ID RS15A_RABIT Reviewed; 130 AA. AC G1TG89; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Small ribosomal subunit protein uS8; DE AltName: Full=40S ribosomal protein S15a; GN Name=RPS15A; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S., RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B., RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J., RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M., RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M., RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D., RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J., RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S., RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A., RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R., RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R., RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C., RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E., RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N., RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0007744|PDB:4KZX, ECO:0007744|PDB:4KZY} RP X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS) OF 40S RIBOSOME, FUNCTION, SUBUNIT, RP AND SUBCELLULAR LOCATION. RX PubMed=23873042; DOI=10.1038/nature12355; RA Lomakin I.B., Steitz T.A.; RT "The initiation of mammalian protein synthesis and mRNA scanning RT mechanism."; RL Nature 500:307-311(2013). RN [3] {ECO:0007744|PDB:4D5L, ECO:0007744|PDB:4D61} RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=25601755; DOI=10.1016/j.molcel.2014.12.016; RA Muhs M., Hilal T., Mielke T., Skabkin M.A., Sanbonmatsu K.Y., Pestova T.V., RA Spahn C.M.; RT "Cryo-EM of ribosomal 80S complexes with termination factors reveals the RT translocated cricket paralysis virus IRES."; RL Mol. Cell 57:422-432(2015). RN [4] {ECO:0007744|PDB:3JAG, ECO:0007744|PDB:3JAH} RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF 2-130 OF RIBOSOME, RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=26245381; DOI=10.1038/nature14896; RA Brown A., Shao S., Murray J., Hegde R.S., Ramakrishnan V.; RT "Structural basis for stop codon recognition in eukaryotes."; RL Nature 524:493-496(2015). RN [5] {ECO:0007744|PDB:5LZS, ECO:0007744|PDB:5LZT} RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046; RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.; RT "Decoding mammalian ribosome-mRNA states by translational GTPase RT complexes."; RL Cell 167:1229-1240(2016). RN [6] {ECO:0007744|PDB:6GZ3} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 2-130 OF RIBOSOME, RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=30517857; DOI=10.1016/j.celrep.2018.11.040; RA Flis J., Holm M., Rundlet E.J., Loerke J., Hilal T., Dabrowski M., RA Burger J., Mielke T., Blanchard S.C., Spahn C.M.T., Budkevich T.V.; RT "tRNA translocation by the eukaryotic 80S ribosome and the impact of GTP RT hydrolysis."; RL Cell Rep. 25:2676-2688(2018). RN [7] {ECO:0007744|PDB:6D90, ECO:0007744|PDB:6D9J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29856316; DOI=10.7554/elife.34062; RA Pisareva V.P., Pisarev A.V., Fernandez I.S.; RT "Dual tRNA mimicry in the Cricket paralysis virus IRES uncovers an RT unexpected similarity with the Hepatitis C Virus IRES."; RL Elife 7:0-0(2018). RN [8] {ECO:0007744|PDB:6MTB, ECO:0007744|PDB:6MTC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 2-130 OF RIBOSOME, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=30355441; DOI=10.7554/elife.40486; RA Brown A., Baird M.R., Yip M.C., Murray J., Shao S.; RT "Structures of translationally inactive mammalian ribosomes."; RL Elife 7:e40486-e40486(2018). RN [9] {ECO:0007744|PDB:6HCF, ECO:0007744|PDB:6HCJ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30293783; DOI=10.1016/j.molcel.2018.08.037; RA Juszkiewicz S., Chandrasekaran V., Lin Z., Kraatz S., Ramakrishnan V., RA Hegde R.S.; RT "ZNF598 is a quality control sensor of collided ribosomes."; RL Mol. Cell 72:469-481(2018). RN [10] {ECO:0007744|PDB:6R5Q, ECO:0007744|PDB:6R6G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 2-130 OF RIBOSOME, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=31246176; DOI=10.7554/elife.46267; RA Shanmuganathan V., Schiller N., Magoulopoulou A., Cheng J., Braunger K., RA Cymer F., Berninghausen O., Beatrix B., Kohno K., von Heijne G., RA Beckmann R.; RT "Structural and mutational analysis of the ribosome-arresting human RT XBP1u."; RL Elife 8:0-0(2019). RN [11] {ECO:0007744|PDB:6P4G, ECO:0007744|PDB:6P4H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=31609474; DOI=10.15252/embj.2019102226; RA Acosta-Reyes F., Neupane R., Frank J., Fernandez I.S.; RT "The Israeli acute paralysis virus IRES captures host ribosomes by RT mimicking a ribosomal state with hybrid tRNAs."; RL EMBO J. 38:e102226-e102226(2019). RN [12] {ECO:0007744|PDB:6SGC} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=31768042; DOI=10.1038/s41594-019-0331-x; RA Chandrasekaran V., Juszkiewicz S., Choi J., Puglisi J.D., Brown A., RA Shao S., Ramakrishnan V., Hegde R.S.; RT "Mechanism of ribosome stalling during translation of a poly(A) tail."; RL Nat. Struct. Mol. Biol. 26:1132-1140(2019). RN [13] {ECO:0007744|PDB:6ZVK, ECO:0007744|PDB:7A01} RP STRUCTURE BY ELECTRON MICROSCOPY (3.49 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=33296660; DOI=10.1016/j.celrep.2020.108476; RA Abaeva I.S., Vicens Q., Bochler A., Soufari H., Simonetti A., Pestova T.V., RA Hashem Y., Hellen C.U.T.; RT "The Halastavi arva virus intergenic region IRES promotes translation by RT the simplest possible initiation mechanism."; RL Cell Rep. 33:108476-108476(2020). RN [14] {ECO:0007744|PDB:6W2S, ECO:0007744|PDB:6W2T} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=32286223; DOI=10.7554/elife.54575; RA Neupane R., Pisareva V.P., Rodriguez C.F., Pisarev A.V., Fernandez I.S.; RT "A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S RT complex via an uAUG intermediate."; RL Elife 9:0-0(2020). RN [15] {ECO:0007744|PDB:7SYI, ECO:0007744|PDB:7SYJ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=35822879; DOI=10.15252/embj.2022110581; RA Brown Z.P., Abaeva I.S., De S., Hellen C.U.T., Pestova T.V., Frank J.; RT "Molecular architecture of 40S translation initiation complexes on the RT hepatitis C virus IRES."; RL EMBO J. 41:e110581-e110581(2022). RN [16] {ECO:0007744|PDB:7UCJ, ECO:0007744|PDB:7UCK} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=35679869; DOI=10.1016/j.molcel.2022.05.016; RA Arango D., Sturgill D., Yang R., Kanai T., Bauer P., Roy J., Wang Z., RA Hosogane M., Schiffers S., Oberdoerffer S.; RT "Direct epitranscriptomic regulation of mammalian translation initiation RT through N4-acetylcytidine."; RL Mol. Cell 82:2797-2814(2022). RN [17] {ECO:0007744|PDB:7ZJW, ECO:0007744|PDB:7ZJX} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=35709277; DOI=10.1126/science.abg3875; RA Hilal T., Killam B.Y., Grozdanovic M., Dobosz-Bartoszek M., Loerke J., RA Buerger J., Mielke T., Copeland P.R., Simonovic M., Spahn C.M.T.; RT "Structure of the mammalian ribosome as it decodes the selenocysteine UGA RT codon."; RL Science 376:1338-1343(2022). RN [18] {ECO:0007744|PDB:7OYD} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=36653451; DOI=10.1038/s41586-022-05623-y; RA Leesch F., Lorenzo-Orts L., Pribitzer C., Grishkovskaya I., Roehsner J., RA Chugunova A., Matzinger M., Roitinger E., Belacic K., Kandolf S., Lin T.Y., RA Mechtler K., Meinhart A., Haselbach D., Pauli A.; RT "A molecular network of conserved factors keeps ribosomes dormant in the RT egg."; RL Nature 613:712-720(2023). CC -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23873042, CC PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). CC Part of the small subunit (SSU) processome, first precursor of the CC small eukaryotic ribosomal subunit (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242, PubMed:30517857). During the assembly CC of the SSU processome in the nucleolus, many ribosome biogenesis CC factors, an RNA chaperone and ribosomal proteins associate with the CC nascent pre-rRNA and work in concert to generate RNA folding, CC modifications, rearrangements and cleavage as well as targeted CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:23873042, CC PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). CC Required for proper erythropoiesis (By similarity). CC {ECO:0000250|UniProtKB:P62244, ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30517857}. CC -!- SUBUNIT: Component of the 40S ribosomal subunit (PubMed:23873042, CC PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857, CC PubMed:29856316, PubMed:30355441, PubMed:30293783, PubMed:31246176, CC PubMed:31609474, PubMed:31768042, PubMed:33296660, PubMed:32286223, CC PubMed:35822879, PubMed:35679869, PubMed:35709277, PubMed:36653451). CC Part of the small subunit (SSU) processome, composed of more than 70 CC proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 CC (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, CC PubMed:30517857, PubMed:29856316, PubMed:30355441, PubMed:30293783, CC PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:33296660, CC PubMed:32286223, PubMed:35822879, PubMed:35679869, PubMed:35709277, CC PubMed:36653451). {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, CC ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, CC ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, CC ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, CC ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35709277, CC ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, CC ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, CC ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, CC ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, CC ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35709277, CC ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P62244}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 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; AAGW02057093; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02057094; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAGW02057095; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_008256009.1; XM_008257787.2. DR PDB; 3JAG; EM; 3.65 A; WW=2-130. DR PDB; 3JAH; EM; 3.45 A; WW=2-130. DR PDB; 3JAI; EM; 3.65 A; WW=2-130. DR PDB; 4D5L; EM; 9.00 A; W=1-130. DR PDB; 4D61; EM; 9.00 A; W=1-130. DR PDB; 4KZX; X-ray; 7.81 A; W=1-130. DR PDB; 4KZY; X-ray; 7.01 A; W=1-130. DR PDB; 4KZZ; X-ray; 7.03 A; W=1-130. DR PDB; 5K0Y; EM; 5.80 A; a=2-130. DR PDB; 5LZS; EM; 3.31 A; WW=1-130. DR PDB; 5LZT; EM; 3.65 A; WW=1-130. DR PDB; 5LZU; EM; 3.75 A; WW=1-130. DR PDB; 5LZV; EM; 3.35 A; WW=1-130. DR PDB; 5LZW; EM; 3.53 A; WW=1-130. DR PDB; 5LZX; EM; 3.67 A; WW=1-130. DR PDB; 5LZY; EM; 3.99 A; WW=1-130. DR PDB; 5LZZ; EM; 3.47 A; WW=1-130. DR PDB; 6D90; EM; 3.20 A; XX=1-130. DR PDB; 6D9J; EM; 3.20 A; XX=1-130. DR PDB; 6GZ3; EM; 3.60 A; BW=2-130. DR PDB; 6HCF; EM; 3.90 A; X1=1-130. DR PDB; 6HCJ; EM; 3.80 A; X2=1-130. DR PDB; 6HCM; EM; 6.80 A; X1=1-130. DR PDB; 6HCQ; EM; 6.50 A; X2=1-130. DR PDB; 6MTB; EM; 3.60 A; WW=2-130. DR PDB; 6MTC; EM; 3.40 A; WW=2-130. DR PDB; 6MTD; EM; 3.30 A; WW=2-130. DR PDB; 6MTE; EM; 3.40 A; WW=2-130. DR PDB; 6P4G; EM; 3.10 A; X=1-130. DR PDB; 6P4H; EM; 3.20 A; X=1-130. DR PDB; 6P5I; EM; 3.10 A; X=1-130. DR PDB; 6P5J; EM; 3.10 A; X=1-130. DR PDB; 6P5K; EM; 3.10 A; X=1-130. DR PDB; 6P5N; EM; 3.20 A; X=1-130. DR PDB; 6R5Q; EM; 3.00 A; TT=2-130. DR PDB; 6R6G; EM; 3.70 A; TT=2-130. DR PDB; 6R6P; EM; 3.10 A; TT=2-130. DR PDB; 6R7Q; EM; 3.90 A; TT=2-130. DR PDB; 6SGC; EM; 2.80 A; X1=1-130. DR PDB; 6W2S; EM; 3.00 A; X=1-130. DR PDB; 6W2T; EM; 3.36 A; X=1-130. DR PDB; 6YAL; EM; 3.00 A; Y=1-130. DR PDB; 6YAM; EM; 3.60 A; Y=1-130. DR PDB; 6YAN; EM; 3.48 A; Y=2-130. DR PDB; 6ZVK; EM; 3.49 A; J5=2-130. DR PDB; 7A01; EM; 3.60 A; J5=2-130. DR PDB; 7JQB; EM; 2.70 A; Y=1-130. DR PDB; 7JQC; EM; 3.30 A; Y=1-130. DR PDB; 7MDZ; EM; 3.20 A; WW=1-130. DR PDB; 7O7Y; EM; 2.20 A; Av=1-130. DR PDB; 7O7Z; EM; 2.40 A; Av=1-130. DR PDB; 7O80; EM; 2.90 A; Av=1-130. DR PDB; 7O81; EM; 3.10 A; Av=1-130. DR PDB; 7OYD; EM; 2.30 A; WW=1-130. DR PDB; 7SYG; EM; 4.30 A; X=1-130. DR PDB; 7SYH; EM; 4.60 A; X=1-130. DR PDB; 7SYI; EM; 4.50 A; X=1-130. DR PDB; 7SYJ; EM; 4.80 A; X=1-130. DR PDB; 7SYK; EM; 4.20 A; X=1-130. DR PDB; 7SYL; EM; 4.50 A; X=1-130. DR PDB; 7SYM; EM; 4.80 A; X=1-130. DR PDB; 7SYN; EM; 4.00 A; X=1-130. DR PDB; 7SYO; EM; 4.60 A; X=1-130. DR PDB; 7SYP; EM; 4.00 A; X=1-130. DR PDB; 7SYQ; EM; 3.80 A; X=1-130. DR PDB; 7SYR; EM; 3.60 A; X=1-130. DR PDB; 7SYS; EM; 3.50 A; X=1-130. DR PDB; 7SYT; EM; 4.40 A; X=1-130. DR PDB; 7SYU; EM; 4.60 A; X=1-130. DR PDB; 7SYV; EM; 3.90 A; X=1-130. DR PDB; 7SYW; EM; 3.70 A; X=1-130. DR PDB; 7SYX; EM; 3.70 A; X=1-130. DR PDB; 7TOQ; EM; 3.10 A; AS22=2-130. DR PDB; 7TOR; EM; 2.90 A; AS22=2-130. DR PDB; 7UCJ; EM; 3.10 A; WW=2-130. DR PDB; 7UCK; EM; 2.80 A; WW=2-130. DR PDB; 7ZJW; EM; 2.80 A; Sh=1-130. DR PDB; 7ZJX; EM; 3.10 A; Sh=1-130. DR PDB; 8BHF; EM; 3.10 A; X3=2-130. DR PDB; 8BTK; EM; 3.50 A; Av=1-130. DR PDB; 8P2K; EM; 2.90 A; Av=1-130. DR PDBsum; 3JAG; -. DR PDBsum; 3JAH; -. DR PDBsum; 3JAI; -. DR PDBsum; 4D5L; -. DR PDBsum; 4D61; -. DR PDBsum; 4KZX; -. DR PDBsum; 4KZY; -. DR PDBsum; 4KZZ; -. DR PDBsum; 5K0Y; -. DR PDBsum; 5LZS; -. DR PDBsum; 5LZT; -. DR PDBsum; 5LZU; -. DR PDBsum; 5LZV; -. DR PDBsum; 5LZW; -. DR PDBsum; 5LZX; -. DR PDBsum; 5LZY; -. DR PDBsum; 5LZZ; -. DR PDBsum; 6D90; -. DR PDBsum; 6D9J; -. DR PDBsum; 6GZ3; -. DR PDBsum; 6HCF; -. DR PDBsum; 6HCJ; -. DR PDBsum; 6HCM; -. DR PDBsum; 6HCQ; -. DR PDBsum; 6MTB; -. DR PDBsum; 6MTC; -. DR PDBsum; 6MTD; -. DR PDBsum; 6MTE; -. DR PDBsum; 6P4G; -. DR PDBsum; 6P4H; -. DR PDBsum; 6P5I; -. DR PDBsum; 6P5J; -. DR PDBsum; 6P5K; -. DR PDBsum; 6P5N; -. DR PDBsum; 6R5Q; -. DR PDBsum; 6R6G; -. DR PDBsum; 6R6P; -. DR PDBsum; 6R7Q; -. DR PDBsum; 6SGC; -. DR PDBsum; 6W2S; -. DR PDBsum; 6W2T; -. DR PDBsum; 6YAL; -. DR PDBsum; 6YAM; -. DR PDBsum; 6YAN; -. DR PDBsum; 6ZVK; -. DR PDBsum; 7A01; -. DR PDBsum; 7JQB; -. DR PDBsum; 7JQC; -. DR PDBsum; 7MDZ; -. DR PDBsum; 7O7Y; -. DR PDBsum; 7O7Z; -. DR PDBsum; 7O80; -. DR PDBsum; 7O81; -. DR PDBsum; 7OYD; -. DR PDBsum; 7SYG; -. DR PDBsum; 7SYH; -. DR PDBsum; 7SYI; -. DR PDBsum; 7SYJ; -. DR PDBsum; 7SYK; -. DR PDBsum; 7SYL; -. DR PDBsum; 7SYM; -. DR PDBsum; 7SYN; -. DR PDBsum; 7SYO; -. DR PDBsum; 7SYP; -. DR PDBsum; 7SYQ; -. DR PDBsum; 7SYR; -. DR PDBsum; 7SYS; -. DR PDBsum; 7SYT; -. DR PDBsum; 7SYU; -. DR PDBsum; 7SYV; -. DR PDBsum; 7SYW; -. DR PDBsum; 7SYX; -. DR PDBsum; 7TOQ; -. DR PDBsum; 7TOR; -. DR PDBsum; 7UCJ; -. DR PDBsum; 7UCK; -. DR PDBsum; 7ZJW; -. DR PDBsum; 7ZJX; -. DR PDBsum; 8BHF; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1TG89; -. DR IntAct; G1TG89; 1. DR PaxDb; 9986-ENSOCUP00000015939; -. DR Ensembl; ENSOCUT00000000179.3; ENSOCUP00000015939.1; ENSOCUG00000000179.4. DR GeneID; 103348569; -. DR eggNOG; KOG1754; Eukaryota. DR HOGENOM; CLU_098428_1_1_1; -. DR OrthoDB; 5472446at2759; -. DR TreeFam; TF300067; -. DR Proteomes; UP000001811; Chromosome 6. DR Bgee; ENSOCUG00000000179; Expressed in autopod skin and 14 other cell types or tissues. DR ExpressionAtlas; G1TG89; baseline. DR HAMAP; MF_01302_A; Ribosomal_S8_A; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62244" FT CHAIN 2..130 FT /note="Small ribosomal subunit protein uS8" FT /id="PRO_0000460066" FT MOD_RES 88 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P62245" SQ SEQUENCE 130 AA; 14840 MW; D4AC1E8864E3A184 CRC64; MVRMNVLADA LKSINNAEKR GKRQVLIRPC SKVIVRFLTV MMKHGYIGEF EIIDDHRAGK IVVNLTGRLN KCGVISPRFD VQLKDLEKWQ NNLLPSRQFG FIVLTTSAGI MDHEEARRKH TGGKILGFFF //