ID RS27_MOUSE Reviewed; 84 AA. AC Q6ZWU9; Q3TLE3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 163. DE RecName: Full=Small ribosomal subunit protein eS27 {ECO:0000305}; DE AltName: Full=40S ribosomal protein S27; GN Name=Rps27 {ECO:0000312|MGI:MGI:1888676}; 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, and NOD; TISSUE=Head, and Thymus; 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] {ECO:0000312|EMBL:AAH55693.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH55693.1}, and FVB/N-3; RC TISSUE=Brain {ECO:0000312|EMBL:AAH55693.1}, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and RC Spleen; 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). Required for CC proper rRNA processing and maturation of 18S rRNAs (By similarity). CC Part of the small subunit (SSU) processome, first precursor of the CC small eukaryotic ribosomal subunit. During the assembly of the SSU CC processome in the nucleolus, many ribosome biogenesis factors, an RNA CC chaperone and ribosomal proteins associate with the nascent pre-rRNA CC and work in concert to generate RNA folding, modifications, CC rearrangements and cleavage as well as targeted degradation of pre- CC ribosomal RNA by the RNA exosome (By similarity). CC {ECO:0000250|UniProtKB:P42677, ECO:0000269|PubMed:36517592}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SUBUNIT: Component of the small ribosomal subunit. Part of the small CC subunit (SSU) processome, composed of more than 70 proteins and the RNA CC chaperone small nucleolar RNA (snoRNA) U3 (By similarity). CC {ECO:0000250|UniProtKB:P42677, ECO:0000269|PubMed:36517592}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P42677}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK014294; BAB29250.1; -; mRNA. DR EMBL; AK088320; BAC40279.1; -; mRNA. DR EMBL; AK166551; BAE38849.1; -; mRNA. DR EMBL; BC048352; AAH48352.1; -; mRNA. DR EMBL; BC055693; AAH55693.1; -; mRNA. DR CCDS; CCDS50970.1; -. DR RefSeq; NP_001177187.1; NM_001190258.1. DR RefSeq; NP_081291.1; NM_027015.4. DR PDB; 7CPU; EM; 2.82 A; Sb=1-84. DR PDB; 7CPV; EM; 3.03 A; Sb=1-84. DR PDBsum; 7CPU; -. DR PDBsum; 7CPV; -. DR AlphaFoldDB; Q6ZWU9; -. DR EMDB; EMD-30432; -. DR EMDB; EMD-30433; -. DR SMR; Q6ZWU9; -. DR BioGRID; 208248; 39. DR BioGRID; 786971; 4. DR IntAct; Q6ZWU9; 2. DR MINT; Q6ZWU9; -. DR STRING; 10090.ENSMUSP00000060523; -. DR iPTMnet; Q6ZWU9; -. DR PhosphoSitePlus; Q6ZWU9; -. DR SwissPalm; Q6ZWU9; -. DR EPD; Q6ZWU9; -. DR jPOST; Q6ZWU9; -. DR MaxQB; Q6ZWU9; -. DR PaxDb; 10090-ENSMUSP00000060523; -. DR PeptideAtlas; Q6ZWU9; -. DR ProteomicsDB; 260855; -. DR Pumba; Q6ZWU9; -. DR TopDownProteomics; Q6ZWU9; -. DR DNASU; 57294; -. DR Ensembl; ENSMUST00000053150.8; ENSMUSP00000060523.6; ENSMUSG00000050621.8. DR Ensembl; ENSMUST00000170122.4; ENSMUSP00000132102.3; ENSMUSG00000090733.7. DR GeneID; 100043813; -. DR GeneID; 57294; -. DR KEGG; mmu:100043813; -. DR KEGG; mmu:57294; -. DR UCSC; uc008qbl.2; mouse. DR AGR; MGI:1888676; -. DR CTD; 6232; -. DR MGI; MGI:1888676; Rps27. DR VEuPathDB; HostDB:ENSMUSG00000050621; -. DR VEuPathDB; HostDB:ENSMUSG00000090733; -. DR eggNOG; KOG1779; Eukaryota. DR GeneTree; ENSGT00950000182891; -. DR HOGENOM; CLU_130128_3_0_1; -. DR InParanoid; Q6ZWU9; -. DR OMA; CASILCQ; -. DR OrthoDB; 5470875at2759; -. DR PhylomeDB; Q6ZWU9; -. DR TreeFam; TF300265; -. DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. 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-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins. DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR Reactome; R-MMU-68877; Mitotic Prometaphase. 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-9648025; EML4 and NUDC in mitotic spindle formation. 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; 100043813; 14 hits in 43 CRISPR screens. DR BioGRID-ORCS; 57294; 28 hits in 57 CRISPR screens. DR ChiTaRS; Rps27; mouse. DR PRO; PR:Q6ZWU9; -. DR Proteomes; UP000000589; Chromosome 3. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q6ZWU9; Protein. DR Bgee; ENSMUSG00000050621; Expressed in adrenal gland and 63 other cell types or tissues. DR ExpressionAtlas; Q6ZWU9; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0014069; C:postsynaptic density; ISO:MGI. DR GO; GO:0098793; C:presynapse; IDA:SynGO. DR GO; GO:0005840; C:ribosome; IDA:SynGO. DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB. DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB. DR GO; GO:0140242; P:translation at postsynapse; IDA:SynGO. DR GO; GO:0140236; P:translation at presynapse; IDA:SynGO. DR Gene3D; 2.20.25.100; Zn-binding ribosomal proteins; 1. DR HAMAP; MF_00371; Ribosomal_eS27; 1. DR InterPro; IPR000592; Ribosomal_eS27. DR InterPro; IPR023407; Ribosomal_eS27_Zn-bd_dom_sf. DR InterPro; IPR011332; Ribosomal_zn-bd. DR PANTHER; PTHR11594; 40S RIBOSOMAL PROTEIN S27; 1. DR PANTHER; PTHR11594:SF1; 40S RIBOSOMAL PROTEIN S27; 1. DR Pfam; PF01667; Ribosomal_S27e; 1. DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1. DR PROSITE; PS01168; RIBOSOMAL_S27E; 1. DR Genevisible; Q6ZWU9; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Zinc; KW Zinc-finger. FT CHAIN 1..84 FT /note="Small ribosomal subunit protein eS27" FT /id="PRO_0000149052" FT ZN_FING 38..60 FT /note="C4-type" FT /evidence="ECO:0000255" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" SQ SEQUENCE 84 AA; 9461 MW; 242C4466AC8A8900 CRC64; MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS TVLCQPTGGK ARLTEGCSFR RKQH //