ID RS17_HUMAN Reviewed; 135 AA. AC P08708; B2R4U4; P0CW22; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 224. DE RecName: Full=Small ribosomal subunit protein eS17 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S17 {ECO:0000305}; GN Name=RPS17 {ECO:0000312|HGNC:HGNC:10397}; GN Synonyms=RPS17L {ECO:0000312|HGNC:HGNC:10397}; 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=3529092; DOI=10.1073/pnas.83.18.6907; RA Chen I.-T., Dixit A., Rhoads D.D., Roufa D.J.; RT "Homologous ribosomal proteins in bacteria, yeast, and humans."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6907-6911(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3240863; DOI=10.1016/0378-1119(88)90109-6; RA Chen I.-T., Roufa D.J.; RT "The transcriptionally active human ribosomal protein S17 gene."; RL Gene 70:107-116(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(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]. RC TISSUE=B-cell, Kidney, Lung, Pancreas, Prostate, and Salivary 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 [7] RP PROTEIN SEQUENCE OF 2-16. 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 INVOLVEMENT IN DBA4. RX PubMed=17647292; DOI=10.1002/humu.20608; RA Cmejla R., Cmejlova J., Handrkova H., Petrak J., Pospisilova D.; RT "Ribosomal protein S17 gene (RPS17) is mutated in Diamond-Blackfan RT anemia."; RL Hum. Mutat. 28:1178-1182(2007). RN [9] RP INVOLVEMENT IN DBA4. RX PubMed=19061985; DOI=10.1016/j.ajhg.2008.11.004; RA Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., RA Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., RA Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., RA Meerpohl J.J., Atsidaftos E., Lipton J.M., Gleizes P.-E., Beggs A.H.; RT "Ribosomal protein L5 and L11 mutations are associated with cleft palate RT and abnormal thumbs in Diamond-Blackfan anemia patients."; RL Am. J. Hum. Genet. 83:769-780(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, AND RP IDENTIFICATION BY MASS 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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 [17] 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 [18] 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [20] 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103, 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 [22] RP UBIQUITINATION AT LYS-103. RX PubMed=36638793; DOI=10.1016/j.cell.2022.12.025; RA Oltion K., Carelli J.D., Yang T., See S.K., Wang H.Y., Kampmann M., RA Taunton J.; RT "An E3 ligase network engages GCN1 to promote the degradation of RT translation factors on stalled ribosomes."; RL Cell 0:0-0(2023). RN [23] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. 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). RN [24] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). CC -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23636399). CC The ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:23636399). Part of the small CC subunit (SSU) processome, first precursor of the small eukaryotic CC ribosomal subunit. During the assembly of the SSU processome in the CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and CC ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23636399). CC Part of the small subunit (SSU) processome, composed of more than 70 CC proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 CC (PubMed:34516797). {ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:34516797}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, CC nucleolus {ECO:0000269|PubMed:34516797}. CC -!- PTM: Ubiquitinated at Lys-103 by RNF14 and RNF25 in response to CC ribosome collisions (ribosome stalling). {ECO:0000269|PubMed:36638793}. CC -!- DISEASE: Diamond-Blackfan anemia 4 (DBA4) [MIM:612527]: A form of CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic CC anemia that usually presents early in infancy. Diamond-Blackfan anemia CC is characterized by a moderate to severe macrocytic anemia, CC erythroblastopenia, and an increased risk of developing leukemia. 30 to CC 40% of Diamond-Blackfan anemia patients present with short stature and CC congenital anomalies, the most frequent being craniofacial (Pierre- CC Robin syndrome and cleft palate), thumb and urogenital anomalies. CC {ECO:0000269|PubMed:17647292, ECO:0000269|PubMed:19061985}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS17 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; M13932; AAA60284.1; -; mRNA. DR EMBL; M18000; AAA60285.1; -; Genomic_DNA. DR EMBL; AK026570; BAB15501.1; -; mRNA. DR EMBL; AK311951; BAG34891.1; -; mRNA. DR EMBL; AC245033; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471188; EAW62454.1; -; Genomic_DNA. DR EMBL; BC009407; AAH09407.1; -; mRNA. DR EMBL; BC019899; AAH19899.1; -; mRNA. DR EMBL; BC022370; AAH22370.1; -; mRNA. DR EMBL; BC049824; AAH49824.1; -; mRNA. DR EMBL; BC070222; AAH70222.1; -; mRNA. DR EMBL; BC062715; AAH62715.1; -; mRNA. DR EMBL; BC071928; AAH71928.1; -; mRNA. DR CCDS; CCDS10320.1; -. DR PIR; JT0405; R4HU17. DR RefSeq; NP_001012.1; NM_001021.4. DR PDB; 4UG0; EM; -; SR=1-135. DR PDB; 4V6X; EM; 5.00 A; AR=1-135. DR PDB; 5A2Q; EM; 3.90 A; R=1-135. DR PDB; 5AJ0; EM; 3.50 A; BR=1-135. DR PDB; 5FLX; EM; 3.90 A; R=1-135. DR PDB; 5LKS; EM; 3.60 A; SR=1-135. DR PDB; 5OA3; EM; 4.30 A; R=1-135. DR PDB; 5T2C; EM; 3.60 A; Az=1-135. DR PDB; 5VYC; X-ray; 6.00 A; R1/R2/R3/R4/R5/R6=1-135. DR PDB; 6FEC; EM; 6.30 A; e=1-126. DR PDB; 6G18; EM; 3.60 A; R=1-135. DR PDB; 6G4S; EM; 4.00 A; R=1-135. DR PDB; 6G4W; EM; 4.50 A; R=1-135. DR PDB; 6G51; EM; 4.10 A; R=1-135. DR PDB; 6G53; EM; 4.50 A; R=1-135. DR PDB; 6G5H; EM; 3.60 A; R=1-135. DR PDB; 6G5I; EM; 3.50 A; R=1-135. DR PDB; 6IP5; EM; 3.90 A; 2y=1-135. DR PDB; 6IP6; EM; 4.50 A; 2y=1-135. DR PDB; 6IP8; EM; 3.90 A; 2y=1-135. DR PDB; 6OLE; EM; 3.10 A; SR=2-135. DR PDB; 6OLF; EM; 3.90 A; SR=2-135. DR PDB; 6OLG; EM; 3.40 A; BR=2-126. DR PDB; 6OLI; EM; 3.50 A; SR=2-135. DR PDB; 6OLZ; EM; 3.90 A; BR=2-126. DR PDB; 6OM0; EM; 3.10 A; SR=2-135. DR PDB; 6OM7; EM; 3.70 A; SR=2-135. DR PDB; 6QZP; EM; 2.90 A; SR=1-135. DR PDB; 6XA1; EM; 2.80 A; SR=2-132. DR PDB; 6Y0G; EM; 3.20 A; SR=1-135. DR PDB; 6Y2L; EM; 3.00 A; SR=1-135. DR PDB; 6Y57; EM; 3.50 A; SR=1-135. DR PDB; 6YBD; EM; 3.30 A; M=1-135. DR PDB; 6YBS; EM; 3.10 A; X=1-135. DR PDB; 6YBW; EM; 3.10 A; M=1-135. DR PDB; 6Z6L; EM; 3.00 A; SR=1-135. DR PDB; 6Z6M; EM; 3.10 A; SR=1-135. DR PDB; 6Z6N; EM; 2.90 A; SR=1-135. DR PDB; 6ZLW; EM; 2.60 A; S=1-135. DR PDB; 6ZM7; EM; 2.70 A; SR=1-135. DR PDB; 6ZME; EM; 3.00 A; SR=1-135. DR PDB; 6ZMI; EM; 2.60 A; SR=1-135. DR PDB; 6ZMO; EM; 3.10 A; SR=1-135. DR PDB; 6ZMT; EM; 3.00 A; S=1-135. DR PDB; 6ZMW; EM; 3.70 A; M=1-135. DR PDB; 6ZN5; EM; 3.20 A; S=2-133. DR PDB; 6ZOJ; EM; 2.80 A; R=1-135. DR PDB; 6ZOK; EM; 2.80 A; R=1-135. DR PDB; 6ZOL; EM; 2.80 A; R=1-135. DR PDB; 6ZON; EM; 3.00 A; w=1-135. DR PDB; 6ZP4; EM; 2.90 A; w=1-135. DR PDB; 6ZUO; EM; 3.10 A; R=1-135. DR PDB; 6ZV6; EM; 2.90 A; R=1-135. DR PDB; 6ZVH; EM; 2.90 A; R=1-135. DR PDB; 6ZVJ; EM; 3.80 A; w=2-131. DR PDB; 6ZXD; EM; 3.20 A; R=1-135. DR PDB; 6ZXE; EM; 3.00 A; R=1-135. DR PDB; 6ZXF; EM; 3.70 A; R=1-135. DR PDB; 6ZXG; EM; 2.60 A; R=1-135. DR PDB; 6ZXH; EM; 2.70 A; R=1-135. DR PDB; 7A09; EM; 3.50 A; w=1-135. DR PDB; 7K5I; EM; 2.90 A; R=1-135. DR PDB; 7MQ8; EM; 3.60 A; NU=1-135. DR PDB; 7MQ9; EM; 3.87 A; NU=1-135. DR PDB; 7MQA; EM; 2.70 A; NU=1-135. DR PDB; 7QP6; EM; 4.70 A; M=1-135. DR PDB; 7QP7; EM; 3.70 A; M=1-135. DR PDB; 7QVP; EM; 3.00 A; RR/SR=1-135. DR PDB; 7R4X; EM; 2.15 A; R=1-135. DR PDB; 7TQL; EM; 3.40 A; S=2-133. DR PDB; 7WTT; EM; 3.10 A; R=1-135. DR PDB; 7WTU; EM; 3.00 A; R=1-135. DR PDB; 7WTV; EM; 3.50 A; R=1-135. DR PDB; 7WTW; EM; 3.20 A; R=1-135. DR PDB; 7WTX; EM; 3.10 A; R=1-135. DR PDB; 7WTZ; EM; 3.00 A; R=1-135. DR PDB; 7WU0; EM; 3.30 A; R=1-135. DR PDB; 7XNX; EM; 2.70 A; SR=1-135. DR PDB; 7XNY; EM; 2.50 A; SR=1-135. DR PDB; 8G5Y; EM; 2.29 A; SR=1-135. DR PDB; 8G5Z; EM; 2.64 A; SR=2-135. DR PDB; 8G60; EM; 2.54 A; SR=1-135. DR PDB; 8G61; EM; 2.94 A; SR=1-135. DR PDB; 8G6J; EM; 2.80 A; SR=1-135. DR PDB; 8GLP; EM; 1.67 A; SR=1-135. DR PDB; 8JDJ; EM; 2.50 A; AD=1-135. DR PDB; 8JDK; EM; 2.26 A; AD=1-135. DR PDB; 8JDL; EM; 2.42 A; AD=1-135. DR PDB; 8JDM; EM; 2.67 A; AD=1-135. DR PDB; 8PPK; EM; 2.98 A; R=1-135. DR PDB; 8PPL; EM; 2.65 A; AR=1-135. DR PDB; 8T4S; EM; 2.60 A; R=1-135. 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; 6YBS; -. 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; 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 PDBsum; 7MQ8; -. DR PDBsum; 7MQ9; -. DR PDBsum; 7MQA; -. DR PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7QVP; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7WTT; -. DR PDBsum; 7WTU; -. DR PDBsum; 7WTV; -. DR PDBsum; 7WTW; -. DR PDBsum; 7WTX; -. DR PDBsum; 7WTZ; -. DR PDBsum; 7WU0; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8T4S; -. DR AlphaFoldDB; P08708; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-10772; -. DR EMDB; EMD-10775; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11301; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11321; -. DR EMDB; EMD-11322; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11440; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11517; -. DR EMDB; EMD-11518; -. DR EMDB; EMD-11519; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14181; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-32800; -. DR EMDB; EMD-32801; -. DR EMDB; EMD-32802; -. DR EMDB; EMD-32803; -. DR EMDB; EMD-32804; -. DR EMDB; EMD-32806; -. DR EMDB; EMD-32807; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-4337; -. DR EMDB; EMD-4348; -. DR EMDB; EMD-4349; -. DR EMDB; EMD-4350; -. DR EMDB; EMD-4351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-4353; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P08708; -. DR BioGRID; 112132; 297. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P08708; -. DR IntAct; P08708; 81. DR MINT; P08708; -. DR STRING; 9606.ENSP00000498019; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P08708; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P08708; -. DR MetOSite; P08708; -. DR PhosphoSitePlus; P08708; -. DR SwissPalm; P08708; -. DR BioMuta; RPS17; -. DR DMDM; 338819320; -. DR EPD; P08708; -. DR jPOST; P08708; -. DR MassIVE; P08708; -. DR PaxDb; 9606-ENSP00000346046; -. DR PeptideAtlas; P08708; -. DR Pumba; P08708; -. DR TopDownProteomics; P08708; -. DR Antibodypedia; 56676; 157 antibodies from 26 providers. DR DNASU; 6218; -. DR Ensembl; ENST00000617731.2; ENSP00000483755.1; ENSG00000278229.2. DR Ensembl; ENST00000647841.1; ENSP00000498019.1; ENSG00000182774.13. DR GeneID; 6218; -. DR KEGG; hsa:6218; -. DR MANE-Select; ENST00000647841.1; ENSP00000498019.1; NM_001021.6; NP_001012.1. DR AGR; HGNC:10397; -. DR CTD; 6218; -. DR DisGeNET; 6218; -. DR GeneCards; RPS17; -. DR GeneReviews; RPS17; -. DR HGNC; HGNC:10397; RPS17. DR HPA; ENSG00000182774; Low tissue specificity. DR MalaCards; RPS17; -. DR MIM; 180472; gene. DR MIM; 612527; phenotype. DR neXtProt; NX_P08708; -. DR OpenTargets; ENSG00000182774; -. DR Orphanet; 124; Diamond-Blackfan anemia. DR PharmGKB; PA34797; -. DR VEuPathDB; HostDB:ENSG00000182774; -. DR eggNOG; KOG0187; Eukaryota. DR GeneTree; ENSGT00390000006548; -. DR HOGENOM; CLU_112958_1_1_1; -. DR InParanoid; P08708; -. DR OMA; HYNKGPR; -. DR OrthoDB; 5480552at2759; -. DR PhylomeDB; P08708; -. DR TreeFam; TF317992; -. DR PathwayCommons; P08708; -. 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-9735869; SARS-CoV-1 modulates host translation machinery. 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; P08708; -. DR SIGNOR; P08708; -. DR BioGRID-ORCS; 6218; 418 hits in 698 CRISPR screens. DR ChiTaRS; RPS17; human. DR GeneWiki; RPS17; -. DR GenomeRNAi; 6218; -. DR Pharos; P08708; Tbio. DR PRO; PR:P08708; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P08708; Protein. DR Bgee; ENSG00000182774; Expressed in ganglionic eminence and 98 other cell types or tissues. DR ExpressionAtlas; P08708; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS: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:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005840; C:ribosome; NAS:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:UniProtKB. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IC:UniProtKB. DR GO; GO:0006413; P:translational initiation; NAS:UniProtKB. DR Gene3D; 1.10.60.20; Ribosomal protein S17e-like; 1. DR HAMAP; MF_00511; Ribosomal_eS17; 1. DR InterPro; IPR001210; Ribosomal_eS17. DR InterPro; IPR018273; Ribosomal_eS17_CS. DR InterPro; IPR036401; Ribosomal_eS17_sf. DR PANTHER; PTHR10732; 40S RIBOSOMAL PROTEIN S17; 1. DR PANTHER; PTHR10732:SF0; 40S RIBOSOMAL PROTEIN S17; 1. DR Pfam; PF00833; Ribosomal_S17e; 1. DR SUPFAM; SSF116820; Rps17e-like; 1. DR PROSITE; PS00712; RIBOSOMAL_S17E; 1. DR Genevisible; P08708; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Diamond-Blackfan anemia; KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8706699" FT CHAIN 2..135 FT /note="Small ribosomal subunit protein eS17" FT /id="PRO_0000141525" FT MOD_RES 19 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P63276" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 130 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT CROSSLNK 103 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 103 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000269|PubMed:36638793, FT ECO:0007744|PubMed:28112733" FT VARIANT 36 FT /note="E -> K (in dbSNP:rs1043734)" FT /id="VAR_034478" FT HELIX 7..20 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 28..37 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 44..61 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 75..81 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:6ZV6" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 100..107 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:7R4X" SQ SEQUENCE 135 AA; 15550 MW; 299AD605C5401325 CRC64; MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP DTKEMLKLLD FGSLSNLQVT QPTVGMNFKT PRGPV //