RS30A_YEAST
ID RS30A_YEAST Reviewed; 63 AA.
AC P0CX33; D6VYT3; Q12087;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=40S ribosomal protein S30-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Small ribosomal subunit protein eS30-A {ECO:0000303|PubMed:24524803};
GN Name=RPS30A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YLR287C-A;
GN ORFNames=L8003.23, YLR287BC;
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 / MRNA], PROTEIN SEQUENCE, AND MASS
RP SPECTROMETRY.
RC STRAIN=YRB141;
RX PubMed=8662789; DOI=10.1074/jbc.271.23.13549;
RA Baker R.T., Williamson N.A., Wettenhall R.E.H.;
RT "The yeast homolog of mammalian ribosomal protein S30 is expressed from a
RT duplicated gene without a ubiquitin-like protein fusion sequence.
RT Evolutionary implications.";
RL J. Biol. Chem. 271:13549-13555(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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.
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-16 AND THR-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
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 [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 (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 -!- MASS SPECTROMETRY: Mass=6987; Mass_error=3.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8662789};
CC -!- MISCELLANEOUS: Present with 37600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS30 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS30 family.
CC {ECO:0000305}.
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DR EMBL; U48700; AAC49317.1; -; Genomic_DNA.
DR EMBL; U48699; AAC49316.1; -; mRNA.
DR EMBL; U17243; AAB67333.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09599.1; -; Genomic_DNA.
DR PIR; S67074; S67074.
DR RefSeq; NP_013390.1; NM_001182175.1.
DR RefSeq; NP_014825.3; NM_001183601.3.
DR PDB; 3J16; EM; -; E=1-63.
DR PDB; 3J6X; EM; 6.10 A; 30=1-63.
DR PDB; 3J6Y; EM; 6.10 A; 30=1-63.
DR PDB; 3J77; EM; 6.20 A; 30=1-63.
DR PDB; 3J78; EM; 6.30 A; 30=1-63.
DR PDB; 4U3M; X-ray; 3.00 A; E0=2-61, e0=2-63.
DR PDB; 4U3N; X-ray; 3.20 A; E0=2-61, e0=2-63.
DR PDB; 4U3U; X-ray; 2.90 A; E0=2-61, e0=2-63.
DR PDB; 4U4N; X-ray; 3.10 A; E0=2-61, e0=2-63.
DR PDB; 4U4O; X-ray; 3.60 A; E0=2-61, e0=2-63.
DR PDB; 4U4Q; X-ray; 3.00 A; E0=2-61, e0=2-63.
DR PDB; 4U4R; X-ray; 2.80 A; E0=2-61, e0=2-63.
DR PDB; 4U4U; X-ray; 3.00 A; E0=2-61, e0=2-63.
DR PDB; 4U4Y; X-ray; 3.20 A; E0=2-61, e0=2-63.
DR PDB; 4U4Z; X-ray; 3.10 A; E0=2-61, e0=2-63.
DR PDB; 4U50; X-ray; 3.20 A; E0=2-61, e0=2-63.
DR PDB; 4U51; X-ray; 3.20 A; E0=2-61, e0=2-63.
DR PDB; 4U52; X-ray; 3.00 A; E0/e0=2-61.
DR PDB; 4U53; X-ray; 3.30 A; E0=2-61, e0=2-63.
DR PDB; 4U55; X-ray; 3.20 A; E0=2-61, e0=2-63.
DR PDB; 4U56; X-ray; 3.45 A; E0=2-61, e0=2-63.
DR PDB; 4U6F; X-ray; 3.10 A; E0=2-61, e0=2-63.
DR PDB; 4V6I; EM; 8.80 A; AZ=1-63.
DR PDB; 4V88; X-ray; 3.00 A; Ae/Ce=1-63.
DR PDB; 4V8Y; EM; 4.30 A; A4=1-63.
DR PDB; 4V8Z; EM; 6.60 A; A4=1-63.
DR PDB; 4V92; EM; 3.70 A; e=7-61.
DR PDB; 5DAT; X-ray; 3.15 A; E0/e0=2-63.
DR PDB; 5DC3; X-ray; 3.25 A; E0/e0=2-63.
DR PDB; 5DGE; X-ray; 3.45 A; E0=2-61, e0=2-63.
DR PDB; 5DGF; X-ray; 3.30 A; E0/e0=2-63.
DR PDB; 5DGV; X-ray; 3.10 A; E0=2-61, e0=2-63.
DR PDB; 5FCI; X-ray; 3.40 A; E0/e0=2-63.
DR PDB; 5FCJ; X-ray; 3.10 A; E0/e0=2-63.
DR PDB; 5I4L; X-ray; 3.10 A; E0/e0=2-63.
DR PDB; 5JUO; EM; 4.00 A; BC=1-63.
DR PDB; 5JUP; EM; 3.50 A; BC=1-63.
DR PDB; 5JUS; EM; 4.20 A; BC=1-63.
DR PDB; 5JUT; EM; 4.00 A; BC=1-63.
DR PDB; 5JUU; EM; 4.00 A; BC=1-63.
DR PDB; 5LL6; EM; 3.90 A; g=1-63.
DR PDB; 5LYB; X-ray; 3.25 A; E0/e0=2-63.
DR PDB; 5M1J; EM; 3.30 A; e2=2-61.
DR PDB; 5MC6; EM; 3.80 A; g=1-63.
DR PDB; 5MEI; X-ray; 3.50 A; e0/f=2-63.
DR PDB; 5NDG; X-ray; 3.70 A; E0/e0=2-61.
DR PDB; 5NDV; X-ray; 3.30 A; E0/e0=2-63.
DR PDB; 5NDW; X-ray; 3.70 A; E0/e0=2-62.
DR PDB; 5OBM; X-ray; 3.40 A; E0/e0=2-63.
DR PDB; 5ON6; X-ray; 3.10 A; e0/f=2-63.
DR PDB; 5TBW; X-ray; 3.00 A; e0/f=2-63.
DR PDB; 5TGA; X-ray; 3.30 A; E0/e0=2-63.
DR PDB; 5TGM; X-ray; 3.50 A; E0/e0=2-63.
DR PDB; 5WYJ; EM; 8.70 A; Sf=1-63.
DR PDB; 5WYK; EM; 4.50 A; Sf=1-63.
DR PDB; 6EML; EM; 3.60 A; g=1-63.
DR PDB; 6FAI; EM; 3.40 A; e=1-63.
DR PDB; 6GQ1; EM; 4.40 A; AU=2-61.
DR PDB; 6GQB; EM; 3.90 A; AU=2-61.
DR PDB; 6GQV; EM; 4.00 A; AU=2-61.
DR PDB; 6HHQ; X-ray; 3.10 A; e0/f=1-63.
DR PDB; 6I7O; EM; 5.30 A; g/gb=2-61.
DR PDB; 6Q8Y; EM; 3.10 A; g=2-61.
DR PDB; 6RBD; EM; 3.47 A; e=1-63.
DR PDB; 6RBE; EM; 3.80 A; e=1-63.
DR PDB; 6S47; EM; 3.28 A; Bf=2-63.
DR PDB; 6SNT; EM; 2.80 A; e=1-63.
DR PDB; 6SV4; EM; 3.30 A; g/gb/gc=1-63.
DR PDB; 6T4Q; EM; 2.60 A; Se=2-61.
DR PDB; 6T7I; EM; 3.20 A; Se=1-63.
DR PDB; 6T7T; EM; 3.10 A; Se=1-63.
DR PDB; 6T83; EM; 4.00 A; 5/eb=1-63.
DR PDB; 6TB3; EM; 2.80 A; g=2-61.
DR PDB; 6TNU; EM; 3.10 A; g=2-61.
DR PDB; 6WDR; EM; 3.70 A; e=1-63.
DR PDB; 6WOO; EM; 2.90 A; ee=9-61.
DR PDB; 6XIQ; EM; 4.20 A; AU=1-63.
DR PDB; 6Y7C; EM; 3.80 A; e=1-63.
DR PDB; 6Z6J; EM; 3.40 A; Se=1-63.
DR PDB; 6Z6K; EM; 3.40 A; Se=1-63.
DR PDB; 6ZCE; EM; 5.30 A; f=1-63.
DR PDB; 6ZU9; EM; 6.20 A; g=1-63.
DR PDB; 6ZVI; EM; 3.00 A; P=2-47.
DR PDB; 7A1G; EM; 3.00 A; g=2-61.
DR PDB; 7B7D; EM; 3.30 A; g=2-61.
DR PDB; 7NRC; EM; 3.90 A; Sg=5-61.
DR PDB; 7NRD; EM; 4.36 A; Sg=2-45.
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; 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; 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; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX33; -.
DR SMR; P0CX33; -.
DR BioGRID; 31553; 253.
DR BioGRID; 34577; 185.
DR IntAct; P0CX33; 11.
DR MINT; P0CX33; -.
DR STRING; 4932.YLR287C-A; -.
DR iPTMnet; P0CX33; -.
DR PaxDb; P0CX33; -.
DR PRIDE; P0CX33; -.
DR TopDownProteomics; P0CX33; -.
DR EnsemblFungi; YLR287C-A_mRNA; YLR287C-A; YLR287C-A.
DR EnsemblFungi; YOR182C_mRNA; YOR182C; YOR182C.
DR GeneID; 850994; -.
DR GeneID; 854354; -.
DR KEGG; sce:YLR287C-A; -.
DR KEGG; sce:YOR182C; -.
DR SGD; S000004278; RPS30A.
DR VEuPathDB; FungiDB:YLR287C-A; -.
DR VEuPathDB; FungiDB:YOR182C; -.
DR eggNOG; KOG0009; Eukaryota.
DR HOGENOM; CLU_010412_5_1_1; -.
DR InParanoid; P0CX33; -.
DR OMA; KKGYNTQ; -.
DR BioCyc; YEAST:G3O-32382-MON; -.
DR PRO; PR:P0CX33; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P0CX33; protein.
DR ExpressionAtlas; P0CX33; baseline and differential.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR InterPro; IPR006846; Ribosomal_S30.
DR Pfam; PF04758; Ribosomal_S30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..63
FT /note="40S ribosomal protein S30-A"
FT /id="PRO_0000174009"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT TURN 9..15
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7A1G"
SQ SEQUENCE 63 AA; 7118 MW; 658C4C1D8D9F88CB CRC64;
MAKVHGSLAR AGKVKSQTPK VEKTEKPKKP KGRAYKRLLY TRRFVNVTLV NGKRRMNPGP
SVQ
