RL22_MOUSE
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 03-AUG-2022, entry version 143.
DE RecName: 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).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:P35268}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P35268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35268}.
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 SMR; P67984; -.
DR BioGRID; 202971; 104.
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; P67984; -.
DR PeptideAtlas; P67984; -.
DR PRIDE; P67984; -.
DR ProteomicsDB; 253299; -.
DR Antibodypedia; 27215; 192 antibodies from 31 providers.
DR DNASU; 19934; -.
DR Ensembl; ENSMUST00000103191; ENSMUSP00000099480; ENSMUSG00000028936.
DR Ensembl; ENSMUST00000139685; ENSMUSP00000118787; ENSMUSG00000028936.
DR Ensembl; ENSMUST00000188151; ENSMUSP00000140276; ENSMUSG00000028936.
DR GeneID; 19934; -.
DR KEGG; mmu:19934; -.
DR UCSC; uc008wah.2; mouse.
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; NTAISMY; -.
DR OrthoDB; 1594080at2759; -.
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 72 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 253 other 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; ISO:MGI.
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: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: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; ISO:MGI.
DR GO; GO:0045182; F:translation regulator activity; IDA:SynGO.
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:0099577; P:regulation of translation at presynapse, modulating synaptic transmission; IDA:SynGO.
DR Gene3D; 3.30.1360.210; -; 1.
DR InterPro; IPR002671; Ribosomal_L22e.
DR InterPro; IPR038526; Ribosomal_L22e_sf.
DR PANTHER; PTHR10064; PTHR10064; 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="60S ribosomal protein L22"
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
