ID   RS26_MOUSE              Reviewed;         115 AA.
AC   P62855; P02383; P70394; Q06722;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Small ribosomal subunit protein eS26 {ECO:0000305};
DE   AltName: Full=40S ribosomal protein S26;
GN   Name=Rps26;
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;
RA   Rocha D., Carrier A., Victorero G., Mattei M.-G., Szatanik M.,
RA   Guenet J.-L., Jordan B.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
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, and FVB/N; TISSUE=Brain, and Colon;
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the small ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592).
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit.
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62854}. Cytoplasm
CC       {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P49171}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:P49171, ECO:0000250|UniProtKB:P62854}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS26 family.
CC       {ECO:0000305}.
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DR   EMBL; U67770; AAB07729.1; -; mRNA.
DR   EMBL; AK008301; BAB25586.1; -; mRNA.
DR   EMBL; AK010689; BAB27121.1; -; mRNA.
DR   EMBL; AK012722; BAB28433.1; -; mRNA.
DR   EMBL; AK018702; BAB31353.1; -; mRNA.
DR   EMBL; BC036987; AAH36987.1; -; mRNA.
DR   EMBL; BC081452; AAH81452.1; -; mRNA.
DR   CCDS; CCDS36090.1; -.
DR   RefSeq; NP_038793.2; NM_013765.2.
DR   PDB; 7CPU; EM; 2.82 A; Sa=1-115.
DR   PDB; 7CPV; EM; 3.03 A; Sa=1-115.
DR   PDB; 7LS1; EM; 3.30 A; F3=1-115.
DR   PDB; 7LS2; EM; 3.10 A; F3=1-115.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P62855; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P62855; -.
DR   BioGRID; 205177; 72.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   IntAct; P62855; 8.
DR   MINT; P62855; -.
DR   STRING; 10090.ENSMUSP00000026420; -.
DR   iPTMnet; P62855; -.
DR   PhosphoSitePlus; P62855; -.
DR   SwissPalm; P62855; -.
DR   EPD; P62855; -.
DR   jPOST; P62855; -.
DR   PaxDb; 10090-ENSMUSP00000026420; -.
DR   PeptideAtlas; P62855; -.
DR   ProteomicsDB; 261003; -.
DR   Pumba; P62855; -.
DR   DNASU; 27370; -.
DR   Ensembl; ENSMUST00000026420.7; ENSMUSP00000026420.6; ENSMUSG00000025362.7.
DR   GeneID; 27370; -.
DR   KEGG; mmu:27370; -.
DR   UCSC; uc007hno.2; mouse.
DR   AGR; MGI:1351628; -.
DR   CTD; 6231; -.
DR   MGI; MGI:1351628; Rps26.
DR   VEuPathDB; HostDB:ENSMUSG00000025362; -.
DR   eggNOG; KOG1768; Eukaryota.
DR   GeneTree; ENSGT00390000002517; -.
DR   HOGENOM; CLU_129451_0_1_1; -.
DR   InParanoid; P62855; -.
DR   OMA; DKAICVT; -.
DR   OrthoDB; 329at2759; -.
DR   PhylomeDB; P62855; -.
DR   TreeFam; TF300234; -.
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; 27370; 29 hits in 75 CRISPR screens.
DR   ChiTaRS; Rps26; mouse.
DR   PRO; PR:P62855; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P62855; Protein.
DR   Bgee; ENSMUSG00000025362; Expressed in epiblast (generic) and 66 other cell types or tissues.
DR   ExpressionAtlas; P62855; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; NAS:SynGO.
DR   GO; GO:0098793; C:presynapse; NAS:SynGO.
DR   GO; GO:0005840; C:ribosome; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0033119; P:negative regulation of RNA splicing; ISO:MGI.
DR   GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR   GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR   Gene3D; 3.30.1740.20; Ribosomal protein S26e; 1.
DR   InterPro; IPR000892; Ribosomal_eS26.
DR   InterPro; IPR047864; Ribosomal_eS26_CS.
DR   InterPro; IPR038551; Ribosomal_eS26_sf.
DR   PANTHER; PTHR12538; 40S RIBOSOMAL PROTEIN S26; 1.
DR   PANTHER; PTHR12538:SF7; 40S RIBOSOMAL PROTEIN S26; 1.
DR   Pfam; PF01283; Ribosomal_S26e; 1.
DR   PROSITE; PS00733; RIBOSOMAL_S26E; 1.
DR   Genevisible; P62855; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endoplasmic reticulum; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..115
FT                   /note="Small ribosomal subunit protein eS26"
FT                   /id="PRO_0000204511"
FT   REGION          85..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62854"
FT   CONFLICT        17
FT                   /note="H -> N (in Ref. 1; AAB07729)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   115 AA;  13015 MW;  F60DF98F8900D968 CRC64;
     MTKKRRNNGR AKKGRGHVQP IRCTNCARCV PKDKAIKKFV IRNIVEAAAV RDISEASVFD
     AYVLPKLYVK LHYCVSCAIH SKVVRNRSRE ARKDRTPPPR FRPAGAAPRP PPKPM
//