RS25_MOUSE
ID RS25_MOUSE Reviewed; 125 AA.
AC P62852; P25111;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=40S ribosomal protein S25;
GN Name=Rps25;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and 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 [3]
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43 AND LYS-52, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-94, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and 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).
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family.
CC {ECO:0000305}.
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DR EMBL; AK012696; BAB28417.1; -; mRNA.
DR EMBL; AK077450; BAC36806.1; -; mRNA.
DR EMBL; BC002088; AAH02088.1; -; mRNA.
DR EMBL; BC027208; AAH27208.1; -; mRNA.
DR EMBL; BC079541; AAH79541.1; -; mRNA.
DR CCDS; CCDS40600.1; -.
DR RefSeq; NP_077228.1; NM_024266.3.
DR PDB; 7CPU; EM; 2.82 A; SZ=1-125.
DR PDB; 7CPV; EM; 3.03 A; SZ=1-125.
DR PDB; 7LS1; EM; 3.30 A; R3=1-125.
DR PDB; 7LS2; EM; 3.10 A; R3=1-125.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P62852; -.
DR SMR; P62852; -.
DR BioGRID; 217620; 87.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P62852; 3.
DR MINT; P62852; -.
DR STRING; 10090.ENSMUSP00000079180; -.
DR iPTMnet; P62852; -.
DR PhosphoSitePlus; P62852; -.
DR SwissPalm; P62852; -.
DR EPD; P62852; -.
DR jPOST; P62852; -.
DR PaxDb; P62852; -.
DR PeptideAtlas; P62852; -.
DR PRIDE; P62852; -.
DR ProteomicsDB; 262732; -.
DR DNASU; 75617; -.
DR Ensembl; ENSMUST00000080300; ENSMUSP00000079180; ENSMUSG00000009927.
DR Ensembl; ENSMUST00000216867; ENSMUSP00000149401; ENSMUSG00000009927.
DR GeneID; 75617; -.
DR KEGG; mmu:75617; -.
DR UCSC; uc009pdm.1; mouse.
DR CTD; 6230; -.
DR MGI; MGI:1922867; Rps25.
DR VEuPathDB; HostDB:ENSMUSG00000009927; -.
DR eggNOG; KOG1767; Eukaryota.
DR GeneTree; ENSGT00390000004856; -.
DR HOGENOM; CLU_129470_0_1_1; -.
DR InParanoid; P62852; -.
DR OMA; RIVHHSG; -.
DR OrthoDB; 1552294at2759; -.
DR PhylomeDB; P62852; -.
DR TreeFam; TF314909; -.
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; 75617; 28 hits in 68 CRISPR screens.
DR ChiTaRS; Rps25; mouse.
DR PRO; PR:P62852; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P62852; protein.
DR Bgee; ENSMUSG00000009927; Expressed in ectoplacental cone and 253 other tissues.
DR ExpressionAtlas; P62852; baseline and differential.
DR Genevisible; P62852; 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; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISO:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR004977; Ribosomal_S25.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12850; PTHR12850; 1.
DR Pfam; PF03297; Ribosomal_S25; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..125
FT /note="40S ribosomal protein S25"
FT /id="PRO_0000192870"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 52
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62851"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62851"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62851"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 125 AA; 13742 MW; B8E05F04FCF2F1A9 CRC64;
MPPKDDKKKK DAGKSAKKDK DPVNKSGGKA KKKKWSKGKV RDKLNNLVLF DKATYDKLCK
EVPNYKLITP AVVSERLKIR GSLARAALQE LLSKGLIKLV SKHRAQVIYT RNTKGGDAPA
AGEDA
