RS22A_YEAST
ID RS22A_YEAST Reviewed; 130 AA.
AC P0C0W1; D6VW01; P04648;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=40S ribosomal protein S22-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP50;
DE AltName: Full=S24;
DE AltName: Full=Small ribosomal subunit protein uS8-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YP58;
DE AltName: Full=YS22;
GN Name=RPS22A {ECO:0000303|PubMed:9559554}; Synonyms=RPS24, RPS24A;
GN OrderedLocusNames=YJL190C; ORFNames=J0355;
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=4000930; DOI=10.1093/nar/13.3.701;
RA Leer R.J., van Raamsdonk-Duin M.M.C., Kraakman P., Mager W.H., Planta R.J.;
RT "The genes for yeast ribosomal proteins S24 and L46 are adjacent and
RT divergently transcribed.";
RL Nucleic Acids Res. 13:701-709(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 PROTEIN SEQUENCE OF 2-44.
RX PubMed=6814480; DOI=10.1021/bi00262a005;
RA Otaka E., Higo K., Osawa S.;
RT "Isolation of seventeen proteins and amino-terminal amino acid sequences of
RT eight proteins from cytoplasmic ribosomes of yeast.";
RL Biochemistry 21:4545-4550(1982).
RN [6]
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 [7]
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 [8]
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 [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 4-130, 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, 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 (4.00 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 [13]
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:22096102}.
CC -!- MISCELLANEOUS: Present with 40400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS8 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC {ECO:0000305}.
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DR EMBL; X01962; CAA25998.1; -; Genomic_DNA.
DR EMBL; X77688; CAA54770.1; -; Genomic_DNA.
DR EMBL; Z49465; CAA89485.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08617.1; -; Genomic_DNA.
DR PIR; A23082; R4BY24.
DR RefSeq; NP_012345.1; NM_001181623.1.
DR PDB; 3J6X; EM; 6.10 A; 22=1-130.
DR PDB; 3J6Y; EM; 6.10 A; 22=1-130.
DR PDB; 3J77; EM; 6.20 A; 22=1-130.
DR PDB; 3J78; EM; 6.30 A; 22=1-130.
DR PDB; 4U3M; X-ray; 3.00 A; D2/d2=2-130.
DR PDB; 4U3N; X-ray; 3.20 A; D2/d2=2-130.
DR PDB; 4U3U; X-ray; 2.90 A; D2/d2=2-130.
DR PDB; 4U4N; X-ray; 3.10 A; D2/d2=2-130.
DR PDB; 4U4O; X-ray; 3.60 A; D2/d2=2-130.
DR PDB; 4U4Q; X-ray; 3.00 A; D2/d2=2-130.
DR PDB; 4U4R; X-ray; 2.80 A; D2/d2=2-130.
DR PDB; 4U4U; X-ray; 3.00 A; D2/d2=2-130.
DR PDB; 4U4Y; X-ray; 3.20 A; D2/d2=2-130.
DR PDB; 4U4Z; X-ray; 3.10 A; D2/d2=2-130.
DR PDB; 4U50; X-ray; 3.20 A; D2/d2=2-130.
DR PDB; 4U51; X-ray; 3.20 A; D2/d2=2-130.
DR PDB; 4U52; X-ray; 3.00 A; D2/d2=2-130.
DR PDB; 4U53; X-ray; 3.30 A; D2/d2=2-130.
DR PDB; 4U55; X-ray; 3.20 A; D2/d2=2-130.
DR PDB; 4U56; X-ray; 3.45 A; D2/d2=2-130.
DR PDB; 4U6F; X-ray; 3.10 A; D2/d2=2-130.
DR PDB; 4V4B; EM; 11.70 A; AH=2-130.
DR PDB; 4V6I; EM; 8.80 A; AH=1-130.
DR PDB; 4V7R; X-ray; 4.00 A; AO/CO=1-130.
DR PDB; 4V88; X-ray; 3.00 A; AW/CW=1-130.
DR PDB; 4V8Y; EM; 4.30 A; AW=1-130.
DR PDB; 4V8Z; EM; 6.60 A; AW=1-130.
DR PDB; 4V92; EM; 3.70 A; W=2-130.
DR PDB; 5DAT; X-ray; 3.15 A; D2=2-130, d2=2-130.
DR PDB; 5DC3; X-ray; 3.25 A; D2/d2=2-130.
DR PDB; 5DGE; X-ray; 3.45 A; D2/d2=2-130.
DR PDB; 5DGF; X-ray; 3.30 A; D2/d2=2-130.
DR PDB; 5DGV; X-ray; 3.10 A; D2/d2=2-130.
DR PDB; 5FCI; X-ray; 3.40 A; D2/d2=2-130.
DR PDB; 5FCJ; X-ray; 3.10 A; D2/d2=2-130.
DR PDB; 5I4L; X-ray; 3.10 A; D2/d2=2-130.
DR PDB; 5JPQ; EM; 7.30 A; z=1-130.
DR PDB; 5JUO; EM; 4.00 A; TB=1-130.
DR PDB; 5JUP; EM; 3.50 A; TB=1-130.
DR PDB; 5JUS; EM; 4.20 A; TB=1-130.
DR PDB; 5JUT; EM; 4.00 A; TB=1-130.
DR PDB; 5JUU; EM; 4.00 A; TB=1-130.
DR PDB; 5LL6; EM; 3.90 A; b=1-130.
DR PDB; 5LYB; X-ray; 3.25 A; D2/d2=2-130.
DR PDB; 5M1J; EM; 3.30 A; W2=2-130.
DR PDB; 5MC6; EM; 3.80 A; b=1-130.
DR PDB; 5MEI; X-ray; 3.50 A; X/d2=2-130.
DR PDB; 5NDG; X-ray; 3.70 A; D2/d2=2-130.
DR PDB; 5NDV; X-ray; 3.30 A; D2/d2=2-130.
DR PDB; 5NDW; X-ray; 3.70 A; D2/d2=2-130.
DR PDB; 5OBM; X-ray; 3.40 A; D2/d2=2-130.
DR PDB; 5ON6; X-ray; 3.10 A; X/d2=2-130.
DR PDB; 5TBW; X-ray; 3.00 A; X/d2=2-130.
DR PDB; 5TGA; X-ray; 3.30 A; D2/d2=2-130.
DR PDB; 5TGM; X-ray; 3.50 A; D2/d2=2-130.
DR PDB; 5TZS; EM; 5.10 A; E=1-130.
DR PDB; 5WLC; EM; 3.80 A; LE=1-130.
DR PDB; 5WYJ; EM; 8.70 A; SX=1-130.
DR PDB; 5WYK; EM; 4.50 A; SX=1-130.
DR PDB; 6EML; EM; 3.60 A; b=1-130.
DR PDB; 6FAI; EM; 3.40 A; W=1-130.
DR PDB; 6GQ1; EM; 4.40 A; AM=2-130.
DR PDB; 6GQB; EM; 3.90 A; AM=2-130.
DR PDB; 6GQV; EM; 4.00 A; AM=2-130.
DR PDB; 6HHQ; X-ray; 3.10 A; X/d2=1-130.
DR PDB; 6I7O; EM; 5.30 A; b/bb=2-130.
DR PDB; 6Q8Y; EM; 3.10 A; b=2-130.
DR PDB; 6RBD; EM; 3.47 A; W=1-130.
DR PDB; 6RBE; EM; 3.80 A; W=1-130.
DR PDB; 6S47; EM; 3.28 A; BX=2-130.
DR PDB; 6SNT; EM; 2.80 A; W=1-130.
DR PDB; 6SV4; EM; 3.30 A; b/bb/bc=1-130.
DR PDB; 6T4Q; EM; 2.60 A; SW=2-130.
DR PDB; 6T7I; EM; 3.20 A; SW=1-130.
DR PDB; 6T7T; EM; 3.10 A; SW=1-130.
DR PDB; 6T83; EM; 4.00 A; Wb/x=1-130.
DR PDB; 6TB3; EM; 2.80 A; b=2-130.
DR PDB; 6TNU; EM; 3.10 A; b=2-130.
DR PDB; 6WDR; EM; 3.70 A; W=2-130.
DR PDB; 6WOO; EM; 2.90 A; WW=2-130.
DR PDB; 6Y7C; EM; 3.80 A; W=1-130.
DR PDB; 6Z6J; EM; 3.40 A; SW=1-130.
DR PDB; 6Z6K; EM; 3.40 A; SW=1-130.
DR PDB; 6ZCE; EM; 5.30 A; X=1-130.
DR PDB; 6ZQA; EM; 4.40 A; DW=1-130.
DR PDB; 6ZQB; EM; 3.90 A; DW=1-130.
DR PDB; 6ZQC; EM; 3.80 A; DW=1-130.
DR PDB; 6ZQD; EM; 3.80 A; DW=1-130.
DR PDB; 6ZQE; EM; 7.10 A; DW=1-130.
DR PDB; 6ZQF; EM; 4.90 A; DW=1-130.
DR PDB; 6ZQG; EM; 3.50 A; DW=1-130.
DR PDB; 6ZU9; EM; 6.20 A; b=1-130.
DR PDB; 6ZVI; EM; 3.00 A; E=2-130.
DR PDB; 7A1G; EM; 3.00 A; b=2-130.
DR PDB; 7AJT; EM; 4.60 A; DW=1-130.
DR PDB; 7AJU; EM; 3.80 A; DW=1-130.
DR PDB; 7B7D; EM; 3.30 A; b=2-130.
DR PDB; 7NRC; EM; 3.90 A; Sb=2-130.
DR PDB; 7NRD; EM; 4.36 A; Sb=2-130.
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; 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; 5JPQ; -.
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; 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; 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; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P0C0W1; -.
DR SMR; P0C0W1; -.
DR BioGRID; 33573; 642.
DR DIP; DIP-5473N; -.
DR IntAct; P0C0W1; 42.
DR MINT; P0C0W1; -.
DR STRING; 4932.YJL190C; -.
DR iPTMnet; P0C0W1; -.
DR MaxQB; P0C0W1; -.
DR PaxDb; P0C0W1; -.
DR PRIDE; P0C0W1; -.
DR TopDownProteomics; P0C0W1; -.
DR EnsemblFungi; YJL190C_mRNA; YJL190C; YJL190C.
DR GeneID; 853249; -.
DR KEGG; sce:YJL190C; -.
DR SGD; S000003726; RPS22A.
DR VEuPathDB; FungiDB:YJL190C; -.
DR eggNOG; KOG1754; Eukaryota.
DR GeneTree; ENSGT00950000183198; -.
DR HOGENOM; CLU_098428_1_1_1; -.
DR InParanoid; P0C0W1; -.
DR OMA; LPAKNFG; -.
DR BioCyc; YEAST:G3O-31622-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; P0C0W1; -.
DR PRO; PR:P0C0W1; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P0C0W1; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR HAMAP; MF_01302_A; Ribosomal_S8_A; 1.
DR InterPro; IPR000630; Ribosomal_S8.
DR InterPro; IPR035987; Ribosomal_S8_sf.
DR PANTHER; PTHR11758; PTHR11758; 1.
DR Pfam; PF00410; Ribosomal_S8; 1.
DR SUPFAM; SSF56047; SSF56047; 1.
DR PROSITE; PS00053; RIBOSOMAL_S8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:6814480"
FT CHAIN 2..130
FT /note="40S ribosomal protein S22-A"
FT /id="PRO_0000126623"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 130 AA; 14626 MW; ED34BEF6A5442CC9 CRC64;
MTRSSVLADA LNAINNAEKT GKRQVLIRPS SKVIIKFLQV MQKHGYIGEF EYIDDHRSGK
IVVQLNGRLN KCGVISPRFN VKIGDIEKWT ANLLPARQFG YVILTTSAGI MDHEEARRKH
VSGKILGFVY
