ID RS19_RABIT Reviewed; 145 AA. AC G1TN62; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Small ribosomal subunit protein eS19; DE AltName: Full=40S ribosomal protein S19; GN Name=RPS19; 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 4-144 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: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 [7] {ECO:0007744|PDB:6R5Q, ECO:0007744|PDB:6R6G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 3-143 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 [8] {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 [9] {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 [10] {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 [11] {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 [12] {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 [13] {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). The ribosome is a CC large ribonucleoprotein complex responsible for the synthesis of CC proteins in the cell (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242). Required for pre-rRNA processing and CC maturation of 40S ribosomal subunits (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242). Part of the small subunit (SSU) CC processome, first precursor of the small eukaryotic ribosomal subunit CC (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). CC During the assembly of the SSU processome in the nucleolus, many CC ribosome biogenesis factors, an RNA chaperone and ribosomal proteins CC associate with the nascent pre-rRNA and work in concert to generate RNA CC folding, 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). CC {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, CC ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23873042, CC PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, CC PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:33296660, CC PubMed:32286223, PubMed:35822879, 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:29856316, CC PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:33296660, CC PubMed:32286223, PubMed:35822879, PubMed:36653451). Interacts with CC RPS19BP1; the interaction is direct and mediates the integration of CC RPS19 in state post-A1 (By similarity). Interacts with RPS19BP1 (By CC similarity). {ECO:0000250|UniProtKB:P39019, CC ECO:0000250|UniProtKB:Q9CZX8, 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:31246176, ECO:0000269|PubMed:31609474, CC ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, CC ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35822879, CC 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:31246176, ECO:0000269|PubMed:31609474, CC ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, CC ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35822879, CC ECO:0000269|PubMed:36653451}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P39019}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 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; AAGW02048164; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002716238.1; XM_002716192.3. DR PDB; 3JAG; EM; 3.65 A; TT=4-144. DR PDB; 3JAH; EM; 3.45 A; TT=4-144. DR PDB; 3JAI; EM; 3.65 A; TT=4-144. DR PDB; 4D5L; EM; 9.00 A; T=1-145. DR PDB; 4D61; EM; 9.00 A; T=1-145. DR PDB; 4KZX; X-ray; 7.81 A; T=1-145. DR PDB; 4KZY; X-ray; 7.01 A; T=1-145. DR PDB; 4KZZ; X-ray; 7.03 A; T=1-145. DR PDB; 5K0Y; EM; 5.80 A; R=4-144. DR PDB; 5LZS; EM; 3.31 A; TT=1-145. DR PDB; 5LZT; EM; 3.65 A; TT=1-145. DR PDB; 5LZU; EM; 3.75 A; TT=1-145. DR PDB; 5LZV; EM; 3.35 A; TT=1-145. DR PDB; 5LZW; EM; 3.53 A; TT=1-145. DR PDB; 5LZX; EM; 3.67 A; TT=1-145. DR PDB; 5LZY; EM; 3.99 A; TT=1-145. DR PDB; 5LZZ; EM; 3.47 A; TT=1-145. DR PDB; 6D90; EM; 3.20 A; UU=1-145. DR PDB; 6D9J; EM; 3.20 A; UU=1-145. DR PDB; 6P4G; EM; 3.10 A; U=1-145. DR PDB; 6P4H; EM; 3.20 A; U=1-145. DR PDB; 6P5I; EM; 3.10 A; U=1-145. DR PDB; 6P5J; EM; 3.10 A; U=1-145. DR PDB; 6P5K; EM; 3.10 A; U=1-145. DR PDB; 6P5N; EM; 3.20 A; U=1-145. DR PDB; 6R5Q; EM; 3.00 A; PP=3-143. DR PDB; 6R6G; EM; 3.70 A; PP=3-143. DR PDB; 6R6P; EM; 3.10 A; PP=3-143. DR PDB; 6R7Q; EM; 3.90 A; PP=3-143. DR PDB; 6SGC; EM; 2.80 A; U1=1-145. DR PDB; 6W2S; EM; 3.00 A; U=1-145. DR PDB; 6W2T; EM; 3.36 A; U=1-145. DR PDB; 6YAL; EM; 3.00 A; V=4-144. DR PDB; 6YAM; EM; 3.60 A; V=1-145. DR PDB; 6YAN; EM; 3.48 A; V=4-144. DR PDB; 6ZVK; EM; 3.49 A; H5=4-144. DR PDB; 7A01; EM; 3.60 A; H5=4-144. DR PDB; 7JQB; EM; 2.70 A; U=1-145. DR PDB; 7JQC; EM; 3.30 A; U=1-145. DR PDB; 7MDZ; EM; 3.20 A; TT=1-145. DR PDB; 7NWG; EM; 3.80 A; U2=1-145. DR PDB; 7OYD; EM; 2.30 A; TT=1-145. DR PDB; 7SYG; EM; 4.30 A; U=1-145. DR PDB; 7SYH; EM; 4.60 A; U=1-145. DR PDB; 7SYI; EM; 4.50 A; U=1-145. DR PDB; 7SYJ; EM; 4.80 A; U=1-145. DR PDB; 7SYK; EM; 4.20 A; U=1-145. DR PDB; 7SYL; EM; 4.50 A; U=1-145. DR PDB; 7SYM; EM; 4.80 A; U=1-145. DR PDB; 7SYN; EM; 4.00 A; U=1-145. DR PDB; 7SYO; EM; 4.60 A; U=1-145. DR PDB; 7SYP; EM; 4.00 A; U=1-145. DR PDB; 7SYQ; EM; 3.80 A; U=1-145. DR PDB; 7SYR; EM; 3.60 A; U=1-145. DR PDB; 7SYS; EM; 3.50 A; U=1-145. DR PDB; 7SYT; EM; 4.40 A; U=1-145. DR PDB; 7SYU; EM; 4.60 A; U=1-145. DR PDB; 7SYV; EM; 3.90 A; U=1-145. DR PDB; 7SYW; EM; 3.70 A; U=1-145. DR PDB; 7SYX; EM; 3.70 A; U=1-145. DR PDB; 8BHF; EM; 3.10 A; U3=3-143. DR PDB; 8BTK; EM; 3.50 A; As=1-145. DR PDB; 8P2K; EM; 2.90 A; As=1-145. 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; 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; 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; 8BHF; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1TN62; -. DR IntAct; G1TN62; 1. DR STRING; 9986.ENSOCUP00000018431; -. DR PaxDb; 9986-ENSOCUP00000018431; -. DR Ensembl; ENSOCUT00000023161.2; ENSOCUP00000018431.1; ENSOCUG00000026336.2. DR GeneID; 100345774; -. DR eggNOG; KOG3411; Eukaryota. DR HOGENOM; CLU_108559_0_1_1; -. DR InParanoid; G1TN62; -. DR OrthoDB; 168043at2759; -. DR TreeFam; TF315008; -. DR Proteomes; UP000001811; Chromosome 14. DR Bgee; ENSOCUG00000026336; Expressed in uterus and 15 other cell types or tissues. DR PROSITE; PS00628; RIBOSOMAL_S19E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Host-virus interaction; Methylation; KW Nucleus; Reference proteome; Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P39019" FT CHAIN 2..145 FT /note="Small ribosomal subunit protein eS19" FT /id="PRO_0000460069" FT MOD_RES 23 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P39019" FT MOD_RES 67 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P39019" FT MOD_RES 111 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P39019" FT MOD_RES 115 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZX8" FT MOD_RES 143 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZX8" SQ SEQUENCE 145 AA; 16204 MW; 181F3CBEF8E56E41 CRC64; MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST ARHLYLRGGA GVGSMTKIYG GRQRNGVMPS HFSRGSKSVA RRVLQALEGL KMVEKDQDWG RKLTPQGQRD LDRIAGQVAA AKKKH //