ID RL28_MOUSE Reviewed; 137 AA. AC P41105; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 185. DE RecName: Full=Large ribosomal subunit protein eL28 {ECO:0000305}; DE AltName: Full=60S ribosomal protein L28; GN Name=Rpl28; 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 TISSUE=Testis; RX PubMed=7515017; DOI=10.1016/0378-1119(94)90284-4; RA Burke P.S., Lium E., Lin C.S., Wolgemuth D.J.; RT "Sequence and expression of a cDNA encoding the mouse homologue of the rat RT ribosomal protein L28."; RL Gene 142:315-316(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Kidney; 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; TISSUE=Colon; 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 PROTEIN SEQUENCE OF 2-20 AND 36-46, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic fibroblast; RA Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.; RL Submitted (FEB-2008) to UniProtKB. RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Liver, 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 [6] {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 {ECO:0000269|PubMed:36517592}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL28 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; X74856; CAA52848.1; -; mRNA. DR EMBL; AK018714; BAB31362.1; -; mRNA. DR EMBL; AK076133; BAC36209.1; -; mRNA. DR EMBL; BC024395; AAH24395.1; -; mRNA. DR CCDS; CCDS39742.1; -. DR PIR; I48738; I48738. DR RefSeq; NP_033107.1; NM_009081.2. DR PDB; 6SWA; EM; 3.10 A; p=2-123. DR PDB; 7CPU; EM; 2.82 A; Lr=1-137. DR PDB; 7CPV; EM; 3.03 A; Lr=1-137. DR PDB; 7LS1; EM; 3.30 A; k2=1-137. DR PDB; 7LS2; EM; 3.10 A; k2=1-137. DR PDB; 9H4N; EM; 2.46 A; k2=2-126. DR PDB; 9QOH; EM; 2.78 A; k2=1-137. DR PDB; 9QQL; EM; 3.09 A; k2=1-137. DR PDB; 9QQP; EM; 2.80 A; k2=1-137. DR PDB; 9QSA; EM; 3.40 A; k2=1-137. DR PDB; 9QWT; EM; 3.10 A; k2=1-137. DR AlphaFoldDB; P41105; -. DR EMDB; EMD-10321; -. DR EMDB; EMD-23500; -. DR EMDB; EMD-23501; -. DR EMDB; EMD-30432; -. DR EMDB; EMD-30433; -. DR EMDB; EMD-51865; -. DR EMDB; EMD-53262; -. DR EMDB; EMD-53307; -. DR EMDB; EMD-53310; -. DR EMDB; EMD-53333; -. DR EMDB; EMD-53427; -. DR SMR; P41105; -. DR BioGRID; 202975; 83. 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 DIP; DIP-59974N; -. DR FunCoup; P41105; 1759. DR IntAct; P41105; 8. DR MINT; P41105; -. DR STRING; 10090.ENSMUSP00000032597; -. DR GlyGen; P41105; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P41105; -. DR MetOSite; P41105; -. DR PhosphoSitePlus; P41105; -. DR SwissPalm; P41105; -. DR jPOST; P41105; -. DR PaxDb; 10090-ENSMUSP00000032597; -. DR PeptideAtlas; P41105; -. DR ProteomicsDB; 299857; -. DR Pumba; P41105; -. DR Antibodypedia; 46430; 181 antibodies from 27 providers. DR DNASU; 19943; -. DR Ensembl; ENSMUST00000032597.12; ENSMUSP00000032597.6; ENSMUSG00000030432.13. DR Ensembl; ENSMUST00000078432.5; ENSMUSP00000104217.2; ENSMUSG00000030432.13. DR GeneID; 19943; -. DR KEGG; mmu:19943; -. DR UCSC; uc009eys.1; mouse. DR AGR; MGI:101839; -. DR CTD; 6158; -. DR MGI; MGI:101839; Rpl28. DR VEuPathDB; HostDB:ENSMUSG00000030432; -. DR eggNOG; KOG3412; Eukaryota. DR GeneTree; ENSGT00390000008732; -. DR HOGENOM; CLU_106801_1_0_1; -. DR InParanoid; P41105; -. DR OMA; WMIIRNC; -. DR OrthoDB; 338850at2759; -. DR PhylomeDB; P41105; -. 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 Reactome; R-MMU-9954709; Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide. DR Reactome; R-MMU-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR Reactome; R-MMU-9954716; ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA. DR BioGRID-ORCS; 19943; 28 hits in 79 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. DR PRO; PR:P41105; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P41105; protein. DR Bgee; ENSMUSG00000030432; Expressed in urinary bladder and 64 other cell types or tissues. DR ExpressionAtlas; P41105; baseline and differential. DR GO; GO:0044297; C:cell body; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; ISO:GO_Central. DR GO; GO:0030425; C:dendrite; ISO:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central. DR GO; GO:0098794; C:postsynapse; NAS:SynGO. DR GO; GO:0098793; C:presynapse; NAS:SynGO. DR GO; GO:0005840; C:ribosome; NAS:SynGO. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; IDA:ComplexPortal. DR GO; GO:1901740; P:negative regulation of myoblast fusion; NAS:ComplexPortal. DR GO; GO:0007283; P:spermatogenesis; NAS:ComplexPortal. DR GO; GO:0006941; P:striated muscle contraction; NAS:ComplexPortal. DR GO; GO:0140242; P:translation at postsynapse; NAS:SynGO. DR GO; GO:0140236; P:translation at presynapse; NAS:SynGO. DR FunFam; 3.30.390.110:FF:000002; 60S ribosomal protein L28; 1. DR Gene3D; 3.30.390.110; -; 1. DR InterPro; IPR002672; Ribosomal_eL28. DR InterPro; IPR029004; Ribosomal_eL28/Mak16. DR PANTHER; PTHR10544; 60S RIBOSOMAL PROTEIN L28; 1. DR Pfam; PF01778; Ribosomal_L28e; 1. DR PDBsum; 6SWA; -. DR PDBsum; 7CPU; -. DR PDBsum; 7CPV; -. DR PDBsum; 7LS1; -. DR PDBsum; 7LS2; -. DR PDBsum; 9H4N; -. DR PDBsum; 9QOH; -. DR PDBsum; 9QQL; -. DR PDBsum; 9QQP; -. DR PDBsum; 9QSA; -. DR PDBsum; 9QWT; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.4" FT CHAIN 2..137 FT /note="Large ribosomal subunit protein eL28" FT /id="PRO_0000122390" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.4" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46779" FT CROSSLNK 58 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46779" FT CROSSLNK 65 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46779" FT HELIX 3..10 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:6SWA" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:6SWA" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:7CPU" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7CPV" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:7LS1" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:7CPU" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:7CPU" FT HELIX 86..98 FT /evidence="ECO:0007829|PDB:7CPU" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:7CPU" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:7LS2" FT HELIX 107..121 FT /evidence="ECO:0007829|PDB:7CPU" SQ SEQUENCE 137 AA; 15733 MW; 44D9CF515F9B687B CRC64; MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEPAADGKGV VVVMKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS QKPVVVKRKR TRPTKSS //