RS20_MOUSE
ID RS20_MOUSE Reviewed; 119 AA.
AC P60867; P17075;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=40S ribosomal protein S20;
GN Name=Rps20;
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; TISSUE=Kidney;
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 TISSUE=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-34 AND LYS-75, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [5]
RP UFMYLATION.
RX PubMed=28575669; DOI=10.1016/j.cell.2017.05.022;
RA Simsek D., Tiu G.C., Flynn R.A., Byeon G.W., Leppek K., Xu A.F.,
RA Chang H.Y., Barna M.;
RT "The mammalian ribo-interactome reveals ribosome functional diversity and
RT heterogeneity.";
RL Cell 169:1051-1065(2017).
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Monoubiquitinated by ZNF598 when a ribosome has stalled during
CC translation of poly(A) sequences, leading to preclude synthesis of a
CC long poly-lysine tail and initiate the ribosome quality control (RQC)
CC pathway to degrade the potentially detrimental aberrant nascent
CC polypeptide. {ECO:0000250|UniProtKB:P60866}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000269|PubMed:28575669}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS10 family.
CC {ECO:0000305}.
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DR EMBL; AK002405; BAB22075.1; -; mRNA.
DR EMBL; AK014594; BAB29450.1; -; mRNA.
DR EMBL; BC011323; AAH11323.1; -; mRNA.
DR CCDS; CCDS17940.1; -.
DR RefSeq; NP_080423.1; NM_026147.6.
DR PDB; 7CPU; EM; 2.82 A; SU=1-119.
DR PDB; 7CPV; EM; 3.03 A; SU=1-119.
DR PDB; 7LS1; EM; 3.30 A; C3=1-119.
DR PDB; 7LS2; EM; 3.10 A; C3=1-119.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P60867; -.
DR SMR; P60867; -.
DR BioGRID; 212179; 77.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR IntAct; P60867; 5.
DR MINT; P60867; -.
DR STRING; 10090.ENSMUSP00000120528; -.
DR iPTMnet; P60867; -.
DR PhosphoSitePlus; P60867; -.
DR SwissPalm; P60867; -.
DR CPTAC; non-CPTAC-3614; -.
DR EPD; P60867; -.
DR jPOST; P60867; -.
DR PaxDb; P60867; -.
DR PeptideAtlas; P60867; -.
DR PRIDE; P60867; -.
DR ProteomicsDB; 299900; -.
DR DNASU; 67427; -.
DR Ensembl; ENSMUST00000138502; ENSMUSP00000120528; ENSMUSG00000028234.
DR GeneID; 67427; -.
DR KEGG; mmu:67427; -.
DR UCSC; uc008rwn.1; mouse.
DR CTD; 6224; -.
DR MGI; MGI:1914677; Rps20.
DR VEuPathDB; HostDB:ENSMUSG00000028234; -.
DR eggNOG; KOG0900; Eukaryota.
DR GeneTree; ENSGT00390000003248; -.
DR HOGENOM; CLU_122625_0_0_1; -.
DR InParanoid; P60867; -.
DR OMA; MANIKKD; -.
DR OrthoDB; 1454256at2759; -.
DR PhylomeDB; P60867; -.
DR TreeFam; TF300222; -.
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; 67427; 24 hits in 64 CRISPR screens.
DR ChiTaRS; Rps20; mouse.
DR PRO; PR:P60867; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P60867; protein.
DR Bgee; ENSMUSG00000028234; Expressed in ventricular zone and 211 other tissues.
DR ExpressionAtlas; P60867; baseline and differential.
DR Genevisible; P60867; 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:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISO:MGI.
DR Gene3D; 3.30.70.600; -; 1.
DR HAMAP; MF_00508; Ribosomal_S10; 1.
DR InterPro; IPR001848; Ribosomal_S10.
DR InterPro; IPR018268; Ribosomal_S10_CS.
DR InterPro; IPR027486; Ribosomal_S10_dom.
DR InterPro; IPR036838; Ribosomal_S10_dom_sf.
DR InterPro; IPR005729; Ribosomal_S10_euk/arc.
DR PANTHER; PTHR11700; PTHR11700; 1.
DR Pfam; PF00338; Ribosomal_S10; 1.
DR PRINTS; PR00971; RIBOSOMALS10.
DR SMART; SM01403; Ribosomal_S10; 1.
DR SUPFAM; SSF54999; SSF54999; 1.
DR TIGRFAMs; TIGR01046; uS10_euk_arch; 1.
DR PROSITE; PS00361; RIBOSOMAL_S10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60866"
FT CHAIN 2..119
FT /note="40S ribosomal protein S20"
FT /id="PRO_0000146684"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P60866"
FT MOD_RES 8
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60866"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60866"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P60866"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P60866"
SQ SEQUENCE 119 AA; 13373 MW; 8802DF7894ADDF94 CRC64;
MAFKDTGKTP VEPEVAIHRI RITLTSRNVK SLEKVCADLI RGAKEKNLKV KGPVRMPTKT
LRITTRKTPC GEGSKTWDRF QMRIHKRLID LHSPSEIVKQ ITSISIEPGV EVEVTIADA
