ID RS30_RABIT Reviewed; 133 AA. AC G1T8A2; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein; DE AltName: Full=FAU ubiquitin like and ribosomal protein S30 fusion; DE Contains: DE RecName: Full=Ubiquitin-like protein FUBI; DE Contains: DE RecName: Full=Small ribosomal subunit protein eS30; DE AltName: Full=40S ribosomal protein S30; GN Name=FAU; 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 79-133 OF 40S RIBOSOME, FUNCTION, RP SUBUNIT, 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 79-133 OF 75-133 OF RP RIBOSOME, 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 79-133 OF 77-133 OF RP RIBOSOME, 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 79-133 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, ECO:0007744|PDB:6D9J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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:6MTB, ECO:0007744|PDB:6MTC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 79-133 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 [8] {ECO:0007744|PDB:6HCF, ECO:0007744|PDB:6HCJ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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 [9] {ECO:0007744|PDB:6R5Q, ECO:0007744|PDB:6R6G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 79-133 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 [10] {ECO:0007744|PDB:6P5I, ECO:0007744|PDB:6P5J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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 [11] {ECO:0007744|PDB:6SGC} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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 [12] {ECO:0007744|PDB:6W2S, ECO:0007744|PDB:6W2T} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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 [13] {ECO:0007744|PDB:7SYO, ECO:0007744|PDB:7SYP} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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 [14] {ECO:0007744|PDB:7UCJ, ECO:0007744|PDB:7UCK} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 79-133 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 [15] {ECO:0007744|PDB:7ZJW, ECO:0007744|PDB:7ZJX} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=35709277; DOI=10.1126/science.abg3875; RA Hilal T., Killam B.Y., Grozdanovic M., Dobosz-Bartoszek M., Loerke J., RA Buerger J., Mielke T., Copeland P.R., Simonovic M., Spahn C.M.T.; RT "Structure of the mammalian ribosome as it decodes the selenocysteine UGA RT codon."; RL Science 376:1338-1343(2022). RN [16] {ECO:0007744|PDB:7OYD} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) OF 79-133 OF RIBOSOME, RP SUBCELLULAR 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: [Ubiquitin-like protein FUBI]: May have pro-apoptotic CC activity. {ECO:0000250|UniProtKB:P62861}. CC -!- FUNCTION: [Small ribosomal subunit protein eS30]: Component of the 40S CC subunit of the ribosome (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242). Contributes to the assembly and CC function of 40S ribosomal subunits (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242). {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242}. CC -!- SUBUNIT: [Small ribosomal subunit protein eS30]: Component of the 40S CC subunit of the ribosome. {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:31246176, ECO:0000269|PubMed:31609474, CC ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35709277, CC ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. CC -!- SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS30]: Cytoplasm 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:31246176, CC ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, CC ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:35679869, CC ECO:0000269|PubMed:35709277, ECO:0000269|PubMed:35822879, CC ECO:0000269|PubMed:36653451}. Nucleus {ECO:0000250|UniProtKB:P62861}. CC -!- PTM: FUBI is cleaved from ribosomal protein S30 by the deubiquitinase CC USP36 before the assembly of ribosomal protein S30 into pre-40S CC ribosomal particles. FUBI removal from ribosomal protein S30 is a CC crucial event for the final maturation of pre-40S particles. CC {ECO:0000250|UniProtKB:P62861}. CC -!- MISCELLANEOUS: FAU encodes a fusion protein consisting of the CC ubiquitin-like protein FUBI at the N terminus and ribosomal protein S30 CC at the C terminus. {ECO:0000250|UniProtKB:P62861}. CC -!- MISCELLANEOUS: [Ubiquitin-like protein FUBI]: Lacks the typical lysine CC residues that participate in Ub's polyubiquitination. However contains CC a C-terminal di-glycine signature after its proteolytic separation from CC ribosomal protein S30 and could theoretically be conjugated onto target CC proteins. {ECO:0000250|UniProtKB:P62861}. CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic CC ribosomal protein eS30 family. {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 RefSeq; XP_002723447.1; XM_002723401.3. DR PDB; 3JAG; EM; 3.65 A; ee=77-133. DR PDB; 3JAH; EM; 3.45 A; ee=77-133. DR PDB; 3JAI; EM; 3.65 A; ee=77-133. DR PDB; 4D5L; EM; 9.00 A; e=75-133. DR PDB; 4D61; EM; 9.00 A; e=75-133. DR PDB; 4KZX; X-ray; 7.81 A; e=1-133. DR PDB; 4KZY; X-ray; 7.01 A; e=1-133. DR PDB; 4KZZ; X-ray; 7.03 A; e=1-133. DR PDB; 5K0Y; EM; 5.80 A; V=75-133. DR PDB; 5LZS; EM; 3.31 A; ee=1-133. DR PDB; 5LZT; EM; 3.65 A; ee=1-133. DR PDB; 5LZU; EM; 3.75 A; ee=1-133. DR PDB; 5LZV; EM; 3.35 A; ee=1-133. DR PDB; 5LZW; EM; 3.53 A; ee=1-133. DR PDB; 5LZX; EM; 3.67 A; ee=1-133. DR PDB; 5LZY; EM; 3.99 A; ee=1-133. DR PDB; 5LZZ; EM; 3.47 A; ee=1-133. DR PDB; 6D90; EM; 3.20 A; ff=1-133. DR PDB; 6D9J; EM; 3.20 A; ff=1-133. DR PDB; 6HCF; EM; 3.90 A; f1=1-133. DR PDB; 6HCJ; EM; 3.80 A; f2=1-133. DR PDB; 6HCM; EM; 6.80 A; f1=1-133. DR PDB; 6HCQ; EM; 6.50 A; f2=1-133. DR PDB; 6MTB; EM; 3.60 A; ee=79-133. DR PDB; 6MTC; EM; 3.40 A; ee=79-133. DR PDB; 6MTD; EM; 3.30 A; ee=79-133. DR PDB; 6MTE; EM; 3.40 A; ee=79-133. DR PDB; 6P4G; EM; 3.10 A; f=1-133. DR PDB; 6P4H; EM; 3.20 A; f=1-133. DR PDB; 6P5I; EM; 3.10 A; f=1-133. DR PDB; 6P5J; EM; 3.10 A; f=1-133. DR PDB; 6P5K; EM; 3.10 A; f=1-133. DR PDB; 6P5N; EM; 3.20 A; f=1-133. DR PDB; 6R5Q; EM; 3.00 A; AA=79-133. DR PDB; 6R6G; EM; 3.70 A; AA=79-133. DR PDB; 6R6P; EM; 3.10 A; AA=79-133. DR PDB; 6R7Q; EM; 3.90 A; AA=79-133. DR PDB; 6SGC; EM; 2.80 A; f1=1-133. DR PDB; 6W2S; EM; 3.00 A; f=1-133. DR PDB; 6W2T; EM; 3.36 A; f=1-133. DR PDB; 6YAL; EM; 3.00 A; i=1-133. DR PDB; 6YAM; EM; 3.60 A; i=75-133. DR PDB; 6YAN; EM; 3.48 A; i=75-133. DR PDB; 7JQB; EM; 2.70 A; f=1-133. DR PDB; 7JQC; EM; 3.30 A; f=1-133. DR PDB; 7MDZ; EM; 3.20 A; ee=1-133. DR PDB; 7NWG; EM; 3.80 A; f2=1-133. DR PDB; 7NWH; EM; 4.10 A; ee=1-133. DR PDB; 7NWI; EM; 3.13 A; ee=1-133. DR PDB; 7O7Y; EM; 2.20 A; AD=1-133. DR PDB; 7O7Z; EM; 2.40 A; AD=1-133. DR PDB; 7O80; EM; 2.90 A; AD=1-133. DR PDB; 7O81; EM; 3.10 A; AD=1-133. DR PDB; 7OYD; EM; 2.30 A; Ee=1-133. DR PDB; 7SYG; EM; 4.30 A; f=1-133. DR PDB; 7SYH; EM; 4.60 A; f=1-133. DR PDB; 7SYI; EM; 4.50 A; f=1-133. DR PDB; 7SYJ; EM; 4.80 A; f=1-133. DR PDB; 7SYK; EM; 4.20 A; f=1-133. DR PDB; 7SYL; EM; 4.50 A; f=1-133. DR PDB; 7SYM; EM; 4.80 A; f=1-133. DR PDB; 7SYN; EM; 4.00 A; f=1-133. DR PDB; 7SYO; EM; 4.60 A; f=1-133. DR PDB; 7SYP; EM; 4.00 A; f=1-133. DR PDB; 7SYQ; EM; 3.80 A; f=1-133. DR PDB; 7SYR; EM; 3.60 A; f=1-133. DR PDB; 7SYS; EM; 3.50 A; f=1-133. DR PDB; 7SYT; EM; 4.40 A; f=1-133. DR PDB; 7SYU; EM; 4.60 A; f=1-133. DR PDB; 7SYV; EM; 3.90 A; f=1-133. DR PDB; 7SYW; EM; 3.70 A; f=1-133. DR PDB; 7SYX; EM; 3.70 A; f=1-133. DR PDB; 7TOQ; EM; 3.10 A; AS30=79-133. DR PDB; 7TOR; EM; 2.90 A; AS30=79-133. DR PDB; 7UCJ; EM; 3.10 A; Ee=79-133. DR PDB; 7UCK; EM; 2.80 A; Ee=79-133. DR PDB; 7ZJW; EM; 2.80 A; SE=1-133. DR PDB; 7ZJX; EM; 3.10 A; SE=1-133. DR PDB; 8BTK; EM; 3.50 A; AD=1-133. DR PDB; 8P2K; EM; 2.90 A; AD=1-133. 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; 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; 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; 7ZJW; -. DR PDBsum; 7ZJX; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1T8A2; -. DR IntAct; G1T8A2; 1. DR PaxDb; 9986-ENSOCUP00000012787; -. DR Ensembl; ENSOCUT00000014874.2; ENSOCUP00000012787.2; ENSOCUG00000014878.3. DR GeneID; 100354401; -. DR eggNOG; KOG0001; Eukaryota. DR eggNOG; KOG0009; Eukaryota. DR HOGENOM; CLU_010412_5_0_1; -. DR OrthoDB; 177691at2759; -. DR TreeFam; TF313779; -. DR Proteomes; UP000001811; Unplaced. DR Bgee; ENSOCUG00000014878; Expressed in uterus and 17 other cell types or tissues. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..133 FT /note="Ubiquitin-like FUBI-ribosomal protein eS30 fusion FT protein" FT /id="PRO_0000460082" FT CHAIN 1..74 FT /note="Ubiquitin-like protein FUBI" FT /evidence="ECO:0000250|UniProtKB:P62861" FT /id="PRO_0000460083" FT CHAIN 75..133 FT /note="Small ribosomal subunit protein eS30" FT /evidence="ECO:0000250|UniProtKB:P62861" FT /id="PRO_0000460084" FT DOMAIN 1..74 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT MOD_RES 125 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P62862" SQ SEQUENCE 133 AA; 14472 MW; 65BA348B25583023 CRC64; MQLFVRAQEL HTLEVTGRET VAQIKAHVAS LEGIAPEDQV VLLAGTPLED EATLGQCGVE ALSTLEVAGR MLGGKVHGSL ARVGKVRGQT LKVAKQEKKK KRTGRAKRRM QYNRRFVNVV PTFGKKKGPN ANS //