ID RS13_RABIT Reviewed; 151 AA. AC G1SP51; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2024, sequence version 3. DT 27-MAR-2024, entry version 85. DE RecName: Full=Small ribosomal subunit protein uS15; DE AltName: Full=40S ribosomal protein S13; GN Name=RPS13; 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 2-151 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 1-226 OF RIBOSOME, RP FUNCTION, 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 2-150 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 2-150 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 2-150 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:6P5I, ECO:0007744|PDB:6P5J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. 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 12-151 OF RIBOSOME, RP SUBCELLULAR 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, SUBCELLULAR RP LOCATION, AND SUBUNIT. 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:7SYO, ECO:0007744|PDB:7SYP} 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 12-150 OF RIBOSOME, RP SUBCELLULAR 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: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 The ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242, PubMed:30517857). Part of the small CC subunit (SSU) processome, first precursor of the small eukaryotic CC ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, CC PubMed:27863242, PubMed:30517857). During the assembly of the SSU CC processome in the nucleolus, many ribosome biogenesis factors, an RNA CC chaperone and ribosomal proteins associate with the nascent pre-rRNA CC and work in concert to generate RNA folding, modifications, CC rearrangements and cleavage as well as targeted degradation of pre- CC ribosomal RNA by the RNA exosome (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242, PubMed:30517857). CC {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, CC ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:30517857}. CC -!- SUBUNIT: Component of the small 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:36653451). Part of the small CC subunit (SSU) processome, composed of more than 70 proteins and the RNA CC chaperone small nucleolar RNA (snoRNA) U3 (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:36653451). CC {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, CC ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, CC ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, CC ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, CC ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, CC ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, 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:35822879, CC ECO:0000269|PubMed:36653451}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P62277}. CC -!- PTM: Ubiquitinated at Lys-27 by RNF14 and RNF25 in response to ribosome CC collisions (ribosome stalling). {ECO:0000250|UniProtKB:P62277}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 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 PDB; 3JAG; EM; 3.65 A; NN=11-151. DR PDB; 3JAH; EM; 3.45 A; NN=11-151. DR PDB; 3JAI; EM; 3.65 A; NN=11-151. DR PDB; 4D5L; EM; 9.00 A; N=1-151. DR PDB; 4D61; EM; 9.00 A; N=1-151. DR PDB; 4KZX; X-ray; 7.81 A; N=1-151. DR PDB; 4KZY; X-ray; 7.01 A; N=1-151. DR PDB; 4KZZ; X-ray; 7.03 A; N=1-151. DR PDB; 5K0Y; EM; 5.80 A; Z=11-151. DR PDB; 5LZS; EM; 3.31 A; NN=1-151. DR PDB; 5LZT; EM; 3.65 A; NN=1-151. DR PDB; 5LZU; EM; 3.75 A; NN=1-151. DR PDB; 5LZV; EM; 3.35 A; NN=1-151. DR PDB; 5LZW; EM; 3.53 A; NN=1-151. DR PDB; 5LZX; EM; 3.67 A; NN=1-151. DR PDB; 5LZY; EM; 3.99 A; NN=1-151. DR PDB; 5LZZ; EM; 3.47 A; NN=1-151. DR PDB; 6D90; EM; 3.20 A; OO=1-151. DR PDB; 6D9J; EM; 3.20 A; OO=1-151. DR PDB; 6GZ3; EM; 3.60 A; BN=11-151. DR PDB; 6HCF; EM; 3.90 A; O1=1-151. DR PDB; 6HCJ; EM; 3.80 A; O2=1-151. DR PDB; 6HCM; EM; 6.80 A; O1=1-151. DR PDB; 6HCQ; EM; 6.50 A; O2=1-151. DR PDB; 6MTB; EM; 3.60 A; NN=11-151. DR PDB; 6MTC; EM; 3.40 A; NN=11-151. DR PDB; 6MTD; EM; 3.30 A; NN=11-151. DR PDB; 6MTE; EM; 3.40 A; NN=11-151. DR PDB; 6P4G; EM; 3.10 A; O=1-151. DR PDB; 6P4H; EM; 3.20 A; O=1-151. DR PDB; 6P5I; EM; 3.10 A; O=1-151. DR PDB; 6P5J; EM; 3.10 A; O=1-151. DR PDB; 6P5K; EM; 3.10 A; O=1-151. DR PDB; 6P5N; EM; 3.20 A; O=1-151. DR PDB; 6R5Q; EM; 3.00 A; QQ=11-151. DR PDB; 6R6G; EM; 3.70 A; QQ=11-151. DR PDB; 6R6P; EM; 3.10 A; QQ=11-151. DR PDB; 6R7Q; EM; 3.90 A; QQ=11-151. DR PDB; 6SGC; EM; 2.80 A; O1=1-151. DR PDB; 6W2S; EM; 3.00 A; O=1-151. DR PDB; 6W2T; EM; 3.36 A; O=1-151. DR PDB; 6YAL; EM; 3.00 A; P=11-151. DR PDB; 6YAM; EM; 3.60 A; P=11-151. DR PDB; 6YAN; EM; 3.48 A; P=11-151. DR PDB; 6ZVK; EM; 3.49 A; F3=11-151. DR PDB; 7A01; EM; 3.60 A; F3=11-151. DR PDB; 7MDZ; EM; 3.20 A; NN=1-151. DR PDB; 7NWG; EM; 3.80 A; O2=11-151. DR PDB; 7NWI; EM; 3.13 A; NN=11-151. DR PDB; 7O7Y; EM; 2.20 A; Am=1-151. DR PDB; 7O7Z; EM; 2.40 A; Am=1-151. DR PDB; 7O80; EM; 2.90 A; Am=1-151. DR PDB; 7O81; EM; 3.10 A; Am=1-151. DR PDB; 7OYD; EM; 2.30 A; NN=1-151. DR PDB; 7SYG; EM; 4.30 A; O=1-151. DR PDB; 7SYH; EM; 4.60 A; O=1-151. DR PDB; 7SYI; EM; 4.50 A; O=1-151. DR PDB; 7SYJ; EM; 4.80 A; O=1-151. DR PDB; 7SYK; EM; 4.20 A; O=1-151. DR PDB; 7SYL; EM; 4.50 A; O=1-151. DR PDB; 7SYM; EM; 4.80 A; O=1-151. DR PDB; 7SYN; EM; 4.00 A; O=1-151. DR PDB; 7SYO; EM; 4.60 A; O=1-151. DR PDB; 7SYP; EM; 4.00 A; O=1-151. DR PDB; 7SYQ; EM; 3.80 A; O=1-151. DR PDB; 7SYR; EM; 3.60 A; O=1-151. DR PDB; 7SYS; EM; 3.50 A; O=1-151. DR PDB; 7SYT; EM; 4.40 A; O=1-151. DR PDB; 7SYU; EM; 4.60 A; O=1-151. DR PDB; 7SYV; EM; 3.90 A; O=1-151. DR PDB; 7SYW; EM; 3.70 A; O=1-151. DR PDB; 7SYX; EM; 3.70 A; O=1-151. DR PDB; 7TOQ; EM; 3.10 A; AS13=11-151. DR PDB; 7TOR; EM; 2.90 A; AS13=11-151. DR PDB; 7UCJ; EM; 3.10 A; NN=11-151. DR PDB; 7UCK; EM; 2.80 A; NN=11-151. DR PDB; 8BHF; EM; 3.10 A; O3=11-151. DR PDB; 8BTK; EM; 3.50 A; Am=1-151. DR PDB; 8P2K; EM; 2.90 A; Am=1-151. 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; 7MDZ; -. DR PDBsum; 7NWG; -. DR PDBsum; 7NWI; -. 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; 8BHF; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1SP51; -. DR IntAct; G1SP51; 1. DR PaxDb; 9986-ENSOCUP00000004803; -. DR Ensembl; ENSOCUT00000005534.4; ENSOCUP00000004803.3; ENSOCUG00000005536.4. DR eggNOG; KOG0400; Eukaryota. DR HOGENOM; CLU_090139_1_0_1; -. DR TreeFam; TF300190; -. DR Proteomes; UP000001811; Unplaced. DR Bgee; ENSOCUG00000005536; Expressed in upper lobe of left lung and 15 other cell types or tissues. DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62277" FT CHAIN 2..151 FT /note="Small ribosomal subunit protein uS15" FT /id="PRO_0000460064" FT MOD_RES 27 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62277" FT MOD_RES 27 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62301" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62277" FT MOD_RES 34 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P62301" FT MOD_RES 38 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62277" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P62277" FT CROSSLNK 43 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62277" SQ SEQUENCE 151 AA; 17222 MW; 23F94D38F87B8D53 CRC64; MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES RIHRLARYYK TKRVLPPNWK YESSTASALV A //