ID RS14_RABIT Reviewed; 151 AA. AC G1T1F0; G1U472; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 11-DEC-2019, sequence version 2. DT 27-MAR-2024, entry version 66. DE RecName: Full=Small ribosomal subunit protein uS11; DE AltName: Full=40S ribosomal protein S14; GN Name=RPS14; 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:4D61} RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF 6-156 OF RIBOSOME, RP FUNCTION, 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 21-156 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 1-156 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:6D90} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. 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} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 21-155 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, 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 [9] {ECO:0007744|PDB:6ZVK, ECO:0007744|PDB:7A01} RP STRUCTURE BY ELECTRON MICROSCOPY (3.49 ANGSTROMS) OF 16-151 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 [10] {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 [11] {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 [12] {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). 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). Part of the small subunit (SSU) CC processome, first precursor of the small eukaryotic ribosomal subunit CC (By similarity). During the assembly of the SSU processome in the CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and CC ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (By similarity). {ECO:0000250|UniProtKB:P62263, 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:33296660, PubMed:32286223, CC PubMed:35822879, PubMed:35679869). Part of the small subunit (SSU) CC processome, composed of more than 70 proteins and the RNA chaperone CC small nucleolar RNA (snoRNA) U3 (By similarity). CC {ECO:0000250|UniProtKB:P62263, 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:32286223, ECO:0000269|PubMed:33296660, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35822879}. 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:32286223, ECO:0000269|PubMed:33296660, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35822879}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P62263}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 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; AAGW02027430; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002710354.1; XM_002710308.3. DR RefSeq; XP_002710355.1; XM_002710309.3. DR RefSeq; XP_008267447.1; XM_008269225.2. DR PDB; 3JAG; EM; 3.65 A; OO=16-151. DR PDB; 3JAH; EM; 3.45 A; OO=16-151. DR PDB; 3JAI; EM; 3.65 A; OO=16-151. DR PDB; 4D5L; EM; 9.00 A; O=18-151. DR PDB; 4D61; EM; 9.00 A; O=1-151. DR PDB; 4KZX; X-ray; 7.81 A; O=18-151. DR PDB; 4KZY; X-ray; 7.01 A; O=18-151. DR PDB; 4KZZ; X-ray; 7.03 A; O=18-151. DR PDB; 5K0Y; EM; 5.80 A; j=16-151. DR PDB; 5LZS; EM; 3.31 A; OO=1-151. DR PDB; 5LZT; EM; 3.65 A; OO=1-151. DR PDB; 5LZU; EM; 3.75 A; OO=1-151. DR PDB; 5LZV; EM; 3.35 A; OO=1-151. DR PDB; 5LZW; EM; 3.53 A; OO=1-151. DR PDB; 5LZX; EM; 3.67 A; OO=1-151. DR PDB; 5LZY; EM; 3.99 A; OO=1-151. DR PDB; 5LZZ; EM; 3.47 A; OO=1-151. DR PDB; 6D90; EM; 3.20 A; PP=18-151. DR PDB; 6D9J; EM; 3.20 A; PP=18-151. DR PDB; 6P4G; EM; 3.10 A; P=1-151. DR PDB; 6P4H; EM; 3.20 A; P=1-151. DR PDB; 6P5I; EM; 3.10 A; P=18-151. DR PDB; 6P5J; EM; 3.10 A; P=18-151. DR PDB; 6P5K; EM; 3.10 A; P=18-151. DR PDB; 6P5N; EM; 3.20 A; P=18-151. DR PDB; 6R5Q; EM; 3.00 A; MM=16-150. DR PDB; 6W2S; EM; 3.00 A; P=18-151. DR PDB; 6W2T; EM; 3.36 A; P=18-151. DR PDB; 6YAL; EM; 3.00 A; Q=1-151. DR PDB; 6YAM; EM; 3.60 A; Q=1-151. DR PDB; 6YAN; EM; 3.48 A; Q=16-151. DR PDB; 6ZVK; EM; 3.49 A; a5=16-151. DR PDB; 7A01; EM; 3.60 A; a5=16-151. DR PDB; 7JQB; EM; 2.70 A; X=1-151. DR PDB; 7JQC; EM; 3.30 A; X=1-151. DR PDB; 7MDZ; EM; 3.20 A; OO=1-151. DR PDB; 7NWG; EM; 3.80 A; P2=1-151. DR PDB; 7NWH; EM; 4.10 A; OO=1-151. DR PDB; 7O7Y; EM; 2.20 A; An=1-151. DR PDB; 7O7Z; EM; 2.40 A; An=1-151. DR PDB; 7O80; EM; 2.90 A; An=1-151. DR PDB; 7O81; EM; 3.10 A; An=1-151. DR PDB; 7SYG; EM; 4.30 A; P=1-151. DR PDB; 7SYH; EM; 4.60 A; P=1-151. DR PDB; 7SYI; EM; 4.50 A; P=1-151. DR PDB; 7SYJ; EM; 4.80 A; P=1-151. DR PDB; 7SYK; EM; 4.20 A; P=1-151. DR PDB; 7SYL; EM; 4.50 A; P=1-151. DR PDB; 7SYM; EM; 4.80 A; P=1-151. DR PDB; 7SYN; EM; 4.00 A; P=1-151. DR PDB; 7SYO; EM; 4.60 A; P=1-151. DR PDB; 7SYP; EM; 4.00 A; P=1-151. DR PDB; 7SYQ; EM; 3.80 A; P=1-151. DR PDB; 7SYR; EM; 3.60 A; P=1-151. DR PDB; 7SYS; EM; 3.50 A; P=1-151. DR PDB; 7SYT; EM; 4.40 A; P=1-151. DR PDB; 7SYU; EM; 4.60 A; P=1-151. DR PDB; 7SYV; EM; 3.90 A; P=1-151. DR PDB; 7SYW; EM; 3.70 A; P=1-151. DR PDB; 7SYX; EM; 3.70 A; P=1-151. DR PDB; 7TOQ; EM; 3.10 A; AS14=33-151. DR PDB; 7TOR; EM; 2.90 A; AS14=33-151. DR PDB; 7UCJ; EM; 3.10 A; OO=33-151. DR PDB; 7UCK; EM; 2.80 A; OO=33-151. DR PDB; 8BHF; EM; 3.10 A; P3=16-151. DR PDB; 8BTK; EM; 3.50 A; An=18-151. DR PDB; 8P2K; EM; 2.90 A; An=18-151. 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; 6P4G; -. DR PDBsum; 6P4H; -. DR PDBsum; 6P5I; -. DR PDBsum; 6P5J; -. DR PDBsum; 6P5K; -. DR PDBsum; 6P5N; -. DR PDBsum; 6R5Q; -. 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; 7O7Y; -. DR PDBsum; 7O7Z; -. DR PDBsum; 7O80; -. DR PDBsum; 7O81; -. 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; G1T1F0; -. DR Ensembl; ENSOCUT00000011505.3; ENSOCUP00000009893.3; ENSOCUG00000011509.3. DR GeneID; 100343884; -. DR GeneID; 100351184; -. DR eggNOG; KOG0407; Eukaryota. DR HOGENOM; CLU_072439_6_0_1; -. DR OrthoDB; 5478893at2759; -. DR TreeFam; TF300125; -. DR Proteomes; UP000001811; Chromosome 1. DR Proteomes; UP000001811; Chromosome 3. DR Bgee; ENSOCUG00000011509; Expressed in uterus and 15 other cell types or tissues. DR HAMAP; MF_01310; Ribosomal_S11; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62263" FT CHAIN 2..151 FT /note="Small ribosomal subunit protein uS11" FT /id="PRO_0000460063" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62263" FT MOD_RES 133 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P62263" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62263" FT CROSSLNK 61 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62263" FT CROSSLNK 63 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62263" FT CROSSLNK 106 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62263" SQ SEQUENCE 151 AA; 16273 MW; 4F4387F9FADAC278 CRC64; MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L //