| Cloned (Comment) | Organism |
|---|---|
| expression of hexahistidine-tagged Abp140p in Saccharomces cerevisiae | Saccharomyces cerevisiae |
| Protein Variants | Comment | Organism |
|---|---|---|
| D466A | no formation of N3-methylcytosine32 | Saccharomyces cerevisiae |
| D547A | decreased activity | Saccharomyces cerevisiae |
| delD602-Q621 | no formation of N3-methylcytosine32 | Saccharomyces cerevisiae |
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| actin filament | subcellular localization of ABP140 to actin filaments is not involved in tRNA modification | Saccharomyces cerevisiae | 5884 | - |
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 71486 | - |
2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE | Saccharomyces cerevisiae |
| 71500 | - |
2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE | Saccharomyces cerevisiae |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + cytosine32 in tRNA1Ser | Saccharomyces cerevisiae | tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency | S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser | - |
? | |
| S-adenosyl-L-methionine + cytosine32 in tRNA1Thr | Saccharomyces cerevisiae | tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency | S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr | - |
? |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q6P1Q9 | - |
- |
| Saccharomyces cerevisiae | Q08641 | - |
- |
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer | (2) | Saccharomyces cerevisiae | |
| S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr | (1) | Saccharomyces cerevisiae |
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HeLa cell | - |
Homo sapiens | - |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + cytosine32 in tRNA1Ser | tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency | Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser | - |
? | |
| S-adenosyl-L-methionine + cytosine32 in tRNA1Ser | tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation | Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser | - |
? | |
| S-adenosyl-L-methionine + cytosine32 in tRNA1Thr | tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency | Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr | - |
? | |
| S-adenosyl-L-methionine + cytosine32 in tRNA1Thr | tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation | Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr | - |
? |
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE | Saccharomyces cerevisiae |
| dimer | 2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE | Saccharomyces cerevisiae |
| Synonyms | Comment | Organism |
|---|---|---|
| ABP140 | - |
Saccharomyces cerevisiae |
| METTL2B | - |
Homo sapiens |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Saccharomyces cerevisiae |
| General Information | Comment | Organism |
|---|---|---|
| malfunction | N3-methylcytosine32 modification is absent in strains that lack the entire ABP140 gene | Saccharomyces cerevisiae |
| malfunction | specific reduction of N3-methylcytosine formation in HeLa cells by siRNA-mediated knock down of METTL2B | Homo sapiens |
| physiological function | N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency | Saccharomyces cerevisiae |