RS20_HUMAN
ID RS20_HUMAN Reviewed; 119 AA.
AC P60866; B2R4F4; B4DW28; P17075; Q5M8S9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=40S ribosomal protein S20;
DE AltName: Full=Small ribosomal subunit protein uS10 {ECO:0000303|PubMed:24524803};
GN Name=RPS20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8479924; DOI=10.1093/nar/21.7.1672;
RA Chu W., Presky D.H., Swerlick R.A., Burns D.K.;
RT "Human ribosomal protein S20 cDNA sequence.";
RL Nucleic Acids Res. 21:1672-1672(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Synovium, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 2-19; 35-41 AND 88-99, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 9-24.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-110.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP UBIQUITINATION AT LYS-4 AND LYS-8, AND MUTAGENESIS OF LYS-4 AND LYS-8.
RX PubMed=28065601; DOI=10.1016/j.molcel.2016.11.039;
RA Juszkiewicz S., Hegde R.S.;
RT "Initiation of quality control during poly(A) translation requires site-
RT specific ribosome ubiquitination.";
RL Mol. Cell 65:743-750(2016).
RN [17]
RP UBIQUITINATION AT LYS-4 AND LYS-8, AND MUTAGENESIS OF LYS-4 AND LYS-8.
RX PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026;
RA Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.;
RT "ZNF598 and RACK1 regulate mammalian ribosome-associated quality control
RT function by mediating regulatory 40S ribosomal ubiquitylation.";
RL Mol. Cell 65:751-760(2017).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- SUBUNIT: Component of the 40S small ribosomal subunit. {ECO:0000250}.
CC -!- INTERACTION:
CC P60866; Q5S007: LRRK2; NbExp=4; IntAct=EBI-353105, EBI-5323863;
CC P60866; Q15843: NEDD8; NbExp=3; IntAct=EBI-353105, EBI-716247;
CC P60866; P36578: RPL4; NbExp=4; IntAct=EBI-353105, EBI-348313;
CC P60866; Q6S8E0: ORF9b; Xeno; NbExp=2; IntAct=EBI-353105, EBI-25489144;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60866-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60866-2; Sequence=VSP_042724;
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 (PubMed:28065601, PubMed:28132843).
CC {ECO:0000269|PubMed:28065601, ECO:0000269|PubMed:28132843}.
CC -!- PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:P60867}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS10 family.
CC {ECO:0000305}.
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DR EMBL; L06498; AAA60286.1; -; mRNA.
DR EMBL; AB061842; BAB79480.1; -; Genomic_DNA.
DR EMBL; AK301342; BAG62890.1; -; mRNA.
DR EMBL; AK311808; BAG34751.1; -; mRNA.
DR EMBL; AC107376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86771.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW86772.1; -; Genomic_DNA.
DR EMBL; BC007507; AAH07507.1; -; mRNA.
DR EMBL; BC087850; AAH87850.1; -; mRNA.
DR EMBL; AB007156; BAA25820.1; -; Genomic_DNA.
DR CCDS; CCDS55231.1; -. [P60866-2]
DR CCDS; CCDS6163.1; -. [P60866-1]
DR PIR; S33710; S33710.
DR RefSeq; NP_001014.1; NM_001023.3. [P60866-1]
DR RefSeq; NP_001139699.1; NM_001146227.1. [P60866-2]
DR PDB; 4UG0; EM; -; SU=1-119.
DR PDB; 4V6X; EM; 5.00 A; AU=1-119.
DR PDB; 5A2Q; EM; 3.90 A; U=1-119.
DR PDB; 5AJ0; EM; 3.50 A; BU=1-119.
DR PDB; 5FLX; EM; 3.90 A; U=1-119.
DR PDB; 5LKS; EM; 3.60 A; SU=1-119.
DR PDB; 5OA3; EM; 4.30 A; U=1-119.
DR PDB; 5T2C; EM; 3.60 A; AB=1-119.
DR PDB; 5VYC; X-ray; 6.00 A; U1/U2/U3/U4/U5/U6=1-119.
DR PDB; 6FEC; EM; 6.30 A; h=16-119.
DR PDB; 6G51; EM; 4.10 A; U=1-119.
DR PDB; 6G53; EM; 4.50 A; U=1-119.
DR PDB; 6G5H; EM; 3.60 A; U=1-119.
DR PDB; 6G5I; EM; 3.50 A; U=1-119.
DR PDB; 6IP5; EM; 3.90 A; 21=1-119.
DR PDB; 6IP6; EM; 4.50 A; 21=1-119.
DR PDB; 6IP8; EM; 3.90 A; 21=1-119.
DR PDB; 6OLE; EM; 3.10 A; SU=16-119.
DR PDB; 6OLF; EM; 3.90 A; SU=16-119.
DR PDB; 6OLG; EM; 3.40 A; BU=20-116.
DR PDB; 6OLI; EM; 3.50 A; SU=16-119.
DR PDB; 6OLZ; EM; 3.90 A; BU=20-116.
DR PDB; 6OM0; EM; 3.10 A; SU=16-119.
DR PDB; 6OM7; EM; 3.70 A; SU=16-119.
DR PDB; 6QZP; EM; 2.90 A; SU=17-119.
DR PDB; 6XA1; EM; 2.80 A; SU=17-116.
DR PDB; 6Y0G; EM; 3.20 A; SU=1-119.
DR PDB; 6Y2L; EM; 3.00 A; SU=1-119.
DR PDB; 6Y57; EM; 3.50 A; SU=1-119.
DR PDB; 6YBS; EM; 3.10 A; h=1-119.
DR PDB; 6Z6L; EM; 3.00 A; SU=1-119.
DR PDB; 6Z6M; EM; 3.10 A; SU=1-119.
DR PDB; 6Z6N; EM; 2.90 A; SU=1-119.
DR PDB; 6ZLW; EM; 2.60 A; V=1-119.
DR PDB; 6ZM7; EM; 2.70 A; SU=1-119.
DR PDB; 6ZME; EM; 3.00 A; SU=1-119.
DR PDB; 6ZMI; EM; 2.60 A; SU=1-119.
DR PDB; 6ZMO; EM; 3.10 A; SU=1-119.
DR PDB; 6ZMT; EM; 3.00 A; V=1-119.
DR PDB; 6ZMW; EM; 3.70 A; h=1-119.
DR PDB; 6ZN5; EM; 3.20 A; V=17-117.
DR PDB; 6ZOJ; EM; 2.80 A; U=1-119.
DR PDB; 6ZOL; EM; 2.80 A; U=1-119.
DR PDB; 6ZON; EM; 3.00 A; h=1-119.
DR PDB; 6ZP4; EM; 2.90 A; h=1-119.
DR PDB; 6ZUO; EM; 3.10 A; U=1-119.
DR PDB; 6ZV6; EM; 2.90 A; U=1-119.
DR PDB; 6ZVH; EM; 2.90 A; U=16-119.
DR PDB; 6ZVJ; EM; 3.80 A; h=19-116.
DR PDB; 6ZXD; EM; 3.20 A; U=1-119.
DR PDB; 6ZXE; EM; 3.00 A; U=1-119.
DR PDB; 6ZXF; EM; 3.70 A; U=1-119.
DR PDB; 6ZXG; EM; 2.60 A; U=1-119.
DR PDB; 6ZXH; EM; 2.70 A; U=1-119.
DR PDB; 7A09; EM; 3.50 A; h=1-119.
DR PDB; 7K5I; EM; 2.90 A; U=1-119.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P60866; -.
DR SMR; P60866; -.
DR BioGRID; 112138; 376.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P60866; -.
DR DIP; DIP-31245N; -.
DR IntAct; P60866; 79.
DR MINT; P60866; -.
DR STRING; 9606.ENSP00000429374; -.
DR GlyGen; P60866; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P60866; -.
DR PhosphoSitePlus; P60866; -.
DR SwissPalm; P60866; -.
DR BioMuta; RPS20; -.
DR DMDM; 46397703; -.
DR EPD; P60866; -.
DR jPOST; P60866; -.
DR MassIVE; P60866; -.
DR MaxQB; P60866; -.
DR PaxDb; P60866; -.
DR PeptideAtlas; P60866; -.
DR PRIDE; P60866; -.
DR ProteomicsDB; 57229; -. [P60866-1]
DR ProteomicsDB; 57230; -. [P60866-2]
DR TopDownProteomics; P60866-1; -. [P60866-1]
DR TopDownProteomics; P60866-2; -. [P60866-2]
DR Antibodypedia; 1248; 237 antibodies from 31 providers.
DR DNASU; 6224; -.
DR Ensembl; ENST00000009589.8; ENSP00000009589.3; ENSG00000008988.11. [P60866-1]
DR Ensembl; ENST00000519807.5; ENSP00000429374.1; ENSG00000008988.11. [P60866-2]
DR Ensembl; ENST00000521262.5; ENSP00000427788.1; ENSG00000008988.11. [P60866-1]
DR Ensembl; ENST00000676461.1; ENSP00000504670.1; ENSG00000008988.11. [P60866-1]
DR Ensembl; ENST00000676918.1; ENSP00000503327.1; ENSG00000008988.11. [P60866-1]
DR Ensembl; ENST00000678039.1; ENSP00000504154.1; ENSG00000008988.11. [P60866-1]
DR Ensembl; ENST00000678683.1; ENSP00000504123.1; ENSG00000008988.11. [P60866-1]
DR GeneID; 6224; -.
DR KEGG; hsa:6224; -.
DR MANE-Select; ENST00000009589.8; ENSP00000009589.3; NM_001023.4; NP_001014.1.
DR UCSC; uc003xsm.3; human. [P60866-1]
DR CTD; 6224; -.
DR DisGeNET; 6224; -.
DR GeneCards; RPS20; -.
DR HGNC; HGNC:10405; RPS20.
DR HPA; ENSG00000008988; Low tissue specificity.
DR MalaCards; RPS20; -.
DR MIM; 603682; gene.
DR neXtProt; NX_P60866; -.
DR OpenTargets; ENSG00000008988; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR Orphanet; 440437; Familial colorectal cancer Type X.
DR PharmGKB; PA34807; -.
DR VEuPathDB; HostDB:ENSG00000008988; -.
DR eggNOG; KOG0900; Eukaryota.
DR GeneTree; ENSGT00390000003248; -.
DR HOGENOM; CLU_122625_0_0_1; -.
DR InParanoid; P60866; -.
DR OMA; MANIKKD; -.
DR OrthoDB; 1454256at2759; -.
DR PhylomeDB; P60866; -.
DR TreeFam; TF300222; -.
DR PathwayCommons; P60866; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P60866; -.
DR SIGNOR; P60866; -.
DR BioGRID-ORCS; 6224; 782 hits in 1020 CRISPR screens.
DR ChiTaRS; RPS20; human.
DR GeneWiki; RPS20; -.
DR GenomeRNAi; 6224; -.
DR Pharos; P60866; Tbio.
DR PRO; PR:P60866; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P60866; protein.
DR Bgee; ENSG00000008988; Expressed in adult organism and 214 other tissues.
DR ExpressionAtlas; P60866; baseline and differential.
DR Genevisible; P60866; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:FlyBase.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
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; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..119
FT /note="40S ribosomal protein S20"
FT /id="PRO_0000146683"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 8
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60867"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60867"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60867"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT VAR_SEQ 112..119
FT /note="VEVTIADA -> LIESTDAEPMDTEGQQYTLRSVFESPGTCPF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042724"
FT MUTAGEN 4
FT /note="K->R: Enhanced readthrough on the poly(A)-stall
FT sequences; when associated with R-8."
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT MUTAGEN 8
FT /note="K->R: Enhanced readthrough on the poly(A)-stall
FT sequences; when associated with R-4."
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 77..93
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 119 AA; 13373 MW; 8802DF7894ADDF94 CRC64;
MAFKDTGKTP VEPEVAIHRI RITLTSRNVK SLEKVCADLI RGAKEKNLKV KGPVRMPTKT
LRITTRKTPC GEGSKTWDRF QMRIHKRLID LHSPSEIVKQ ITSISIEPGV EVEVTIADA
