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 27-MAR-2024, entry version 100. DE RecName: Full=Small ribosomal subunit protein uS12A {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S23-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=RP37; DE AltName: Full=S28; 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}. 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; 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; 7MPI; EM; 3.05 A; BX=2-145. DR PDB; 7MPJ; EM; 2.70 A; BX=2-145. DR PDB; 7N8B; EM; 3.05 A; BX=2-145. DR PDB; 7NRC; EM; 3.90 A; Sc=2-145. DR PDB; 7NRD; EM; 4.36 A; Sc=2-145. DR PDB; 7SUK; EM; 3.99 A; SR=41-144. DR PDB; 7WTL; EM; 3.30 A; SX=1-145. DR PDB; 7WTM; EM; 3.50 A; SX=1-145. DR PDB; 7WTN; EM; 3.40 A; SX=1-145. DR PDB; 7WTO; EM; 3.50 A; SX=1-145. DR PDB; 7WTP; EM; 3.80 A; SX=1-145. DR PDB; 7WTQ; EM; 3.70 A; SX=1-145. DR PDB; 7WTR; EM; 3.50 A; SX=1-145. DR PDB; 7ZPQ; EM; 3.47 A; AX=2-145. DR PDB; 7ZRS; EM; 4.80 A; AX=2-145. DR PDB; 7ZUW; EM; 4.30 A; AX=2-145. DR PDB; 7ZUX; EM; 2.50 A; DX=2-145. DR PDB; 7ZW0; EM; 2.40 A; sc=1-145. DR PDB; 8BQD; EM; 3.90 A; c=2-145. DR PDB; 8BQX; EM; 3.80 A; c=2-145. DR PDB; 8C00; EM; 2.90 A; c=1-145. DR PDB; 8C01; EM; 2.70 A; c=1-145. DR PDB; 8C83; EM; 3.00 A; c=1-145. DR PDB; 8CAH; EM; 3.00 A; c=1-145. DR PDB; 8CAS; EM; 3.30 A; c=1-145. DR PDB; 8CBJ; EM; 3.80 A; X=1-145. DR PDB; 8CCS; EM; 1.97 A; z=1-145. DR PDB; 8CDL; EM; 2.72 A; z=1-145. DR PDB; 8CDR; EM; 2.04 A; z=1-145. DR PDB; 8CEH; EM; 2.05 A; z=1-145. DR PDB; 8CF5; EM; 2.71 A; z=1-145. DR PDB; 8CG8; EM; 2.57 A; z=1-145. DR PDB; 8CGN; EM; 2.28 A; z=1-145. DR PDB; 8CIV; EM; 2.47 A; z=1-145. DR PDB; 8CKU; EM; 3.11 A; z=1-145. DR PDB; 8CMJ; EM; 3.79 A; z=1-145. DR PDB; 8EVQ; EM; 2.72 A; BX=1-145. DR PDB; 8EVR; EM; 2.87 A; BX=1-145. DR PDB; 8EVS; EM; 2.62 A; BX=1-145. DR PDB; 8EVT; EM; 2.20 A; BX=1-145. DR PDB; 8EWB; EM; 2.87 A; BX=1-145. DR PDB; 8EWC; EM; 2.45 A; BX=1-145. 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; 7MPI; -. DR PDBsum; 7MPJ; -. DR PDBsum; 7N8B; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7SUK; -. DR PDBsum; 7WTL; -. DR PDBsum; 7WTM; -. DR PDBsum; 7WTN; -. DR PDBsum; 7WTO; -. DR PDBsum; 7WTP; -. DR PDBsum; 7WTQ; -. DR PDBsum; 7WTR; -. DR PDBsum; 7ZPQ; -. DR PDBsum; 7ZRS; -. DR PDBsum; 7ZUW; -. DR PDBsum; 7ZUX; -. DR PDBsum; 7ZW0; -. DR PDBsum; 8BQD; -. DR PDBsum; 8BQX; -. DR PDBsum; 8C00; -. DR PDBsum; 8C01; -. DR PDBsum; 8C83; -. DR PDBsum; 8CAH; -. DR PDBsum; 8CAS; -. DR PDBsum; 8CBJ; -. DR PDBsum; 8CCS; -. DR PDBsum; 8CDL; -. DR PDBsum; 8CDR; -. DR PDBsum; 8CEH; -. DR PDBsum; 8CF5; -. DR PDBsum; 8CG8; -. DR PDBsum; 8CGN; -. DR PDBsum; 8CIV; -. DR PDBsum; 8CKU; -. DR PDBsum; 8CMJ; -. DR PDBsum; 8EVQ; -. DR PDBsum; 8EVR; -. DR PDBsum; 8EVS; -. DR PDBsum; 8EVT; -. DR PDBsum; 8EWB; -. DR PDBsum; 8EWC; -. DR AlphaFoldDB; P0CX29; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0949; -. DR EMDB; EMD-0950; -. DR EMDB; EMD-0951; -. DR EMDB; EMD-0952; -. DR EMDB; EMD-0953; -. DR EMDB; EMD-0954; -. DR EMDB; EMD-0955; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-10713; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11160; -. DR EMDB; EMD-11357; -. DR EMDB; EMD-11358; -. DR EMDB; EMD-11359; -. DR EMDB; EMD-11360; -. DR EMDB; EMD-11361; -. DR EMDB; EMD-11362; -. DR EMDB; EMD-11363; -. DR EMDB; EMD-11439; -. DR EMDB; EMD-11457; -. DR EMDB; EMD-11608; -. DR EMDB; EMD-11807; -. DR EMDB; EMD-11808; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16609; -. DR EMDB; EMD-16616; -. DR EMDB; EMD-16634; -. DR EMDB; EMD-16648; -. DR EMDB; EMD-16684; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-16729; -. DR EMDB; EMD-21644; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-22196; -. DR EMDB; EMD-22198; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-25441; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28636; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-28643; -. DR EMDB; EMD-30574; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-30585; -. DR EMDB; EMD-30588; -. DR EMDB; EMD-32790; -. DR EMDB; EMD-32791; -. DR EMDB; EMD-32792; -. DR EMDB; EMD-32793; -. DR EMDB; EMD-32794; -. DR EMDB; EMD-32795; -. DR EMDB; EMD-32796; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-4214; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4792; -. DR EMDB; EMD-4793; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-8473; -. DR EMDB; EMD-9964; -. DR SMR; P0CX29; -. DR BioGRID; 33363; 275. DR BioGRID; 36298; 91. DR IntAct; P0CX29; 11. DR MINT; P0CX29; -. DR STRING; 4932.YGR118W; -. DR iPTMnet; P0CX29; -. DR MaxQB; P0CX29; -. DR PaxDb; 4932-YGR118W; -. DR PeptideAtlas; 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 AGR; SGD:S000003350; -. 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 OrthoDB; 5480587at2759; -. DR BioCyc; YEAST:G3O-30825-MONOMER; -. 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-72649; Translation initiation complex formation. 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-9629569; Protein hydroxylation. 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 BioGRID-ORCS; 853015; 5 hits in 10 CRISPR screens. DR BioGRID-ORCS; 856250; 1 hit in 10 CRISPR screens. 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; Nucleic acid-binding proteins; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006032; Ribosomal_uS12. DR InterPro; IPR005680; Ribosomal_uS12_euk/arc. DR NCBIfam; TIGR00982; uS12_E_A; 1. DR PANTHER; PTHR11652; 30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER; 1. DR PANTHER; PTHR11652:SF14; 40S RIBOSOMAL PROTEIN S23; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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="Small ribosomal subunit protein uS12A" 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..22 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 27..34 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 36..39 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 47..60 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:6FAI" FT STRAND 68..76 FT /evidence="ECO:0007829|PDB:8C01" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:8C01" FT HELIX 90..95 FT /evidence="ECO:0007829|PDB:8C01" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:8C01" 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:8C01" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:6ZVI" FT HELIX 132..136 FT /evidence="ECO:0007829|PDB:8C01" SQ SEQUENCE 145 AA; 16038 MW; 5A89ADF540DA1311 CRC64; MGKGKPRGLN SARKLRVHRR NNRWAENNYK KRLLGTAFKS SPFGGSSHAK GIVLEKLGIE SKQPNSAIRK CVRVQLIKNG KKVTAFVPND GCLNFVDEND EVLLAGFGRK GKAKGDIPGV RFKVVKVSGV SLLALWKEKK EKPRS //