RS23A_YEAST
ID RS23A_YEAST Reviewed; 145 AA.
AC P0CX29; D6VUP9; P32827;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=40S ribosomal protein S23-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP37;
DE AltName: Full=S28;
DE AltName: Full=Small ribosomal subunit protein uS12-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS14;
GN Name=RPS23A {ECO:0000303|PubMed:9559554}; Synonyms=RPS28A;
GN OrderedLocusNames=YGR118W; ORFNames=G6178;
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=8496146; DOI=10.1016/s0021-9258(18)82058-0;
RA Alksne L.E., Warner J.R.;
RT "A novel cloning strategy reveals the gene for the yeast homologue to
RT Escherichia coli ribosomal protein S12.";
RL J. Biol. Chem. 268:10813-10819(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8905931;
RX DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT element and 11 new open reading frames.";
RL Yeast 12:1273-1277(1996).
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 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-56, 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 [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 HYDROXYLATION AT PRO-64, AND MUTAGENESIS OF PRO-64 AND ASN-65.
RX PubMed=24550462; DOI=10.1073/pnas.1311750111;
RA Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
RA Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J.,
RA Wolf A., Schofield C.J.;
RT "Hydroxylation of the eukaryotic ribosomal decoding center affects
RT translational accuracy.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
RN [11]
RP 3D-STRUCTURE MODELING OF 28-145, 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 OF 28-145, 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 (4.00 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 (3.00 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: Hydroxylation at Pro-64 affects translation termination
CC efficiency. The stereochemistry of the 3,4-dihydroxyproline has not yet
CC been determined. {ECO:0000269|PubMed:24550462}.
CC -!- MISCELLANEOUS: Present with 10600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS12 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; M96570; AAA16235.1; -; Unassigned_RNA.
DR EMBL; Z72903; CAA97128.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08210.1; -; Genomic_DNA.
DR PIR; A46703; A46703.
DR RefSeq; NP_011633.3; NM_001181247.3.
DR RefSeq; NP_015457.1; NM_001184229.1.
DR PDB; 3J6X; EM; 6.10 A; 23=1-145.
DR PDB; 3J6Y; EM; 6.10 A; 23=1-145.
DR PDB; 3J77; EM; 6.20 A; 23=1-145.
DR PDB; 3J78; EM; 6.30 A; 23=1-145.
DR PDB; 4U3M; X-ray; 3.00 A; D3/d3=2-145.
DR PDB; 4U3N; X-ray; 3.20 A; D3/d3=2-145.
DR PDB; 4U3U; X-ray; 2.90 A; D3/d3=2-145.
DR PDB; 4U4N; X-ray; 3.10 A; D3/d3=2-145.
DR PDB; 4U4O; X-ray; 3.60 A; D3/d3=2-145.
DR PDB; 4U4Q; X-ray; 3.00 A; D3/d3=2-145.
DR PDB; 4U4R; X-ray; 2.80 A; D3/d3=2-145.
DR PDB; 4U4U; X-ray; 3.00 A; D3/d3=2-145.
DR PDB; 4U4Y; X-ray; 3.20 A; D3/d3=2-145.
DR PDB; 4U4Z; X-ray; 3.10 A; D3/d3=2-145.
DR PDB; 4U50; X-ray; 3.20 A; D3/d3=2-145.
DR PDB; 4U51; X-ray; 3.20 A; D3/d3=2-145.
DR PDB; 4U52; X-ray; 3.00 A; D3/d3=2-145.
DR PDB; 4U53; X-ray; 3.30 A; D3/d3=2-145.
DR PDB; 4U55; X-ray; 3.20 A; D3/d3=2-145.
DR PDB; 4U56; X-ray; 3.45 A; D3/d3=2-145.
DR PDB; 4U6F; X-ray; 3.10 A; D3/d3=2-145.
DR PDB; 4V4B; EM; 11.70 A; AL=28-145.
DR PDB; 4V6I; EM; 8.80 A; AL=1-145.
DR PDB; 4V7H; EM; 8.90 A; L=28-145.
DR PDB; 4V7R; X-ray; 4.00 A; AP/CP=1-145.
DR PDB; 4V88; X-ray; 3.00 A; AX/CX=1-145.
DR PDB; 4V8Y; EM; 4.30 A; AX=1-145.
DR PDB; 4V8Z; EM; 6.60 A; AX=1-145.
DR PDB; 4V92; EM; 3.70 A; X=2-143.
DR PDB; 5DAT; X-ray; 3.15 A; D3/d3=2-145.
DR PDB; 5DC3; X-ray; 3.25 A; D3/d3=2-145.
DR PDB; 5DGE; X-ray; 3.45 A; D3/d3=2-145.
DR PDB; 5DGF; X-ray; 3.30 A; D3/d3=2-145.
DR PDB; 5DGV; X-ray; 3.10 A; D3/d3=2-145.
DR PDB; 5FCI; X-ray; 3.40 A; D3/d3=2-145.
DR PDB; 5FCJ; X-ray; 3.10 A; D3/d3=2-145.
DR PDB; 5I4L; X-ray; 3.10 A; D3/d3=2-145.
DR PDB; 5JUO; EM; 4.00 A; UB=1-145.
DR PDB; 5JUP; EM; 3.50 A; UB=1-145.
DR PDB; 5JUS; EM; 4.20 A; UB=1-145.
DR PDB; 5JUT; EM; 4.00 A; UB=1-145.
DR PDB; 5JUU; EM; 4.00 A; UB=1-145.
DR PDB; 5LL6; EM; 3.90 A; c=1-145.
DR PDB; 5M1J; EM; 3.30 A; X2=2-145.
DR PDB; 5MC6; EM; 3.80 A; c=1-145.
DR PDB; 5MEI; X-ray; 3.50 A; Y/d3=2-145.
DR PDB; 5NDG; X-ray; 3.70 A; D3/d3=2-145.
DR PDB; 5NDV; X-ray; 3.30 A; D3/d3=2-145.
DR PDB; 5NDW; X-ray; 3.70 A; D3/d3=2-145.
DR PDB; 5OBM; X-ray; 3.40 A; D3/d3=2-145.
DR PDB; 5ON6; X-ray; 3.10 A; Y/d3=2-145.
DR PDB; 5TBW; X-ray; 3.00 A; Y/d3=2-145.
DR PDB; 5TGA; X-ray; 3.30 A; D3/d3=2-145.
DR PDB; 5TZS; EM; 5.10 A; r=1-145.
DR PDB; 5WYJ; EM; 8.70 A; SY=1-145.
DR PDB; 5WYK; EM; 4.50 A; SY=1-145.
DR PDB; 6EML; EM; 3.60 A; c=1-145.
DR PDB; 6FAI; EM; 3.40 A; X=1-145.
DR PDB; 6GQ1; EM; 4.40 A; AN=2-145.
DR PDB; 6GQB; EM; 3.90 A; AN=2-145.
DR PDB; 6GQV; EM; 4.00 A; AN=2-145.
DR PDB; 6HHQ; X-ray; 3.10 A; Y/d3=1-145.
DR PDB; 6I7O; EM; 5.30 A; c/cb=2-145.
DR PDB; 6KE6; EM; 3.40 A; SY=1-145.
DR PDB; 6LQP; EM; 3.20 A; SY=1-145.
DR PDB; 6LQQ; EM; 4.10 A; SY=1-145.
DR PDB; 6LQR; EM; 8.60 A; SY=1-145.
DR PDB; 6LQS; EM; 3.80 A; SY=1-145.
DR PDB; 6LQT; EM; 4.90 A; SY=1-145.
DR PDB; 6LQU; EM; 3.70 A; SY=1-145.
DR PDB; 6LQV; EM; 4.80 A; SY=1-145.
DR PDB; 6Q8Y; EM; 3.10 A; c=2-145.
DR PDB; 6RBD; EM; 3.47 A; X=1-145.
DR PDB; 6RBE; EM; 3.80 A; X=1-145.
DR PDB; 6S47; EM; 3.28 A; BY=2-145.
DR PDB; 6SNT; EM; 2.80 A; X=1-145.
DR PDB; 6SV4; EM; 3.30 A; c/cb/cc=1-145.
DR PDB; 6T4Q; EM; 2.60 A; SX=2-145.
DR PDB; 6T7I; EM; 3.20 A; SX=1-145.
DR PDB; 6T7T; EM; 3.10 A; SX=1-145.
DR PDB; 6T83; EM; 4.00 A; Xb/y=1-145.
DR PDB; 6TB3; EM; 2.80 A; c=2-145.
DR PDB; 6TNU; EM; 3.10 A; c=2-145.
DR PDB; 6WDR; EM; 3.70 A; X=2-145.
DR PDB; 6WOO; EM; 2.90 A; XX=1-144.
DR PDB; 6XIQ; EM; 4.20 A; AN=1-145.
DR PDB; 6XIR; EM; 3.20 A; AN=1-145.
DR PDB; 6Y7C; EM; 3.80 A; X=1-145.
DR PDB; 6Z6J; EM; 3.40 A; SX=1-145.
DR PDB; 6Z6K; EM; 3.40 A; SX=1-145.
DR PDB; 6ZCE; EM; 5.30 A; Y=1-145.
DR PDB; 6ZQA; EM; 4.40 A; DX=1-145.
DR PDB; 6ZQB; EM; 3.90 A; DX=1-145.
DR PDB; 6ZQC; EM; 3.80 A; DX=1-145.
DR PDB; 6ZQD; EM; 3.80 A; DX=1-145.
DR PDB; 6ZQE; EM; 7.10 A; DX=1-145.
DR PDB; 6ZQF; EM; 4.90 A; DX=1-145.
DR PDB; 6ZQG; EM; 3.50 A; DX=1-145.
DR PDB; 6ZU9; EM; 6.20 A; c=1-145.
DR PDB; 6ZVI; EM; 3.00 A; H=2-145.
DR PDB; 7A1G; EM; 3.00 A; c=2-145.
DR PDB; 7AJT; EM; 4.60 A; DX=1-145.
DR PDB; 7AJU; EM; 3.80 A; DX=1-145.
DR PDB; 7B7D; EM; 3.30 A; c=2-145.
DR PDB; 7D4I; EM; 4.00 A; SY=1-145.
DR PDB; 7D5S; EM; 4.60 A; SY=1-145.
DR PDB; 7D5T; EM; 6.00 A; SY=1-145.
DR PDB; 7D63; EM; 12.30 A; SY=1-145.
DR PDB; 7NRC; EM; 3.90 A; Sc=2-145.
DR PDB; 7NRD; EM; 4.36 A; Sc=2-145.
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; 4V7H; -.
DR PDBsum; 4V7R; -.
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; 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; 5TZS; -.
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; 6ZQA; -.
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; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0CX29; -.
DR SMR; P0CX29; -.
DR BioGRID; 33363; 233.
DR BioGRID; 36298; 86.
DR IntAct; P0CX29; 11.
DR MINT; P0CX29; -.
DR STRING; 4932.YGR118W; -.
DR iPTMnet; P0CX29; -.
DR MaxQB; P0CX29; -.
DR PaxDb; P0CX29; -.
DR PRIDE; P0CX29; -.
DR EnsemblFungi; YGR118W_mRNA; YGR118W; YGR118W.
DR EnsemblFungi; YPR132W_mRNA; YPR132W; YPR132W.
DR GeneID; 853015; -.
DR GeneID; 856250; -.
DR KEGG; sce:YGR118W; -.
DR KEGG; sce:YPR132W; -.
DR SGD; S000003350; RPS23A.
DR VEuPathDB; FungiDB:YGR118W; -.
DR VEuPathDB; FungiDB:YPR132W; -.
DR eggNOG; KOG1749; Eukaryota.
DR HOGENOM; CLU_115574_0_1_1; -.
DR InParanoid; P0CX29; -.
DR OMA; KFRWSQR; -.
DR BioCyc; YEAST:G3O-30825-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 EvolutionaryTrace; P0CX29; -.
DR PRO; PR:P0CX29; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P0CX29; protein.
DR ExpressionAtlas; P0CX29; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:1990145; P:maintenance of translational fidelity; IDA:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd03367; Ribosomal_S23; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006032; Ribosomal_S12/S23.
DR InterPro; IPR005680; Ribosomal_S23_euk/arc.
DR PANTHER; PTHR11652; PTHR11652; 1.
DR Pfam; PF00164; Ribosom_S12_S23; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00982; uS12_E_A; 1.
DR PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydroxylation; Isopeptide bond;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..145
FT /note="40S ribosomal protein S23-A"
FT /id="PRO_0000146482"
FT MOD_RES 64
FT /note="3,4-dihydroxyproline"
FT /evidence="ECO:0000269|PubMed:24550462"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 64
FT /note="P->A: Lethal mutation."
FT /evidence="ECO:0000269|PubMed:24550462"
FT MUTAGEN 65
FT /note="N->A: Lethal mutation."
FT /evidence="ECO:0000269|PubMed:24550462"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 145 AA; 16038 MW; 5A89ADF540DA1311 CRC64;
MGKGKPRGLN SARKLRVHRR NNRWAENNYK KRLLGTAFKS SPFGGSSHAK GIVLEKLGIE
SKQPNSAIRK CVRVQLIKNG KKVTAFVPND GCLNFVDEND EVLLAGFGRK GKAKGDIPGV
RFKVVKVSGV SLLALWKEKK EKPRS
