RS4X_MOUSE
ID RS4X_MOUSE Reviewed; 263 AA.
AC P62702; P12631; P12750; P27576; P55831; Q14727; Q9CXN0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=40S ribosomal protein S4, X isoform;
GN Name=Rps4x; Synonyms=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=1783379; DOI=10.1016/0888-7543(91)90037-f;
RA Zinn A.R., Bressler S.L., Beer-Romero P., Adler D.A., Chapman V.M.,
RA Page D.C., Disteche C.M.;
RT "Inactivation of the Rps4 gene on the mouse X chromosome.";
RL Genomics 11:1097-1101(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-237.
RX PubMed=1740345; DOI=10.1016/0888-7543(92)90386-7;
RA Hamvas R.M., Zinn A.R., Keer J.T., Fisher E.M., Beer-Romero P., Brown S.D.,
RA Page D.C.;
RT "Rps4 maps near the inactivation center on the mouse X chromosome.";
RL Genomics 12:363-367(1992).
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, 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 -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family.
CC {ECO:0000305}.
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DR EMBL; M73436; AAA40075.1; -; mRNA.
DR EMBL; AK014210; BAB29207.1; -; mRNA.
DR EMBL; BC009100; AAH09100.1; -; mRNA.
DR EMBL; M77296; AAA40072.1; -; Genomic_DNA.
DR CCDS; CCDS41083.1; -.
DR RefSeq; NP_033120.1; NM_009094.2.
DR PDB; 7CPU; EM; 2.82 A; SE=1-263.
DR PDB; 7CPV; EM; 3.03 A; SE=1-263.
DR PDB; 7LS1; EM; 3.30 A; r2=1-263.
DR PDB; 7LS2; EM; 3.10 A; r2=1-263.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62702; -.
DR SMR; P62702; -.
DR BioGRID; 203011; 155.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR CORUM; P62702; -.
DR IntAct; P62702; 4.
DR MINT; P62702; -.
DR STRING; 10090.ENSMUSP00000033683; -.
DR iPTMnet; P62702; -.
DR PhosphoSitePlus; P62702; -.
DR SwissPalm; P62702; -.
DR EPD; P62702; -.
DR jPOST; P62702; -.
DR PaxDb; P62702; -.
DR PeptideAtlas; P62702; -.
DR PRIDE; P62702; -.
DR ProteomicsDB; 260847; -.
DR Antibodypedia; 27877; 189 antibodies from 30 providers.
DR DNASU; 20102; -.
DR Ensembl; ENSMUST00000033683; ENSMUSP00000033683; ENSMUSG00000031320.
DR GeneID; 20102; -.
DR KEGG; mmu:20102; -.
DR UCSC; uc009tyl.2; mouse.
DR CTD; 6191; -.
DR MGI; MGI:98158; Rps4x.
DR VEuPathDB; HostDB:ENSMUSG00000031320; -.
DR eggNOG; KOG0378; Eukaryota.
DR GeneTree; ENSGT00390000005569; -.
DR HOGENOM; CLU_060400_1_0_1; -.
DR InParanoid; P62702; -.
DR OMA; PARASIC; -.
DR OrthoDB; 1065966at2759; -.
DR PhylomeDB; P62702; -.
DR TreeFam; TF300612; -.
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; 20102; 25 hits in 53 CRISPR screens.
DR ChiTaRS; Rps4x; mouse.
DR PRO; PR:P62702; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P62702; protein.
DR Bgee; ENSMUSG00000031320; Expressed in epiblast (generic) and 61 other tissues.
DR ExpressionAtlas; P62702; baseline and differential.
DR Genevisible; P62702; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
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:0005844; C:polysome; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005840; C:ribosome; ISS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; ISA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd06087; KOW_RPS4; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.740; -; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_00485; Ribosomal_S4e; 1.
DR InterPro; IPR032277; 40S_S4_C.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041982; KOW_RPS4.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR000876; Ribosomal_S4e.
DR InterPro; IPR013845; Ribosomal_S4e_central_region.
DR InterPro; IPR038237; Ribosomal_S4e_central_sf.
DR InterPro; IPR013843; Ribosomal_S4e_N.
DR InterPro; IPR018199; Ribosomal_S4e_N_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11581; PTHR11581; 1.
DR Pfam; PF16121; 40S_S4_C; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF00900; Ribosomal_S4e; 1.
DR Pfam; PF08071; RS4NT; 1.
DR Pfam; PF01479; S4; 1.
DR PIRSF; PIRSF002116; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR PROSITE; PS00528; RIBOSOMAL_S4E; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Ubl conjugation.
FT CHAIN 1..263
FT /note="40S ribosomal protein S4, X isoform"
FT /id="PRO_0000130809"
FT DOMAIN 42..104
FT /note="S4 RNA-binding"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62701"
FT CONFLICT 9
FT /note="L -> M (in Ref. 2; BAB29207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29598 MW; 87200E545A8958B0 CRC64;
MARGPKKHLK RVAAPKHWML DKLTGVFAPR PSTGPHKLRE CLPLIIFLRN RLKYALTGDE
VKKICMQRFI KIDGKVRTDI TYPAGFMDVI SIDKTGENFR LIYDTKGRFA VHRITPEEAK
YKLCKVRKIF VGTKGIPHLV THDARTIRYP DPLIKVNDTI QIDLETGKIT DFIKFDTGNL
CMVTGGANLG RIGVITNRER HPGSFDVVHV KDANGNSFAT RLSNIFVIGK GNKPWISLPR
GKGIRLTIAE ERDKRLAAKQ SSG
