ID RS18_RABIT Reviewed; 152 AA. AC G1TPG3; G1SZI5; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Small ribosomal subunit protein uS13; DE AltName: Full=40S ribosomal protein S18; GN Name=RPS18; 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:3JAG, ECO:0007744|PDB:3JAH} RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF 6-142 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 [3] {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 [4] {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 [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 4-142 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 2-145 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 2-145 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: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:26245381, CC PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857). CC The ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:26245381, PubMed:23873042, CC PubMed:25601755, 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. 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}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 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; AAGW02017742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002714578.1; XM_002714532.3. DR RefSeq; XP_002720764.1; XM_002720718.3. DR RefSeq; XP_017200532.1; XM_017345043.1. DR PDB; 3JAG; EM; 3.65 A; SS=10-146. DR PDB; 3JAH; EM; 3.45 A; SS=10-146. DR PDB; 3JAI; EM; 3.65 A; SS=10-146. DR PDB; 4D5L; EM; 9.00 A; S=1-152. DR PDB; 4D61; EM; 9.00 A; S=1-152. DR PDB; 4KZX; X-ray; 7.81 A; S=1-152. DR PDB; 4KZY; X-ray; 7.01 A; S=1-152. DR PDB; 4KZZ; X-ray; 7.03 A; S=1-152. DR PDB; 5K0Y; EM; 5.80 A; L=6-142. DR PDB; 5LZS; EM; 3.31 A; SS=1-152. DR PDB; 5LZT; EM; 3.65 A; SS=1-152. DR PDB; 5LZU; EM; 3.75 A; SS=1-152. DR PDB; 5LZV; EM; 3.35 A; SS=1-152. DR PDB; 5LZW; EM; 3.53 A; SS=1-152. DR PDB; 5LZX; EM; 3.67 A; SS=1-152. DR PDB; 5LZY; EM; 3.99 A; SS=1-152. DR PDB; 5LZZ; EM; 3.47 A; SS=1-152. DR PDB; 6D90; EM; 3.20 A; TT=1-152. DR PDB; 6D9J; EM; 3.20 A; TT=1-152. DR PDB; 6GZ3; EM; 3.60 A; BS=4-142. DR PDB; 6HCF; EM; 3.90 A; T1=1-152. DR PDB; 6HCJ; EM; 3.80 A; T2=1-152. DR PDB; 6HCM; EM; 6.80 A; T1=1-152. DR PDB; 6HCQ; EM; 6.50 A; T2=1-152. DR PDB; 6MTB; EM; 3.60 A; SS=2-145. DR PDB; 6MTC; EM; 3.40 A; SS=2-145. DR PDB; 6MTD; EM; 3.30 A; SS=2-145. DR PDB; 6MTE; EM; 3.40 A; SS=2-145. DR PDB; 6P4G; EM; 3.10 A; T=1-152. DR PDB; 6P4H; EM; 3.20 A; T=1-152. DR PDB; 6P5I; EM; 3.10 A; T=1-152. DR PDB; 6P5J; EM; 3.10 A; T=1-152. DR PDB; 6P5K; EM; 3.10 A; T=1-152. DR PDB; 6P5N; EM; 3.20 A; T=1-152. DR PDB; 6R5Q; EM; 3.00 A; II=2-145. DR PDB; 6R6G; EM; 3.70 A; II=2-145. DR PDB; 6R6P; EM; 3.10 A; II=2-145. DR PDB; 6R7Q; EM; 3.90 A; II=2-145. DR PDB; 6SGC; EM; 2.80 A; T1=1-152. DR PDB; 6W2S; EM; 3.00 A; T=1-152. DR PDB; 6W2T; EM; 3.36 A; T=1-152. DR PDB; 6YAL; EM; 3.00 A; U=1-152. DR PDB; 6YAM; EM; 3.60 A; U=1-152. DR PDB; 6YAN; EM; 3.48 A; U=6-147. DR PDB; 6ZVK; EM; 3.49 A; G5=6-142. DR PDB; 7A01; EM; 3.60 A; G5=6-142. DR PDB; 7JQB; EM; 2.70 A; T=1-152. DR PDB; 7JQC; EM; 3.30 A; T=1-152. DR PDB; 7MDZ; EM; 3.20 A; SS=1-152. DR PDB; 7NWG; EM; 3.80 A; T2=1-152. DR PDB; 7NWH; EM; 4.10 A; SS=1-152. DR PDB; 7NWI; EM; 3.13 A; SS=6-142. DR PDB; 7O7Y; EM; 2.20 A; Ar=1-152. DR PDB; 7O7Z; EM; 2.40 A; Ar=1-152. DR PDB; 7O80; EM; 2.90 A; Ar=1-152. DR PDB; 7O81; EM; 3.10 A; Ar=1-152. DR PDB; 7OYD; EM; 2.30 A; SS=1-152. DR PDB; 7SYG; EM; 4.30 A; T=1-152. DR PDB; 7SYH; EM; 4.60 A; T=1-152. DR PDB; 7SYI; EM; 4.50 A; T=1-152. DR PDB; 7SYJ; EM; 4.80 A; T=1-152. DR PDB; 7SYK; EM; 4.20 A; T=1-152. DR PDB; 7SYL; EM; 4.50 A; T=1-152. DR PDB; 7SYM; EM; 4.80 A; T=1-152. DR PDB; 7SYN; EM; 4.00 A; T=1-152. DR PDB; 7SYO; EM; 4.60 A; T=1-152. DR PDB; 7SYP; EM; 4.00 A; T=1-152. DR PDB; 7SYQ; EM; 3.80 A; T=1-152. DR PDB; 7SYR; EM; 3.60 A; T=1-152. DR PDB; 7SYS; EM; 3.50 A; T=1-152. DR PDB; 7SYT; EM; 4.40 A; T=1-152. DR PDB; 7SYU; EM; 4.60 A; T=1-152. DR PDB; 7SYV; EM; 3.90 A; T=1-152. DR PDB; 7SYW; EM; 3.70 A; T=1-152. DR PDB; 7SYX; EM; 3.70 A; T=1-152. DR PDB; 7TOQ; EM; 3.10 A; AS18=2-145. DR PDB; 7TOR; EM; 2.90 A; AS18=2-145. DR PDB; 7UCJ; EM; 3.10 A; SS=2-145. DR PDB; 7UCK; EM; 2.80 A; SS=2-145. DR PDB; 8BHF; EM; 3.10 A; T3=6-149. DR PDB; 8BTK; EM; 3.50 A; Ar=1-152. DR PDB; 8P2K; EM; 2.90 A; Ar=1-152. 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; 7NWG; -. DR PDBsum; 7NWH; -. 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 PaxDb; 9986-ENSOCUP00000018898; -. DR Ensembl; ENSOCUT00000014693.3; ENSOCUP00000018898.1; ENSOCUG00000014699.3. DR Ensembl; ENSOCUT00000052459.1; ENSOCUP00000028190.1; ENSOCUG00000010546.3. DR GeneID; 100349921; -. DR GeneID; 100356144; -. DR eggNOG; KOG3311; Eukaryota. DR HOGENOM; CLU_103849_0_1_1; -. DR OrthoDB; 5480189at2759; -. DR TreeFam; TF317649; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000010546; Expressed in upper lobe of left lung and 15 other cell types or tissues. DR HAMAP; MF_01315; Ribosomal_S13_S18; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62269" FT CHAIN 2..152 FT /note="Small ribosomal subunit protein uS13" FT /id="PRO_0000460071" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P62269" FT MOD_RES 94 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62269" FT MOD_RES 106 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62269" FT CROSSLNK 91 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62269" FT CROSSLNK 94 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P62269" FT CROSSLNK 106 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P62269" SQ SEQUENCE 152 AA; 17719 MW; 4DAF0662C3F37F22 CRC64; MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK //