RS13_HUMAN
ID RS13_HUMAN Reviewed; 151 AA.
AC P62277; B2R549; P19116; Q02546; Q29200; Q498Y0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=40S ribosomal protein S13;
DE AltName: Full=Small ribosomal subunit protein uS15 {ECO:0000303|PubMed:24524803};
GN Name=RPS13;
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].
RX PubMed=8332508; DOI=10.1093/nar/21.12.2945;
RA Chadeneau C., Lemoullac B., Denis M.G.;
RT "Cloning and analysis of the human S13 ribosomal protein cDNA.";
RL Nucleic Acids Res. 21:2945-2945(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Filipenko M.L.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8920921; DOI=10.1006/bbrc.1996.1668;
RA Kenmochi N., Higa S., Yoshihama M., Tanaka T.;
RT "U14 snoRNAs are encoded in introns of human ribosomal protein S13 gene.";
RL Biochem. Biophys. Res. Commun. 228:371-374(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, Brain, Muscle, Pancreas, and Placenta;
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 2-8, AND CLEAVAGE OF INITIATOR METHIONINE.
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-127.
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
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 [15]
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 [16]
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(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 -!- INTERACTION:
CC P62277; Q5S007: LRRK2; NbExp=3; IntAct=EBI-351850, EBI-5323863;
CC P62277; Q99558: MAP3K14; NbExp=3; IntAct=EBI-351850, EBI-358011;
CC P62277; Q53EL6: PDCD4; NbExp=2; IntAct=EBI-351850, EBI-935824;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000305}.
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DR EMBL; L01124; AAA60283.1; -; mRNA.
DR EMBL; X79239; CAA55821.1; -; mRNA.
DR EMBL; D88010; BAA13528.1; -; Genomic_DNA.
DR EMBL; AK312060; BAG34996.1; -; mRNA.
DR EMBL; CH471064; EAW68448.1; -; Genomic_DNA.
DR EMBL; BC000475; AAH00475.1; -; mRNA.
DR EMBL; BC006772; AAH06772.1; -; mRNA.
DR EMBL; BC029732; AAH29732.1; -; mRNA.
DR EMBL; BC066322; AAH66322.1; -; mRNA.
DR EMBL; BC100032; AAI00033.1; -; mRNA.
DR EMBL; L05090; AAC15854.1; -; mRNA.
DR CCDS; CCDS7823.1; -.
DR PIR; S34109; S34109.
DR RefSeq; NP_001008.1; NM_001017.2.
DR PDB; 4UG0; EM; -; SN=1-151.
DR PDB; 4V6X; EM; 5.00 A; AN=1-151.
DR PDB; 5A2Q; EM; 3.90 A; N=1-151.
DR PDB; 5AJ0; EM; 3.50 A; BN=1-151.
DR PDB; 5FLX; EM; 3.90 A; N=1-151.
DR PDB; 5LKS; EM; 3.60 A; SN=1-151.
DR PDB; 5OA3; EM; 4.30 A; N=1-151.
DR PDB; 5T2C; EM; 3.60 A; AN=1-151.
DR PDB; 5VYC; X-ray; 6.00 A; N1/N2/N3/N4/N5/N6=1-151.
DR PDB; 6FEC; EM; 6.30 A; Z=2-151.
DR PDB; 6G18; EM; 3.60 A; N=1-151.
DR PDB; 6G4S; EM; 4.00 A; N=1-151.
DR PDB; 6G4W; EM; 4.50 A; N=1-151.
DR PDB; 6G51; EM; 4.10 A; N=1-151.
DR PDB; 6G53; EM; 4.50 A; N=1-151.
DR PDB; 6G5H; EM; 3.60 A; N=1-151.
DR PDB; 6G5I; EM; 3.50 A; N=1-151.
DR PDB; 6IP5; EM; 3.90 A; 3K=1-151.
DR PDB; 6IP6; EM; 4.50 A; 3K=1-151.
DR PDB; 6IP8; EM; 3.90 A; 3K=1-151.
DR PDB; 6OLE; EM; 3.10 A; SN=2-151.
DR PDB; 6OLF; EM; 3.90 A; SN=2-151.
DR PDB; 6OLG; EM; 3.40 A; BN=2-150.
DR PDB; 6OLI; EM; 3.50 A; SN=2-151.
DR PDB; 6OLZ; EM; 3.90 A; BN=2-150.
DR PDB; 6OM0; EM; 3.10 A; SN=2-151.
DR PDB; 6OM7; EM; 3.70 A; SN=2-151.
DR PDB; 6QZP; EM; 2.90 A; SN=2-151.
DR PDB; 6XA1; EM; 2.80 A; SN=2-151.
DR PDB; 6Y0G; EM; 3.20 A; SN=1-151.
DR PDB; 6Y2L; EM; 3.00 A; SN=1-151.
DR PDB; 6Y57; EM; 3.50 A; SN=1-151.
DR PDB; 6YBD; EM; 3.30 A; I=1-151.
DR PDB; 6YBW; EM; 3.10 A; I=1-151.
DR PDB; 6Z6L; EM; 3.00 A; SN=1-151.
DR PDB; 6Z6M; EM; 3.10 A; SN=1-151.
DR PDB; 6Z6N; EM; 2.90 A; SN=1-151.
DR PDB; 6ZLW; EM; 2.60 A; N=1-151.
DR PDB; 6ZM7; EM; 2.70 A; SN=1-151.
DR PDB; 6ZME; EM; 3.00 A; SN=1-151.
DR PDB; 6ZMI; EM; 2.60 A; SN=1-151.
DR PDB; 6ZMO; EM; 3.10 A; SN=1-151.
DR PDB; 6ZMT; EM; 3.00 A; N=1-151.
DR PDB; 6ZMW; EM; 3.70 A; I=1-151.
DR PDB; 6ZN5; EM; 3.20 A; N=2-150.
DR PDB; 6ZOJ; EM; 2.80 A; N=1-151.
DR PDB; 6ZOK; EM; 2.80 A; N=1-151.
DR PDB; 6ZON; EM; 3.00 A; m=1-151.
DR PDB; 6ZP4; EM; 2.90 A; m=1-151.
DR PDB; 6ZUO; EM; 3.10 A; N=1-151.
DR PDB; 6ZV6; EM; 2.90 A; N=1-151.
DR PDB; 6ZVH; EM; 2.90 A; N=2-151.
DR PDB; 6ZVJ; EM; 3.80 A; m=2-150.
DR PDB; 6ZXD; EM; 3.20 A; N=1-151.
DR PDB; 6ZXE; EM; 3.00 A; N=1-151.
DR PDB; 6ZXF; EM; 3.70 A; N=1-151.
DR PDB; 6ZXG; EM; 2.60 A; N=1-151.
DR PDB; 6ZXH; EM; 2.70 A; N=1-151.
DR PDB; 7A09; EM; 3.50 A; m=1-151.
DR PDB; 7JQB; EM; 2.70 A; P=1-151.
DR PDB; 7JQC; EM; 3.30 A; P=1-151.
DR PDB; 7K5I; EM; 2.90 A; N=1-151.
DR PDB; 7MQ8; EM; 3.60 A; NF=1-151.
DR PDB; 7MQ9; EM; 3.87 A; NF=1-151.
DR PDB; 7MQA; EM; 2.70 A; NF=1-151.
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; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
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; 6YBD; -.
DR PDBsum; 6YBW; -.
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; 6ZOK; -.
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; 7JQB; -.
DR PDBsum; 7JQC; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P62277; -.
DR SMR; P62277; -.
DR BioGRID; 112121; 390.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62277; -.
DR IntAct; P62277; 111.
DR MINT; P62277; -.
DR STRING; 9606.ENSP00000435777; -.
DR DrugBank; DB11638; Artenimol.
DR MoonProt; P62277; -.
DR GlyGen; P62277; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62277; -.
DR PhosphoSitePlus; P62277; -.
DR SwissPalm; P62277; -.
DR BioMuta; RPS13; -.
DR DMDM; 50403608; -.
DR EPD; P62277; -.
DR jPOST; P62277; -.
DR MassIVE; P62277; -.
DR MaxQB; P62277; -.
DR PaxDb; P62277; -.
DR PeptideAtlas; P62277; -.
DR PRIDE; P62277; -.
DR ProteomicsDB; 57384; -.
DR TopDownProteomics; P62277; -.
DR Antibodypedia; 42458; 239 antibodies from 28 providers.
DR DNASU; 6207; -.
DR Ensembl; ENST00000525634.6; ENSP00000435777.1; ENSG00000110700.7.
DR GeneID; 6207; -.
DR KEGG; hsa:6207; -.
DR MANE-Select; ENST00000525634.6; ENSP00000435777.1; NM_001017.3; NP_001008.1.
DR UCSC; uc001mmp.4; human.
DR CTD; 6207; -.
DR DisGeNET; 6207; -.
DR GeneCards; RPS13; -.
DR HGNC; HGNC:10386; RPS13.
DR HPA; ENSG00000110700; Low tissue specificity.
DR MIM; 180476; gene.
DR neXtProt; NX_P62277; -.
DR OpenTargets; ENSG00000110700; -.
DR PharmGKB; PA34785; -.
DR VEuPathDB; HostDB:ENSG00000110700; -.
DR eggNOG; KOG0400; Eukaryota.
DR GeneTree; ENSGT00390000017491; -.
DR HOGENOM; CLU_090139_1_0_1; -.
DR InParanoid; P62277; -.
DR OMA; EEHPKDM; -.
DR OrthoDB; 1387147at2759; -.
DR PhylomeDB; P62277; -.
DR TreeFam; TF300190; -.
DR PathwayCommons; P62277; -.
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; P62277; -.
DR SIGNOR; P62277; -.
DR BioGRID-ORCS; 6207; 801 hits in 1053 CRISPR screens.
DR ChiTaRS; RPS13; human.
DR GeneWiki; RPS13; -.
DR GenomeRNAi; 6207; -.
DR Pharos; P62277; Tbio.
DR PRO; PR:P62277; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P62277; protein.
DR Bgee; ENSG00000110700; Expressed in monocyte and 98 other tissues.
DR ExpressionAtlas; P62277; baseline and differential.
DR Genevisible; P62277; 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:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1.
DR InterPro; IPR012606; Ribosomal_S13/S15_N.
DR InterPro; IPR000589; Ribosomal_S15.
DR InterPro; IPR023029; Ribosomal_S15P.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR PANTHER; PTHR11885; PTHR11885; 1.
DR Pfam; PF08069; Ribosomal_S13_N; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR SMART; SM01386; Ribosomal_S13_N; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699"
FT CHAIN 2..151
FT /note="40S ribosomal protein S13"
FT /id="PRO_0000115661"
FT MOD_RES 27
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 27
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62301"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62301"
FT MOD_RES 38
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 82
FT /note="P -> S (in Ref. 8; AAC15854)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 86..104
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 109..131
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7JQB"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 151 AA; 17222 MW; 23F94D38F87B8D53 CRC64;
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES
RIHRLARYYK TKRVLPPNWK YESSTASALV A
