ID RT17_HUMAN Reviewed; 130 AA. AC Q9Y2R5; Q86X15; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 24-JAN-2024, entry version 189. DE RecName: Full=Small ribosomal subunit protein uS17m {ECO:0000303|PubMed:25838379}; DE AltName: Full=28S ribosomal protein S17, mitochondrial; DE Short=MRP-S17; DE Short=S17mt; DE Flags: Precursor; GN Name=MRPS17; Synonyms=RPMS17; ORFNames=HSPC011; 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 [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175; RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., RA Wang Y.-X., Chen S.-J., Chen Z.; RT "Identification of genes expressed in human CD34(+) hematopoietic RT stem/progenitor cells by expressed sequence tags and efficient full-length RT cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11402041; DOI=10.1074/jbc.m103236200; RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., RA Watanabe K.; RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification RT of protein components in the 28S small subunit."; RL J. Biol. Chem. 276:33181-33195(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Uterus; 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 [4] RP IDENTIFICATION. RX PubMed=11279123; DOI=10.1074/jbc.m100727200; RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.; RT "The small subunit of the mammalian mitochondrial ribosome: identification RT of the full complement of ribosomal proteins present."; RL J. Biol. Chem. 276:19363-19374(2001). RN [5] {ECO:0007744|PDB:3J9M} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25838379; DOI=10.1126/science.aaa1193; RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.; RT "Ribosome. The structure of the human mitochondrial ribosome."; RL Science 348:95-98(2015). CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt- CC SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural CC role, and 52 different proteins. {ECO:0000269|PubMed:25838379}. CC -!- INTERACTION: CC Q9Y2R5; P28799: GRN; NbExp=3; IntAct=EBI-1046443, EBI-747754; CC Q9Y2R5; O76024: WFS1; NbExp=3; IntAct=EBI-1046443, EBI-720609; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 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; AF077035; AAD27768.1; -; mRNA. DR EMBL; AB049950; BAB41003.1; -; mRNA. DR EMBL; BC047445; AAH47445.2; -; mRNA. DR EMBL; BC054031; AAH54031.1; -; mRNA. DR CCDS; CCDS5520.1; -. DR RefSeq; NP_057053.1; NM_015969.2. DR PDB; 3J9M; EM; 3.50 A; AN=1-130. DR PDB; 6NU2; EM; 3.90 A; AN=5-111. DR PDB; 6NU3; EM; 4.40 A; AN=1-130. DR PDB; 6RW4; EM; 2.97 A; N=1-130. DR PDB; 6RW5; EM; 3.14 A; N=1-130. DR PDB; 6VLZ; EM; 2.97 A; AN=1-130. DR PDB; 6VMI; EM; 2.96 A; AN=1-130. DR PDB; 6ZM5; EM; 2.89 A; AN=1-130. DR PDB; 6ZM6; EM; 2.59 A; AN=1-130. DR PDB; 6ZS9; EM; 4.00 A; AN=1-130. DR PDB; 6ZSA; EM; 4.00 A; AN=1-130. DR PDB; 6ZSB; EM; 4.50 A; AN=1-130. DR PDB; 6ZSC; EM; 3.50 A; AN=1-130. DR PDB; 6ZSD; EM; 3.70 A; AN=1-130. DR PDB; 6ZSE; EM; 5.00 A; AN=1-130. DR PDB; 6ZSG; EM; 4.00 A; AN=1-130. DR PDB; 7A5F; EM; 4.40 A; N6=1-130. DR PDB; 7A5G; EM; 4.33 A; N6=1-130. DR PDB; 7A5I; EM; 3.70 A; N6=1-130. DR PDB; 7A5K; EM; 3.70 A; N6=1-130. DR PDB; 7L08; EM; 3.49 A; AN=1-130. DR PDB; 7OG4; EM; 3.80 A; AN=1-130. DR PDB; 7P2E; EM; 2.40 A; N=1-130. DR PDB; 7PNX; EM; 2.76 A; N=1-130. DR PDB; 7PNY; EM; 3.06 A; N=1-130. DR PDB; 7PNZ; EM; 3.09 A; N=1-130. DR PDB; 7PO0; EM; 2.90 A; N=1-130. DR PDB; 7PO1; EM; 2.92 A; N=1-130. DR PDB; 7PO2; EM; 3.09 A; N=1-130. DR PDB; 7PO3; EM; 2.92 A; N=1-130. DR PDB; 7QI4; EM; 2.21 A; AN=1-130. DR PDB; 7QI5; EM; 2.63 A; AN=1-130. DR PDB; 7QI6; EM; 2.98 A; AN=1-130. DR PDB; 8ANY; EM; 2.85 A; AN=1-130. DR PDB; 8CSP; EM; 2.66 A; N=1-130. DR PDB; 8CSQ; EM; 2.54 A; N=1-130. DR PDB; 8CSR; EM; 2.54 A; N=1-130. DR PDB; 8CSS; EM; 2.36 A; N=1-130. DR PDB; 8CST; EM; 2.85 A; N=1-130. DR PDB; 8CSU; EM; 3.03 A; N=1-130. DR PDB; 8OIR; EM; 3.10 A; AN=1-130. DR PDB; 8OIS; EM; 3.00 A; AN=1-130. DR PDBsum; 3J9M; -. DR PDBsum; 6NU2; -. DR PDBsum; 6NU3; -. DR PDBsum; 6RW4; -. DR PDBsum; 6RW5; -. DR PDBsum; 6VLZ; -. DR PDBsum; 6VMI; -. DR PDBsum; 6ZM5; -. DR PDBsum; 6ZM6; -. DR PDBsum; 6ZS9; -. DR PDBsum; 6ZSA; -. DR PDBsum; 6ZSB; -. DR PDBsum; 6ZSC; -. DR PDBsum; 6ZSD; -. DR PDBsum; 6ZSE; -. DR PDBsum; 6ZSG; -. DR PDBsum; 7A5F; -. DR PDBsum; 7A5G; -. DR PDBsum; 7A5I; -. DR PDBsum; 7A5K; -. DR PDBsum; 7L08; -. DR PDBsum; 7OG4; -. DR PDBsum; 7P2E; -. DR PDBsum; 7PNX; -. DR PDBsum; 7PNY; -. DR PDBsum; 7PNZ; -. DR PDBsum; 7PO0; -. DR PDBsum; 7PO1; -. DR PDBsum; 7PO2; -. DR PDBsum; 7PO3; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8CSP; -. DR PDBsum; 8CSQ; -. DR PDBsum; 8CSR; -. DR PDBsum; 8CSS; -. DR PDBsum; 8CST; -. DR PDBsum; 8CSU; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIS; -. DR AlphaFoldDB; Q9Y2R5; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-10021; -. DR EMDB; EMD-10022; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-13170; -. DR EMDB; EMD-13555; -. DR EMDB; EMD-13556; -. DR EMDB; EMD-13557; -. DR EMDB; EMD-13558; -. DR EMDB; EMD-13559; -. DR EMDB; EMD-13560; -. DR EMDB; EMD-13561; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16898; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-26966; -. DR EMDB; EMD-26967; -. DR EMDB; EMD-26968; -. DR EMDB; EMD-26969; -. DR EMDB; EMD-26970; -. DR EMDB; EMD-26971; -. DR SMR; Q9Y2R5; -. DR BioGRID; 119506; 239. DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit. DR CORUM; Q9Y2R5; -. DR IntAct; Q9Y2R5; 34. DR MINT; Q9Y2R5; -. DR STRING; 9606.ENSP00000285298; -. DR iPTMnet; Q9Y2R5; -. DR PhosphoSitePlus; Q9Y2R5; -. DR SwissPalm; Q9Y2R5; -. DR BioMuta; MRPS17; -. DR DMDM; 13633951; -. DR EPD; Q9Y2R5; -. DR jPOST; Q9Y2R5; -. DR MassIVE; Q9Y2R5; -. DR MaxQB; Q9Y2R5; -. DR PaxDb; 9606-ENSP00000285298; -. DR PeptideAtlas; Q9Y2R5; -. DR ProteomicsDB; 85880; -. DR Pumba; Q9Y2R5; -. DR TopDownProteomics; Q9Y2R5; -. DR Antibodypedia; 66312; 83 antibodies from 20 providers. DR DNASU; 51373; -. DR Ensembl; ENST00000285298.9; ENSP00000285298.4; ENSG00000239789.6. DR GeneID; 51373; -. DR KEGG; hsa:51373; -. DR MANE-Select; ENST00000285298.9; ENSP00000285298.4; NM_015969.3; NP_057053.1. DR UCSC; uc003trd.4; human. DR AGR; HGNC:14047; -. DR CTD; 51373; -. DR DisGeNET; 51373; -. DR GeneCards; MRPS17; -. DR HGNC; HGNC:14047; MRPS17. DR HPA; ENSG00000239789; Low tissue specificity. DR MIM; 611980; gene. DR neXtProt; NX_Q9Y2R5; -. DR OpenTargets; ENSG00000239789; -. DR PharmGKB; PA31002; -. DR VEuPathDB; HostDB:ENSG00000239789; -. DR eggNOG; KOG3447; Eukaryota. DR GeneTree; ENSGT00530000064130; -. DR InParanoid; Q9Y2R5; -. DR OrthoDB; 3672702at2759; -. DR PhylomeDB; Q9Y2R5; -. DR TreeFam; TF326484; -. DR PathwayCommons; Q9Y2R5; -. DR Reactome; R-HSA-5368286; Mitochondrial translation initiation. DR Reactome; R-HSA-5389840; Mitochondrial translation elongation. DR Reactome; R-HSA-5419276; Mitochondrial translation termination. DR SignaLink; Q9Y2R5; -. DR SIGNOR; Q9Y2R5; -. DR BioGRID-ORCS; 51373; 132 hits in 1160 CRISPR screens. DR ChiTaRS; MRPS17; human. DR GeneWiki; MRPS17; -. DR GenomeRNAi; 51373; -. DR Pharos; Q9Y2R5; Tdark. DR PRO; PR:Q9Y2R5; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9Y2R5; Protein. DR Bgee; ENSG00000239789; Expressed in gastrocnemius and 101 other cell types or tissues. DR ExpressionAtlas; Q9Y2R5; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; HDA:UniProtKB. DR GO; GO:0032543; P:mitochondrial translation; HDA:UniProtKB. DR GO; GO:0006412; P:translation; NAS:UniProtKB. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000266; Ribosomal_uS17. DR InterPro; IPR039193; Ribosomal_uS17m_metazoa. DR PANTHER; PTHR24088; 28S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL; 1. DR PANTHER; PTHR24088:SF2; 28S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL; 1. DR Pfam; PF00366; Ribosomal_S17; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR Genevisible; Q9Y2R5; HS. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; Transit peptide. FT TRANSIT 1..20 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 21..130 FT /note="Small ribosomal subunit protein uS17m" FT /id="PRO_0000030623" FT STRAND 12..22 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 25..35 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 42..52 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 73..86 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:8CSS" SQ SEQUENCE 130 AA; 14502 MW; 5346917E78F7C6C3 CRC64; MSVVRSSVHA RWIVGKVIGT KMQKTAKVRV TRLVLDPYLL KYFNKRKTYF AHDALQQCTV GDIVLLRALP VPRAKHVKHE LAEIVFKVGK VIDPVTGKPC AGTTYLESPL SSETTQLSKN LEELNISSAQ //