At least 92 distinct tRNA nucleotide base modifications have been found. The modifications are made post-transcriptionally by a large group of disparate enzymes located in the nucleus, cytosol, and mitochondria (reviewed in Boschi-Muller and Motorin 2013, Jackman and Alfonzo 2013, Gu et al. 2014, Helm and Alfonzo 2014, Li and Mason 2014). Modifications near the anticodon and near the 3' end affect interaction of the tRNA with ribosomes and tRNA synthetases, respectively, while modifications in other regions of the tRNA affect folding and stability of the tRNA (reviewed in Hou et al. 2015). Mutations in tRNA modification enzymes are associated with human diseases (reviewed in Sarin and Leidel 2014, Torres et al. 2014).
View original pathway at Reactome.
Maas S, Gerber AP, Rich A.; ''Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes.''; PubMedEurope PMCScholia
Chen YC, Brooks AF, Goodenough-Lashua DM, Kittendorf JD, Showalter HD, Garcia GA.; ''Evolution of eukaryal tRNA-guanine transglycosylase: insight gained from the heterocyclic substrate recognition by the wild-type and mutant human and Escherichia coli tRNA-guanine transglycosylases.''; PubMedEurope PMCScholia
Songe-Møller L, van den Born E, Leihne V, Vågbø CB, Kristoffersen T, Krokan HE, Kirpekar F, Falnes PØ, Klungland A.; ''Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding.''; PubMedEurope PMCScholia
Yarham JW, Lamichhane TN, Pyle A, Mattijssen S, Baruffini E, Bruni F, Donnini C, Vassilev A, He L, Blakely EL, Griffin H, Santibanez-Koref M, Bindoff LA, Ferrero I, Chinnery PF, McFarland R, Maraia RJ, Taylor RW.; ''Defective i6A37 modification of mitochondrial and cytosolic tRNAs results from pathogenic mutations in TRIT1 and its substrate tRNA.''; PubMedEurope PMCScholia
Begley U, Sosa MS, Avivar-Valderas A, Patil A, Endres L, Estrada Y, Chan CT, Su D, Dedon PC, Aguirre-Ghiso JA, Begley T.; ''A human tRNA methyltransferase 9-like protein prevents tumour growth by regulating LIN9 and HIF1-α.''; PubMedEurope PMCScholia
Khoddami V, Cairns BR.; ''Identification of direct targets and modified bases of RNA cytosine methyltransferases.''; PubMedEurope PMCScholia
Lecointe F, Simos G, Sauer A, Hurt EC, Motorin Y, Grosjean H.; ''Characterization of yeast protein Deg1 as pseudouridine synthase (Pus3) catalyzing the formation of psi 38 and psi 39 in tRNA anticodon loop.''; PubMedEurope PMCScholia
Fernandez-Vizarra E, Berardinelli A, Valente L, Tiranti V, Zeviani M.; ''Nonsense mutation in pseudouridylate synthase 1 (PUS1) in two brothers affected by myopathy, lactic acidosis and sideroblastic anaemia (MLASA).''; PubMedEurope PMCScholia
Liu J, Strâby KB.; ''The human tRNA(m(2)(2)G(26))dimethyltransferase: functional expression and characterization of a cloned hTRM1 gene.''; PubMedEurope PMCScholia
Kato T, Daigo Y, Hayama S, Ishikawa N, Yamabuki T, Ito T, Miyamoto M, Kondo S, Nakamura Y.; ''A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis.''; PubMedEurope PMCScholia
Auxilien S, Guérineau V, Szweykowska-Kulińska Z, Golinelli-Pimpaneau B.; ''The human tRNA m (5) C methyltransferase Misu is multisite-specific.''; PubMedEurope PMCScholia
Schlieker CD, Van der Veen AG, Damon JR, Spooner E, Ploegh HL.; ''A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway.''; PubMedEurope PMCScholia
Smaldino PJ, Read DF, Pratt-Hyatt M, Hopper AK, Engelke DR.; ''The cytoplasmic and nuclear populations of the eukaryote tRNA-isopentenyl transferase have distinct functions with implications in human cancer.''; PubMedEurope PMCScholia
Golovko A, Hjälm G, Sitbon F, Nicander B.; ''Cloning of a human tRNA isopentenyl transferase.''; PubMedEurope PMCScholia
Hou YM, Gamper H, Yang W.; ''Post-transcriptional modifications to tRNA--a response to the genetic code degeneracy.''; PubMedEurope PMCScholia
Brambillasca S, Altkrueger A, Colombo SF, Friederich A, Eickelmann P, Mark M, Borgese N, Solimena M.; ''CDK5 regulatory subunit-associated protein 1-like 1 (CDKAL1) is a tail-anchored protein in the endoplasmic reticulum (ER) of insulinoma cells.''; PubMedEurope PMCScholia
Goll MG, Kirpekar F, Maggert KA, Yoder JA, Hsieh CL, Zhang X, Golic KG, Jacobsen SE, Bestor TH.; ''Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2.''; PubMedEurope PMCScholia
Guo D, Hu K, Lei Y, Wang Y, Ma T, He D.; ''Identification and characterization of a novel cytoplasm protein ICF45 that is involved in cell cycle regulation.''; PubMedEurope PMCScholia
Igoillo-Esteve M, Genin A, Lambert N, Désir J, Pirson I, Abdulkarim B, Simonis N, Drielsma A, Marselli L, Marchetti P, Vanderhaeghen P, Eizirik DL, Wuyts W, Julier C, Chakera AJ, Ellard S, Hattersley AT, Abramowicz M, Cnop M.; ''tRNA methyltransferase homolog gene TRMT10A mutation in young onset diabetes and primary microcephaly in humans.''; PubMedEurope PMCScholia
Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S.; ''tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.''; PubMedEurope PMCScholia
Chen J, Patton JR.; ''Pseudouridine synthase 3 from mouse modifies the anticodon loop of tRNA.''; PubMedEurope PMCScholia
Pastore C, Topalidou I, Forouhar F, Yan AC, Levy M, Hunt JF.; ''Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification.''; PubMedEurope PMCScholia
Anderson J, Phan L, Cuesta R, Carlson BA, Pak M, Asano K, Björk GR, Tamame M, Hinnebusch AG.; ''The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.''; PubMedEurope PMCScholia
Li S, Mason CE.; ''The pivotal regulatory landscape of RNA modifications.''; PubMedEurope PMCScholia
Lamichhane TN, Mattijssen S, Maraia RJ.; ''Human cells have a limited set of tRNA anticodon loop substrates of the tRNA isopentenyltransferase TRIT1 tumor suppressor.''; PubMedEurope PMCScholia
Ozanick S, Krecic A, Andersland J, Anderson JT.; ''The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans.''; PubMedEurope PMCScholia
Chen YC, Kelly VP, Stachura SV, Garcia GA.; ''Characterization of the human tRNA-guanine transglycosylase: confirmation of the heterodimeric subunit structure.''; PubMedEurope PMCScholia
Guy MP, Phizicky EM.; ''Conservation of an intricate circuit for crucial modifications of the tRNAPhe anticodon loop in eukaryotes.''; PubMedEurope PMCScholia
Waas WF, Druzina Z, Hanan M, Schimmel P.; ''Role of a tRNA base modification and its precursors in frameshifting in eukaryotes.''; PubMedEurope PMCScholia
Boland C, Hayes P, Santa-Maria I, Nishimura S, Kelly VP.; ''Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized heteromeric transglycosylase.''; PubMedEurope PMCScholia
Young AP, Bandarian V.; ''Radical mediated ring formation in the biosynthesis of the hypermodified tRNA base wybutosine.''; PubMedEurope PMCScholia
Squires JE, Patel HR, Nousch M, Sibbritt T, Humphreys DT, Parker BJ, Suter CM, Preiss T.; ''Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA.''; PubMedEurope PMCScholia
Torres AG, Piñeyro D, Rodríguez-Escribà M, Camacho N, Reina O, Saint-Léger A, Filonava L, Batlle E, Ribas de Pouplana L.; ''Inosine modifications in human tRNAs are incorporated at the precursor tRNA level.''; PubMedEurope PMCScholia
Sarin LP, Leidel SA.; ''Modify or die?--RNA modification defects in metazoans.''; PubMedEurope PMCScholia
Costessi A, Mahrour N, Sharma V, Stunnenberg R, Stoel MA, Tijchon E, Conaway JW, Conaway RC, Stunnenberg HG.; ''The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by the human tumour antigen PRAME.''; PubMedEurope PMCScholia
Sibert BS, Fischel-Ghodsian N, Patton JR.; ''Partial activity is seen with many substitutions of highly conserved active site residues in human Pseudouridine synthase 1.''; PubMedEurope PMCScholia
Haag S, Warda AS, Kretschmer J, Günnigmann MA, Höbartner C, Bohnsack MT.; ''NSUN6 is a human RNA methyltransferase that catalyzes formation of m5C72 in specific tRNAs.''; PubMedEurope PMCScholia
Konevega AL, Soboleva NG, Makhno VI, Semenkov YP, Wintermeyer W, Rodnina MV, Katunin VI.; ''Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions.''; PubMedEurope PMCScholia
Jurkowski TP, Shanmugam R, Helm M, Jeltsch A.; ''Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase.''; PubMedEurope PMCScholia
Guy MP, Shaw M, Weiner CL, Hobson L, Stark Z, Rose K, Kalscheuer VM, Gecz J, Phizicky EM.; ''Defects in tRNA Anticodon Loop 2'-O-Methylation Are Implicated in Nonsyndromic X-Linked Intellectual Disability due to Mutations in FTSJ1.''; PubMedEurope PMCScholia
Helm M, Alfonzo JD.; ''Posttranscriptional RNA Modifications: playing metabolic games in a cell's chemical Legoland.''; PubMedEurope PMCScholia
Cartlidge RA, Knebel A, Peggie M, Alexandrov A, Phizicky EM, Cohen P.; ''The tRNA methylase METTL1 is phosphorylated and inactivated by PKB and RSK in vitro and in cells.''; PubMedEurope PMCScholia
Jurkowski TP, Meusburger M, Phalke S, Helm M, Nellen W, Reuter G, Jeltsch A.; ''Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism.''; PubMedEurope PMCScholia
Torres AG, Batlle E, Ribas de Pouplana L.; ''Role of tRNA modifications in human diseases.''; PubMedEurope PMCScholia
Spinola M, Galvan A, Pignatiello C, Conti B, Pastorino U, Nicander B, Paroni R, Dragani TA.; ''Identification and functional characterization of the candidate tumor suppressor gene TRIT1 in human lung cancer.''; PubMedEurope PMCScholia
Alexandrov A, Martzen MR, Phizicky EM.; ''Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA.''; PubMedEurope PMCScholia
Brzezicha B, Schmidt M, Makalowska I, Jarmolowski A, Pienkowska J, Szweykowska-Kulinska Z.; ''Identification of human tRNA:m5C methyltransferase catalysing intron-dependent m5C formation in the first position of the anticodon of the pre-tRNA Leu (CAA).''; PubMedEurope PMCScholia
Vilardo E, Nachbagauer C, Buzet A, Taschner A, Holzmann J, Rossmanith W.; ''A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase--extensive moonlighting in mitochondrial tRNA biogenesis.''; PubMedEurope PMCScholia
Bykhovskaya Y, Casas K, Mengesha E, Inbal A, Fischel-Ghodsian N.; ''Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA).''; PubMedEurope PMCScholia
Shaheen R, Han L, Faqeih E, Ewida N, Alobeid E, Phizicky EM, Alkuraya FS.; ''A homozygous truncating mutation in PUS3 expands the role of tRNA modification in normal cognition.''; PubMedEurope PMCScholia
Arragain S, Handelman SK, Forouhar F, Wei FY, Tomizawa K, Hunt JF, Douki T, Fontecave M, Mulliez E, Atta M.; ''Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA.''; PubMedEurope PMCScholia
Perche-Letuvée P, Molle T, Forouhar F, Mulliez E, Atta M.; ''Wybutosine biosynthesis: structural and mechanistic overview.''; PubMedEurope PMCScholia
Fu D, Brophy JA, Chan CT, Atmore KA, Begley U, Paules RS, Dedon PC, Begley TJ, Samson LD.; ''Human AlkB homolog ABH8 Is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival.''; PubMedEurope PMCScholia
The CTU1:CTU2:URM1 complex transfers a thiol group from the thiolcarboxylated C-terminus of URM1 to uridine-34 residues of tRNAs, yielding 2-thiouridine-34 (Schlieker et al. 2008). The same reaction is catalyzed by TRMU (MTU1) in mitochondria.
The METTL1:WDR4 complex transfers a methyl group from S-adenosylmethionine to guanosine-46 of tRNA(Phe), yielding 7-methylguanosine-46 (Alexandrov et al. 2002, Cartlidge et al. 2005). A homologous complex, Trm8p:Trm82p, exists in Saccharomyces cerevisiae and catalyzes the same reaction.
DUS2 catalyzes the reduction of the 5,6 double bond in uridine residues in the D-loop of tRNAs, yielding 5,6-dihydrouridine (Kato et al. 2005). By inference with the homolog from Saccharomyces cerevisiae, Smm1p (Dus2p), NADH or NADPH is the reducing agent.
The ADAT2:ADAT3 heterodimer (hetADAT) deaminates adenosine-34 in 8 human tRNAs: tRNA(Ala-AGC), tRNA(Arg-ACG), tRNA(Ile-AAT), tRNA(leu-AAG), tRNA(Pro-AGG), tRNA(Ser-AGA), tRNA(Thr-AGT), tRNA(Val-AAC) (Torres et al. 2015). The deamination occurs in the nucleus on precursor tRNAs from which the 5' leaders and 3' trailers have not yet been cleaved. The corresponding homologues in Saccharomyces cerevisiae are Tad2p and Tad3p.
ADAT1 deaminates adenosine-37 of tRNA(Ala) yielding inosine-37, which may then be methylated to N1-methylinosine-37 (Maas et al. 1999). The homologue in Saccharomyces, Tad1p, catalyzes the same reaction, indicating the deamination of adenosine-37 is highly conserved in eukaryotes.
The shorter isoform of PUS1, PUS1-2, converts uridine to pseudouridine in the anticodon stem of tRNAs in the nucleus (Fernandez-Vizarra et al. 2007, Sibert et al. 2008). The longer isoform of PUS1 (PUS1-1) is present in mitochondria; a shorter isoform of PUS1 (PUS1-2) possessing a different N-terminus is present in the nucleus (Fernandez-Vizarra et al. 2007). In contrast, the yeast Saccharomyces cerevisiae has 2 genes: PUS1 which encodes the nuclear enzyme and PUS2 which encodes the mitochodrial enzyme. PUS1 and its substrates are conserved from yeast to humans. Like the yeast homologue, Pus1p, human PUS1 may also act on additional tRNAs, pre-tRNAs, and U2 snRNA. Mutations in PUS1 cause mitochondrial myopathy and sideroblastic anemia (MLASA) (Bykhovskaya et al. 2004, Fernandez-Vizarra et al. 2007).
NSUN2 transfers a methyl group from S-adenosylmethionine to the 5 positions of cytidine-34 and cytidine-48 in tRNA(Leu)(CAA) (Brzezicha et al. 2006, Auxilien et al. 2012, Squires et al. 2012, Khoddami and Cairns 2013). Methylation of cytidine-34 occurs on the uspliced precursor tRNA(Leu)(CAA) (Brzezicha et al. 2006, Auxilien et al. 2012); methylation of cytidine-48 occurs on either the spliced or unspliced tRNA(Leu)(CAA) (Auxilien et al. 2012).
TRMT1 (hTRM1) transfers two methyl groups from two molecules of S-adenosylmethionine to the 2 position of guanosine-26 of tRNA(Tyr), yielding 2-dimethylguanosine (Liu and Straby 2000). TRMT1 can dimethylate both spliced and unspliced tRNA (Liu and Straby 2000).
TRDMT1 (DNMT2) transfers a methyl group from S-adenosylmethionine to the 5 position of cytidine-38 of tRNA(Asp) (Goll et al. 2006, Jurkowski et al. 2008, Jurkowski et al. 2012). TRDMT1 uses a similar mechanism to DNA methyltransferases (DNMT1, DNMT3A, DNMT3B) (Jurkowski et al. 2008).
THG1L (THG1) adds a guanosine triphosphate residue to the 5' end of tRNA(His), a 3'-5' addition that contrasts with the usual 5'-3' directionality of nucleotide polymerases (Hyde et al. 2010).
The transglycosylase complex QTRT1:QTRTD1 exchanges guanine for queuine at nucleotide 34 of tRNA(Tyr) (Chen et al. 2010, Chen et al. 2011). The QTRT1 subunit is responsible for the transglycosylase activity. Eukaryotes are unable to synthesize queuine and must obtain it from dietary sources or symbiotic gut flora. As inferred from the mouse homologs, QTRT1:QTRTD1 associates with the outer mitochondrial membrane (Boland et al. 2009). The homologous enzyme in Escherichia coli is tgt.
The TRMT6:TRMT61A complex transfers a methyl group from S-adenosylmethionine to the 1 position of adenosine-58 of tRNA(Met) (Ozanick et al. 2005). Based on the location of the homologous complex (GCD10:GCD14) in yeast (Anderson et al. 1998), methylation by the TRMT6:TRMT61A complex is inferred to occur in the nucleus.
TRIT1 transfers a dimethylallyl group (isopentenyl group) from dimethylallyl diphosphate to the N6 position of adenosine-37 in tRNA(Ser), yielding N6-dimethylallyladenosine-37 (N6-isopentenyladenosine-37) (Golovko et al. 2000, Spinola et al. 2005, Lamichhane et al. 2013, Yarham et al. 2014, Smaldino et al. 2015). TRIT1 modifies both cytosolic and mitochondrial tRNAs and a mutation in TRIT1 causes mitochondrial respiratory defects (Yarham et al. 2014). Expression of TRIT1 is down-regulated in lung adenocarcinomas compared with normal tissue (Spinola et al. 2005). The homologue in Saccharomyces cerevisiae, MOD5, catalyzes the same reaction.
As inferred from the yeast homologs (EKC complex, KEOPS complex, BUD32:CGI121:KAE1:PCC1), the EKC complex (LAGE3:OSGEP:TP53RK:TPRKB) transfers a threonylcarbamoyl group from L-threonylcarbamoyladenylate to adenosine-37 of tRNAs, yielding threonylcarbamoyladenosine-37.
NSUN2 transfers methyl groups from S-adenosylmethionine to the 5 positions of cytidine-48 and cytidine-49 of tRNA(Asp)(GUC) (Squires et al. 2012, Khoddami et al. 2013).
NSUN2 transfers methyl groups from S-adenosylmethionine to the 5 positions of cytidine-40, cytidine-48, cytidine-49, and cytidine-50 of tRNA(Gly)(GCC) (Auxilien et al. 2012, Khoddami and Cairns 2013).
ALKBH8:Fe2+ transfers a methyl group from S-adenosylmethionine (AdoMet) to 5-carboxymethyluridine-34 of tRNA, yielding 5-methoxycarbonylmethyluridine-34 (5-(2-methoxy-2-oxoethyl)uridine-34) (Fu et al. 2010, Songe-Møller et al. 2010). The corresponding homologue in Saccharomyces, Trm9p, catalyzes the same reaction.
As inferred from homologues in Saccharomyces cerevisiae, TRMT11 (catalytic subunit) and TRMT112 (zinc-binding subunit) form a complex which methylates the 2 position of guanosine-10 in tRNA (Purushothaman et al. 2005).
KIAA1456 (TRM9L, hTRM9L) transfers a methyl group from S-adenosylmethionine (AdoMet) to 5-carboxymethyluridine in tRNA, yielding 5-methoxycarbonylmethyluridine (5-(2-methoxy-2-oxoethyl)uridine) (Begley et al. 2013). The subcellular location of the reaction is unknown.
The CDKAL1:4Fe-4S complex methylthiolates N6-threonylcarbamoyladenosine-37 in several tRNAs (Arragain et al. 2010). The source of the methyl group is S-adenosylmethionine (AdoMet). The source of the sulfur is unknown. The homologue in Bacillus subtilis, mtaB, catalyzes the same reaction (Arragain et al. 2010). CDKAL1 is located on the cytosolic face of the endoplasmic reticulum therefore the reaction is presumed to occur in the cytosol (Brambillasca et al. 2012).
As inferred from the homologue in Saccharmyces cerivisiae, PUS7 converts uridine to pseudouridine at nucleotide 13 of cytoplasmic tRNA and at nucleotide 35 of unspliced tRNA(Tyr). PUS7 also synthesizes pseudouridine in U2 snRNA and in pre-tRNA(Tyr). Pus7p is a nuclear protein according to global analysis of protein locations in yeast.
As inferred from the homologue in Saccharomyces cerevisiae, TRMT10A methylates the 1 position of guanosine at nucleotide 9 of tRNAs. TRMT10A is located in the nucleus (Igoillo-Esteve et al. 2013). A nonsense mutation in TRMT10A causes diabetes and microcephaly (Igoillo-Esteve et al. 2013).
As inferred from the yeast homolog, TRMT13 methylates the 2' hydroxyl group of adenosine-4 in the acceptor stems of tRNA(His). The subcellular location of the reaction is unknown. Yeast lacking TRM13 do not have an obvious growth defect.
As inferred from the yeast homolog, TRMT13 methylates the 2' hydroxyl group of cytidine-4 in the acceptor stems of tRNA(Gly) and tRNA(Pro). The subcellular location of the reaction is unknown. Yeast lacking TRM13 do not have an obvious growth defect.
As inferred from the yeast homolog, TRMT44 methylates the 2' hydroxyl group of uridine-44 in tRNA(Ser). In yeast 2'-O-methyluridine-44 together with N(4)-acetylcytidine appears to be required to maintain abundance of tRNA(Ser).
PUS3 catalyzes the modification (isomerization) of uridine to pseudouridine at nucleotides 38 and 39 in the anticodon loops of tRNAs (Shaheen et al. 2016). Homologues of PUS3 in mouse (Chen and Patton 2000) and yeast (Lecointe et al. 1998) catalyze the same reaction, and both the PUS3 gene family and the modification are highly conserved. Deletion of DEG1 encoding Pus3p in budding yeast (Saccharomyces cerevisiae) causes slow growth (Lecointe et al. 1998) while a truncating mutation in human PUS3 causes a reduction in pseudouridines 38 and 39 with consequent intellectual disability (Shaheen et al. 2016).
NSUN6 methylates position 5 of the cytosine ring of cytidine-72 in the acceptor stem of tRNA(Cys) and tRNA(Thr) (Haag et al. 2015). As the reaction occurs in the cytoplasm and requires the 3' CCA on the tRNA substrates, it is believed to occur late in tRNA biogenesis
FTSJ1 methylates the 2'‑hydroxyl group of cytidine‑32 and guanosine‑34 in the anticodon loop of tRNA(Phe), as well as C32 and N34 of other substrate tRNAs (Guy and Phizicky 2015a, Guy et al. 2015b). Based on the functional and sequence homology between human FTSJ1 and yeast Trm7 the reaction is inferred to occur in the cytosol. THADA is required together with FTSJ1 for the methylation reaction at C32, based on its complementation of trm732 mutants in yeast, but the function of THADA has not been directly demonstrated in human cells (Guy and Phizicky 2015a).
FTSJ1 methylates the 2'‑hydroxyl group of cytidine‑32 and guanosine‑34 in the anticodon loop of tRNA(Phe), as well as C32 and N34 of other substrate tRNAs (Guy and Phizicky 2015a, Guy et al. 2015b). Based on the functional and sequence homology between human FTSJ1 and yeast Trm7 the reaction is inferred to occur in the cytosol. THADA is required together with FTSJ1 for the methylation reaction at C32, based on its complementation of trm732 mutants in yeast, but the function of THADA has not been directly demonstrated in human cells (Guy and Phizicky 2015a).
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DataNodes
wybutosine at G37
of tRNA(Phe)containing
2-methylthio-N6-threonylcarbamoylA-37containing
5-methoxycarbonylmethylU-34containing
threonylcarbamoylA-37containing
threonylcarbamoylA-37U-13, pre-tRNA(Tyr)
containing U-35pseudoU-13, pre-tRNA(Tyr) containing
pseudoU-35containing
5-carboxymethylU-34containing
5-methoxycarbonylmethylU-34containing
5-mC-48,49containing
C-48,C-49containing
2-thioU-34containing
5mC-40,48,49,50containing
C-40,C-48,C-49,C-50containing
2'-O-methylC-4tRNA(Leu)(CAA) containing
5mC-34,48tRNA(Leu)(CAA)
containing C-34,48Annotated Interactions
CDKAL1 is located on the cytosolic face of the endoplasmic reticulum therefore the reaction is presumed to occur in the cytosol (Brambillasca et al. 2012).
containing
2-methylthio-N6-threonylcarbamoylA-37containing
5-methoxycarbonylmethylU-34containing
threonylcarbamoylA-37containing
threonylcarbamoylA-37U-13, pre-tRNA(Tyr)
containing U-35pseudoU-13, pre-tRNA(Tyr) containing
pseudoU-35containing
5-carboxymethylU-34containing
5-methoxycarbonylmethylU-34containing
5-mC-48,49containing
C-48,C-49containing
2-thioU-34containing
5mC-40,48,49,50containing
C-40,C-48,C-49,C-50containing
2'-O-methylC-4tRNA(Leu)(CAA) containing
5mC-34,48tRNA(Leu)(CAA)
containing C-34,48