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Information on EC 2.1.1.203 - tRNA (cytosine34-C5)-methyltransferase and Organism(s) Homo sapiens and UniProt Accession Q08J23
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2.1.1.203 tRNA (cytosine34-C5)-methyltransferaseIUBMB Comments
The human enzyme is specific for C5-methylation of cytosine34 in tRNA precursors. The intron in the human pre-tRNALeu(CAA) is indispensable for the C5-methylation of cytosine in the first position of the anticodon. It is not able to form 5-methylcytosine at positions 48 and 49 of human and yeast tRNA precursors .
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Word Map
- 2.1.1.203
- 5-methylcytosine
-
anticodon
- homocysteine
-
wobble
-
ualcan
- 5-formylcytosine
-
biallelic
-
omnibus
-
shrinkage
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hyperhomocysteinemia
- encephalomyopathy
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nsun2-mediated
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epitranscriptome
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early-onset
- medicine
- pharmacology
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
+
=
+
+
cytosine34 in tRNA precursor
=
+
5-methylcytosine34 in tRNA precursor
Synonyms
nsun3, nop2/sun domain family member 2, htrm4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
the formation of 5-methylcytosine34 is a strictly intron-dependent process
PATHWAY SOURCE
PATHWAYS
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytosine34-C5)-methyltransferase
The human enzyme is specific for C5-methylation of cytosine34 in tRNA precursors. The intron in the human pre-tRNALeu(CAA) is indispensable for the C5-methylation of cytosine in the first position of the anticodon. It is not able to form 5-methylcytosine at positions 48 and 49 of human and yeast tRNA precursors [1].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
specific modification of cytosine34 in the intron-containing yeast pre-tRNALeu(CAA)
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
S-adenosyl-L-methionine + cytosine34 in tRNALeu(CAG) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNALeu(CAG) precursor
-
-
-
?
S-adenosyl-L-methionine + cytidine34 in mitochondrial tRNA
S-adenosyl-L-homocysteine + 5-methylcytidine34 in mitochondrial tRNA
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in mitochondrial tRNAMet precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in mitochondrial tRNAMet precursor
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in mitochondrial tRNAMet(AUA) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in mitochondrial tRNAMet(AUA) precursor
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
-
-
-
-
?
S-adenosyl-L-methionine + microRNA 125b
S-adenosyl-L-homocysteine + ?
-
the tRNA methyltransferase NSun2 methylates primary (pri-miR-125b), precursor (pre-miR-125b), and mature microRNA 125b (miR-125b) in vitro and in vivo
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-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
specific modification of cytosine34 in the intron-containing yeast pre-tRNALeu(CAA). The hTrm4 MTase has a much narrower specificity against the yeast substrates than its yeast orthologue. The human enzyme is not able to form 5-methylcytosine34 at positions 48 and 49 of human and yeast tRNA precursors. Intron in the human pre-tRNALeu(CAA) is indispensable for the C5-methylation of cytosine in the first position of the anticodon. The modification of C34 depends on the nucleotide sequence surrounding the position to be modified and on the structure of intron-containing prolongated anticodon stem
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-
?
S-adenosyl-L-methionine + cytosine34 in mitochondrial tRNAMet(AUA) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in mitochondrial tRNAMet(AUA) precursor
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-
-
?
S-adenosyl-L-methionine + cytosine34 in mitochondrial tRNAMet(AUA) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in mitochondrial tRNAMet(AUA) precursor
secondary structure of human mt-tRNAMet with modifications f5C and pseudouridine. The anticodon pairs with AUG and AUA codons, overview
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-
?
additional information
?
-
levels of m5C changes site-specifically and dynamically in response to oxidative stress. All individual m5C sites showing significantly different methylation levels in NSUN2-rescued cells after 2 or 4 hours of stress. Methylation levels within the same tRNA molecule are independent from each other
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-
-
additional information
?
-
NSUN2-methylated tRNA sites are located in the anticodon loop (C34) and the VL (C46, C47), number of m5C per tRNA in all tRNAs or tRNA leucine, mass spectrometry, overview
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-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
specific modification of cytosine34 in the intron-containing yeast pre-tRNALeu(CAA)
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNALeu(CAG) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNALeu(CAG) precursor
-
-
-
?
S-adenosyl-L-methionine + cytidine34 in mitochondrial tRNA
S-adenosyl-L-homocysteine + 5-methylcytidine34 in mitochondrial tRNA
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in mitochondrial tRNAMet precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in mitochondrial tRNAMet precursor
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in mitochondrial tRNAMet(AUA) precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in mitochondrial tRNAMet(AUA) precursor
-
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
-
-
-
-
?
S-adenosyl-L-methionine + microRNA 125b
S-adenosyl-L-homocysteine + ?
-
the tRNA methyltransferase NSun2 methylates primary (pri-miR-125b), precursor (pre-miR-125b), and mature microRNA 125b (miR-125b) in vitro and in vivo
-
-
?
additional information
?
-
levels of m5C changes site-specifically and dynamically in response to oxidative stress. All individual m5C sites showing significantly different methylation levels in NSUN2-rescued cells after 2 or 4 hours of stress. Methylation levels within the same tRNA molecule are independent from each other
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
NSUN2 localizes to the nucleolus of Purkinje cells in the cerebellum
additional information
-
simultaneous overexpression of NSUN2 and METTL1, EC 2.1.1.33, is widely observed among human cancers
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
two of the seven NSUN proteins (NSUN3 and NSUN4) are synthesized on cytoplasmic ribosomes but localize to mitochondria
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no obvious mitochondrial-targeting sequence is present in the N-terminal region of NSUN3, immunohistochemic analysis shows that NSUN3 predominantly localized in mitochondria
NSUN3 has been shown to localize to the mitochondrial matrix, its mitochondrial import has not been determined
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
loss-of-function mutations in the human NSUN3 gene causes mitochondrial disorders. NSUN2-depleted cells show attenuated changes to protein synthesis rates. Protein synthesis rates of rescued NSUN2-/- cells (NSUN2) are comparable to NSUN2+/+ cells and slightly, but not significantly, reduced when the enzymatic dead version of NSUN2 K190M is expressed. Cell stress causes a strong but temporary reduction of protein synthesis, which is attenuated by loss of NSUN2. Stress induces a site-specific and dynamic loss of m5C. Mitochondrial activity is reduced and catabolic pathways enhanced in the absence of NSUN2
metabolism
the nucleolus, where NSUN2 resides, can act as a stress sensor. Nucleophosmin (NPMI) is a marker for nucleolar stress, and a rapid, strong down-regulation of both NPMI and NSUN2 is observed upon arsenite treatment. Additional NSUN family members residing in the mitochondria (NSUN3, NSUN4) and cytoplasm (NSUN6) are similarly repressed in response to arsenite stress
physiological function
evolution
-
nonessential tRNA modifications by methyltransferases are evolutionarily conserved and have been reported to stabilize mature tRNA molecules and prevent rapid tRNA decay. The tRNA modifying enzymes, NSUN2 and METTL1, EC 2.1.1.33, are mammalian orthologues of yeast Trm4 and Trm8, which are required for protecting tRNA against tRNA decay
malfunction
metabolism
during the maturation of the cytoplasmic tRNALeu(CAA), an m5C34 modification is also installed by the multisite-specific NSUN2 (cf. EC 2.1.1.202)
physiological function
additional information
catalytic mechanism of the enzyme, comparison of NSUN family enzymes, overview. The NSUN family enzymes use the cysteine located in amino acid motif VI for the nucleophilic attack on carbon 6 of the target cytosine in RNA. In all seven human NSUN variants, the catalytic cysteine is preceded by threonine. Hydrogen bonding with the backbone carbonyl of proline and the aspartate side chain in motif IV orients the base in the active site and assists bond formation by transient protonation of the endocyclic N3 of cytidine. The activated nucleobase then accepts a methyl group from the properly positioned SAM cofactor, resulting in the formation of a carbon-carbon bond and generation of S-adenosylhomocysteine (SAH). To complete the reaction, the covalently bound methylated RNA has to be released from the protein. This elimination is assisted by the cysteine located in motif IV of NSUN proteins. This cysteine is located next to the conserved proline and acts as a base to deprotonate the tetrahedral carbon and initiate the elimination reaction that restores the unsaturated m5C heterocycle
physiological function
specific modification of cytosine34 in the intron-containing yeast pre-tRNALeu(CAA)
physiological function
cytosine-5 RNA methylation links protein synthesis to cell metabolism. NSUN2 functions in the cell cycle to adapt dynamic protein synthesis in response to stress. Cytosine-5 RNA methylation is a metabolic sensor of external stress. NSUN2 regulates cell cycle phases and global protein synthesis during the cellular stress response. Cell stress causes a strong but temporary reduction of protein synthesis, which is attenuated by loss of NSUN2. In response to stress, the percentage of NSUN2+/+ cells decreased in the G1/G0-phase but increased in the S-phase and G2/M-phase of the cell cycle. In contrast, the cell cycle progression of NSUN2-/- cells remained stable, indicating that NSUN2-/- cells fail to adapt the cell cycle phases to the stress stimulus. A tight regulation of global protein synthesis might be needed to avoid accumulation of proteins during cell cycle arrest and repair. Dynamic changes of site-specific m5C levels require NSUN2. Site-specific tRNA methylation determines tRNA-derived fragments (tRFs) biogenesis in response to oxidative stress
malfunction
-
mutation G679R causes NSUN2 to fail to localize within the nucleolus. NSUN2, besides other RNA-methyltransferase-encoding genes, is involved in neurological disorders like intellectual disability, also called mental retardation, phenotypes, overview
malfunction
-
combined knockdown of NSUN2 and METTL1, EC 2.1.1.33, in HeLa cells drastically potentiate sensitivity of cells to 5-fluorouracil, but does not affect cisplatin- and paclitaxel-induced cytotoxicity, synergistic effects of NSUN2 and METTL1 double knockdown, which causes rapid tRNA(ValAAC) degradation induced by destabilizing 5-fluorouracil
malfunction
mutation of the cysteine in motif IV in human NSUN3 to alanine or serine results in a stable covalent intermediate. Lack of NSUN3 (or ALKBH1) impairs mitochondrial translation, leading to decreased cell proliferation. Mutations in NSUN3 that lead to either aberrant splicing and frameshifting (p.Glu42Valfs*11) or the introduction of a premature stop codon (c.295C>T/p.Arg99*) have been detected in patients with a mitochondrial deficiency disorder characterized by developmental disability microcephaly, failure to thrive, recurrent increased lactate levels in plasma, muscular weakness, proximal accentuated, external ophthalmoplegia, and convergence nystagmus. Furthermore, mitochondrial disease-associated point mutations with the gene encoding mt-tRNAMet that lead to A37G and C39U substitutions have been shown to impede methylation of C34 by NSUN3. In both cases, lack of NSUN3-mediated modification impairs mitochondrial translation, leading to reduced mitochondrial function. Reduced mitochondrial translation affects the normal differentiation program
malfunction
NSUN3-knockout cells show strong reduction in mitochondrial protein synthesis and reduced oxygen consumption, leading to deficient mitochondrial activity. Reconstitution of formation of 5-methylcytidine (m5C) at position 34 (m5C34) on mt-tRNAMet with recombinant NSUN3 in the presence of AdoMet. Two disease-associated point mutations in mt-tRNAMet that impair m5C34 formation by NSUN3, are determined, indicating that a lack of f5C34 has pathological consequences. Loss of NSUN3 causes mitochondrial dysfunction, phenotype, overview
physiological function
-
NSUN2 encodes a methyltransferase that catalyzes the intron-dependent formation of 5-methylcytosine at C34 of tRNA-leu(CAA). It also functions in spindle assembly during mitosis as well as chromosome segregation
physiological function
-
methylation by NSun2 inhibits the processing of pri-miR- 125b2 into pre-miR-125b2, decreases the cleavage of pre-miR-125b2 into miR-125, and attenuates the recruitment of RISC by miR-125, thereby repressing the function of miR-125b in silencing gene expression
physiological function
-
NSUN2 (NOP2/Sun domain family, member 2) is a NOL1/NOP2/SUN domain-containing tRNA (cytosine-5-)-methyltransferase. Nonessential tRNA modifications by methyltransferases are evolutionarily conserved and have been reported to stabilize mature tRNA molecules and prevent rapid tRNA decay. The tRNA modifying enzyme NSUN2 is a mammalian orthologues of yeast Trm4, which is required for protecting tRNA against tRNA decay. Enzyme NUSN2 is not a critical regulator of cancer cell growth
physiological function
in human mitochondria, the AUA codon encodes methionine via a mitochondrial transfer RNA for methionine (mt-tRNAMet) that contains 5-formylcytidine (f5C) at the first position of the anticodon (position 34). f5C34 is required for deciphering the AUA codon during protein synthesis. Biogenesis of f5C34 is initiated by S-adenosylmethionine (AdoMet)-dependent methylation catalyzed by NSUN3, a methyltransferase in mitochondria. NSUN3 methylase initiates 5-formylcytidine biogenesis in human mitochondrial tRNAMet. NSUN3 is essential for f5C34 formation
physiological function
NSUN3 is a mitochondrial tRNA m5C methyltransferase that specifically targets the wobble position (C34) of mt-tRNAMet. The wobble base modification(s) installed by NSUN3 and ALKBH1 likely serve to expand codon recognition by mt-tRNAMet, enabling it to fulfil these diverse functions. Mt-tRNAMet-C34 is almost fully modified in vivo, and, although bisulfite and reduced bisulfite sequencing analyses indicate the presence of some m5C at this position, the majority undergoes further oxidation by ALKBH1 to generate 5-formylcytosine (f5C), structures of modified nucleotides at position 34 and the modification pathway. 5-Formylcytosine (f5C) has a well-established role in expanding codon recognition by mt-tRNAMet during mitochondrial translation. Modification of mt-tRNAMet by NSUN3 occurs in the mitochondria
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NSUN2_HUMAN
767
0
86471
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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NSUN2 is phosphorylated at Ser139 by Aurora-B to inhibit its enzymatic activity during mitosis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A37G
naturally occurring mutation, mitochondrial disease-associated point mutations with the gene encoding mt-tRNAMet that lead to A37G substitution, impede methylation of C34 by NSUN3, lack of NSUN3-mediated modification impairs mitochondrial translation, leading to reduced mitochondrial function
C39U
naturally occurring mutation, mitochondrial disease-associated point mutations with the gene encoding mt-tRNAMet that lead to C39U substitution, impede methylation of C34 by NSUN3, lack of NSUN3-mediated modification impairs mitochondrial translation, leading to reduced mitochondrial function
G679R
-
site-directed mutaegensis, the mutation to arginine at this residue causes NSUN2 to fail to localize within the nucleolus
additional information
additional information
generation of enzyme depeleted NSUN2-/- cells. Rescue for loss of NSUN2 by reexpressing the wild-type or enzymatic dead protein. The number of m5C per tRNA in all tRNAs or tRNA leucine is quantified by mass spectrometry in NSUN2-/- cells reexpressing wild-type NSUN2, the catalytically inactive NSUN2 K190M mutant, or the empty vector control. Reexpression of NSUN2 significantly restores 525 methylation sites when compared to the empty vector control and 431 sites when compared to K190M-overexpressing cells
additional information
-
combined knockdown of NSUN2 and METTL1, EC 2.1.1.33, in HeLa cells
additional information
generation of NSUN3 knockout cells. When the knockout strain is rescued by plasmid-encoded NSUN3, f5C34 in mt-tRNAMet is partially restored
additional information
-
generation of NSUN3 knockout cells. When the knockout strain is rescued by plasmid-encoded NSUN3, f5C34 in mt-tRNAMet is partially restored
additional information
mutation of the cysteine in motif IV in human NSUN3 to alanine or serine results in a stable covalent intermediate. Mutations in NSUN3 that lead to either aberrant splicing and frameshifting (p.Glu42Valfs*11) or the introduction of a premature stop codon (c.295C>T/p.Arg99*) have been detected in patients with a mitochondrial deficiency disorder
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged NSun2 from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the human Trm4 (hTrm4) cDNA in yeast partially complements the lack of the endogenous Trm4p enzyme
transient expression of C-terminally Flag-tagged NSUN3 in HeLa cells, immunohistochemic analysis shows that NSUN3 predominantly localized in mitochondria
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of NSUN2 and at least three of its m5C RNA methyltransferase family members are repressed in response to oxidative stress. Rapid and strong downregulation of NSUN2 upon arsenite treatment
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
this methyltransferase is a novel downstream Myctarget which mediates Myc-induced cell proliferation and growth. Therefore, the characterization of hTrm4 substrate specificity can be essential since this enzyme is a potential target for cancer therapies
pharmacology
-
enzymes NSUN2 and METTL1 are implicated in 5-fluorouracil sensitivity in HeLa cells. Interfering with methylation of tRNAs might provide a promising rationale to improve 5-fluorouracil chemotherapy of cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Nucleic Acids Res.
34
6034-6043
2006
Homo sapiens (Q08J23), Homo sapiens
Khan, M.A.; Rafiq, M.A.; Noor, A.; Hussain, S.; Flores, J.V.; Rupp, V.; Vincent, A.K.; Malli, R.; Ali, G.; Khan, F.S.; Ishak, G.E.; Doherty, D.; Weksberg, R.; Ayub, M.; Windpassinger, C.; Ibrahim, S.; Frye, M.; Ansar, M.; Vincent, J.B.
Mutation in NSUN2, which encodes an RNA methyltransferase, causes autosomal-recessive intellectual disability
Am. J. Hum. Genet.
90
856-863
2012
Homo sapiens, Mus musculus
Yuan, S.; Tang, H.; Xing, J.; Fan, X.; Cai, X.; Li, Q.; Han, P.; Luo, Y.; Zhang, Z.; Jiang, B.; Dou, Y.; Gorospe, M.; Wang, W.
Methylation by NSun2 represses the levels and function of microRNA 125b
Mol. Cell. Biol.
34
3630-3641
2014
Homo sapiens
Okamoto, M.; Fujiwara, M.; Hori, M.; Okada, K.; Yazama, F.; Konishi, H.; Xiao, Y.; Qi, G.; Shimamoto, F.; Ota, T.; Temme, A.; Tatsuka, M.
tRNA modifying enzymes, NSUN2 and METTL1, determine sensitivity to 5-fluorouracil in HeLa cells
PLoS Genet.
10
e1004639
2014
Homo sapiens
Bohnsack, K.; Hoebartner, C.; Bohnsack, M.
Eukaryotic 5-methylcytosine (M5C) RNA methyltransferases mechanisms, cellular functions, and links to disease
Genes (Basel)
10
102
2019
Homo sapiens (Q9H649), Saccharomyces cerevisiae (Q9H649)
Nakano, S.; Suzuki, T.; Kawarada, L.; Iwata, H.; Asano, K.; Suzuki, T.
NSUN3 methylase initiates 5-formylcytidine biogenesis in human mitochondrial tRNAMet
Nat. Chem. Biol.
12
546-551
2016
Homo sapiens (Q9H649), Homo sapiens
Gkatza, N.A.; Castro, C.; Harvey, R.F.; Heiss, M.; Popis, M.C.; Blanco, S.; Borneloev, S.; Sajini, A.A.; Gleeson, J.G.; Griffin, J.L.; West, J.A.; Kellner, S.; Willis, A.E.; Dietmann, S.; Frye, M.
Cytosine-5 RNA methylation links protein synthesis to cell metabolism
PLoS Biol.
17
e3000297
2019
Homo sapiens (Q08J23)
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