1-56.
DR PDB; 3J6X; EM; 6.10 A; 64=1-155.
DR PDB; 3J6Y; EM; 6.10 A; 64=1-155.
DR PDB; 3J77; EM; 6.20 A; 74=1-155.
DR PDB; 3J78; EM; 6.30 A; 74=1-155.
DR PDB; 4U3M; X-ray; 3.00 A; N4/n4=1-155.
DR PDB; 4U3N; X-ray; 3.20 A; N4/n4=1-155.
DR PDB; 4U3U; X-ray; 2.90 A; N4/n4=1-155.
DR PDB; 4U4N; X-ray; 3.10 A; N4/n4=1-155.
DR PDB; 4U4O; X-ray; 3.60 A; N4/n4=1-155.
DR PDB; 4U4Q; X-ray; 3.00 A; N4/n4=1-155.
DR PDB; 4U4R; X-ray; 2.80 A; N4/n4=1-155.
DR PDB; 4U4U; X-ray; 3.00 A; N4/n4=1-155.
DR PDB; 4U4Y; X-ray; 3.20 A; N4/n4=1-155.
DR PDB; 4U4Z; X-ray; 3.10 A; N4/n4=1-155.
DR PDB; 4U50; X-ray; 3.20 A; N4/n4=1-155.
DR PDB; 4U51; X-ray; 3.20 A; N4/n4=1-155.
DR PDB; 4U52; X-ray; 3.00 A; N4/n4=1-155.
DR PDB; 4U53; X-ray; 3.30 A; N4/n4=1-155.
DR PDB; 4U55; X-ray; 3.20 A; N4/n4=1-155.
DR PDB; 4U56; X-ray; 3.45 A; N4/n4=1-155.
DR PDB; 4U6F; X-ray; 3.10 A; N4/n4=1-155.
DR PDB; 4V4B; EM; 11.70 A; BS=1-56.
DR PDB; 4V6I; EM; 8.80 A; BZ=1-155.
DR PDB; 4V7R; X-ray; 4.00 A; BV/DV=1-155.
DR PDB; 4V88; X-ray; 3.00 A; BW/DW=1-155.
DR PDB; 4V8T; EM; 8.10 A; W=1-155.
DR PDB; 4V8Y; EM; 4.30 A; BW=1-155.
DR PDB; 4V8Z; EM; 6.60 A; BW=1-155.
DR PDB; 4V91; EM; 3.70 A; W=1-155.
DR PDB; 5APN; EM; 3.91 A; W=1-155.
DR PDB; 5APO; EM; 3.41 A; W=1-155.
DR PDB; 5DAT; X-ray; 3.15 A; N4/n4=1-155.
DR PDB; 5DC3; X-ray; 3.25 A; N4/n4=1-155.
DR PDB; 5DGE; X-ray; 3.45 A; N4/n4=1-155.
DR PDB; 5DGF; X-ray; 3.30 A; N4/n4=1-155.
DR PDB; 5DGV; X-ray; 3.10 A; N4/n4=1-155.
DR PDB; 5FCI; X-ray; 3.40 A; N4/n4=1-155.
DR PDB; 5FCJ; X-ray; 3.10 A; N4/n4=1-155.
DR PDB; 5GAK; EM; 3.88 A; Y=1-155.
DR PDB; 5H4P; EM; 3.07 A; W=1-155.
DR PDB; 5I4L; X-ray; 3.10 A; N4=1-98, n4=1-135.
DR PDB; 5JUO; EM; 4.00 A; BA=1-155.
DR PDB; 5JUP; EM; 3.50 A; BA=1-155.
DR PDB; 5JUS; EM; 4.20 A; BA=1-155.
DR PDB; 5JUT; EM; 4.00 A; BA=1-155.
DR PDB; 5JUU; EM; 4.00 A; BA=1-155.
DR PDB; 5LYB; X-ray; 3.25 A; N4=1-98, n4=1-135.
DR PDB; 5M1J; EM; 3.30 A; W5=1-98.
DR PDB; 5MC6; EM; 3.80 A; AE=1-155.
DR PDB; 5MEI; X-ray; 3.50 A; 7/CY=1-98.
DR PDB; 5NDG; X-ray; 3.70 A; N4/n4=1-155.
DR PDB; 5NDV; X-ray; 3.30 A; N4/n4=1-155.
DR PDB; 5NDW; X-ray; 3.70 A; N4/n4=1-155.
DR PDB; 5OBM; X-ray; 3.40 A; N4=1-155, n4=1-135.
DR PDB; 5ON6; X-ray; 3.10 A; 7/CY=1-98.
DR PDB; 5T62; EM; 3.30 A; j=1-155.
DR PDB; 5T6R; EM; 4.50 A; j=1-155.
DR PDB; 5TBW; X-ray; 3.00 A; 7/CY=1-98.
DR PDB; 5TGA; X-ray; 3.30 A; N4/n4=1-135.
DR PDB; 5TGM; X-ray; 3.50 A; N4=1-98, n4=1-135.
DR PDB; 6GQ1; EM; 4.40 A; W=1-63.
DR PDB; 6GQB; EM; 3.90 A; W=1-64.
DR PDB; 6GQV; EM; 4.00 A; W=1-62.
DR PDB; 6HD7; EM; 3.40 A; Y=1-155.
DR PDB; 6HHQ; X-ray; 3.10 A; 7/CY=1-155.
DR PDB; 6I7O; EM; 5.30 A; AE/XE=1-135.
DR PDB; 6N8M; EM; 3.50 A; j=1-155.
DR PDB; 6N8N; EM; 3.80 A; j=1-155.
DR PDB; 6N8O; EM; 3.50 A; j=1-155.
DR PDB; 6OIG; EM; 3.80 A; W=1-135.
DR PDB; 6Q8Y; EM; 3.10 A; AE=1-67.
DR PDB; 6QIK; EM; 3.10 A; v=1-155.
DR PDB; 6QT0; EM; 3.40 A; v=1-155.
DR PDB; 6QTZ; EM; 3.50 A; v=1-155.
DR PDB; 6R84; EM; 3.60 A; Y=1-62.
DR PDB; 6R86; EM; 3.40 A; Y=1-62.
DR PDB; 6R87; EM; 3.40 A; Y=1-62.
DR PDB; 6RI5; EM; 3.30 A; v=1-155.
DR PDB; 6RZZ; EM; 3.20 A; v=1-155.
DR PDB; 6S05; EM; 3.90 A; v=1-155.
DR PDB; 6S47; EM; 3.28 A; AY=1-155.
DR PDB; 6SNT; EM; 2.80 A; at=1-155.
DR PDB; 6SV4; EM; 3.30 A; AE/XE/zE=1-135.
DR PDB; 6T4Q; EM; 2.60 A; LW=1-126.
DR PDB; 6T7T; EM; 3.10 A; LW=1-155.
DR PDB; 6T83; EM; 4.00 A; H/Wy=1-155.
DR PDB; 6TB3; EM; 2.80 A; AE=1-126.
DR PDB; 6TNU; EM; 3.10 A; AE=1-126.
DR PDB; 6WOO; EM; 2.90 A; W=2-63.
DR PDB; 6Z6J; EM; 3.40 A; LW=1-155.
DR PDB; 6Z6K; EM; 3.40 A; LW=1-155.
DR PDB; 7AZY; EM; 2.88 A; f=1-155.
DR PDB; 7B7D; EM; 3.30 A; LS=1-126.
DR PDB; 7NRC; EM; 3.90 A; LY=1-65.
DR PDB; 7NRD; EM; 4.36 A; LY=1-61.
DR PDBsum; 2X7N; -.
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; 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; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
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; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P04449; -.
DR SMR; P04449; -.
DR BioGRID; 33215; 296.
DR IntAct; P04449; 27.
DR MINT; P04449; -.
DR STRING; 4932.YGL031C; -.
DR iPTMnet; P04449; -.
DR MaxQB; P04449; -.
DR PaxDb; P04449; -.
DR PRIDE; P04449; -.
DR EnsemblFungi; YGL031C_mRNA; YGL031C; YGL031C.
DR GeneID; 852852; -.
DR KEGG; sce:YGL031C; -.
DR SGD; S000002999; RPL24A.
DR VEuPathDB; FungiDB:YGL031C; -.
DR eggNOG; KOG1722; Eukaryota.
DR GeneTree; ENSGT00950000183105; -.
DR HOGENOM; CLU_106411_0_0_1; -.
DR InParanoid; P04449; -.
DR OMA; MKVETCV; -.
DR BioCyc; YEAST:G3O-30547-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; P04449; -.
DR PRO; PR:P04449; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P04449; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
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; IBA:GO_Central.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
DR Gene3D; 2.30.170.20; -; 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR000988; Ribosomal_L24e-rel.
DR InterPro; IPR023442; Ribosomal_L24e_CS.
DR PANTHER; PTHR10792; PTHR10792; 1.
DR Pfam; PF01246; Ribosomal_L24e; 1.
DR PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..155
FT /note="60S ribosomal protein L24-A"
FT /id="PRO_0000136894"
FT REGION 66..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24000"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4U4U"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 113..128
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 155 AA; 17614 MW; 9A79C4E409515716 CRC64;
MKVEIDSFSG AKIYPGRGTL FVRGDSKIFR FQNSKSASLF KQRKNPRRIA WTVLFRKHHK
KGITEEVAKK RSRKTVKAQR PITGASLDLI KERRSLKPEV RKANREEKLK ANKEKKKAEK
AARKAEKAKS AGTQSSKFSK QQAKGAFQKV AATSR
