RS5_MOUSE
ID RS5_MOUSE Reviewed; 204 AA.
AC P97461; O08607;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=40S ribosomal protein S5;
DE Contains:
DE RecName: Full=40S ribosomal protein S5, N-terminally processed;
GN Name=Rps5;
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].
RX PubMed=9202169; DOI=10.1016/s0167-4889(97)00054-2;
RA Vanegas N., Castaneda V., Santamaria D., Hernandez P., Schvartzman J.B.,
RA Krimer D.B.;
RT "Cloning, sequencing and expression in MEL cells of a cDNA encoding the
RT mouse ribosomal protein S5.";
RL Biochim. Biophys. Acta 1357:1-4(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DAB/2J;
RA Vizirianakis I.S., Pappas I.S., Tsiftsoglou A.S.;
RT "Cloning, sequencing and expression of a cDNA coding for the mouse S5
RT ribosomal protein in differentiating murine erythroleukemia (MEL) cells.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, 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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000305}.
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DR EMBL; U78085; AAB63526.1; -; mRNA.
DR EMBL; Y12431; CAA73041.1; -; mRNA.
DR CCDS; CCDS20817.1; -.
DR RefSeq; NP_033121.2; NM_009095.2.
DR PDB; 7LS1; EM; 3.30 A; s2=1-204.
DR PDB; 7LS2; EM; 3.10 A; s2=1-204.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P97461; -.
DR SMR; P97461; -.
DR BioGRID; 203012; 97.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P97461; 1.
DR STRING; 10090.ENSMUSP00000004554; -.
DR iPTMnet; P97461; -.
DR PhosphoSitePlus; P97461; -.
DR SwissPalm; P97461; -.
DR EPD; P97461; -.
DR jPOST; P97461; -.
DR MaxQB; P97461; -.
DR PaxDb; P97461; -.
DR PeptideAtlas; P97461; -.
DR PRIDE; P97461; -.
DR ProteomicsDB; 256936; -.
DR TopDownProteomics; P97461; -.
DR DNASU; 20103; -.
DR GeneID; 20103; -.
DR KEGG; mmu:20103; -.
DR CTD; 6193; -.
DR MGI; MGI:1097682; Rps5.
DR eggNOG; KOG3291; Eukaryota.
DR InParanoid; P97461; -.
DR OrthoDB; 1532160at2759; -.
DR PhylomeDB; P97461; -.
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; 20103; 25 hits in 71 CRISPR screens.
DR ChiTaRS; Rps5; mouse.
DR PRO; PR:P97461; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97461; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006450; P:regulation of translational fidelity; ISO:MGI.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR CDD; cd14867; uS7_Eukaryote; 1.
DR Gene3D; 1.10.455.10; -; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01028; uS7_euk_arch; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..204
FT /note="40S ribosomal protein S5"
FT /id="PRO_0000124527"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P46782"
FT CHAIN 2..204
FT /note="40S ribosomal protein S5, N-terminally processed"
FT /id="PRO_0000370370"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P46782"
FT MOD_RES 2
FT /note="N-acetylthreonine; in 40S ribosomal protein S5, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P46782"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46782"
FT MOD_RES 47
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46782"
FT CROSSLNK 47
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46782"
FT CONFLICT 168
FT /note="N -> T (in Ref. 2; CAA73041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 22889 MW; 9F59F6EA070DE278 CRC64;
MTEWEAATPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR
FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII HLLTGENPLQ VLVNAIINSG
PREDSTRIGR AGTVRRQAVD VSPLRRVNQA IWLLCTGARE AAFRNIKNIA ECLADELINA
AKGSSNSYAI KKKDELERVA KSNR
