ID RL3_MOUSE Reviewed; 403 AA. AC P27659; O89071; Q91VJ6; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 27-MAR-2024, entry version 182. DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000305}; DE AltName: Full=60S ribosomal protein L3; DE AltName: Full=J1 protein; GN Name=Rpl3; 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]. RX PubMed=2628163; DOI=10.1101/gad.3.12b.2062; RA Peckham I., Sobel S., Comer J., Jaenisch R., Barklis E.; RT "Retrovirus activation in embryonal carcinoma cells by cellular RT promoters."; RL Genes Dev. 3:2062-2071(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1711497; DOI=10.1016/0378-1119(91)90409-5; RA Petersen R., Sobel S., Wang C.T., Jaenisch R., Barklis E.; RT "Cellular transcripts encoded at a locus which permits retrovirus RT expression in mouse embryonic cells."; RL Gene 101:177-183(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD; RC TISSUE=Bone marrow, Brain cortex, Heart, Kidney, Liver, Lung, Mammary RC gland, and Thymus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb, and Mammary tumor; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 183-299. RC STRAIN=BALB/cJ; TISSUE=Spleen; RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5; RA Chu C.C., Paul W.E.; RT "Expressed genes in interleukin-4 treated B cells identified by cDNA RT representational difference analysis."; RL Mol. Immunol. 35:487-502(1998). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136; LYS-286 AND LYS-373, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP INTERACTION WITH DHX33. RX PubMed=26100019; DOI=10.1128/mcb.00315-15; RA Zhang Y., You J., Wang X., Weber J.; RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation."; RL Mol. Cell. Biol. 35:2918-2931(2015). RN [11] {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 (PubMed:36517592). CC Interacts with DHX33 (PubMed:26100019). {ECO:0000269|PubMed:26100019, CC ECO:0000269|PubMed:36517592}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P39023}. Cytoplasm CC {ECO:0000269|PubMed:36517592}. CC -!- PTM: Constitutively monomethylated at His-245 by METTL18. Methylation CC at His-245 regulates translation elongation by slowing ribosome CC traversal on tyrosine codons: slower elongation provides enough time CC for proper folding of synthesized proteins and prevents cellular CC aggregation of tyrosine-rich proteins. It is not required for CC incorporation of RPL3 into ribosomes. {ECO:0000250|UniProtKB:P39023}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 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; Y00225; CAA68370.1; -; mRNA. DR EMBL; U89417; AAC36524.1; -; mRNA. DR EMBL; AK088993; BAC40691.1; -; mRNA. DR EMBL; AK144518; BAE25922.1; -; mRNA. DR EMBL; AK144816; BAE26078.1; -; mRNA. DR EMBL; AK146502; BAE27217.1; -; mRNA. DR EMBL; AK149494; BAE28917.1; -; mRNA. DR EMBL; AK151596; BAE30536.1; -; mRNA. DR EMBL; AK166433; BAE38773.1; -; mRNA. DR EMBL; AK166825; BAE39049.1; -; mRNA. DR EMBL; AK167787; BAE39818.1; -; mRNA. DR EMBL; AK167947; BAE39950.1; -; mRNA. DR EMBL; AK168040; BAE40022.1; -; mRNA. DR EMBL; AK168059; BAE40037.1; -; mRNA. DR EMBL; AK168126; BAE40095.1; -; mRNA. DR EMBL; AK168128; BAE40097.1; -; mRNA. DR EMBL; AK168224; BAE40178.1; -; mRNA. DR EMBL; AK168744; BAE40585.1; -; mRNA. DR EMBL; AK169060; BAE40848.1; -; mRNA. DR EMBL; AK169235; BAE41003.1; -; mRNA. DR EMBL; AK169321; BAE41075.1; -; mRNA. DR EMBL; AK170819; BAE42051.1; -; mRNA. DR EMBL; CH466550; EDL04616.1; -; Genomic_DNA. DR EMBL; BC009655; AAH09655.1; -; mRNA. DR EMBL; BC083134; AAH83134.1; -; mRNA. DR EMBL; BC094059; AAH94059.1; -; mRNA. DR EMBL; BC158039; AAI58040.1; -; mRNA. DR CCDS; CCDS37144.1; -. DR RefSeq; NP_038790.2; NM_013762.2. DR PDB; 6SWA; EM; 3.10 A; B=1-403. DR PDB; 7CPU; EM; 2.82 A; LB=1-403. DR PDB; 7CPV; EM; 3.03 A; LB=1-403. DR PDB; 7LS1; EM; 3.30 A; E2=1-403. DR PDB; 7LS2; EM; 3.10 A; E2=1-403. DR PDBsum; 6SWA; -. DR PDBsum; 7CPU; -. DR PDBsum; 7CPV; -. DR PDBsum; 7LS1; -. DR PDBsum; 7LS2; -. DR AlphaFoldDB; P27659; -. DR EMDB; EMD-10321; -. DR EMDB; EMD-23500; -. DR EMDB; EMD-23501; -. DR EMDB; EMD-30432; -. DR EMDB; EMD-30433; -. DR SMR; P27659; -. DR BioGRID; 205174; 90. DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit. DR ComplexPortal; CPX-7662; 60S cytosolic large ribosomal subunit, testis-specific variant. DR CORUM; P27659; -. DR IntAct; P27659; 3. DR MINT; P27659; -. DR STRING; 10090.ENSMUSP00000080354; -. DR GlyGen; P27659; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P27659; -. DR MetOSite; P27659; -. DR PhosphoSitePlus; P27659; -. DR SwissPalm; P27659; -. DR EPD; P27659; -. DR jPOST; P27659; -. DR MaxQB; P27659; -. DR PaxDb; 10090-ENSMUSP00000080354; -. DR PeptideAtlas; P27659; -. DR ProteomicsDB; 299902; -. DR Pumba; P27659; -. DR Antibodypedia; 1245; 328 antibodies from 30 providers. DR DNASU; 27367; -. DR Ensembl; ENSMUST00000081650.15; ENSMUSP00000080354.8; ENSMUSG00000060036.15. DR GeneID; 27367; -. DR KEGG; mmu:27367; -. DR UCSC; uc007wvb.2; mouse. DR AGR; MGI:1351605; -. DR CTD; 6122; -. DR MGI; MGI:1351605; Rpl3. DR VEuPathDB; HostDB:ENSMUSG00000060036; -. DR eggNOG; KOG0746; Eukaryota. DR GeneTree; ENSGT00390000017606; -. DR HOGENOM; CLU_033361_2_1_1; -. DR InParanoid; P27659; -. DR OMA; QRTEYNK; -. DR OrthoDB; 20251at2759; -. DR PhylomeDB; P27659; -. DR TreeFam; TF300555; -. 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; 27367; 22 hits in 57 CRISPR screens. DR ChiTaRS; Rpl3; mouse. DR PRO; PR:P27659; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; P27659; Protein. DR Bgee; ENSMUSG00000060036; Expressed in ventricular zone and 65 other cell types or tissues. DR ExpressionAtlas; P27659; 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:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005840; C:ribosome; ISO:MGI. DR GO; GO:0045202; C:synapse; ISO:MGI. DR GO; GO:0008097; F:5S rRNA binding; 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:0071353; P:cellular response to interleukin-4; IDA:MGI. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.1430.10; -; 1. DR Gene3D; 4.10.960.10; Ribosomal protein L3, domain 3; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR045077; L3_arc_euk. DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf. DR InterPro; IPR000597; Ribosomal_uL3. DR InterPro; IPR019926; Ribosomal_uL3_CS. DR InterPro; IPR009000; Transl_B-barrel_sf. DR PANTHER; PTHR11363:SF4; 60S RIBOSOMAL PROTEIN L3; 1. DR PANTHER; PTHR11363; 60S RIBOSOMAL PROTEIN L3-RELATED; 1. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. DR Genevisible; P27659; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Ubl conjugation. FT CHAIN 1..403 FT /note="Large ribosomal subunit protein uL3" FT /id="PRO_0000077229" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 136 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 245 FT /note="Tele-methylhistidine" FT /evidence="ECO:0000250|UniProtKB:P39023" FT MOD_RES 286 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 294 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P39023" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P39023" FT MOD_RES 366 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P39023" FT MOD_RES 373 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT CROSSLNK 39 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 224 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 226 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 286 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 294 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 366 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 386 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 393 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CROSSLNK 399 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P39023" FT CONFLICT 265 FT /note="S -> T (in Ref. 1; CAA68370)" FT /evidence="ECO:0000305" SQ SEQUENCE 403 AA; 46110 MW; 87AA82D9B2A8481E CRC64; MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDASKP VHLTAFLGYK AGMTHIVREV DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR TFKTVFAEHI SDECKRRFYK NWHKSKKKAF TKYCKKWQDD TGKKQLEKDF NSMKKYCQVI RIIAHTQMRL LPLRQKKAHL MEIQVNGGTV AEKLDWARER LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL PRKTHRGLRK VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK NNASTDYDLS DKSINPLGGF VHYGEVTNDF IMLKGCVVGT KKRVLTLRKS LLVQTKRRAL EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE EGA //