Cloned (Comment) | Organism |
---|---|
alternative splicing of the full-length DNMT2 premRNA occurs in preimplantation embryos | Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | the major function of the N-terminal domain is to determine subcellular localization of the enzyme | Homo sapiens | - |
- |
additional information | the major function of the N-terminal domain is to determine subcellular localization of the enzyme | Bos taurus | - |
- |
additional information | the major function of the N-terminal domain is to determine subcellular localization of the enzyme | Mus musculus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | ? | - |
? | |
additional information | Bos taurus | the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | ? | - |
? | |
additional information | Mus musculus | the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | ? | - |
? | |
S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Homo sapiens | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Bos taurus | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Mus musculus | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Homo sapiens | - |
- |
- |
Mus musculus | O55055 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | early | Homo sapiens | - |
embryo | early | Mus musculus | - |
embryo | early, DNMT2 gene transcript in bovine preimplantation embryos is expressed at the 2-cell, 4-cell, 8-cell, 16-cell, morula and blastocyst stage embryos | Bos taurus | - |
additional information | developmental expression analysis of DNMT2, overview | Mus musculus | - |
additional information | in humans, DNMT2 mRNA is not transcribed in either any follicular stages of primordial, primary and secondary or in the GV, MI, and MII oocytes at Day 0 or Day 1, except for presence of a limited expression of DNMT2 in the MII oocytes, developmental expression analysis of DNMT2, overview | Homo sapiens | - |
additional information | the Dnmt2 mRNA is present at very low levels during early bovine preimplantation development, but its expression remarkably increases at morula stage, developmental expression analysis of DNMT2, overview | Bos taurus | - |
oocyte | - |
Homo sapiens | - |
oocyte | - |
Bos taurus | - |
oocyte | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | Homo sapiens | ? | - |
? | |
additional information | the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | Bos taurus | ? | - |
? | |
additional information | the enzyme DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | Mus musculus | ? | - |
? | |
S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Homo sapiens | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Bos taurus | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Mus musculus | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Dnmt2 | - |
Homo sapiens |
Dnmt2 | - |
Bos taurus |
Dnmt2 | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Homo sapiens | |
S-adenosyl-L-methionine | - |
Bos taurus | |
S-adenosyl-L-methionine | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
evolution | DNMT2 exhibits different expression patterns in different mammalian species. General structure of mammalian DNMTs: the enzymes are composed of three main parts: N-terminal regulatory domain, central linker region, and C-terminal catalytic domain. The N-terminal regulatory domain includes the following subdomains: charge rich-region, proliferating cell nuclear antigen-binding, nuclear localization signal, cytosine-rich zinc finger DNA-binding, polybromo homology, and tetrapeptide chromatin binding. The C-terminal catalytic domain includes six conserved motifs: the motif I contains an AdoMet binding site, the motif IV binds to substrate cytosine at its active site, the motif VI involves glutamyl residues serving as a donor, the motif IX maintains stability of the substrate-binding site, and the motif X functions in formation of the AdoMet binding site. DNMT2 is structurally and functionally different from other DNMTs because it does not possess the N-terminal regulatory domain | Homo sapiens |
evolution | DNMT2 exhibits different expression patterns in different mammalian species. General structure of mammalian DNMTs: the enzymes are composed of three main parts: N-terminal regulatory domain, central linker region, and C-terminal catalytic domain. The N-terminal regulatory domain includes the following subdomains: charge rich-region, proliferating cell nuclear antigen-binding, nuclear localization signal, cytosine-rich zinc finger DNA-binding, polybromo homology, and tetrapeptide chromatin binding. The C-terminal catalytic domain includes six conserved motifs: the motif I contains an AdoMet binding site, the motif IV binds to substrate cytosine at its active site, the motif VI involves glutamyl residues serving as a donor, the motif IX maintains stability of the substrate-binding site, and the motif X functions in formation of the AdoMet binding site. DNMT2 is structurally and functionally different from other DNMTs because it does not possess the N-terminal regulatory domain | Bos taurus |
evolution | DNMT2 exhibits different expression patterns in different mammalian species. General structure of mammalian DNMTs: the enzymes are composed of three main parts: N-terminal regulatory domain, central linker region, and C-terminal catalytic domain. The N-terminal regulatory domain includes the following subdomains: charge rich-region, proliferating cell nuclear antigen-binding, nuclear localization signal, cytosine-rich zinc finger DNA-binding, polybromo homology, and tetrapeptide chromatin binding. The C-terminal catalytic domain includes six conserved motifs: the motif I contains an AdoMet binding site, the motif IV binds to substrate cytosine at its active site, the motif VI involves glutamyl residues serving as a donor, the motif IX maintains stability of the substrate-binding site, and the motif X functions in formation of the AdoMet binding site. DNMT2 is structurally and functionally different from other DNMTs because it does not possess the N-terminal regulatory domain | Mus musculus |
malfunction | the Dnmt2 knockout mouse model does not exhibit any phenotypic defects in the mouse model. The enzyme knockout causes disruption of RNA methyltransferase activity | Mus musculus |
malfunction | the enzyme knockout causes disruption of RNA methyltransferase activity | Homo sapiens |
malfunction | the enzyme knockout causes disruption of RNA methyltransferase activity | Bos taurus |
physiological function | though DNMT2 has a catalytic domain at its C-terminus, it cannot catalyze either de novo or maintenance methylation process due to the absence of the N-terminal domain that enables other DNMT enzymes to bind DNA sequences and other regulatory proteins. DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | Homo sapiens |
physiological function | though DNMT2 has a catalytic domain at its C-terminus, it cannot catalyze either de novo or maintenance methylation process due to the absence of the N-terminal domain that enables other DNMT enzymes to bind DNA sequences and other regulatory proteins. DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | Bos taurus |
physiological function | though DNMT2 has a catalytic domain at its C-terminus, it cannot catalyze either de novo or maintenance methylation process due to the absence of the N-terminal domain that enables other DNMT enzymes to bind DNA sequences and other regulatory proteins. DNMT2 is responsible for methylation of cytosine 38 in the anticodon loop of aspartic acid transfer RNA instead of transferring methyl group to the cytosine residues of DNA | Mus musculus |