RS2_MOUSE
ID RS2_MOUSE Reviewed; 293 AA.
AC P25444;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=40S ribosomal protein S2;
DE AltName: Full=40S ribosomal protein S4;
DE AltName: Full=Protein LLRep3;
GN Name=Rps2; Synonyms=Llrep3, Rps4;
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=3405219; DOI=10.1128/mcb.8.7.2797-2803.1988;
RA Heller D.L., Gianola K.M., Leinwand L.A.;
RT "A highly conserved mouse gene with a propensity to form pseudogenes in
RT mammals.";
RL Mol. Cell. Biol. 8:2797-2803(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster;
RA Smith J.B., Nguyen T.T.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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).
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 a role in the assembly and function of the 40S ribosomal
CC subunit. Mutations in this protein affects the control of translational
CC fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly. {ECO:0000250|UniProtKB:P25443}.
CC -!- SUBUNIT: Interacts with zinc finger protein ZNF277 (via zinc-finger
CC domains); the interaction is direct; the interaction is extra-
CC ribosomal. Interaction with ZNF277 competes with the binding of RPS2 to
CC protein arginine methyltransferase PRMT3.
CC {ECO:0000250|UniProtKB:P15880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15880}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P15880}. Note=Probably
CC localized to nucleolus and cytoplasm in complex with ZNF277.
CC {ECO:0000250|UniProtKB:P15880}.
CC -!- PTM: Citrullinated by PADI4 in the Arg/Gly-rich region. {ECO:0000250}.
CC -!- PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple
CC sites in the Arg/Gly-rich region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40074.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M20632; AAA40074.1; ALT_FRAME; mRNA.
DR EMBL; AF283559; AAG13953.1; -; mRNA.
DR EMBL; BC002186; AAH02186.1; -; mRNA.
DR CCDS; CCDS37493.1; -.
DR PIR; A31139; A31139.
DR RefSeq; NP_032529.2; NM_008503.5.
DR PDB; 7CPU; EM; 2.82 A; SC=1-293.
DR PDB; 7CPV; EM; 3.03 A; SC=1-293.
DR PDB; 7LS1; EM; 3.30 A; J3=1-293.
DR PDB; 7LS2; EM; 3.10 A; J3=1-293.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P25444; -.
DR SMR; P25444; -.
DR BioGRID; 201174; 116.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR STRING; 10090.ENSMUSP00000092502; -.
DR iPTMnet; P25444; -.
DR PhosphoSitePlus; P25444; -.
DR SwissPalm; P25444; -.
DR CPTAC; non-CPTAC-3872; -.
DR EPD; P25444; -.
DR jPOST; P25444; -.
DR PaxDb; P25444; -.
DR PeptideAtlas; P25444; -.
DR PRIDE; P25444; -.
DR ProteomicsDB; 260857; -.
DR TopDownProteomics; P25444; -.
DR Antibodypedia; 23349; 209 antibodies from 30 providers.
DR DNASU; 16898; -.
DR Ensembl; ENSMUST00000054289; ENSMUSP00000092502; ENSMUSG00000044533.
DR Ensembl; ENSMUST00000170715; ENSMUSP00000131474; ENSMUSG00000044533.
DR GeneID; 16898; -.
DR KEGG; mmu:16898; -.
DR UCSC; uc008axy.2; mouse.
DR CTD; 6187; -.
DR MGI; MGI:105110; Rps2.
DR VEuPathDB; HostDB:ENSMUSG00000044533; -.
DR eggNOG; KOG0877; Eukaryota.
DR GeneTree; ENSGT00940000153095; -.
DR InParanoid; P25444; -.
DR OMA; DLKNWVP; -.
DR OrthoDB; 1197354at2759; -.
DR TreeFam; TF300806; -.
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-3214858; RMTs methylate histone arginines.
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-8876725; Protein methylation.
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; 16898; 30 hits in 71 CRISPR screens.
DR ChiTaRS; Rps2; mouse.
DR PRO; PR:P25444; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P25444; protein.
DR Bgee; ENSMUSG00000044533; Expressed in ventricular zone and 64 other tissues.
DR ExpressionAtlas; P25444; baseline and differential.
DR Genevisible; P25444; MM.
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; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISO:MGI.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CHAIN 2..293
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131674"
FT DOMAIN 102..165
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 275
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CONFLICT 270
FT /note="T -> S (in Ref. 1; AAA40074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31231 MW; 9092DB564AA624C9 CRC64;
MADDAGAAGG PGGPGGPGLG GRGGFRGGFG SGLRGRGRGR GRGRGRGRGA RGGKAEDKEW
IPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ
RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV
PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT
FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT
