RS24A_YEAST
ID RS24A_YEAST Reviewed; 135 AA.
AC P0CX31; D3DLX9; P26782;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=40S ribosomal protein S24-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP50;
DE AltName: Full=Small ribosomal subunit protein eS24-A {ECO:0000303|PubMed:24524803};
GN Name=RPS24A {ECO:0000303|PubMed:9559554}; Synonyms=RPS24EA;
GN OrderedLocusNames=YER074W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 2-16, 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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-21, 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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.00 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 small ribosomal subunit (SSU). 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. Also partially
CC acetylated by NatC. {ECO:0000269|PubMed:10601260,
CC ECO:0000269|PubMed:1544921}.
CC -!- MISCELLANEOUS: There are 2 genes for eS24 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS24 family.
CC {ECO:0000305}.
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DR EMBL; U18814; AAB64613.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07733.1; -; Genomic_DNA.
DR PIR; S48410; S48410.
DR RefSeq; NP_010997.3; NM_001178965.3.
DR RefSeq; NP_012195.1; NM_001179419.1.
DR PDB; 3J16; EM; -; D=1-135.
DR PDB; 3J6X; EM; 6.10 A; 24=1-135.
DR PDB; 3J6Y; EM; 6.10 A; 24=1-135.
DR PDB; 3J77; EM; 6.20 A; 24=1-135.
DR PDB; 3J78; EM; 6.30 A; 24=1-135.
DR PDB; 4U3M; X-ray; 3.00 A; D4/d4=2-135.
DR PDB; 4U3N; X-ray; 3.20 A; D4/d4=2-135.
DR PDB; 4U3U; X-ray; 2.90 A; D4/d4=2-135.
DR PDB; 4U4N; X-ray; 3.10 A; D4/d4=2-135.
DR PDB; 4U4O; X-ray; 3.60 A; D4/d4=2-135.
DR PDB; 4U4Q; X-ray; 3.00 A; D4/d4=2-135.
DR PDB; 4U4R; X-ray; 2.80 A; D4/d4=2-135.
DR PDB; 4U4U; X-ray; 3.00 A; D4/d4=2-135.
DR PDB; 4U4Y; X-ray; 3.20 A; D4/d4=2-135.
DR PDB; 4U4Z; X-ray; 3.10 A; D4/d4=2-135.
DR PDB; 4U50; X-ray; 3.20 A; D4/d4=2-135.
DR PDB; 4U51; X-ray; 3.20 A; D4/d4=2-135.
DR PDB; 4U52; X-ray; 3.00 A; D4/d4=2-135.
DR PDB; 4U53; X-ray; 3.30 A; D4/d4=2-135.
DR PDB; 4U55; X-ray; 3.20 A; D4/d4=2-135.
DR PDB; 4U56; X-ray; 3.45 A; D4/d4=2-135.
DR PDB; 4U6F; X-ray; 3.10 A; D4/d4=2-135.
DR PDB; 4V6I; EM; 8.80 A; AU=1-135.
DR PDB; 4V88; X-ray; 3.00 A; AY/CY=1-135.
DR PDB; 4V8Y; EM; 4.30 A; AY=1-135.
DR PDB; 4V8Z; EM; 6.60 A; AY=1-135.
DR PDB; 4V92; EM; 3.70 A; Y=2-135.
DR PDB; 5DAT; X-ray; 3.15 A; D4/d4=2-135.
DR PDB; 5DC3; X-ray; 3.25 A; D4/d4=2-135.
DR PDB; 5DGE; X-ray; 3.45 A; D4/d4=2-135.
DR PDB; 5DGF; X-ray; 3.30 A; D4/d4=2-135.
DR PDB; 5DGV; X-ray; 3.10 A; D4/d4=2-135.
DR PDB; 5FCI; X-ray; 3.40 A; D4/d4=2-135.
DR PDB; 5FCJ; X-ray; 3.10 A; D4/d4=2-135.
DR PDB; 5I4L; X-ray; 3.10 A; D4/d4=2-135.
DR PDB; 5JUO; EM; 4.00 A; VB=1-135.
DR PDB; 5JUP; EM; 3.50 A; VB=1-135.
DR PDB; 5JUS; EM; 4.20 A; VB=1-135.
DR PDB; 5JUT; EM; 4.00 A; VB=1-135.
DR PDB; 5JUU; EM; 4.00 A; VB=1-135.
DR PDB; 5LL6; EM; 3.90 A; d=1-135.
DR PDB; 5LYB; X-ray; 3.25 A; D4/d4=2-135.
DR PDB; 5M1J; EM; 3.30 A; Y2=2-135.
DR PDB; 5MC6; EM; 3.80 A; d=1-135.
DR PDB; 5MEI; X-ray; 3.50 A; Z/d4=2-135.
DR PDB; 5NDG; X-ray; 3.70 A; D4/d4=2-135.
DR PDB; 5NDV; X-ray; 3.30 A; D4/d4=2-135.
DR PDB; 5NDW; X-ray; 3.70 A; D4/d4=2-135.
DR PDB; 5OBM; X-ray; 3.40 A; D4/d4=2-135.
DR PDB; 5ON6; X-ray; 3.10 A; Z/d4=2-135.
DR PDB; 5TBW; X-ray; 3.00 A; Z/d4=2-135.
DR PDB; 5TGA; X-ray; 3.30 A; D4/d4=2-135.
DR PDB; 5TGM; X-ray; 3.50 A; D4/d4=2-135.
DR PDB; 5TZS; EM; 5.10 A; F=1-135.
DR PDB; 5WLC; EM; 3.80 A; LF=1-135.
DR PDB; 5WYJ; EM; 8.70 A; SZ=1-135.
DR PDB; 5WYK; EM; 4.50 A; SZ=1-135.
DR PDB; 6EML; EM; 3.60 A; d=1-135.
DR PDB; 6FAI; EM; 3.40 A; Y=1-135.
DR PDB; 6GQ1; EM; 4.40 A; AO=2-135.
DR PDB; 6GQB; EM; 3.90 A; AO=2-135.
DR PDB; 6GQV; EM; 4.00 A; AO=2-135.
DR PDB; 6HHQ; X-ray; 3.10 A; Z/d4=1-135.
DR PDB; 6I7O; EM; 5.30 A; d/db=2-135.
DR PDB; 6KE6; EM; 3.40 A; SZ=1-135.
DR PDB; 6LQP; EM; 3.20 A; SZ=1-135.
DR PDB; 6LQQ; EM; 4.10 A; SZ=1-135.
DR PDB; 6LQR; EM; 8.60 A; SZ=1-135.
DR PDB; 6LQS; EM; 3.80 A; SZ=1-135.
DR PDB; 6LQT; EM; 4.90 A; SZ=1-135.
DR PDB; 6LQU; EM; 3.70 A; SZ=1-135.
DR PDB; 6LQV; EM; 4.80 A; SZ=1-135.
DR PDB; 6Q8Y; EM; 3.10 A; d=2-133.
DR PDB; 6RBD; EM; 3.47 A; Y=1-135.
DR PDB; 6RBE; EM; 3.80 A; Y=1-135.
DR PDB; 6S47; EM; 3.28 A; BZ=2-135.
DR PDB; 6SNT; EM; 2.80 A; Y=1-135.
DR PDB; 6SV4; EM; 3.30 A; d/db/dc=1-135.
DR PDB; 6T4Q; EM; 2.60 A; SY=2-135.
DR PDB; 6T7I; EM; 3.20 A; SY=1-135.
DR PDB; 6T7T; EM; 3.10 A; SY=1-135.
DR PDB; 6T83; EM; 4.00 A; Yb/z=1-135.
DR PDB; 6TB3; EM; 2.80 A; d=2-135.
DR PDB; 6TNU; EM; 3.10 A; d=2-135.
DR PDB; 6WDR; EM; 3.70 A; Y=2-135.
DR PDB; 6WOO; EM; 2.90 A; YY=2-135.
DR PDB; 6XIQ; EM; 4.20 A; AO=1-135.
DR PDB; 6XIR; EM; 3.20 A; AO=1-135.
DR PDB; 6Y7C; EM; 3.80 A; Y=1-135.
DR PDB; 6Z6J; EM; 3.40 A; SY=1-135.
DR PDB; 6Z6K; EM; 3.40 A; SY=1-135.
DR PDB; 6ZCE; EM; 5.30 A; Z=1-135.
DR PDB; 6ZQB; EM; 3.90 A; DY=1-135.
DR PDB; 6ZQC; EM; 3.80 A; DY=1-135.
DR PDB; 6ZQD; EM; 3.80 A; DY=1-135.
DR PDB; 6ZQE; EM; 7.10 A; DY=1-135.
DR PDB; 6ZQF; EM; 4.90 A; DY=1-135.
DR PDB; 6ZQG; EM; 3.50 A; DY=1-135.
DR PDB; 6ZU9; EM; 6.20 A; d=1-135.
DR PDB; 6ZVI; EM; 3.00 A; I=2-135.
DR PDB; 7A1G; EM; 3.00 A; d=2-135.
DR PDB; 7AJT; EM; 4.60 A; DY=1-135.
DR PDB; 7AJU; EM; 3.80 A; DY=1-135.
DR PDB; 7B7D; EM; 3.30 A; d=2-135.
DR PDB; 7D4I; EM; 4.00 A; SZ=1-135.
DR PDB; 7D5T; EM; 6.00 A; SZ=1-135.
DR PDB; 7D63; EM; 12.30 A; SZ=1-135.
DR PDB; 7NRC; EM; 3.90 A; Sd=2-135.
DR PDB; 7NRD; EM; 4.36 A; Sd=2-135.
DR PDBsum; 3J16; -.
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; 4V6I; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LL6; -.
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; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5TZS; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
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; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX31; -.
DR SMR; P0CX31; -.
DR BioGRID; 34923; 111.
DR BioGRID; 36817; 371.
DR IntAct; P0CX31; 60.
DR MINT; P0CX31; -.
DR STRING; 4932.YER074W; -.
DR CarbonylDB; P0CX31; -.
DR iPTMnet; P0CX31; -.
DR MaxQB; P0CX31; -.
DR PaxDb; P0CX31; -.
DR PRIDE; P0CX31; -.
DR TopDownProteomics; P0CX31; -.
DR EnsemblFungi; YER074W_mRNA; YER074W; YER074W.
DR EnsemblFungi; YIL069C_mRNA; YIL069C; YIL069C.
DR GeneID; 854741; -.
DR GeneID; 856805; -.
DR KEGG; sce:YER074W; -.
DR KEGG; sce:YIL069C; -.
DR SGD; S000000876; RPS24A.
DR VEuPathDB; FungiDB:YER074W; -.
DR VEuPathDB; FungiDB:YIL069C; -.
DR eggNOG; KOG3424; Eukaryota.
DR HOGENOM; CLU_107248_1_0_1; -.
DR InParanoid; P0CX31; -.
DR OMA; TFGFRTH; -.
DR BioCyc; YEAST:G3O-30245-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-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
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 PRO; PR:P0CX31; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P0CX31; protein.
DR ExpressionAtlas; P0CX31; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR HAMAP; MF_00545; Ribosomal_S24e; 1.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001976; Ribosomal_S24e.
DR InterPro; IPR018098; Ribosomal_S24e_CS.
DR PANTHER; PTHR10496; PTHR10496; 1.
DR Pfam; PF01282; Ribosomal_S24e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS00529; RIBOSOMAL_S24E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT CHAIN 2..135
FT /note="40S ribosomal protein S24-A"
FT /id="PRO_0000137636"
FT REGION 102..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921, ECO:0007744|PubMed:22814378"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 16
FT /note="P -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 135 AA; 15329 MW; 81B82D361207442A CRC64;
MSDAVTIRTR KVISNPLLAR KQFVVDVLHP NRANVSKDEL REKLAEVYKA EKDAVSVFGF
RTQFGGGKSV GFGLVYNSVA EAKKFEPTYR LVRYGLAEKV EKASRQQRKQ KKNRDKKIFG
TGKRLAKKVA RRNAD
