ID MET17_HUMAN Reviewed; 456 AA. AC Q9H7H0; Q9BSH1; Q9BZH2; Q9BZH3; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Methyltransferase-like protein 17, mitochondrial {ECO:0000305}; DE EC=2.1.1.- {ECO:0000305}; DE AltName: Full=False p73 target gene protein {ECO:0000303|Ref.1}; DE AltName: Full=Methyltransferase 11 domain-containing protein 1 {ECO:0000303|PubMed:24137763}; DE AltName: Full=Protein RSM22 homolog, mitochondrial {ECO:0000303|PubMed:11278769}; DE Flags: Precursor; GN Name=METTL17; Synonyms=METT11D1 {ECO:0000303|PubMed:24137763}; 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 [GENOMIC DNA / MRNA] (ISOFORM 3). RC TISSUE=Mammary cancer; RA Zheng X., Chen X.; RT "Human genomic sequence of a false p73 target gene."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-346. 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; 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 [5] RP IDENTIFICATION. RX PubMed=11278769; DOI=10.1074/jbc.m010864200; RA Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A., RA Jacquier A.; RT "Identification of 12 new yeast mitochondrial ribosomal proteins including RT 6 that have no prokaryotic homologues."; RL J. Biol. Chem. 276:15861-15867(2001). RN [6] RP VARIANT SER-173. RX PubMed=24137763; DOI=10.1007/s10545-009-0968-4; RA Smits P., Rodenburg R.J., Smeitink J.A., van den Heuvel L.P.; RT "Sequence variants in four candidate genes (NIPSNAP1, GBAS, CHCHD1 and RT METT11D1) in patients with combined oxidative phosphorylation system RT deficiencies."; RL J. Inherit. Metab. Dis. 33 Suppl. 3:S13-19(2010). CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent RNA CC methyltransferase required to stabilize the mitochondrial small CC ribosomal subunit (mt-SSU). Required for protein translation in CC mitochondria. {ECO:0000250|UniProtKB:Q3U2U7}. CC -!- SUBUNIT: Interacts with mitochondrial small ribosomal subunit (mt-SSU) CC subunits MRPS15 and MRPS27. {ECO:0000250|UniProtKB:Q3U2U7}. CC -!- INTERACTION: CC Q9H7H0; P54253: ATXN1; NbExp=5; IntAct=EBI-749353, EBI-930964; CC Q9H7H0; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-749353, EBI-739580; CC Q9H7H0; Q8NA61: CBY2; NbExp=4; IntAct=EBI-749353, EBI-741724; CC Q9H7H0; Q8NHQ1: CEP70; NbExp=7; IntAct=EBI-749353, EBI-739624; CC Q9H7H0; Q6A162: KRT40; NbExp=4; IntAct=EBI-749353, EBI-10171697; CC Q9H7H0; Q99750: MDFI; NbExp=5; IntAct=EBI-749353, EBI-724076; CC Q9H7H0; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-749353, EBI-10172526; CC Q9H7H0; Q8ND90: PNMA1; NbExp=7; IntAct=EBI-749353, EBI-302345; CC Q9H7H0; Q15427: SF3B4; NbExp=4; IntAct=EBI-749353, EBI-348469; CC Q9H7H0; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-749353, EBI-1105213; CC Q9H7H0; Q13077: TRAF1; NbExp=7; IntAct=EBI-749353, EBI-359224; CC Q9H7H0; Q15654: TRIP6; NbExp=5; IntAct=EBI-749353, EBI-742327; CC Q9H7H0-2; P54253: ATXN1; NbExp=6; IntAct=EBI-11098807, EBI-930964; CC Q9H7H0-2; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-11098807, EBI-739580; CC Q9H7H0-2; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-11098807, EBI-3866279; CC Q9H7H0-2; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-11098807, EBI-11524851; CC Q9H7H0-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-11098807, EBI-739624; CC Q9H7H0-2; O76011: KRT34; NbExp=3; IntAct=EBI-11098807, EBI-1047093; CC Q9H7H0-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-11098807, EBI-10171697; CC Q9H7H0-2; Q99750: MDFI; NbExp=6; IntAct=EBI-11098807, EBI-724076; CC Q9H7H0-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11098807, EBI-16439278; CC Q9H7H0-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-11098807, EBI-10172526; CC Q9H7H0-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11098807, EBI-11522433; CC Q9H7H0-2; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-11098807, EBI-2949792; CC Q9H7H0-2; Q8ND90: PNMA1; NbExp=6; IntAct=EBI-11098807, EBI-302345; CC Q9H7H0-2; P55072: VCP; NbExp=3; IntAct=EBI-11098807, EBI-355164; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:Q3U2U7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H7H0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H7H0-2; Sequence=VSP_029720; CC Name=3; CC IsoId=Q9H7H0-3; Sequence=VSP_029721; CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Rsm22 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; AF321002; AAK08200.1; -; mRNA. DR EMBL; AF321003; AAK08201.1; -; Genomic_DNA. DR EMBL; AK024512; BAB14919.1; -; mRNA. DR EMBL; CH471078; EAW66433.1; -; Genomic_DNA. DR EMBL; CH471078; EAW66434.1; -; Genomic_DNA. DR EMBL; BC005053; AAH05053.1; -; mRNA. DR CCDS; CCDS41913.1; -. [Q9H7H0-3] DR CCDS; CCDS9562.1; -. [Q9H7H0-1] DR RefSeq; NP_001025162.1; NM_001029991.1. [Q9H7H0-3] DR RefSeq; NP_073571.1; NM_022734.2. [Q9H7H0-1] DR PDB; 8CSP; EM; 2.66 A; 7=1-456. DR PDB; 8CSQ; EM; 2.54 A; 7=1-456. DR PDB; 8CSR; EM; 2.54 A; 7=1-456. DR PDB; 8CSS; EM; 2.36 A; 7=1-456. DR PDB; 8CST; EM; 2.85 A; 7=1-456. DR PDB; 8CSU; EM; 3.03 A; 7=1-456. DR PDBsum; 8CSP; -. DR PDBsum; 8CSQ; -. DR PDBsum; 8CSR; -. DR PDBsum; 8CSS; -. DR PDBsum; 8CST; -. DR PDBsum; 8CSU; -. DR AlphaFoldDB; Q9H7H0; -. 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; Q9H7H0; -. DR BioGRID; 122261; 433. DR IntAct; Q9H7H0; 45. DR MINT; Q9H7H0; -. DR STRING; 9606.ENSP00000372445; -. DR iPTMnet; Q9H7H0; -. DR PhosphoSitePlus; Q9H7H0; -. DR BioMuta; METTL17; -. DR DMDM; 74718673; -. DR EPD; Q9H7H0; -. DR jPOST; Q9H7H0; -. DR MassIVE; Q9H7H0; -. DR MaxQB; Q9H7H0; -. DR PaxDb; 9606-ENSP00000372445; -. DR PeptideAtlas; Q9H7H0; -. DR ProteomicsDB; 81121; -. [Q9H7H0-1] DR ProteomicsDB; 81122; -. [Q9H7H0-2] DR ProteomicsDB; 81123; -. [Q9H7H0-3] DR Pumba; Q9H7H0; -. DR Antibodypedia; 7177; 96 antibodies from 16 providers. DR DNASU; 64745; -. DR Ensembl; ENST00000339374.11; ENSP00000343041.6; ENSG00000165792.18. [Q9H7H0-1] DR Ensembl; ENST00000382985.8; ENSP00000372445.4; ENSG00000165792.18. [Q9H7H0-3] DR Ensembl; ENST00000556670.6; ENSP00000450794.2; ENSG00000165792.18. [Q9H7H0-2] DR GeneID; 64745; -. DR KEGG; hsa:64745; -. DR MANE-Select; ENST00000339374.11; ENSP00000343041.6; NM_022734.3; NP_073571.1. DR UCSC; uc001vym.5; human. [Q9H7H0-1] DR AGR; HGNC:19280; -. DR CTD; 64745; -. DR DisGeNET; 64745; -. DR GeneCards; METTL17; -. DR HGNC; HGNC:19280; METTL17. DR HPA; ENSG00000165792; Low tissue specificity. DR MIM; 616091; gene. DR neXtProt; NX_Q9H7H0; -. DR OpenTargets; ENSG00000165792; -. DR PharmGKB; PA145008140; -. DR VEuPathDB; HostDB:ENSG00000165792; -. DR eggNOG; KOG2539; Eukaryota. DR GeneTree; ENSGT00390000006103; -. DR HOGENOM; CLU_033285_2_0_1; -. DR InParanoid; Q9H7H0; -. DR OMA; PRKHPGI; -. DR OrthoDB; 146346at2759; -. DR PhylomeDB; Q9H7H0; -. DR TreeFam; TF313708; -. DR PathwayCommons; Q9H7H0; -. DR SignaLink; Q9H7H0; -. DR BioGRID-ORCS; 64745; 366 hits in 1180 CRISPR screens. DR ChiTaRS; METTL17; human. DR GenomeRNAi; 64745; -. DR Pharos; Q9H7H0; Tbio. DR PRO; PR:Q9H7H0; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9H7H0; Protein. DR Bgee; ENSG00000165792; Expressed in right adrenal gland cortex and 186 other cell types or tissues. DR ExpressionAtlas; Q9H7H0; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB. DR GO; GO:0006412; P:translation; IEA:InterPro. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR015324; Ribosomal_Rsm22-like. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR13184; 37S RIBOSOMAL PROTEIN S22; 1. DR PANTHER; PTHR13184:SF5; METHYLTRANSFERASE LIKE; 1. DR Pfam; PF09243; Rsm22; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR Genevisible; Q9H7H0; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Methyltransferase; Mitochondrion; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide. FT TRANSIT 1..19 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 20..456 FT /note="Methyltransferase-like protein 17, mitochondrial" FT /id="PRO_0000312163" FT VAR_SEQ 422..430 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029720" FT VAR_SEQ 423..456 FT /note="DLYRCARVSSWGDLLPVLTPSAFPPSTAQDPSES -> YGGCDQNQWDVAGS FT CSPRQHLFPQGFVSLCPCQLLGRSFTCAYSVCVSSIYGSGSL (in isoform 3)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_029721" FT VARIANT 173 FT /note="A -> S (in dbSNP:rs72661115)" FT /evidence="ECO:0000269|PubMed:24137763" FT /id="VAR_072388" FT VARIANT 289 FT /note="G -> A (in dbSNP:rs2297717)" FT /id="VAR_037422" FT VARIANT 346 FT /note="A -> P (in dbSNP:rs2771350)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_037423" FT CONFLICT 53 FT /note="P -> S (in Ref. 1; AAK08200)" FT /evidence="ECO:0000305" FT CONFLICT 318 FT /note="E -> G (in Ref. 1; AAK08200)" FT /evidence="ECO:0000305" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 43..46 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:8CSP" FT HELIX 65..74 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 81..96 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 103..116 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:8CSU" FT HELIX 133..139 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:8CSU" FT HELIX 152..180 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 198..207 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 221..231 FT /evidence="ECO:0007829|PDB:8CSS" FT TURN 232..234 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:8CSR" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:8CSR" FT STRAND 259..266 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 274..286 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 288..299 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 300..314 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 340..345 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 349..354 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 365..377 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 398..404 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 410..416 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 417..420 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 422..430 FT /evidence="ECO:0007829|PDB:8CSS" SQ SEQUENCE 456 AA; 50734 MW; A23E9EF33C4BD3A1 CRC64; MAAALKCLLT LGRWCPGLGV APQARALAAL VPGVTQVDNK SGFLQKRPHR QHPGILKLPH VRLPQALANG AQLLLLGSAG PTMENQVQTL TSYLWSRHLP VEPEELQRRA RHLEKKFLEN PDLSQTEEKL RGAVLHALRK TTYHWQELSY TEGLSLVYMA ARLDGGFAAV SRAFHEIRAR NPAFQPQTLM DFGSGTGSVT WAAHSIWGQS LREYMCVDRS AAMLVLAEKL LKGGSESGEP YIPGVFFRQF LPVSPKVQFD VVVSAFSLSE LPSKADRTEV VQTLWRKTGH FLVLVENGTK AGHSLLMDAR DLVLKGKEKS PLDPRPGFVF APCPHELPCP QLTNLACSFS QAYHPIPFSW NKKPKEEKFS MVILARGSPE EAHRWPRITQ PVLKRPRHVH CHLCCPDGHM QHAVLTARRH GRDLYRCARV SSWGDLLPVL TPSAFPPSTA QDPSES //