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Information on EC 2.1.1.311 - 25S rRNA (cytosine2278-C5)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.311
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.311 25S rRNA (cytosine2278-C5)-methyltransferase
IUBMB Comments
The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show+
=
+
+
cytosine2278 in 25S rRNA
=
+
5-methylcytosine2278 in 25S rRNA
Synonyms
28S rRNA (cytosine-C(5))-methyltransferase, CG42358, Nsun-5, Nsun5, RCM1, ribosomal RNA cytosine methyltransferase 1, Y53F4B, YNL022C, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Nsun5
RCM1
ribosomal RNA cytosine methyltransferase 1
YNL022C
RCM1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:25S rRNA (cytosine2278-C5)-methyltransferase
The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cytidine in 28S rRNA + S-adenosyl-L-methionine
5-methylcytidine in 28S rRNA + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
cytidine2278 in 25S rRNA + S-adenosyl-L-methionine
5-methylcytidine2278 in 25S rRNA + S-adenosyl-L-homocysteine
cytidine3381 in 26S rRNA + S-adenosyl-L-methionine
5-methylcytidine3381 in 26S rRNA + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
cytidine3438 in 28S rRNA + S-adenosyl-L-methionine
5-methylcytidine3438 in 28S rRNA + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
cytidine3782 in 28S rRNA + S-adenosyl-L-methionine
5-methylcytidine3782 in 28S rRNA + S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
cytidine2278 in 25S rRNA + S-adenosyl-L-methionine
5-methylcytidine2278 in 25S rRNA + S-adenosyl-L-homocysteine
Substrates: Rcm1 is necessary and sufficient for the formation of a large C2278-methylated subpopulation of ribosomes, under normal and oxidative stress conditions
Products: -
Products: -
?
cytidine2278 in 25S rRNA + S-adenosyl-L-methionine
5-methylcytidine2278 in 25S rRNA + S-adenosyl-L-homocysteine
Substrates: Rcm1 is necessary and sufficient for the formation of a large C2278-methylated subpopulation of ribosomes, under normal and oxidative stress conditions
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is responsible for the methylation at cytosine2278 of the 25S ribosomal RNA
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: Rcm1 is necessary and sufficient for the formation of a large C2278-methylated subpopulation of ribosomes, both under normal and oxidative stress conditions
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the methylated residues m5C2278 stabilizes the structure of 25S rRNA and consequently the association of ribosomal proteins with the large ribosomal subunit
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is specific for cytosine2278 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is responsible for the methylation at cytosine2278 of the 25S ribosomal RNA
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is specific for cytosine2278 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: Rcm1 is necessary and sufficient for the formation of a large C2278-methylated subpopulation of ribosomes, both under normal and oxidative stress conditions
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is specific for cytosine2278 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the methylated residues m5C2278 stabilizes the structure of 25S rRNA and consequently the association of ribosomal proteins with the large ribosomal subunit
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is responsible for the methylation at cytosine2278 of the 25S ribosomal RNA
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: Rcm1 is necessary and sufficient for the formation of a large C2278-methylated subpopulation of ribosomes, both under normal and oxidative stress conditions
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the methylated residues m5C2278 stabilizes the structure of 25S rRNA and consequently the association of ribosomal proteins with the large ribosomal subunit
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the enzyme is responsible for the methylation at cytosine2278 of the 25S ribosomal RNA
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: Rcm1 is necessary and sufficient for the formation of a large C2278-methylated subpopulation of ribosomes, both under normal and oxidative stress conditions
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine2278 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA
Substrates: the methylated residues m5C2278 stabilizes the structure of 25S rRNA and consequently the association of ribosomal proteins with the large ribosomal subunit
Products: -
Products: -
?
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
RNA polymerase I activity and the N-terminal domain are required for nucleolar localization of NSUN5
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
deletion of Rcm1 specifically abolishes the methylation of m5C 2278 in the 25S rRNA. The loss of m5C2278 results in anisomycin hypersensitivity. The deletion of rcm1 does not result in any significant growth defect at 30 and 37°C. Deletion of rcm1 does not disturb the 60S stoichiometry and polysome assembly
malfunction
loss of Rcm1 alters the structural conformation of the ribosome in close proximity to C2278, as well as translational fidelity, and favours recruitment of a distinct subset of oxidative stress-responsive mRNAs into polysomes
malfunction
haploinsufficiency of the NSUN5 gene in fibroblasts from William Beuren syndrome patients causes partial loss of cytidine3782 modification in 28S rRNA
malfunction
-
deletion of Rcm1 specifically abolishes the methylation of m5C 2278 in the 25S rRNA. The loss of m5C2278 results in anisomycin hypersensitivity. The deletion of rcm1 does not result in any significant growth defect at 30 and 37°C. Deletion of rcm1 does not disturb the 60S stoichiometry and polysome assembly
-
malfunction
-
loss of Rcm1 alters the structural conformation of the ribosome in close proximity to C2278, as well as translational fidelity, and favours recruitment of a distinct subset of oxidative stress-responsive mRNAs into polysomes
-
physiological function
the methylated residues m5C2278 stabilizes the structure of 25S rRNA and consequently the association of ribosomal proteins with the large ribosomal subunit
physiological function
loss of Rcm1 alters the structural conformation of the ribosome at C2278, and translational fidelity, and favours recruitment of a subset of oxidative stress-responsive mRNAs into polysomes. The loss increases chronological lifespan and reduces replicative lifespan
physiological function
reduction of Nsun5 by RNAi increases chronological lifespan and survival on elevated temperature
physiological function
reduction of Nsun5 by RNAi increases lifespan and survival upon treatment with paraquat
physiological function
NSUN5 loss generates an unmethylated status at the C3782 position of 28S rRNA that drives an overall depletion of protein synthesis, and leads to the emergence of an adaptive translational program for survival under conditions of cellular stress
physiological function
loss of NSUN5 impairs growth of cells, reduces global protein translation but does not affect ribosome biogenesis and fidelity
physiological function
deletion of exon 1 of the Nsun5 gene in mice leads to a decrease in body weight by about 10% in both sexes. Expression of mouse Nsun5 can rescue loss of Nsun5 in human cells
physiological function
knockdown of NSUN5 impairs the proliferation capacity of esophageal cancer cells and arrests cell cycle at the G0/G1 phase.Enforced expression of NSUN5 accelerates esophageal cancer progression. Deficiency of NSUN5 significantly reduces tumor growth in a cell?based xenograft mouse model. NSUN5 positively regulates expression of METTL1 binding directly to the METTL1 transcript
physiological function
-
loss of Rcm1 alters the structural conformation of the ribosome at C2278, and translational fidelity, and favours recruitment of a subset of oxidative stress-responsive mRNAs into polysomes. The loss increases chronological lifespan and reduces replicative lifespan
-
physiological function
-
the methylated residues m5C2278 stabilizes the structure of 25S rRNA and consequently the association of ribosomal proteins with the large ribosomal subunit
-
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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). RCM1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
490
0
56177
Swiss-Prot
-
NSUN5_MOUSE
465
0
51030
Swiss-Prot
other Location (Reliability: 3)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C308S
C308S
contrary to wild-type, mutant does not rescue C3782 methylation defects
C308S
contrary to wild-type, mutant does not rescue C3782 methylation defects
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulated in chronologically aged yeast cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
human glioma cells undergo DNA methylation-associated epigenetic silencing of NSUN5. NSUN5 epigenetic inactivation renders the gliomas sensitive to bioactivatable substrates of the stress-related enzyme NQO1 and is a hallmark of glioma patients with long-term survival for this disease
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schosserer, M.; Minois, N.; Angerer, T.B.; Amring, M.; Dellago, H.; Harreither, E.; Calle-Perez, A.; Pircher, A.; Gerstl, M.P.; Pfeifenberger, S.; Brandl, C.; Sonntagbauer, M.; Kriegner, A.; Linder, A.; Weinhaeusel, A.; Mohr, T.; Steiger, M.; Mattanovich, D.; Rinnerthaler, M.; Karl, T.; Sharma, S.
Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating organismal lifespan
Nat. Commun.
6
6158
2015
Caenorhabditis elegans (Q9NAA7), Drosophila melanogaster (Q9VDZ4), Saccharomyces cerevisiae (P53972), Saccharomyces cerevisiae ATCC 204508 (P53972)
brenda
Sharma, S.; Yang, J.; Watzinger, P.; Koetter, P.; Entian, K.D.
Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively
Nucleic Acids Res.
41
9062-9076
2013
Saccharomyces cerevisiae (P53972), Saccharomyces cerevisiae ATCC 204508 (P53972)
brenda
Gigova, A.; Duggimpudi, S.; Pollex, T.; Schaefer, M.; Kos, M.
A cluster of methylations in the domain IV of 25S rRNA is required for ribosome stability
RNA
20
1632-1644
2014
Saccharomyces cerevisiae (P53972), Saccharomyces cerevisiae ATCC 204508 (P53972)
brenda
Janin, M.; Ortiz-Barahona, V.; Castro de Moura, M.; Martinez-Cardus, A.; Llinas-Arias, P.; Soler, M.; Nachmani, D.; Pelletier, J.; Schumann, U.; Calleja-Cervantes, M.E.; Moran, S.; Guil , S.
Epigenetic loss of RNA-methyltransferase NSUN5 in glioma targets ribosomes to drive a stress adaptive translational program
Acta Neuropathol.
138
1053-1074
2019
Homo sapiens (Q96P11)
brenda
Cui, Y.; Hu, Z.; Zhang, C.
RNA methyltransferase NSUN5 promotes esophageal cancer via 5-methylcytosine modification of METTL1
Mol. Carcinog.
64
399-409
2025
Homo sapiens (Q96P11)
brenda
Heissenberger, C.; Liendl, L.; Nagelreiter, F.; Gonskikh, Y.; Yang, G.; Stelzer, E.M.; Krammer, T.L.; Micutkova, L.
Loss of the ribosomal RNA methyltransferase NSUN5 impairs global protein synthesis and normal growth
Nucleic Acids Res.
47
11807-11825
2019
Homo sapiens (Q96P11), Mus musculus (Q8K4F6)
brenda
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