RS3_MOUSE
ID RS3_MOUSE Reviewed; 243 AA.
AC P62908; P17073; P47933;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=40S ribosomal protein S3;
DE EC=4.2.99.18 {ECO:0000269|PubMed:7775413};
GN Name=Rps3;
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=Kidney;
RA Harper M., Terol-Garay E., Hraba-Renevey S., Kress M.M.;
RT "Primary sequence of the mouse ribosomal protein S3.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary 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 PROTEIN SEQUENCE OF 75-81 AND 227-240, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7775413; DOI=10.1074/jbc.270.23.13620;
RA Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S.;
RT "Implication of mammalian ribosomal protein S3 in the processing of DNA
RT damage.";
RL J. Biol. Chem. 270:13620-13629(1995).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14988002; DOI=10.1016/s0014-5793(04)00074-2;
RA Jang C.Y., Lee J.Y., Kim J.;
RT "RpS3, a DNA repair endonuclease and ribosomal protein, is involved in
RT apoptosis.";
RL FEBS Lett. 560:81-85(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND IDENTIFICATION BY
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP INTERACTION WITH CRY1.
RX PubMed=19129230; DOI=10.1093/nar/gkn1013;
RA Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
RT "Molecular characterization of Mybbp1a as a co-repressor on the Period2
RT promoter.";
RL Nucleic Acids Res. 37:1115-1126(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND THR-242, AND
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 [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [10]
RP UFMYLATION.
RX PubMed=28575669; DOI=10.1016/j.cell.2017.05.022;
RA Simsek D., Tiu G.C., Flynn R.A., Byeon G.W., Leppek K., Xu A.F.,
RA Chang H.Y., Barna M.;
RT "The mammalian ribo-interactome reveals ribosome functional diversity and
RT heterogeneity.";
RL Cell 169:1051-1065(2017).
CC -!- FUNCTION: Involved in translation as a component of the 40S small
CC ribosomal subunit (By similarity). Has endonuclease activity and plays
CC a role in repair of damaged DNA (PubMed:7775413). Cleaves
CC phosphodiester bonds of DNAs containing altered bases with broad
CC specificity and cleaves supercoiled DNA more efficiently than relaxed
CC DNA (By similarity). Displays high binding affinity for 7,8-dihydro-8-
CC oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen
CC species (ROS) (By similarity). Has also been shown to bind with similar
CC affinity to intact and damaged DNA (By similarity). Stimulates the N-
CC glycosylase activity of the base excision protein OGG1 (By similarity).
CC Enhances the uracil excision activity of UNG1 (By similarity). Also
CC stimulates the cleavage of the phosphodiester backbone by APEX1 (By
CC similarity). When located in the mitochondrion, reduces cellular ROS
CC levels and mitochondrial DNA damage (By similarity). Has also been
CC shown to negatively regulate DNA repair in cells exposed to hydrogen
CC peroxide (By similarity). Plays a role in regulating transcription as
CC part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65
CC subunit, enhances binding of the complex to DNA and promotes
CC transcription of target genes (By similarity). Represses its own
CC translation by binding to its cognate mRNA (By similarity). Binds to
CC and protects TP53/p53 from MDM2-mediated ubiquitination (By
CC similarity). Involved in spindle formation and chromosome movement
CC during mitosis by regulating microtubule polymerization (By
CC similarity). Involved in induction of apoptosis through its role in
CC activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by
CC interacting with the E2F1 transcription factor and acting
CC synergistically with it to up-regulate pro-apoptotic proteins
CC BCL2L11/BIM and HRK/Dp5 (By similarity). Interacts with TRADD following
CC exposure to UV radiation and induces apoptosis by caspase-dependent JNK
CC activation (By similarity). {ECO:0000250|UniProtKB:P23396,
CC ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:7775413}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC Evidence={ECO:0000269|PubMed:7775413};
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with HNRPD. Interacts with PRMT1; the interaction methylates
CC RPS3. Interacts with SUMO1; the interaction sumoylates RPS3. Interacts
CC with UBC9. Interacts with CDK1; the interaction phosphorylates RPS3.
CC Interacts with PRKCD; the interaction phosphorylates RPS3. Interacts
CC with PKB/AKT; the interaction phosphorylates RPS3. Interacts with E2F1;
CC the interaction occurs in the absence of nerve growth factor and
CC increases transcription of pro-apoptotic proteins BCL2L11/BIM and
CC HRK/Dp5. Interacts with the base excision repair proteins APEX1 and
CC OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity.
CC Interacts with UNG; the interaction increases the uracil excision
CC activity of UNG1. Interacts with HSP90; the interaction prevents the
CC ubiquitination and proteasome-dependent degradation of RPS3 and is
CC suppressed by increased ROS levels. Interacts with TOM70; the
CC interaction promotes translocation of RPS3 to the mitochondrion.
CC Interacts (via N-terminus) with RELA (via N-terminus); the interaction
CC enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex.
CC Interacts with NFKBIA; the interaction is direct and may bridge the
CC interaction between RPS3 and RELA. Interacts with IKKB; the interaction
CC phosphorylates RPS3 and enhances its translocation to the nucleus.
CC Interacts (via KH domain) with MDM2 and TP53. Interacts with TRADD.
CC Interacts with CRY1. {ECO:0000250|UniProtKB:P23396,
CC ECO:0000269|PubMed:19129230}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14988002}. Nucleus
CC {ECO:0000269|PubMed:14988002}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P23396}. Note=In normal cells, located mainly in
CC the cytoplasm with small amounts in the nucleus but translocates to the
CC nucleus in cells undergoing apoptosis. Nuclear translocation is also
CC induced by DNA damaging agents such as hydrogen peroxide (By
CC similarity). Accumulates in the mitochondrion in response to increased
CC ROS levels (By similarity). Localizes to the spindle during mitosis (By
CC similarity). Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:P23396,
CC ECO:0000269|PubMed:14988002}.
CC -!- PTM: Methylation by PRMT1 is required for import into the nucleolus and
CC for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Sumoylation by SUMO1 enhances protein stability through increased
CC resistance to proteolysis. Sumoylation occurs at one or more of the
CC three consensus sites, Lys-18, Lys-214 and Lys-230.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase.
CC Phosphorylation by PRKCD occurs on a non-ribosomal-associated form
CC which results in translocation of RPS3 to the nucleus and enhances its
CC endonuclease activity. Phosphorylated on Ser-209 by IKKB in response to
CC activation of the NF-kappa-B p65-p50 complex which enhances the
CC association of RPS3 with importin-alpha and mediates the nuclear
CC translocation of RPS3. Phosphorylation by MAPK is required for
CC translocation to the nucleus following exposure of cells to DNA
CC damaging agents such as hydrogen peroxide. Phosphorylation by PKB/AKT
CC mediates RPS3 nuclear translocation, enhances RPS3 endonuclease
CC activity and suppresses RPS3-induced neuronal apoptosis.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Ubiquitinated. This is prevented by interaction with HSP90 which
CC stabilizes the protein. Monoubiquitinated at Lys-214 by ZNF598 when a
CC ribosome has stalled during translation of poly(A) sequences, leading
CC to preclude synthesis of a long poly-lysine tail and initiate the
CC ribosome quality control (RQC) pathway to degrade the potentially
CC detrimental aberrant nascent polypeptide.
CC {ECO:0000250|UniProtKB:P23396}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000269|PubMed:28575669}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000305}.
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DR EMBL; X76772; CAA54167.1; -; mRNA.
DR EMBL; BC010721; AAH10721.1; -; mRNA.
DR CCDS; CCDS40031.1; -.
DR PIR; S41170; S41170.
DR RefSeq; NP_036182.1; NM_012052.2.
DR PDB; 7CPU; EM; 2.82 A; SD=1-243.
DR PDB; 7CPV; EM; 3.03 A; SD=1-243.
DR PDB; 7LS1; EM; 3.30 A; q2=1-243.
DR PDB; 7LS2; EM; 3.10 A; q2=1-243.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62908; -.
DR BMRB; P62908; -.
DR SMR; P62908; -.
DR BioGRID; 205106; 126.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR CORUM; P62908; -.
DR IntAct; P62908; 10.
DR MINT; P62908; -.
DR STRING; 10090.ENSMUSP00000032998; -.
DR iPTMnet; P62908; -.
DR PhosphoSitePlus; P62908; -.
DR SwissPalm; P62908; -.
DR CPTAC; non-CPTAC-3873; -.
DR EPD; P62908; -.
DR jPOST; P62908; -.
DR PaxDb; P62908; -.
DR PeptideAtlas; P62908; -.
DR PRIDE; P62908; -.
DR ProteomicsDB; 260854; -.
DR DNASU; 27050; -.
DR Ensembl; ENSMUST00000032998; ENSMUSP00000032998; ENSMUSG00000030744.
DR GeneID; 27050; -.
DR KEGG; mmu:27050; -.
DR UCSC; uc009ilr.2; mouse.
DR CTD; 6188; -.
DR MGI; MGI:1350917; Rps3.
DR VEuPathDB; HostDB:ENSMUSG00000030744; -.
DR eggNOG; KOG3181; Eukaryota.
DR GeneTree; ENSGT00390000008610; -.
DR HOGENOM; CLU_058591_2_1_1; -.
DR InParanoid; P62908; -.
DR OMA; YIKKCGE; -.
DR OrthoDB; 1135751at2759; -.
DR PhylomeDB; P62908; -.
DR TreeFam; TF300901; -.
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; 27050; 34 hits in 99 CRISPR screens.
DR ChiTaRS; Rps3; mouse.
DR PRO; PR:P62908; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P62908; protein.
DR Bgee; ENSMUSG00000030744; Expressed in ear vesicle and 135 other tissues.
DR ExpressionAtlas; P62908; baseline and differential.
DR Genevisible; P62908; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0071159; C:NF-kappaB complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0032357; F:oxidized purine DNA binding; ISO:MGI.
DR GO; GO:0032358; F:oxidized pyrimidine DNA binding; ISO:MGI.
DR GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0097100; F:supercoiled DNA binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045738; P:negative regulation of DNA repair; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1905053; P:positive regulation of base-excision repair; ISO:MGI.
DR GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; ISO:MGI.
DR GO; GO:1902546; P:positive regulation of DNA N-glycosylase activity; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:CAFA.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:CAFA.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0061481; P:response to TNF agonist; ISO:MGI.
DR GO; GO:0051225; P:spindle assembly; ISO:MGI.
DR Gene3D; 3.30.1140.32; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR001351; Ribosomal_S3_C.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR018280; Ribosomal_S3_CS.
DR InterPro; IPR005703; Ribosomal_S3_euk/arc.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR SUPFAM; SSF54821; SSF54821; 1.
DR TIGRFAMs; TIGR01008; uS3_euk_arch; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; Lyase; Membrane; Methylation; Mitochondrion;
KW Mitochondrion inner membrane; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW Transcription; Transcription regulation; Translation regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CHAIN 2..243
FT /note="40S ribosomal protein S3"
FT /id="PRO_0000130321"
FT DOMAIN 21..92
FT /note="KH type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00118"
FT REGION 200..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 6
FT /note="Phosphoserine; by PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 42
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 64
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 65
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 67
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 70
FT /note="Phosphothreonine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 132
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 209
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P23396"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P23396"
SQ SEQUENCE 243 AA; 26674 MW; 6B9BB34FDEE04AAF CRC64;
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG
VLGIKVKIML PWDPSGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV
PTA
