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show all sequences of 2.1.1.204

Dynamic expression of DNA methyltransferases (DNMTs) in oocytes and early embryos

Uysal, F.; Akkoyunlu, G.; Ozturk, S.; Biochimie 116, 103-113 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
alternative splicing of the full-length DNMT2 premRNA occurs in preimplantation embryos
Bos taurus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
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
Homo sapiens
-
-
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Mus musculus
O55055
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
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
-
embryo
early
Homo sapiens
-
embryo
early
Mus musculus
-
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
-
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
developmental expression analysis of DNMT2, overview
Mus musculus
-
oocyte
-
Bos taurus
-
oocyte
-
Homo sapiens
-
oocyte
-
Mus musculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
735727
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
735727
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
735727
Mus musculus
?
-
-
-
-
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
735727
Homo sapiens
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
735727
Bos taurus
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
735727
Mus musculus
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Bos taurus
S-adenosyl-L-methionine
-
Mus musculus
S-adenosyl-L-methionine
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
alternative splicing of the full-length DNMT2 premRNA occurs in preimplantation embryos
Bos taurus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Bos taurus
S-adenosyl-L-methionine
-
Mus musculus
S-adenosyl-L-methionine
-
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
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
Homo sapiens
-
-
additional information
the major function of the N-terminal domain is to determine subcellular localization of the enzyme
Mus musculus
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
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
-
embryo
early
Homo sapiens
-
embryo
early
Mus musculus
-
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
-
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
developmental expression analysis of DNMT2, overview
Mus musculus
-
oocyte
-
Bos taurus
-
oocyte
-
Homo sapiens
-
oocyte
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
735727
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
735727
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
735727
Mus musculus
?
-
-
-
-
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
735727
Homo sapiens
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
735727
Bos taurus
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
735727
Mus musculus
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
-
-
?
General Information
General Information
Commentary
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
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
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
Mus musculus
malfunction
the enzyme knockout causes disruption of RNA methyltransferase activity
Bos taurus
malfunction
the enzyme knockout causes disruption of RNA methyltransferase activity
Homo sapiens
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
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
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
Mus musculus
General Information (protein specific)
General Information
Commentary
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
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
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
Mus musculus
malfunction
the enzyme knockout causes disruption of RNA methyltransferase activity
Bos taurus
malfunction
the enzyme knockout causes disruption of RNA methyltransferase activity
Homo sapiens
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
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
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
Mus musculus
Other publictions for EC 2.1.1.204
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735726
Elhardt
Somatic cancer mutations in th ...
Homo sapiens
Biochimie
112
66-72
2015
-
-
1
-
13
-
-
-
-
1
-
1
-
1
-
-
1
-
-
1
-
-
1
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1
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1
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1
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1
1
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13
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1
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1
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1
-
1
-
-
1
-
1
-
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1
-
-
-
-
2
2
-
-
-
735727
Uysal
Dynamic expression of DNA meth ...
Bos taurus, Homo sapiens, Mus musculus
Biochimie
116
103-113
2015
-
-
1
-
-
-
-
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3
-
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6
-
3
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9
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6
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3
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1
3
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3
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6
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9
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6
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9
9
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735864
Burgess
Conservation of tRNA and rRNA ...
Arabidopsis thaliana
BMC Plant Biol.
15
199
2015
-
-
-
-
-
-
-
-
1
-
-
2
-
14
-
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2
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1
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1
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1
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2
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2
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3
3
-
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-
736018
Tuorto
The tRNA methyltransferase Dnm ...
Mus musculus, Mus musculus C57BL/6
EMBO J.
34
2350-2362
2015
-
-
-
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1
-
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8
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2
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8
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10
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1
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1
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1
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8
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8
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10
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2
2
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736905
Mueller
Dynamic modulation of Dnmt2-de ...
Dictyostelium discoideum, Schizosaccharomyces pombe
Nucleic Acids Res.
43
10952-10962
2015
2
-
1
-
2
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2
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4
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2
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7
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2
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2
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2
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2
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1
2
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2
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2
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4
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7
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2
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2
-
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3
2
2
3
-
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736775
Militello
A map of 5-methylcytosine resi ...
no activity in Trypanosoma brucei
Mol. Biochem. Parasitol.
193
122-126
2014
-
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-
-
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1
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736856
Khoddami
Identification of direct targe ...
Homo sapiens
Nat. Biotechnol.
31
458-464
2013
-
-
-
-
-
-
2
-
-
-
-
4
-
1
-
-
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1
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1
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-
5
-
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1
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1
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2
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4
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1
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5
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-
-
-
-
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-
1
1
-
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718931
Jurkowski
Mapping the tRNA binding site ...
Homo sapiens
Biochemistry
51
4438-4444
2012
-
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1
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24
-
-
-
-
1
-
1
-
2
-
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1
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3
1
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1
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1
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1
1
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24
-
-
-
-
-
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1
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1
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1
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3
1
-
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-
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1
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1
1
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708588
Schaefer
RNA methylation by Dnmt2 prote ...
Drosophila melanogaster
Genes Dev.
24
1590-1595
2010
-
-
-
-
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-
-
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1
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1
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1
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5
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2
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1
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1
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1
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