ID TRM7_HUMAN Reviewed; 329 AA. AC Q9UET6; B2RCJ0; O75670; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000305}; DE EC=2.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03162, ECO:0000269|PubMed:32558197, ECO:0000269|PubMed:33771871, ECO:0000305|PubMed:36720500}; DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000255|HAMAP-Rule:MF_03162}; DE AltName: Full=Protein ftsJ homolog 1 {ECO:0000255|HAMAP-Rule:MF_03162}; GN Name=FTSJ1 {ECO:0000255|HAMAP-Rule:MF_03162}; ORFNames=JM23; 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] (ISOFORM 2). RA Pengue G., Lutfiyya L.L., Mazzarella R.; RT "A human and yeast gene involved in cell division."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., RA Meindl A.; RT "Transcription map in Xp11.23."; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). 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] (ISOFORM 1). RC TISSUE=Lymph; 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 INVOLVEMENT IN XLID9, AND TISSUE SPECIFICITY. RX PubMed=15162322; DOI=10.1086/422507; RA Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V., RA Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P., RA Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H.; RT "Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine- RT binding protein cause nonsyndromic X-linked mental retardation."; RL Am. J. Hum. Genet. 75:305-309(2004). RN [8] RP INVOLVEMENT IN XLID9, AND TISSUE SPECIFICITY. RX PubMed=15342698; DOI=10.1136/jmg.2004.019000; RA Ramser J., Winnepenninckx B., Lenski C., Errijgers V., Platzer M., RA Schwartz C.E., Meindl A., Kooy R.F.; RT "A splice site mutation in the methyltransferase gene FTSJ1 in Xp11.23 is RT associated with non-syndromic mental retardation in a large Belgian family RT (MRX9)."; RL J. Med. Genet. 41:679-683(2004). RN [9] RP INVOLVEMENT IN XLID9. RX PubMed=18081026; DOI=10.1002/ajmg.b.30638; RG Japanese Mental Retardation Consortium; RA Takano K., Nakagawa E., Inoue K., Kamada F., Kure S., Goto Y.; RT "A loss-of-function mutation in the FTSJ1 gene causes nonsyndromic X-linked RT mental retardation in a Japanese family."; RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B:479-484(2008). RN [10] RP INVOLVEMENT IN XLID9. RX PubMed=18401546; DOI=10.1007/s10038-008-0287-x; RA Dai L., Xing L., Gong P., Zhang K., Gao X., Zheng Z., Zhou J., Guo Y., RA Guo S., Zhang F.; RT "Positive association of the FTSJ1 gene polymorphisms with nonsyndromic X- RT linked mental retardation in young Chinese male subjects."; RL J. Hum. Genet. 53:592-597(2008). RN [11] RP INVOLVEMENT IN XLID9. RX PubMed=19012053; DOI=10.1080/01677060802337299; RA Gong P., Li J., Dai L., Zhang K., Zheng Z., Gao X., Zhang F.; RT "Genetic variations in FTSJ1 influence cognitive ability in young males in RT the Chinese Han population."; RL J. Neurogenet. 22:277-287(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, 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 FUNCTION. RX PubMed=25404562; DOI=10.1261/rna.047639.114; RA Guy M.P., Phizicky E.M.; RT "Conservation of an intricate circuit for crucial modifications of the RT tRNAPhe anticodon loop in eukaryotes."; RL RNA 21:61-74(2015). RN [18] RP FUNCTION. RX PubMed=32393790; DOI=10.1038/s41419-020-2525-x; RA He Q., Yang L., Gao K., Ding P., Chen Q., Xiong J., Yang W., Song Y., RA Wang L., Wang Y., Ling L., Wu W., Yan J., Zou P., Chen Y., Zhai R.; RT "FTSJ1 regulates tRNA 2'-O-methyladenosine modification and suppresses the RT malignancy of NSCLC via inhibiting DRAM1 expression."; RL Cell Death Dis. 11:348-348(2020). RN [19] RP ERRATUM OF PUBMED:32393790. RX PubMed=32488007; DOI=10.1038/s41419-020-2623-9; RA He Q., Yang L., Gao K., Ding P., Chen Q., Xiong J., Yang W., Song Y., RA Wang L., Wang Y., Ling L., Wu W., Yan J., Zou P., Chen Y., Zhai R.; RL Cell Death Dis. 11:418-418(2020). RN [20] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDR6, AND SUBCELLULAR RP LOCATION. RX PubMed=32558197; DOI=10.15252/embr.202050095; RA Li J., Wang Y.N., Xu B.S., Liu Y.P., Zhou M., Long T., Li H., Dong H., RA Nie Y., Chen P.R., Wang E.D., Liu R.J.; RT "Intellectual disability-associated gene ftsj1 is responsible for 2'-O- RT methylation of specific tRNAs."; RL EMBO Rep. 21:e50095-e50095(2020). RN [21] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=32198346; DOI=10.1038/s41467-020-15140-z; RA Trzaska C., Amand S., Bailly C., Leroy C., Marchand V., RA Duvernois-Berthet E., Saliou J.M., Benhabiles H., Werkmeister E., RA Chassat T., Guilbert R., Hannebique D., Mouray A., Copin M.C., Moreau P.A., RA Adriaenssens E., Kulozik A., Westhof E., Tulasne D., Motorin Y., RA Rebuffat S., Lejeune F.; RT "2,6-Diaminopurine as a highly potent corrector of UGA nonsense RT mutations."; RL Nat. Commun. 11:1509-1509(2020). RN [22] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDR6, AND INVOLVEMENT IN RP XLID9. RX PubMed=33771871; DOI=10.1126/sciadv.abf3072; RA Nagayoshi Y., Chujo T., Hirata S., Nakatsuka H., Chen C.W., Takakura M., RA Miyauchi K., Ikeuchi Y., Carlyle B.C., Kitchen R.R., Suzuki T., RA Katsuoka F., Yamamoto M., Goto Y., Tanaka M., Natsume K., Nairn A.C., RA Suzuki T., Tomizawa K., Wei F.Y.; RT "Loss of Ftsj1 perturbs codon-specific translation efficiency in the brain RT and is associated with X-linked intellectual disability."; RL Sci. Adv. 7:eabf3072-eabf3072(2021). RN [23] RP CHARACTERIZATION OF VARIANT XLID9 PRO-26, FUNCTION, AND INVOLVEMENT IN RP XLID9. RX PubMed=26310293; DOI=10.1002/humu.22897; RA Guy M.P., Shaw M., Weiner C.L., Hobson L., Stark Z., Rose K., RA Kalscheuer V.M., Gecz J., Phizicky E.M.; RT "Defects in tRNA Anticodon Loop 2'-O-Methylation Are Implicated in RT Nonsyndromic X-Linked Intellectual Disability due to Mutations in FTSJ1."; RL Hum. Mutat. 36:1176-1187(2015). RN [24] RP CHARACTERIZATION OF VARIANT XLID9 PRO-26, FUNCTION, CATALYTIC ACTIVITY, AND RP INVOLVEMENT IN XLID9. RX PubMed=36720500; DOI=10.26508/lsa.202201877; RA Brazane M., Dimitrova D.G., Pigeon J., Paolantoni C., Ye T., Marchand V., RA Da Silva B., Schaefer E., Angelova M.T., Stark Z., Delatycki M., RA Dudding-Byth T., Gecz J., Placais P.Y., Teysset L., Preat T., Piton A., RA Hassan B.A., Roignant J.Y., Motorin Y., Carre C.; RT "The ribose methylation enzyme FTSJ1 has a conserved role in neuron RT morphology and learning performance."; RL Life. Sci Alliance 6:e202201877-e202201877(2023). CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and CC 34 of the tRNA anticodon loop of substrate tRNAs (PubMed:25404562, CC PubMed:32558197, PubMed:32198346, PubMed:33771871, PubMed:26310293, CC PubMed:36720500). Requisite for faithful cytoplasmic translation CC (PubMed:32393790). Requires THADA for methylation of the nucleotide at CC position 32 of the anticodon loop of substrate tRNAs (PubMed:26310293, CC PubMed:25404562). Requires WDR6 for methylation of the nucleotide at CC position 34 of the anticodon loop of substrate tRNAs (PubMed:32558197, CC PubMed:33771871). Promotes translation efficiency of the UUU codon CC (PubMed:32558197). Plays a role in neurogenesis (PubMed:36720500). CC Required for expression of genes involved in neurogenesis, CC mitochondrial translation and energy generation, and lipid biosynthesis CC (PubMed:36720500, PubMed:33771871). Requisite for RNA-mediated gene CC silencing (PubMed:36720500). May modify position 32 in tRNA(Arg(ACG)), CC tRNA(Arg(CCG)), tRNA(Arg(UCG)), tRNA(Cys(GCA)), tRNA(Cys(ACA)), CC tRNA(Gln(CUG)), tRNA(Gln(UUG)), tRNA(Gly(CCC)), CC tRNA(Leu(CAG))/tRNA(Leu(CAA)), tRNA(Leu(A/IAG)), tRNA(Leu(UAG)), CC tRNA(Phe(GAA)), tRNA(Pro(AGG))/tRNA(Pro(CGG))/tRNA(Pro(UGG)) and CC tRNA(Trp(CCA)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), CC tRNA(Sec(UCA)), and tRNA(Trp(CCA)) (PubMed:32558197, PubMed:32198346, CC PubMed:33771871, PubMed:26310293, PubMed:36720500). CC {ECO:0000269|PubMed:25404562, ECO:0000269|PubMed:26310293, CC ECO:0000269|PubMed:32198346, ECO:0000269|PubMed:32393790, CC ECO:0000269|PubMed:32558197, ECO:0000269|PubMed:33771871, CC ECO:0000269|PubMed:36720500}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine CC = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) + CC 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA- CC COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; CC EC=2.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_03162, CC ECO:0000269|PubMed:32558197, ECO:0000269|PubMed:33771871, CC ECO:0000305|PubMed:36720500}; CC -!- ACTIVITY REGULATION: Inhibited by 2,6-diaminopurine (DAP); inhibition CC promotes UGA stop-codon readthrough during translation by CC misincorporation of tRNA(Trp) in the nascent polypeptide. CC {ECO:0000269|PubMed:32198346}. CC -!- SUBUNIT: Interacts with WDR6; the interaction is direct, and required CC for 2'-O-methylation of position 34 in substrate tRNAs. CC {ECO:0000269|PubMed:32558197, ECO:0000269|PubMed:33771871}. CC -!- INTERACTION: CC Q9UET6; Q9Y5P4-2: CERT1; NbExp=3; IntAct=EBI-1055987, EBI-11156432; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32558197}. Nucleus CC {ECO:0000269|PubMed:32558197}. Note=Predominantly cytoplasmic. CC {ECO:0000269|PubMed:32558197}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UET6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UET6-2; Sequence=VSP_041419; CC -!- TISSUE SPECIFICITY: Found in fetal brain, lung, liver and kidney CC (PubMed:15162322). Widely expressed in adult tissue; with high CC expression in heart and liver, lower expression in skeletal muscle, CC kidney, and pancreas and also lowly expressed in brain and lung CC (PubMed:15342698). In the adult brain, expressed in amygdala, caudate CC nucleus, corpus callosum, hippocampus and thalamus (PubMed:15162322). CC {ECO:0000269|PubMed:15162322, ECO:0000269|PubMed:15342698}. CC -!- DISEASE: Intellectual developmental disorder, X-linked 9 (XLID9) CC [MIM:309549]: A disorder characterized by significantly below average CC general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. CC Intellectual deficiency is the only primary symptom of non-syndromic X- CC linked forms, while syndromic forms present with associated physical, CC neurological and/or psychiatric manifestations. CC {ECO:0000269|PubMed:15162322, ECO:0000269|PubMed:15342698, CC ECO:0000269|PubMed:18081026, ECO:0000269|PubMed:18401546, CC ECO:0000269|PubMed:19012053, ECO:0000269|PubMed:26310293, CC ECO:0000269|PubMed:33771871, ECO:0000269|PubMed:36720500}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RNA methyltransferase RlmE family. TRM7 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03162}. 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; AF063015; AAC33734.1; -; mRNA. DR EMBL; AJ005892; CAA06749.1; -; mRNA. DR EMBL; AK315138; BAG37587.1; -; mRNA. DR EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471224; EAW50782.1; -; Genomic_DNA. DR EMBL; BC023584; AAH23584.1; -; mRNA. DR CCDS; CCDS14294.1; -. [Q9UET6-1] DR CCDS; CCDS14295.1; -. [Q9UET6-2] DR RefSeq; NP_001269086.1; NM_001282157.1. DR RefSeq; NP_036412.1; NM_012280.3. [Q9UET6-1] DR RefSeq; NP_803188.1; NM_177439.2. [Q9UET6-2] DR RefSeq; XP_005272652.1; XM_005272595.1. [Q9UET6-2] DR AlphaFoldDB; Q9UET6; -. DR SMR; Q9UET6; -. DR BioGRID; 117291; 81. DR IntAct; Q9UET6; 42. DR MINT; Q9UET6; -. DR STRING; 9606.ENSP00000326948; -. DR GlyGen; Q9UET6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UET6; -. DR PhosphoSitePlus; Q9UET6; -. DR BioMuta; FTSJ1; -. DR DMDM; 12643879; -. DR EPD; Q9UET6; -. DR jPOST; Q9UET6; -. DR MassIVE; Q9UET6; -. DR MaxQB; Q9UET6; -. DR PaxDb; 9606-ENSP00000326948; -. DR PeptideAtlas; Q9UET6; -. DR ProteomicsDB; 84153; -. [Q9UET6-1] DR ProteomicsDB; 84154; -. [Q9UET6-2] DR Pumba; Q9UET6; -. DR Antibodypedia; 445; 177 antibodies from 20 providers. DR DNASU; 24140; -. DR Ensembl; ENST00000019019.6; ENSP00000019019.2; ENSG00000068438.15. [Q9UET6-2] DR Ensembl; ENST00000348411.3; ENSP00000326948.2; ENSG00000068438.15. [Q9UET6-1] DR GeneID; 24140; -. DR KEGG; hsa:24140; -. DR MANE-Select; ENST00000348411.3; ENSP00000326948.2; NM_012280.4; NP_036412.1. DR UCSC; uc004djn.3; human. [Q9UET6-1] DR AGR; HGNC:13254; -. DR CTD; 24140; -. DR DisGeNET; 24140; -. DR GeneCards; FTSJ1; -. DR HGNC; HGNC:13254; FTSJ1. DR HPA; ENSG00000068438; Low tissue specificity. DR MalaCards; FTSJ1; -. DR MIM; 300499; gene. DR MIM; 309549; phenotype. DR neXtProt; NX_Q9UET6; -. DR OpenTargets; ENSG00000068438; -. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA28417; -. DR VEuPathDB; HostDB:ENSG00000068438; -. DR eggNOG; KOG1099; Eukaryota. DR GeneTree; ENSGT00730000111146; -. DR HOGENOM; CLU_009422_1_2_1; -. DR InParanoid; Q9UET6; -. DR OMA; FIVCLNF; -. DR OrthoDB; 119516at2759; -. DR PhylomeDB; Q9UET6; -. DR TreeFam; TF314897; -. DR PathwayCommons; Q9UET6; -. DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol. DR SignaLink; Q9UET6; -. DR BioGRID-ORCS; 24140; 19 hits in 782 CRISPR screens. DR ChiTaRS; FTSJ1; human. DR GeneWiki; FTSJ1; -. DR GenomeRNAi; 24140; -. DR Pharos; Q9UET6; Tbio. DR PRO; PR:Q9UET6; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9UET6; Protein. DR Bgee; ENSG00000068438; Expressed in stromal cell of endometrium and 211 other cell types or tissues. DR ExpressionAtlas; Q9UET6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB. DR GO; GO:0106339; F:tRNA (cytidine(32)-2'-O)-methyltransferase activity; IMP:UniProtKB. DR GO; GO:0106340; F:tRNA (guanine(34)-2'-O)-methyltransferase activity; IMP:UniProtKB. DR GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IDA:UniProtKB. DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IMP:UniProtKB. DR GO; GO:0022008; P:neurogenesis; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IMP:UniProtKB. DR GO; GO:0006400; P:tRNA modification; TAS:Reactome. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IMP:UniProtKB. DR GO; GO:0002130; P:wobble position ribose methylation; IDA:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_01547; RNA_methyltr_E; 1. DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1. DR InterPro; IPR028590; RNA_methyltr_E_TRM7. DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom. DR InterPro; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1. DR PANTHER; PTHR10920:SF12; TRNA (CYTIDINE(32)_GUANOSINE(34)-2'-O)-METHYLTRANSFERASE-RELATED; 1. DR Pfam; PF01728; FtsJ; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR Genevisible; Q9UET6; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Disease variant; Intellectual disability; KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1..329 FT /note="tRNA (cytidine(32)/guanosine(34)-2'-O)- FT methyltransferase" FT /id="PRO_0000155575" FT REGION 221..240 FT /note="Required for binding to WDR6" FT /evidence="ECO:0000269|PubMed:32558197" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162" FT BINDING 53 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162" FT BINDING 55 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162" FT BINDING 75 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162" FT BINDING 91 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162" FT BINDING 116 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162" FT MOD_RES 271 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 219..220 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_041419" FT VARIANT 26 FT /note="A -> P (in XLID9; severely decreases methylation of FT guanosine in tRNA(Phe) and cytidine in tRNA(Trp); FT methylation of cytidine in tRNA(Phe) appears normal)" FT /evidence="ECO:0000269|PubMed:26310293, FT ECO:0000269|PubMed:36720500" FT /id="VAR_088175" SQ SEQUENCE 329 AA; 36079 MW; 9A85D63A4FA80615 CRC64; MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA APGSWSQVLS QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE IIQHFKGCPA DLVVCDGAPD VTGLHDVDEY MQAQLLLAAL NIATHVLKPG GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA KPRSSRNSSI EAFAVCQGYD PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD LSSYDSDRSY PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV DTFPQPLAAP QCHTLLAPEM EDNEMSCSP //