ID   RM17_HUMAN              Reviewed;         175 AA.
AC   Q9NRX2; D3DQU3; Q6IAH8; Q96Q53; Q9C066;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Large ribosomal subunit protein bL17m {ECO:0000303|PubMed:25278503};
DE   AltName: Full=39S ribosomal protein L17, mitochondrial;
DE            Short=L17mt;
DE            Short=MRP-L17;
DE   AltName: Full=LYST-interacting protein 2;
DE   Flags: Precursor;
GN   Name=MRPL17; Synonyms=LIP2;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Adrenal gland;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11984006; DOI=10.1007/bf03402003;
RA   Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y.,
RA   Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S.,
RA   Kingsmore S.F.;
RT   "The Chediak-Higashi protein interacts with SNARE complex and signal
RT   transduction proteins.";
RL   Mol. Med. 8:56-64(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adipose tissue;
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 MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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=Mammary 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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-175.
RX   PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA   Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA   Watanabe K., Tanaka T.;
RT   "The human mitochondrial ribosomal protein genes: mapping of 54 genes to
RT   the chromosomes and implications for human disorders.";
RL   Genomics 77:65-70(2001).
RN   [8]
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   [9]
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   [10]
RP   STRUCTURE BY NMR OF 28-136.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the mitochondrial ribosomal protein L17 isolog.";
RL   Submitted (NOV-2005) to the PDB data bank.
RN   [11] {ECO:0007744|PDB:3J7Y}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=25278503; DOI=10.1126/science.1258026;
RA   Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA   Scheres S.H., Ramakrishnan V.;
RT   "Structure of the large ribosomal subunit from human mitochondria.";
RL   Science 346:718-722(2014).
RN   [12] {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).
RN   [13] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=28892042; DOI=10.1038/nsmb.3464;
RA   Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA   Amunts A., Ramakrishnan V.;
RT   "Structures of the human mitochondrial ribosome in native states of
RT   assembly.";
RL   Nat. Struct. Mol. Biol. 24:866-869(2017).
CC   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature
CC       mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC       large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC       (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC       a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC       (mt-tRNA(Val)), which plays an integral structural role, and 52
CC       different proteins. {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- INTERACTION:
CC       Q9NRX2; P52597: HNRNPF; NbExp=3; IntAct=EBI-7825154, EBI-352986;
CC       Q9NRX2; Q8WUN7: UBTD2; NbExp=3; IntAct=EBI-7825154, EBI-12867288;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- TISSUE SPECIFICITY: Detected in adrenal gland, mammary gland and
CC       adipose tissue. {ECO:0000269|PubMed:10931946}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG49441.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF164797; AAF80761.1; -; mRNA.
DR   EMBL; AF141338; AAG49441.1; ALT_FRAME; mRNA.
DR   EMBL; AK026857; BAB15575.1; -; mRNA.
DR   EMBL; CR457177; CAG33458.1; -; mRNA.
DR   EMBL; CH471064; EAW68681.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68682.1; -; Genomic_DNA.
DR   EMBL; BC012306; AAH12306.1; -; mRNA.
DR   EMBL; AB051620; BAB54948.1; -; Genomic_DNA.
DR   CCDS; CCDS31412.1; -.
DR   RefSeq; NP_071344.1; NM_022061.3.
DR   PDB; 2CQM; NMR; -; A=28-136.
DR   PDB; 3J7Y; EM; 3.40 A; O=1-175.
DR   PDB; 3J9M; EM; 3.50 A; O=1-175.
DR   PDB; 5OOL; EM; 3.06 A; O=1-175.
DR   PDB; 5OOM; EM; 3.03 A; O=1-175.
DR   PDB; 6I9R; EM; 3.90 A; O=1-175.
DR   PDB; 6NU2; EM; 3.90 A; O=9-160.
DR   PDB; 6NU3; EM; 4.40 A; O=1-175.
DR   PDB; 6VLZ; EM; 2.97 A; O=1-175.
DR   PDB; 6VMI; EM; 2.96 A; O=1-175.
DR   PDB; 6ZM5; EM; 2.89 A; O=1-175.
DR   PDB; 6ZM6; EM; 2.59 A; O=1-175.
DR   PDB; 6ZS9; EM; 4.00 A; XO=1-175.
DR   PDB; 6ZSA; EM; 4.00 A; XO=1-175.
DR   PDB; 6ZSB; EM; 4.50 A; XO=1-175.
DR   PDB; 6ZSC; EM; 3.50 A; XO=1-175.
DR   PDB; 6ZSD; EM; 3.70 A; XO=1-175.
DR   PDB; 6ZSE; EM; 5.00 A; XO=1-175.
DR   PDB; 6ZSG; EM; 4.00 A; XO=1-175.
DR   PDB; 7A5F; EM; 4.40 A; O3=1-175.
DR   PDB; 7A5G; EM; 4.33 A; O3=1-175.
DR   PDB; 7A5H; EM; 3.30 A; O=1-175.
DR   PDB; 7A5I; EM; 3.70 A; O3=1-175.
DR   PDB; 7A5J; EM; 3.10 A; O=1-175.
DR   PDB; 7A5K; EM; 3.70 A; O3=1-175.
DR   PDB; 7L08; EM; 3.49 A; O=1-175.
DR   PDB; 7L20; EM; 3.15 A; O=1-175.
DR   PDB; 7O9K; EM; 3.10 A; O=1-175.
DR   PDB; 7O9M; EM; 2.50 A; O=1-175.
DR   PDB; 7ODR; EM; 2.90 A; O=1-175.
DR   PDB; 7ODS; EM; 3.10 A; O=1-175.
DR   PDB; 7ODT; EM; 3.10 A; O=1-175.
DR   PDB; 7OF0; EM; 2.20 A; O=1-175.
DR   PDB; 7OF2; EM; 2.70 A; O=1-175.
DR   PDB; 7OF3; EM; 2.70 A; O=1-175.
DR   PDB; 7OF4; EM; 2.70 A; O=1-175.
DR   PDB; 7OF5; EM; 2.90 A; O=1-175.
DR   PDB; 7OF6; EM; 2.60 A; O=1-175.
DR   PDB; 7OF7; EM; 2.50 A; O=1-175.
DR   PDB; 7OG4; EM; 3.80 A; XO=1-175.
DR   PDB; 7OI6; EM; 5.70 A; O=1-175.
DR   PDB; 7OI7; EM; 3.50 A; O=1-175.
DR   PDB; 7OI8; EM; 3.50 A; O=1-175.
DR   PDB; 7OI9; EM; 3.30 A; O=1-175.
DR   PDB; 7OIA; EM; 3.20 A; O=1-175.
DR   PDB; 7OIB; EM; 3.30 A; O=1-175.
DR   PDB; 7OIC; EM; 3.10 A; O=1-175.
DR   PDB; 7OID; EM; 3.70 A; O=1-175.
DR   PDB; 7OIE; EM; 3.50 A; O=1-175.
DR   PDB; 7PD3; EM; 3.40 A; O=1-175.
DR   PDB; 7PO4; EM; 2.56 A; O=1-175.
DR   PDB; 7QH6; EM; 3.08 A; O=1-175.
DR   PDB; 7QH7; EM; 2.89 A; O=9-160.
DR   PDB; 7QI4; EM; 2.21 A; O=1-175.
DR   PDB; 7QI5; EM; 2.63 A; O=1-175.
DR   PDB; 7QI6; EM; 2.98 A; O=1-175.
DR   PDB; 8ANY; EM; 2.85 A; O=1-175.
DR   PDB; 8OIR; EM; 3.10 A; BV=1-175.
DR   PDB; 8OIT; EM; 2.90 A; BV=1-175.
DR   PDBsum; 2CQM; -.
DR   PDBsum; 3J7Y; -.
DR   PDBsum; 3J9M; -.
DR   PDBsum; 5OOL; -.
DR   PDBsum; 5OOM; -.
DR   PDBsum; 6I9R; -.
DR   PDBsum; 6NU2; -.
DR   PDBsum; 6NU3; -.
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; 7A5H; -.
DR   PDBsum; 7A5I; -.
DR   PDBsum; 7A5J; -.
DR   PDBsum; 7A5K; -.
DR   PDBsum; 7L08; -.
DR   PDBsum; 7L20; -.
DR   PDBsum; 7O9K; -.
DR   PDBsum; 7O9M; -.
DR   PDBsum; 7ODR; -.
DR   PDBsum; 7ODS; -.
DR   PDBsum; 7ODT; -.
DR   PDBsum; 7OF0; -.
DR   PDBsum; 7OF2; -.
DR   PDBsum; 7OF3; -.
DR   PDBsum; 7OF4; -.
DR   PDBsum; 7OF5; -.
DR   PDBsum; 7OF6; -.
DR   PDBsum; 7OF7; -.
DR   PDBsum; 7OG4; -.
DR   PDBsum; 7OI6; -.
DR   PDBsum; 7OI7; -.
DR   PDBsum; 7OI8; -.
DR   PDBsum; 7OI9; -.
DR   PDBsum; 7OIA; -.
DR   PDBsum; 7OIB; -.
DR   PDBsum; 7OIC; -.
DR   PDBsum; 7OID; -.
DR   PDBsum; 7OIE; -.
DR   PDBsum; 7PD3; -.
DR   PDBsum; 7PO4; -.
DR   PDBsum; 7QH6; -.
DR   PDBsum; 7QH7; -.
DR   PDBsum; 7QI4; -.
DR   PDBsum; 7QI5; -.
DR   PDBsum; 7QI6; -.
DR   PDBsum; 8ANY; -.
DR   PDBsum; 8OIR; -.
DR   PDBsum; 8OIT; -.
DR   AlphaFoldDB; Q9NRX2; -.
DR   EMDB; EMD-0514; -.
DR   EMDB; EMD-0515; -.
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-11643; -.
DR   EMDB; EMD-11644; -.
DR   EMDB; EMD-11645; -.
DR   EMDB; EMD-11646; -.
DR   EMDB; EMD-12763; -.
DR   EMDB; EMD-12764; -.
DR   EMDB; EMD-12845; -.
DR   EMDB; EMD-12846; -.
DR   EMDB; EMD-12847; -.
DR   EMDB; EMD-12865; -.
DR   EMDB; EMD-12867; -.
DR   EMDB; EMD-12868; -.
DR   EMDB; EMD-12869; -.
DR   EMDB; EMD-12870; -.
DR   EMDB; EMD-12871; -.
DR   EMDB; EMD-12872; -.
DR   EMDB; EMD-12877; -.
DR   EMDB; EMD-12919; -.
DR   EMDB; EMD-12920; -.
DR   EMDB; EMD-12921; -.
DR   EMDB; EMD-12922; -.
DR   EMDB; EMD-12923; -.
DR   EMDB; EMD-12924; -.
DR   EMDB; EMD-12925; -.
DR   EMDB; EMD-12926; -.
DR   EMDB; EMD-12927; -.
DR   EMDB; EMD-13329; -.
DR   EMDB; EMD-13562; -.
DR   EMDB; EMD-13965; -.
DR   EMDB; EMD-13967; -.
DR   EMDB; EMD-13980; -.
DR   EMDB; EMD-13981; -.
DR   EMDB; EMD-13982; -.
DR   EMDB; EMD-15544; -.
DR   EMDB; EMD-16897; -.
DR   EMDB; EMD-16899; -.
DR   EMDB; EMD-21233; -.
DR   EMDB; EMD-21242; -.
DR   EMDB; EMD-23096; -.
DR   EMDB; EMD-23121; -.
DR   EMDB; EMD-3842; -.
DR   EMDB; EMD-3843; -.
DR   EMDB; EMD-4434; -.
DR   SMR; Q9NRX2; -.
DR   BioGRID; 121968; 169.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q9NRX2; -.
DR   IntAct; Q9NRX2; 43.
DR   MINT; Q9NRX2; -.
DR   STRING; 9606.ENSP00000288937; -.
DR   GlyGen; Q9NRX2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NRX2; -.
DR   PhosphoSitePlus; Q9NRX2; -.
DR   SwissPalm; Q9NRX2; -.
DR   BioMuta; MRPL17; -.
DR   DMDM; 74752931; -.
DR   EPD; Q9NRX2; -.
DR   jPOST; Q9NRX2; -.
DR   MassIVE; Q9NRX2; -.
DR   MaxQB; Q9NRX2; -.
DR   PaxDb; 9606-ENSP00000288937; -.
DR   PeptideAtlas; Q9NRX2; -.
DR   ProteomicsDB; 82433; -.
DR   Pumba; Q9NRX2; -.
DR   TopDownProteomics; Q9NRX2; -.
DR   Antibodypedia; 64019; 71 antibodies from 19 providers.
DR   DNASU; 63875; -.
DR   Ensembl; ENST00000288937.7; ENSP00000288937.6; ENSG00000158042.9.
DR   GeneID; 63875; -.
DR   KEGG; hsa:63875; -.
DR   MANE-Select; ENST00000288937.7; ENSP00000288937.6; NM_022061.4; NP_071344.1.
DR   UCSC; uc001men.3; human.
DR   AGR; HGNC:14053; -.
DR   CTD; 63875; -.
DR   DisGeNET; 63875; -.
DR   GeneCards; MRPL17; -.
DR   HGNC; HGNC:14053; MRPL17.
DR   HPA; ENSG00000158042; Low tissue specificity.
DR   MIM; 611830; gene.
DR   neXtProt; NX_Q9NRX2; -.
DR   OpenTargets; ENSG00000158042; -.
DR   PharmGKB; PA30946; -.
DR   VEuPathDB; HostDB:ENSG00000158042; -.
DR   eggNOG; KOG3280; Eukaryota.
DR   GeneTree; ENSGT00390000010698; -.
DR   HOGENOM; CLU_074407_3_2_1; -.
DR   InParanoid; Q9NRX2; -.
DR   OMA; YKGNPYP; -.
DR   OrthoDB; 2907681at2759; -.
DR   PhylomeDB; Q9NRX2; -.
DR   TreeFam; TF105844; -.
DR   PathwayCommons; Q9NRX2; -.
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; Q9NRX2; -.
DR   SIGNOR; Q9NRX2; -.
DR   BioGRID-ORCS; 63875; 470 hits in 1176 CRISPR screens.
DR   ChiTaRS; MRPL17; human.
DR   EvolutionaryTrace; Q9NRX2; -.
DR   GeneWiki; MRPL17; -.
DR   GenomeRNAi; 63875; -.
DR   Pharos; Q9NRX2; Tdark.
DR   PRO; PR:Q9NRX2; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9NRX2; Protein.
DR   Bgee; ENSG00000158042; Expressed in stromal cell of endometrium and 178 other cell types or tissues.
DR   ExpressionAtlas; Q9NRX2; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR   Gene3D; 3.90.1030.10; Ribosomal protein L17; 1.
DR   InterPro; IPR000456; Ribosomal_bL17.
DR   InterPro; IPR036373; Ribosomal_bL17_sf.
DR   NCBIfam; TIGR00059; L17; 1.
DR   PANTHER; PTHR14413:SF16; 39S RIBOSOMAL PROTEIN L17, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR14413; RIBOSOMAL PROTEIN L17; 1.
DR   Pfam; PF01196; Ribosomal_L17; 1.
DR   SUPFAM; SSF64263; Prokaryotic ribosomal protein L17; 1.
DR   Genevisible; Q9NRX2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q3T0L3"
FT   CHAIN           9..175
FT                   /note="Large ribosomal subunit protein bL17m"
FT                   /id="PRO_0000237331"
FT   REGION          155..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        105
FT                   /note="T -> A (in Ref. 2; CAG33458)"
FT                   /evidence="ECO:0000305"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:3J7Y"
FT   HELIX           22..39
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          40..45
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           46..65
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           70..79
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:5OOL"
FT   HELIX           85..91
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           93..97
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           144..159
FT                   /evidence="ECO:0007829|PDB:7OF0"
SQ   SEQUENCE   175 AA;  20050 MW;  48C73425104200EA CRC64;
     MRLSVAAAIS HGRVFRRMGL GPESRIHLLR NLLTGLVRHE RIEAPWARVD EMRGYAEKLI
     DYGKLGDTNE RAMRMADFWL TEKDLIPKLF QVLAPRYKDQ TGGYTRMLQI PNRSLDRAKM
     AVIEYKGNCL PPLPLPRRDS HLTLLNQLLQ GLRQDLRQSQ EASNHSSHTA QTPGI
//