ID RL22_MOUSE Reviewed; 128 AA. AC P67984; P41104; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 151. DE RecName: Full=Large ribosomal subunit protein eL22 {ECO:0000305}; DE AltName: Full=60S ribosomal protein L22; DE AltName: Full=Heparin-binding protein HBp15; GN Name=Rpl22; 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=BALB/cJ; TISSUE=Submandibular gland; RX PubMed=8135813; DOI=10.1006/bbrc.1994.1286; RA Fujita Y., Okamoto T., Noshiro M., Kato Y., Takada K., Sato J.D., Ozaki T., RA McKeehan W.L., Crabb J.W., Whitney R.G.; RT "A novel heparin-binding protein, HBp15, is identified as mammalian RT ribosomal protein L22."; RL Biochem. Biophys. Res. Commun. 199:706-713(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor, and Salivary 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, 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 [4] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-69, AND IDENTIFICATION BY MASS RP 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 [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 {ECO:0000269|PubMed:36517592}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL22 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; D17653; BAA04546.1; -; mRNA. DR EMBL; BC007139; AAH07139.1; -; mRNA. DR EMBL; BC021344; AAH21344.1; -; mRNA. DR CCDS; CCDS18999.1; -. DR PIR; JC2119; JC2119. DR RefSeq; NP_033105.1; NM_009079.3. DR PDB; 6SWA; EM; 3.10 A; S=1-128. DR PDB; 7CPU; EM; 2.82 A; LU=1-128. DR PDB; 7CPV; EM; 3.03 A; LU=1-128. DR PDB; 7LS1; EM; 3.30 A; O2=1-128. DR PDB; 7LS2; EM; 3.10 A; O2=1-128. DR PDBsum; 6SWA; -. DR PDBsum; 7CPU; -. DR PDBsum; 7CPV; -. DR PDBsum; 7LS1; -. DR PDBsum; 7LS2; -. DR AlphaFoldDB; P67984; -. DR EMDB; EMD-10321; -. DR EMDB; EMD-23500; -. DR EMDB; EMD-23501; -. DR EMDB; EMD-30432; -. DR EMDB; EMD-30433; -. DR SMR; P67984; -. DR BioGRID; 202971; 108. DR BioGRID; 3417155; 1. DR IntAct; P67984; 4. DR MINT; P67984; -. DR STRING; 10090.ENSMUSP00000118787; -. DR iPTMnet; P67984; -. DR PhosphoSitePlus; P67984; -. DR SwissPalm; P67984; -. DR EPD; P67984; -. DR jPOST; P67984; -. DR PaxDb; 10090-ENSMUSP00000118787; -. DR PeptideAtlas; P67984; -. DR ProteomicsDB; 253299; -. DR Pumba; P67984; -. DR Antibodypedia; 27215; 209 antibodies from 31 providers. DR DNASU; 19934; -. DR Ensembl; ENSMUST00000103191.11; ENSMUSP00000099480.5; ENSMUSG00000028936.16. DR Ensembl; ENSMUST00000139685.8; ENSMUSP00000118787.2; ENSMUSG00000028936.16. DR Ensembl; ENSMUST00000188151.2; ENSMUSP00000140276.2; ENSMUSG00000028936.16. DR GeneID; 19934; -. DR KEGG; mmu:19934; -. DR UCSC; uc008wah.2; mouse. DR AGR; MGI:99262; -. DR CTD; 6146; -. DR MGI; MGI:99262; Rpl22. DR VEuPathDB; HostDB:ENSMUSG00000028936; -. DR eggNOG; KOG3434; Eukaryota. DR GeneTree; ENSGT00940000153314; -. DR HOGENOM; CLU_105624_0_1_1; -. DR InParanoid; P67984; -. DR OMA; WIRFIST; -. DR OrthoDB; 2879766at2759; -. DR PhylomeDB; P67984; -. DR TreeFam; TF313018; -. 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; 19934; 6 hits in 77 CRISPR screens. DR ChiTaRS; Rpl22; mouse. DR PRO; PR:P67984; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P67984; Protein. DR Bgee; ENSMUSG00000028936; Expressed in urinary bladder urothelium and 256 other cell types or tissues. DR ExpressionAtlas; P67984; baseline and differential. DR Genevisible; P67984; MM. DR GO; GO:0005737; C:cytoplasm; ISS:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0098794; C:postsynapse; NAS:SynGO. DR GO; GO:0098793; C:presynapse; IDA:SynGO. DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI. DR GO; GO:0005840; C:ribosome; IDA:MGI. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0008201; F:heparin binding; IDA:MGI. DR GO; GO:0042802; F:identical protein 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:0046632; P:alpha-beta T cell differentiation; IMP:MGI. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR GO; GO:0140242; P:translation at postsynapse; NAS:SynGO. DR GO; GO:0140236; P:translation at presynapse; IDA:SynGO. DR Gene3D; 3.30.1360.210; -; 1. DR InterPro; IPR002671; Ribosomal_eL22. DR InterPro; IPR038526; Ribosomal_eL22_sf. DR PANTHER; PTHR10064; 60S RIBOSOMAL PROTEIN L22; 1. DR PANTHER; PTHR10064:SF2; 60S RIBOSOMAL PROTEIN L22; 1. DR Pfam; PF01776; Ribosomal_L22e; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Heparin-binding; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding. FT CHAIN 1..128 FT /note="Large ribosomal subunit protein eL22" FT /id="PRO_0000215502" FT MOD_RES 62 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P35268" FT MOD_RES 69 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" SQ SEQUENCE 128 AA; 14759 MW; 3F29D8BE70DEF96C CRC64; MAPVKKLVAK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN GKAGNLGGGV VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL RVVANSKESY ELRYFQINQD EEEEEDED //