RL23A_MOUSE
ID RL23A_MOUSE Reviewed; 156 AA.
AC P62751; P29316; P39024; Q92774;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=60S ribosomal protein L23a;
GN Name=Rpl23a;
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=Liver;
RA Fan Y., Friedman C., Trask B.J.;
RT "cDNA cloning, genomic structure, and chromosomal localization of a novel
RT murine ribosomal protein L23a gene.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Liver;
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 IDENTIFICATION BY 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 CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT ALA-2.
RX PubMed=20668449; DOI=10.1038/nature09343;
RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and
RT retinoblastoma protein.";
RL Nature 466:1125-1128(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, 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 [6]
RP CITRULLINATION AT ARG-41.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
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. Binds a specific region on the 26S rRNA. May
CC promote p53/TP53 degradation possibly through the stimulation of MDM2-
CC mediated TP53 polyubiquitination. {ECO:0000250|UniProtKB:P62750}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with LYAR
CC and GNL2. Interacts with MDM2; this interaction may promote MDM2-
CC mediated p53/TP53 polyubiquitination. Directly interacts (via BIB
CC domain) with IPO5, IPO7, KPNB1 and TNPO1; these interactions are
CC involved in RPL23A nuclear import for the assembly of ribosomal
CC subunits. Interacts with IPO8. {ECO:0000250|UniProtKB:P62750}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62750}. Nucleus
CC {ECO:0000250|UniProtKB:P62750}. Note=Although RPL23A is functional
CC within the cytoplasm, the assembly of ribosomal subunits occurs in the
CC nucleus. RPL23A nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7,
CC KPNB1/importin-beta or TPNO1/Trn. {ECO:0000250|UniProtKB:P62750}.
CC -!- DOMAIN: The N-terminal beta-like import receptor binding (BIB) domain
CC mediates interaction with IPO5, IPO7, KPNB1 and TNPO1.
CC {ECO:0000250|UniProtKB:P62750}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000269|PubMed:20668449}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 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; AF452721; AAQ04686.1; -; mRNA.
DR EMBL; BC026656; AAH26656.1; -; mRNA.
DR EMBL; BC029892; AAH29892.1; -; mRNA.
DR CCDS; CCDS25093.1; -.
DR RefSeq; NP_997406.1; NM_207523.2.
DR PDB; 6SWA; EM; 3.10 A; V=1-156.
DR PDB; 7LS1; EM; 3.30 A; R2=1-156.
DR PDB; 7LS2; EM; 3.10 A; R2=1-156.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62751; -.
DR SMR; P62751; -.
DR BioGRID; 234500; 81.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-59973N; -.
DR IntAct; P62751; 9.
DR MINT; P62751; -.
DR STRING; 10090.ENSMUSP00000099541; -.
DR iPTMnet; P62751; -.
DR PhosphoSitePlus; P62751; -.
DR EPD; P62751; -.
DR jPOST; P62751; -.
DR PaxDb; P62751; -.
DR PeptideAtlas; P62751; -.
DR PRIDE; P62751; -.
DR ProteomicsDB; 253249; -.
DR Ensembl; ENSMUST00000102483; ENSMUSP00000099541; ENSMUSG00000058546.
DR GeneID; 268449; -.
DR KEGG; mmu:268449; -.
DR UCSC; uc007kil.3; mouse.
DR CTD; 6147; -.
DR MGI; MGI:3040672; Rpl23a.
DR VEuPathDB; HostDB:ENSMUSG00000058546; -.
DR eggNOG; KOG1751; Eukaryota.
DR GeneTree; ENSGT00950000182901; -.
DR HOGENOM; CLU_037562_0_2_1; -.
DR InParanoid; P62751; -.
DR OMA; IPHVPRM; -.
DR OrthoDB; 1436090at2759; -.
DR PhylomeDB; P62751; -.
DR TreeFam; TF314116; -.
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; 268449; 26 hits in 63 CRISPR screens.
DR ChiTaRS; Rpl23a; mouse.
DR PRO; PR:P62751; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P62751; protein.
DR Bgee; ENSMUSG00000058546; Expressed in ectoplacental cone and 62 other tissues.
DR ExpressionAtlas; P62751; baseline and differential.
DR Genevisible; P62751; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:1904841; F:TORC2 complex binding; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR019985; Ribosomal_L23.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR005633; Ribosomal_L23/L25_N.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR Pfam; PF03939; Ribosomal_L23eN; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR TIGRFAMs; TIGR03636; uL23_arch; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20668449"
FT CHAIN 2..156
FT /note="60S ribosomal protein L23a"
FT /id="PRO_0000129468"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..74
FT /note="Beta-like import receptor binding (BIB) domain"
FT /evidence="ECO:0000250|UniProtKB:P62750"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..64
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine; by NTM1"
FT /evidence="ECO:0000269|PubMed:20668449"
FT MOD_RES 41
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62750"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62750"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62750"
SQ SEQUENCE 156 AA; 17695 MW; 3980E77B47FAB70E CRC64;
MAPKAKKEAP APPKAEAKAK ALKAKKAVLK GVHSHKKKKI RTSPTFRRPK TLRLRRQPKY
PRKSAPRRNK LDHYAIIKFP LTTESAMKKI EDNNTLVFIV DVKANKHQIK QAVKKLYDID
VAKVNTLIRP DGEKKAYVRL APDYDALDVA NKIGII
