ID RS28_RABIT Reviewed; 69 AA. AC G1TIB4; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Small ribosomal subunit protein eS28; DE AltName: Full=40S ribosomal protein S28; GN Name=RPS28; 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 8-68 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 7-68 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 7-68 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 7-68 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: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. 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 PubMed:30517857). 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:P62857, 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 40S 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, cytosol CC {ECO:0000250|UniProtKB:P62857}. 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}. Rough endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q6QAT1}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P62857}. Note=Detected on cytosolic polysomes CC (By similarity). Detected in ribosomes that are associated with the CC rough endoplasmic reticulum (By similarity). CC {ECO:0000250|UniProtKB:P62857, ECO:0000250|UniProtKB:Q6QAT1}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 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; cc=8-68. DR PDB; 3JAH; EM; 3.45 A; cc=8-68. DR PDB; 3JAI; EM; 3.65 A; cc=8-68. DR PDB; 4D5L; EM; 9.00 A; c=1-69. DR PDB; 4D61; EM; 9.00 A; c=1-69. DR PDB; 4KZX; X-ray; 7.81 A; c=1-69. DR PDB; 4KZY; X-ray; 7.01 A; c=1-69. DR PDB; 4KZZ; X-ray; 7.03 A; c=1-69. DR PDB; 5K0Y; EM; 5.80 A; l=5-68. DR PDB; 5LZS; EM; 3.31 A; cc=1-69. DR PDB; 5LZT; EM; 3.65 A; cc=1-69. DR PDB; 5LZU; EM; 3.75 A; cc=1-69. DR PDB; 5LZV; EM; 3.35 A; cc=1-69. DR PDB; 5LZW; EM; 3.53 A; cc=1-69. DR PDB; 5LZX; EM; 3.67 A; cc=1-69. DR PDB; 5LZY; EM; 3.99 A; cc=1-69. DR PDB; 5LZZ; EM; 3.47 A; cc=1-69. DR PDB; 6D90; EM; 3.20 A; dd=1-69. DR PDB; 6D9J; EM; 3.20 A; dd=1-69. DR PDB; 6GZ3; EM; 3.60 A; Bc=7-68. DR PDB; 6HCF; EM; 3.90 A; d1=1-69. DR PDB; 6HCJ; EM; 3.80 A; d2=1-69. DR PDB; 6HCM; EM; 6.80 A; d1=1-69. DR PDB; 6HCQ; EM; 6.50 A; d2=1-69. DR PDB; 6MTB; EM; 3.60 A; cc=7-68. DR PDB; 6MTC; EM; 3.40 A; cc=7-68. DR PDB; 6MTD; EM; 3.30 A; cc=7-68. DR PDB; 6MTE; EM; 3.40 A; cc=7-68. DR PDB; 6P4G; EM; 3.10 A; d=1-69. DR PDB; 6P4H; EM; 3.20 A; d=1-69. DR PDB; 6P5I; EM; 3.10 A; d=1-69. DR PDB; 6P5J; EM; 3.10 A; d=1-69. DR PDB; 6P5K; EM; 3.10 A; d=1-69. DR PDB; 6P5N; EM; 3.20 A; d=1-69. DR PDB; 6R5Q; EM; 3.00 A; FF=7-68. DR PDB; 6R6G; EM; 3.70 A; FF=7-68. DR PDB; 6R6P; EM; 3.10 A; FF=7-68. DR PDB; 6R7Q; EM; 3.90 A; FF=7-68. DR PDB; 6SGC; EM; 2.80 A; d1=1-69. DR PDB; 6W2S; EM; 3.00 A; d=1-69. DR PDB; 6W2T; EM; 3.36 A; d=1-69. DR PDB; 6YAL; EM; 3.00 A; d=1-69. DR PDB; 6YAM; EM; 3.60 A; d=1-69. DR PDB; 6YAN; EM; 3.48 A; d=5-68. DR PDB; 6ZVK; EM; 3.49 A; f3=5-68. DR PDB; 7A01; EM; 3.60 A; f3=5-68. DR PDB; 7JQB; EM; 2.70 A; d=1-69. DR PDB; 7JQC; EM; 3.30 A; d=1-69. DR PDB; 7MDZ; EM; 3.20 A; cc=1-69. DR PDB; 7NWG; EM; 3.80 A; d2=1-69. DR PDB; 7NWH; EM; 4.10 A; cc=1-69. DR PDB; 7NWI; EM; 3.13 A; cc=1-69. DR PDB; 7O7Y; EM; 2.20 A; AB=1-69. DR PDB; 7O7Z; EM; 2.40 A; AB=1-69. DR PDB; 7O80; EM; 2.90 A; AB=1-69. DR PDB; 7O81; EM; 3.10 A; AB=1-69. DR PDB; 7OYD; EM; 2.30 A; Cc=1-69. DR PDB; 7SYG; EM; 4.30 A; d=1-69. DR PDB; 7SYH; EM; 4.60 A; d=1-69. DR PDB; 7SYI; EM; 4.50 A; d=1-69. DR PDB; 7SYJ; EM; 4.80 A; d=1-69. DR PDB; 7SYK; EM; 4.20 A; d=1-69. DR PDB; 7SYL; EM; 4.50 A; d=1-69. DR PDB; 7SYM; EM; 4.80 A; d=1-69. DR PDB; 7SYN; EM; 4.00 A; d=1-69. DR PDB; 7SYO; EM; 4.60 A; d=1-69. DR PDB; 7SYP; EM; 4.00 A; d=1-69. DR PDB; 7SYQ; EM; 3.80 A; d=1-69. DR PDB; 7SYR; EM; 3.60 A; d=1-69. DR PDB; 7SYS; EM; 3.50 A; d=1-69. DR PDB; 7SYT; EM; 4.40 A; d=1-69. DR PDB; 7SYU; EM; 4.60 A; d=1-69. DR PDB; 7SYV; EM; 3.90 A; d=1-69. DR PDB; 7SYW; EM; 3.70 A; d=1-69. DR PDB; 7SYX; EM; 3.70 A; d=1-69. DR PDB; 7TOQ; EM; 3.10 A; AS28=7-68. DR PDB; 7TOR; EM; 2.90 A; AS28=7-68. DR PDB; 7UCJ; EM; 3.10 A; Cc=7-68. DR PDB; 7UCK; EM; 2.80 A; Cc=7-68. DR PDB; 8BHF; EM; 3.10 A; d3=7-68. DR PDB; 8BTK; EM; 3.50 A; AB=1-69. DR PDB; 8P2K; EM; 2.90 A; AB=1-69. 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 AlphaFoldDB; G1TIB4; -. DR IntAct; G1TIB4; 1. DR STRING; 9986.ENSOCUP00000016683; -. DR PaxDb; 9986-ENSOCUP00000016683; -. DR Ensembl; ENSOCUT00000030802.1; ENSOCUP00000016683.1; ENSOCUG00000021484.1. DR eggNOG; KOG3502; Eukaryota. DR HOGENOM; CLU_178987_1_0_1; -. DR InParanoid; G1TIB4; -. DR TreeFam; TF300136; -. DR Proteomes; UP000001811; Unplaced. DR Bgee; ENSOCUG00000021484; Expressed in uterus and 18 other cell types or tissues. DR HAMAP; MF_00292; Ribosomal_S28e; 1. DR PROSITE; PS00961; RIBOSOMAL_S28E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Nucleus; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. FT CHAIN 1..69 FT /note="Small ribosomal subunit protein eS28" FT /id="PRO_0000460081" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P62859" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62857" SQ SEQUENCE 69 AA; 7841 MW; 49902FE9376EB74F CRC64; MDTSRVQPIK LARVTKVLGR TGSQGQCTQV RVEFMDDTSR SIIRNVKGPV REGDVLTLLE SEREARRLR //