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Database: UniProt
Entry: G1T8A2
LinkDB: G1T8A2
Original site: G1T8A2 
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}.
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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
//
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