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Literature summary for 2.1.1.204 extracted from

  • Uysal, F.; Akkoyunlu, G.; Ozturk, S.
    Dynamic expression of DNA methyltransferases (DNMTs) in oocytes and early embryos (2015), Biochimie, 116, 103-113.
    View publication on PubMed
Search for more literature for 2.1.1.204

Cloned(Commentary)

Cloned (Comment) Organism
alternative splicing of the full-length DNMT2 premRNA occurs in preimplantation embryos Bos taurus

Localization

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Mus musculus O55055
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryo early Homo sapiens
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embryo early Mus musculus
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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
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additional information developmental expression analysis of DNMT2, overview Mus musculus
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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
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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
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oocyte
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 Homo sapiens
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oocyte
-
 Bos taurus
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oocyte
-
 Mus musculus
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
Dnmt2
-
 Homo sapiens
Dnmt2
-
 Bos taurus
Dnmt2
-
 Mus musculus

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Homo sapiens
S-adenosyl-L-methionine
-
 Bos taurus
S-adenosyl-L-methionine
-
 Mus musculus

General Information

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