ID RS12_RABIT Reviewed; 132 AA. AC G1SFR8; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Small ribosomal subunit protein eS12; DE AltName: Full=40S ribosomal protein S12 {ECO:0000255|RuleBase:RU000670}; GN Name=RPS12; 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 9-132 OF RIBOSOME, RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. 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 SUBUNIT, AND SUBCELLULAR LOCATION. 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 11-130 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 14-130 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 50-132 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 [10] {ECO:0007744|PDB:6R5Q, ECO:0007744|PDB:6R6G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 14-130 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, 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 [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 9-132 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 [14] {ECO:0007744|PDB:6W2S, ECO:0007744|PDB:6W2T} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP 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 [15] {ECO:0007744|PDB:7SYI, ECO:0007744|PDB:7SYJ, ECO:0007744|PDB:7SYO, ECO:0007744|PDB:7SYP} 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:7ZJW, ECO:0007744|PDB:7ZJX} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP 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). CC -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor CC of the small eukaryotic ribosomal subunit (PubMed:23873042, CC PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). 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, PubMed:30517857). CC Subunit of the 40S ribosomal complex (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242, PubMed:30517857). 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: Part of the small subunit (SSU) processome, composed of more CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 CC (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, CC PubMed:30517857, PubMed:29856316, PubMed:30355441, PubMed:30293783, CC PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:33296660, CC PubMed:32286223, PubMed:35822879, PubMed:35709277). Subunit of the 40S CC ribosomal complex (PubMed:23873042, PubMed:25601755, PubMed:26245381, CC PubMed:27863242, PubMed:30517857, PubMed:29856316, PubMed:30355441, CC PubMed:30293783, PubMed:31246176, PubMed:31609474, PubMed:31768042, CC PubMed:33296660, PubMed:32286223, PubMed:35822879, PubMed:35709277). 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:35709277, CC 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: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:35709277, ECO:0000269|PubMed:35822879}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P25398}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS12 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; AAGW02028778; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002714875.1; XM_002714829.3. DR PDB; 3JAG; EM; 3.65 A; MM=9-132. DR PDB; 3JAH; EM; 3.45 A; MM=9-132. DR PDB; 3JAI; EM; 3.65 A; MM=9-132. DR PDB; 4D5L; EM; 9.00 A; M=1-132. DR PDB; 4D61; EM; 9.00 A; M=1-132. DR PDB; 4KZX; X-ray; 7.81 A; M=1-132. DR PDB; 4KZY; X-ray; 7.01 A; M=1-132. DR PDB; 4KZZ; X-ray; 7.03 A; M=1-132. DR PDB; 5K0Y; EM; 5.80 A; r=9-132. DR PDB; 5LZS; EM; 3.31 A; MM=1-132. DR PDB; 5LZT; EM; 3.65 A; MM=1-132. DR PDB; 5LZU; EM; 3.75 A; MM=1-132. DR PDB; 5LZV; EM; 3.35 A; MM=1-132. DR PDB; 5LZW; EM; 3.53 A; MM=1-132. DR PDB; 5LZX; EM; 3.67 A; MM=1-132. DR PDB; 5LZY; EM; 3.99 A; MM=1-132. DR PDB; 5LZZ; EM; 3.47 A; MM=1-132. DR PDB; 6D90; EM; 3.20 A; NN=1-132. DR PDB; 6D9J; EM; 3.20 A; NN=1-132. DR PDB; 6GZ3; EM; 3.60 A; BM=11-130. DR PDB; 6HCF; EM; 3.90 A; N1=1-132. DR PDB; 6HCJ; EM; 3.80 A; N2=1-132. DR PDB; 6HCM; EM; 6.80 A; N1=1-132. DR PDB; 6HCQ; EM; 6.50 A; N2=1-132. DR PDB; 6MTB; EM; 3.60 A; MM=14-130. DR PDB; 6MTC; EM; 3.40 A; MM=14-130. DR PDB; 6MTD; EM; 3.30 A; MM=14-130. DR PDB; 6MTE; EM; 3.40 A; MM=14-130. DR PDB; 6P4G; EM; 3.10 A; N=1-132. DR PDB; 6P4H; EM; 3.20 A; N=1-132. DR PDB; 6P5I; EM; 3.10 A; N=1-132. DR PDB; 6P5J; EM; 3.10 A; N=1-132. DR PDB; 6P5K; EM; 3.10 A; N=1-132. DR PDB; 6P5N; EM; 3.20 A; N=1-132. DR PDB; 6R5Q; EM; 3.00 A; RR=14-130. DR PDB; 6R6G; EM; 3.70 A; RR=14-130. DR PDB; 6R6P; EM; 3.10 A; RR=14-130. DR PDB; 6R7Q; EM; 3.90 A; RR=14-130. DR PDB; 6SGC; EM; 2.80 A; N1=1-132. DR PDB; 6W2S; EM; 3.00 A; N=1-132. DR PDB; 6W2T; EM; 3.36 A; N=1-132. DR PDB; 6YAL; EM; 3.00 A; O=1-132. DR PDB; 6YAM; EM; 3.60 A; O=1-132. DR PDB; 6YAN; EM; 3.48 A; O=9-132. DR PDB; 6ZVK; EM; 3.49 A; e3=9-132. DR PDB; 7A01; EM; 3.60 A; e3=9-132. DR PDB; 7JQB; EM; 2.70 A; N=1-132. DR PDB; 7JQC; EM; 3.30 A; N=1-132. DR PDB; 7MDZ; EM; 3.20 A; MM=1-132. DR PDB; 7NWG; EM; 3.80 A; N2=10-132. DR PDB; 7NWH; EM; 4.10 A; MM=10-132. DR PDB; 7NWI; EM; 3.13 A; MM=9-132. DR PDB; 7O7Y; EM; 2.20 A; Al=1-132. DR PDB; 7O7Z; EM; 2.40 A; Al=1-132. DR PDB; 7O80; EM; 2.90 A; Al=1-132. DR PDB; 7O81; EM; 3.10 A; Al=1-132. DR PDB; 7SYG; EM; 4.30 A; N=1-132. DR PDB; 7SYH; EM; 4.60 A; N=1-132. DR PDB; 7SYI; EM; 4.50 A; N=1-132. DR PDB; 7SYJ; EM; 4.80 A; N=1-132. DR PDB; 7SYK; EM; 4.20 A; N=1-132. DR PDB; 7SYL; EM; 4.50 A; N=1-132. DR PDB; 7SYM; EM; 4.80 A; N=1-132. DR PDB; 7SYN; EM; 4.00 A; N=1-132. DR PDB; 7SYO; EM; 4.60 A; N=1-132. DR PDB; 7SYP; EM; 4.00 A; N=1-132. DR PDB; 7SYQ; EM; 3.80 A; N=1-132. DR PDB; 7SYR; EM; 3.60 A; N=1-132. DR PDB; 7SYS; EM; 3.50 A; N=1-132. DR PDB; 7SYT; EM; 4.40 A; N=1-132. DR PDB; 7SYU; EM; 4.60 A; N=1-132. DR PDB; 7SYV; EM; 3.90 A; N=1-132. DR PDB; 7SYW; EM; 3.70 A; N=1-132. DR PDB; 7SYX; EM; 3.70 A; N=1-132. DR PDB; 7TOQ; EM; 3.10 A; AS12=14-130. DR PDB; 7TOR; EM; 2.90 A; AS12=14-130. DR PDB; 7ZJW; EM; 2.80 A; SX=1-132. DR PDB; 7ZJX; EM; 3.10 A; SX=1-132. DR PDB; 8BHF; EM; 3.10 A; N3=14-130. DR PDB; 8BTK; EM; 3.50 A; Al=1-132. DR PDB; 8P2K; EM; 2.90 A; Al=1-132. 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; 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; 7ZJW; -. DR PDBsum; 7ZJX; -. DR PDBsum; 8BHF; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1SFR8; -. DR IntAct; G1SFR8; 1. DR STRING; 9986.ENSOCUP00000001378; -. DR PaxDb; 9986-ENSOCUP00000001378; -. DR Ensembl; ENSOCUT00000001606.4; ENSOCUP00000001378.2; ENSOCUG00000001606.4. DR GeneID; 100345945; -. DR eggNOG; KOG3406; Eukaryota. DR HOGENOM; CLU_110343_1_1_1; -. DR InParanoid; G1SFR8; -. DR OrthoDB; 5045908at2759; -. DR TreeFam; TF300196; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000001606; Expressed in upper lobe of left lung and 15 other cell types or tissues. DR PROSITE; PS01189; RIBOSOMAL_S12E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P25398" FT CHAIN 2..132 FT /note="Small ribosomal subunit protein eS12" FT /id="PRO_0000460061" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P25398" FT MOD_RES 129 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P63323" SQ SEQUENCE 132 AA; 14515 MW; 45AD1274D55FFA25 CRC64; MAEEGIAAGG VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC VLASNCDEPM YVKLVEALCA EHQINLIKVD DNKKLGEWVG LCKIDREGKP RKVVGCSCVV VKDYGKESQA KDVIEEYFKC KK //