RS17_HUMAN
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 03-AUG-2022, entry version 215.
DE RecName: Full=40S ribosomal protein S17 {ECO:0000305};
DE AltName: Full=Small ribosomal subunit protein eS17 {ECO:0000303|PubMed:24524803};
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 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 -!- 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}.
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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 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 AlphaFoldDB; P08708; -.
DR SMR; P08708; -.
DR BioGRID; 112132; 238.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P08708; -.
DR IntAct; P08708; 76.
DR MINT; P08708; -.
DR STRING; 9606.ENSP00000346046; -.
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; P08708; -.
DR PeptideAtlas; P08708; -.
DR PRIDE; P08708; -.
DR TopDownProteomics; P08708; -.
DR Antibodypedia; 56676; 148 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 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; Blackfan-Diamond 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; GMAFRGP; -.
DR OrthoDB; 1459807at2759; -.
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-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; 397 hits in 635 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 96 other tissues.
DR ExpressionAtlas; P08708; baseline and differential.
DR Genevisible; P08708; 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:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005840; C:ribosome; NAS: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; IC:FlyBase.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP: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; -; 1.
DR HAMAP; MF_00511; Ribosomal_S17e; 1.
DR InterPro; IPR001210; Ribosomal_S17e.
DR InterPro; IPR018273; Ribosomal_S17e_CS.
DR InterPro; IPR036401; RPS17e-like_sf.
DR PANTHER; PTHR10732; PTHR10732; 1.
DR Pfam; PF00833; Ribosomal_S17e; 1.
DR SUPFAM; SSF116820; SSF116820; 1.
DR PROSITE; PS00712; RIBOSOMAL_S17E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Diamond-Blackfan anemia; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699"
FT CHAIN 2..135
FT /note="40S ribosomal protein S17"
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:0007744|PubMed:28112733"
FT VARIANT 36
FT /note="E -> K (in dbSNP:rs1043734)"
FT /id="VAR_034478"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 135 AA; 15550 MW; 299AD605C5401325 CRC64;
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR
IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP DTKEMLKLLD FGSLSNLQVT
QPTVGMNFKT PRGPV
