2.1.1.204: tRNA (cytosine38-C5)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (cytosine38-C5)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.204
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2.1.1.204
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methyltransferases
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n6-methyladenosine
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5-methylcytosine
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mtases
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2'-o-methylation
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epitranscriptomic
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methyltransferase-like
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2'-o-methyltransferase
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piwi-interacting
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mettl16
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spout
- 2.1.1.204
- methyltransferases
- n6-methyladenosine
- 5-methylcytosine
- mtases
-
2'-o-methylation
-
epitranscriptomic
-
methyltransferase-like
-
2'-o-methyltransferase
-
piwi-interacting
- mettl16
-
spout
Reaction
Synonyms
(cytosine-5) RNA methyltransferase, cytosine-5 tRNA methyltransferase, dDnmt2, DNA methyltransferase 2, DnmA, Dnmt2, DNMT2 methyltransferase, EC 2.1.1.29, hDNMT2, Pf-DNMT2, PMT1, pombe methyltransferase 1, RCMT, RNA methyltransferase, spDnmt2, transfer RNA aspartic acid methyltransferase 1, TRDMT1, tRNA aspartic acid methyltransferase 1, tRNA-aspartic acid methyltransferase 1
ECTree
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Localization
Localization on EC 2.1.1.204 - tRNA (cytosine38-C5)-methyltransferase
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additional information
granular cytoplasmic distribution with minor signals in the nucleus. Large structures appear in the cytoplasm and in the nucleus upon heat stress
human DNMT2 protein (hDNMT2) is primarily localized to the cytoplasm of transfected mouse 3T3 fibroblasts
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Dnmt2 is both a cytoplasmic and a nuclear protein. A significant amount of Dnmt2 is bound to the nuclear matrix. Dnmt2-EGFP(enhanced-green-fluorescent-protein) enters prophase nuclei and shows a spindle-like localization pattern during mitotic divisions. This localization is microtubule dependent. Dnmt2 can access DNA during mitotic cell divisions
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the major function of the N-terminal domain is to determine subcellular localization of the enzyme
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additional information
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the major function of the N-terminal domain is to determine subcellular localization of the enzyme
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additional information
the major function of the N-terminal domain is to determine subcellular localization of the enzyme
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