RS23_MOUSE
ID RS23_MOUSE Reviewed; 143 AA.
AC P62267; P39028; Q542K7;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=40S ribosomal protein S23;
GN Name=Rps23;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, Kidney, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54, 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 ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. Plays an important role in translational accuracy.
CC {ECO:0000250|UniProtKB:P62266}.
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit.
CC {ECO:0000250|UniProtKB:P62266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62266}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62266}. Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q6SA96}. Note=Detected on cytosolic polysomes
CC (By similarity). Detected in ribosomes that are associated with the
CC rough endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:P62266, ECO:0000250|UniProtKB:Q6SA96}.
CC -!- PTM: Hydroxylation at Pro-62 affects translation termination
CC efficiency. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
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DR EMBL; AK002573; BAB22198.1; -; mRNA.
DR EMBL; AK010594; BAB27050.1; -; mRNA.
DR EMBL; AK010608; BAB27058.1; -; mRNA.
DR EMBL; AK012438; BAB28238.1; -; mRNA.
DR EMBL; AK013720; BAB28969.1; -; mRNA.
DR EMBL; AK050580; BAC34329.1; -; mRNA.
DR EMBL; AK088085; BAC40136.1; -; mRNA.
DR EMBL; AK166994; BAE39173.1; -; mRNA.
DR EMBL; AK168587; BAE40456.1; -; mRNA.
DR EMBL; BC002145; AAH02145.1; -; mRNA.
DR EMBL; BC054435; AAH54435.1; -; mRNA.
DR EMBL; BC078418; AAH78418.1; -; mRNA.
DR CCDS; CCDS26674.1; -.
DR RefSeq; NP_077137.1; NM_024175.3.
DR PDB; 7CPU; EM; 2.82 A; SX=1-143.
DR PDB; 7CPV; EM; 3.03 A; SX=1-143.
DR PDB; 7LS1; EM; 3.30 A; E3=1-143.
DR PDB; 7LS2; EM; 3.10 A; E3=1-143.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62267; -.
DR SMR; P62267; -.
DR BioGRID; 211500; 92.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P62267; 3.
DR STRING; 10090.ENSMUSP00000054490; -.
DR iPTMnet; P62267; -.
DR PhosphoSitePlus; P62267; -.
DR SwissPalm; P62267; -.
DR CPTAC; non-CPTAC-3670; -.
DR EPD; P62267; -.
DR jPOST; P62267; -.
DR MaxQB; P62267; -.
DR PaxDb; P62267; -.
DR PeptideAtlas; P62267; -.
DR PRIDE; P62267; -.
DR ProteomicsDB; 262731; -.
DR TopDownProteomics; P62267; -.
DR DNASU; 66475; -.
DR Ensembl; ENSMUST00000051955; ENSMUSP00000054490; ENSMUSG00000049517.
DR GeneID; 66475; -.
DR KEGG; mmu:66475; -.
DR UCSC; uc007rjq.2; mouse.
DR CTD; 6228; -.
DR MGI; MGI:1913725; Rps23.
DR VEuPathDB; HostDB:ENSMUSG00000049517; -.
DR eggNOG; KOG1749; Eukaryota.
DR GeneTree; ENSGT00550000074784; -.
DR HOGENOM; CLU_115574_0_1_1; -.
DR InParanoid; P62267; -.
DR OMA; KFRWSQR; -.
DR OrthoDB; 1402984at2759; -.
DR PhylomeDB; P62267; -.
DR TreeFam; TF300871; -.
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-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
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; 66475; 14 hits in 38 CRISPR screens.
DR ChiTaRS; Rps23; mouse.
DR PRO; PR:P62267; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P62267; protein.
DR Bgee; ENSMUSG00000049517; Expressed in epiblast (generic) and 62 other tissues.
DR Genevisible; P62267; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1990145; P:maintenance of translational fidelity; ISS:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISO:MGI.
DR GO; GO:0006412; P:translation; ISS:UniProtKB.
DR CDD; cd03367; Ribosomal_S23; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006032; Ribosomal_S12/S23.
DR InterPro; IPR005680; Ribosomal_S23_euk/arc.
DR PANTHER; PTHR11652; PTHR11652; 1.
DR Pfam; PF00164; Ribosom_S12_S23; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00982; uS12_E_A; 1.
DR PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Hydroxylation;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..143
FT /note="40S ribosomal protein S23"
FT /id="PRO_0000146458"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 62
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62266"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62266"
SQ SEQUENCE 143 AA; 15808 MW; 8417A48B8CF0A8E5 CRC64;
MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI VLEKVGVEAK
QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF
KVVKVANVSL LALYKGKKER PRS
