MET17_HUMAN
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 03-AUG-2022, entry version 140.
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}.
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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 AlphaFoldDB; Q9H7H0; -.
DR SMR; Q9H7H0; -.
DR BioGRID; 122261; 428.
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; Q9H7H0; -.
DR PeptideAtlas; Q9H7H0; -.
DR PRIDE; Q9H7H0; -.
DR ProteomicsDB; 81121; -. [Q9H7H0-1]
DR ProteomicsDB; 81122; -. [Q9H7H0-2]
DR ProteomicsDB; 81123; -. [Q9H7H0-3]
DR Antibodypedia; 7177; 72 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 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; SKHAICR; -.
DR OrthoDB; 1439584at2759; -.
DR PhylomeDB; Q9H7H0; -.
DR TreeFam; TF313708; -.
DR PathwayCommons; Q9H7H0; -.
DR SignaLink; Q9H7H0; -.
DR BioGRID-ORCS; 64745; 343 hits in 1091 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 184 other tissues.
DR ExpressionAtlas; Q9H7H0; baseline and differential.
DR Genevisible; Q9H7H0; HS.
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; -; 1.
DR InterPro; IPR015324; Ribosomal_Rsm22-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF09243; Rsm22; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome;
KW 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"
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
