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Literature summary for 2.1.1.204 extracted from

  • Shanmugam, R.; Fierer, J.; Kaiser, S.; Helm, M.; Jurkowski, T.P.; Jeltsch, A.
    Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences (2015), Cell Discov., 1, 15010 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.204

Protein Variants

Protein Variants Comment Organism
additional information generation of Dnmt2 knockout (KO) cells Homo sapiens
additional information generation of Dnmt2 knockout murine embryonic fibroblast cells Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetic model Mus musculus
additional information
-
 additional information Michaelis-Menten kinetic model Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + cytosine38 in tRNAAsp Mus musculus
-
 S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
 ?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp Homo sapiens
-
 S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens O14717
-
-
Mus musculus O55055
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryonic fibroblast
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
 Mus musculus S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
 ?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
 Homo sapiens S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
 ?

Synonyms

Synonyms Comment Organism
Dnmt2
-
 Mus musculus
Dnmt2
-
 Homo sapiens
RNA methyltransferase
-
 Mus musculus
RNA methyltransferase
-
 Homo sapiens
TRDMT1
-
 Mus musculus
TRDMT1
-
 Homo sapiens

Cofactor

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

General Information

General Information Comment Organism
malfunction a 30% reduced charging level of tRNA-Asp is observed in Dnmt2 knockout (KO) murine embryonic fibroblast cells. Synthesis of endogenous proteins with poly-Asp sequences is reduced in Dnmt2 KO cells. Protein degradation does not cause reduction of protein level in Dnmt2 KO cells Mus musculus
metabolism analysis of aminoacylation of C38-methylated and unmethylated tRNAAsp Mus musculus
metabolism analysis of aminoacylation of C38-methylated and unmethylated tRNAAsp Homo sapiens
physiological function Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp. Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences. Mouse aspartyl-tRNA synthetase shows a 4 to 5fold preference for C38-methylated tRNA-Asp. Dnmt2-mediated C38 methylation of tRNA-Asp regulates the translation of proteins containing poly-Asp sequences. Cytosine-38 methylation of tRNAAsp increases the rate of its aminoacylation Mus musculus
physiological function Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp. Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences. Proteins containing poly-Asp sequences in the human proteome often have roles in transcriptional regulation and gene expression. Hence, the Dnmt2-mediated methylation of tRNA-Asp exhibits a post-transcriptional regulatory role by controlling the synthesis of a group of target proteins containing poly-Asp sequences. Cytosine-38 methylation of tRNAAsp increases the rate of its aminoacylation Homo sapiens