ID RL18_MOUSE Reviewed; 188 AA. AC P35980; Q9CQF1; Q9D987; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 178. DE RecName: Full=Large ribosomal subunit protein eL18 {ECO:0000305}; DE AltName: Full=60S ribosomal protein L18; GN Name=Rpl18; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Lung; RX PubMed=8359697; DOI=10.1016/0378-1119(93)90433-4; RA Hou E.W., Li S.S.L.; RT "Sequence analysis of mouse cDNAs encoding ribosomal proteins L12 and RT L18."; RL Gene 130:287-290(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [5] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV} RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=36517592; DOI=10.1038/s41586-022-05508-0; RA Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D., RA Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T., RA Guo X., Qin Y., Sha J.; RT "A male germ-cell-specific ribosome controls male fertility."; RL Nature 0:0-0(2022). CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). CC The ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:36517592). CC {ECO:0000269|PubMed:36517592}. CC -!- SUBUNIT: Component of the large ribosomal subunit. CC {ECO:0000269|PubMed:36517592}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q07020}. Cytoplasm CC {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q95342}. 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:Q07020, ECO:0000250|UniProtKB:Q95342}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 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; L04128; AAA40067.1; -; mRNA. DR EMBL; AK007263; BAB24923.1; -; mRNA. DR EMBL; AK009044; BAB26043.1; -; mRNA. DR EMBL; AK010510; BAB26993.1; -; mRNA. DR EMBL; AK012580; BAB28332.1; -; mRNA. DR EMBL; BC082290; AAH82290.1; -; mRNA. DR CCDS; CCDS39958.1; -. DR PIR; JN0779; JN0779. DR RefSeq; NP_033103.2; NM_009077.2. DR PDB; 6SWA; EM; 3.10 A; P=1-188. DR PDB; 7CPU; EM; 2.82 A; LQ=1-188. DR PDB; 7CPV; EM; 3.03 A; LQ=1-188. DR PDB; 7LS1; EM; 3.30 A; K2=1-188. DR PDB; 7LS2; EM; 3.10 A; K2=1-188. DR PDBsum; 6SWA; -. DR PDBsum; 7CPU; -. DR PDBsum; 7CPV; -. DR PDBsum; 7LS1; -. DR PDBsum; 7LS2; -. DR AlphaFoldDB; P35980; -. DR EMDB; EMD-10321; -. DR EMDB; EMD-23500; -. DR EMDB; EMD-23501; -. DR EMDB; EMD-30432; -. DR EMDB; EMD-30433; -. DR SMR; P35980; -. DR BioGRID; 202968; 87. DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit. DR ComplexPortal; CPX-7662; 60S cytosolic large ribosomal subunit, testis-specific variant. DR ComplexPortal; CPX-7663; 60S cytosolic large ribosomal subunit, striated muscle variant. DR CORUM; P35980; -. DR IntAct; P35980; 4. DR MINT; P35980; -. DR STRING; 10090.ENSMUSP00000147816; -. DR GlyGen; P35980; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P35980; -. DR PhosphoSitePlus; P35980; -. DR SwissPalm; P35980; -. DR EPD; P35980; -. DR jPOST; P35980; -. DR PaxDb; 10090-ENSMUSP00000103365; -. DR PeptideAtlas; P35980; -. DR ProteomicsDB; 254890; -. DR Pumba; P35980; -. DR DNASU; 19899; -. DR Ensembl; ENSMUST00000072503.13; ENSMUSP00000072320.7; ENSMUSG00000059070.17. DR Ensembl; ENSMUST00000210640.2; ENSMUSP00000147816.2; ENSMUSG00000059070.17. DR GeneID; 19899; -. DR KEGG; mmu:19899; -. DR UCSC; uc009gww.1; mouse. DR AGR; MGI:98003; -. DR CTD; 6141; -. DR MGI; MGI:98003; Rpl18. DR VEuPathDB; HostDB:ENSMUSG00000059070; -. DR eggNOG; KOG1714; Eukaryota. DR GeneTree; ENSGT00390000012976; -. DR HOGENOM; CLU_080024_0_0_1; -. DR InParanoid; P35980; -. DR OMA; DHTTKQH; -. DR OrthoDB; 1122253at2759; -. DR PhylomeDB; P35980; -. DR TreeFam; TF300202; -. DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits. DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR BioGRID-ORCS; 19899; 26 hits in 55 CRISPR screens. DR ChiTaRS; Rpl18; mouse. DR PRO; PR:P35980; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P35980; Protein. DR Bgee; ENSMUSG00000059070; Expressed in epiblast (generic) and 67 other cell types or tissues. DR ExpressionAtlas; P35980; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI. DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; ISO:MGI. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB. DR Gene3D; 3.100.10.10; -; 1. DR InterPro; IPR000039; Ribosomal_eL18. DR InterPro; IPR021132; Ribosomal_eL18/eL18-A/B/_CS. DR InterPro; IPR021131; Ribosomal_uL15/eL18. DR InterPro; IPR036227; Ribosomal_uL15/eL18_sf. DR PANTHER; PTHR10934; 60S RIBOSOMAL PROTEIN L18; 1. DR PANTHER; PTHR10934:SF2; 60S RIBOSOMAL PROTEIN L18; 1. DR Pfam; PF17135; Ribosomal_L18; 1. DR SUPFAM; SSF52080; Ribosomal proteins L15p and L18e; 1. DR PROSITE; PS01106; RIBOSOMAL_L18E; 1. DR Genevisible; P35980; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Isopeptide bond; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW Ubl conjugation. FT CHAIN 1..188 FT /note="Large ribosomal subunit protein eL18" FT /id="PRO_0000132770" FT REGION 150..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 165..188 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 158 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q07020" FT CROSSLNK 119 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q07020" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q07020" FT CONFLICT 59 FT /note="P -> S (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="A -> V (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="K -> R (in Ref. 2; BAB24923)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="A -> G (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" FT CONFLICT 147..150 FT /note="EVYR -> DVFP (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="A -> V (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" FT CONFLICT 160..162 FT /note="HSH -> YSQ (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" FT CONFLICT 173..174 FT /note="KF -> RL (in Ref. 1; AAA40067)" FT /evidence="ECO:0000305" SQ SEQUENCE 188 AA; 21645 MW; 9489EFE201ABF7A1 CRC64; MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR LFMSRTNRPP LSLSRMIRKM KLPGRENKTA VVVGTVTDDV RILEVPKLKV CALRVSSRAR SRILKAGGKI LTFDQLALES PKGRGTVLLS GPRKGREVYR HFGKAPGTPH SHTKPYVRSK GRKFERARGR RASRGYKN //