RS8_MOUSE
ID RS8_MOUSE Reviewed; 208 AA.
AC P62242; P09058; Q8C2G6;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=40S ribosomal protein S8;
GN Name=Rps8;
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 STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=7694236; DOI=10.1093/nar/21.20.4845;
RA Su Y., Raj N.B.K., Au W.-C., Pitha P.M.;
RT "Primary sequence of the mouse ribosomal protein S8.";
RL Nucleic Acids Res. 21:4845-4845(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Thymus, and Tongue;
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=C3H/He, and C57BL/6J; TISSUE=Brain, Colon, and Osteoblast;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-37 AND LYS-128, AND
RP IDENTIFICATION BY MASS 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}. Membrane
CC {ECO:0000250|UniProtKB:P62241}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62241}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family.
CC {ECO:0000305}.
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DR EMBL; X73829; CAA52050.1; -; mRNA.
DR EMBL; AK009023; BAB26032.1; -; mRNA.
DR EMBL; AK010650; BAB27090.1; -; mRNA.
DR EMBL; AK011048; BAB27359.1; -; mRNA.
DR EMBL; AK011058; BAB27366.1; -; mRNA.
DR EMBL; AK011642; BAB27754.1; -; mRNA.
DR EMBL; AK012435; BAB28236.1; -; mRNA.
DR EMBL; AK012665; BAB28394.1; -; mRNA.
DR EMBL; AK088660; BAC40485.1; -; mRNA.
DR EMBL; BC027217; AAH27217.1; -; mRNA.
DR EMBL; BC051446; AAH51446.1; -; mRNA.
DR EMBL; BC081465; AAH81465.1; -; mRNA.
DR CCDS; CCDS18530.1; -.
DR PIR; S42110; S42110.
DR RefSeq; NP_033124.1; NM_009098.2.
DR PDB; 7CPU; EM; 2.82 A; SI=1-208.
DR PDB; 7CPV; EM; 3.03 A; SI=1-208.
DR PDB; 7LS1; EM; 3.30 A; u=1-208.
DR PDB; 7LS2; EM; 3.10 A; u=1-208.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62242; -.
DR SMR; P62242; -.
DR BioGRID; 203017; 110.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR CORUM; P62242; -.
DR IntAct; P62242; 6.
DR MINT; P62242; -.
DR STRING; 10090.ENSMUSP00000099757; -.
DR iPTMnet; P62242; -.
DR PhosphoSitePlus; P62242; -.
DR SwissPalm; P62242; -.
DR EPD; P62242; -.
DR jPOST; P62242; -.
DR PaxDb; P62242; -.
DR PeptideAtlas; P62242; -.
DR PRIDE; P62242; -.
DR ProteomicsDB; 262736; -.
DR TopDownProteomics; P62242; -.
DR Antibodypedia; 32545; 177 antibodies from 26 providers.
DR DNASU; 20116; -.
DR Ensembl; ENSMUST00000102696; ENSMUSP00000099757; ENSMUSG00000047675.
DR GeneID; 20116; -.
DR KEGG; mmu:20116; -.
DR UCSC; uc008uic.1; mouse.
DR CTD; 6202; -.
DR MGI; MGI:98166; Rps8.
DR VEuPathDB; HostDB:ENSMUSG00000047675; -.
DR eggNOG; KOG3283; Eukaryota.
DR GeneTree; ENSGT00390000012433; -.
DR HOGENOM; CLU_080597_1_1_1; -.
DR InParanoid; P62242; -.
DR OMA; VGRCDGY; -.
DR OrthoDB; 1278610at2759; -.
DR PhylomeDB; P62242; -.
DR TreeFam; TF300041; -.
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; 20116; 25 hits in 57 CRISPR screens.
DR ChiTaRS; Rps8; mouse.
DR PRO; PR:P62242; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P62242; protein.
DR Bgee; ENSMUSG00000047675; Expressed in ventricular zone and 61 other tissues.
DR ExpressionAtlas; P62242; baseline and differential.
DR Genevisible; P62242; 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; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR Gene3D; 1.10.168.20; -; 1.
DR InterPro; IPR042563; Ribosomal_protein_S8e_euk.
DR InterPro; IPR001047; Ribosomal_S8e.
DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR InterPro; IPR018283; Ribosomal_S8e_CS.
DR PANTHER; PTHR10394; PTHR10394; 1.
DR Pfam; PF01201; Ribosomal_S8e; 1.
DR TIGRFAMs; TIGR00307; eS8; 1.
DR PROSITE; PS01193; RIBOSOMAL_S8E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62241"
FT CHAIN 2..208
FT /note="40S ribosomal protein S8"
FT /id="PRO_0000122241"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62241"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P62241"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62241"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62241"
FT CONFLICT 70
FT /note="E -> V (in Ref. 2; BAC40485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 24205 MW; 407FDF59171F7422 CRC64;
MGISRDNWHK RRKTGGKRKP YHKKRKYELG RPAANTKIGP RRIHTVRVRG GNKKYRALRL
DVGNFSWGSE CCTRKTRIID VVYNASNNEL VRTKTLVKNC IVLIDSTPYR QWYESHYALP
LGRKKGAKLT PEEEEILNKK RSKKIQKKYD ERKKNAKISS LLEEQFQQGK LLACIASRPG
QCGRADGYVL EGKELEFYLR KIKARKGK
