Cloned (Comment) | Organism |
---|---|
gene METTL11A | Mus musculus |
gene METTL11A, cloning of the His-tagged human enzyme using vector pET-100/DTOPO that carries a His6 tag in the linker region MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDHPFT, which is incorporated before the initiator methionine residue of the cloned protein, and expression in Escherichia coli strain BL21(DE3) | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the intact dimethylated Rpl12ab species isolated from the YBR261C/tae1 deletion strain is fragmented, and a b20 ion is detected with the addition of one methyl group, suggesting partial methylation of lysine 3. Neither of these species is dimethylated at the N-terminal residue. Rps25a/Rps25b isolated from the YBR261C/tae1 deletion strain is 28 Da less than the wild type, and the fragmentation data indicate no methylation is present | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Mus musculus | 5829 | - |
cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b. The yeast RPS25A and RPS25B genes and differ only at a single amino acid residue | ? | - |
? | |
S-adenosyl-L-methionine + Rpl12ab | Saccharomyces cerevisiae | methylation of Rpl12ab at the N-terminal proline residue | ? | - |
? | |
S-adenosyl-L-methionine + Rps25a | Saccharomyces cerevisiae | - |
? | - |
? | |
S-adenosyl-L-methionine + Rps25b | Saccharomyces cerevisiae | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9BV86 | gene METTL11A | - |
Mus musculus | - |
genes METTL11A and METTL11B | - |
Saccharomyces cerevisiae | - |
strains BY4742 and BY4741 and the YBR261C/tae1 deletion strain in each background, gene YBR261C/TAE1 | - |
Purification (Comment) | Organism |
---|---|
native enzyme partially from heart cell cytosol | Mus musculus |
recombinant His-tagged METTL11A from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
heart | high enzyme expression levels | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b. The yeast RPS25A and RPS25B genes and differ only at a single amino acid residue | Saccharomyces cerevisiae | ? | - |
? | |
additional information | the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, but the proline residue in position 1 is a preferred substrate | Homo sapiens | ? | - |
? | |
additional information | the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The yeast enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, although to a lesser extent, the proline residue in position 1 is a preferred substrate | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + APKQQLSKY | synthetic peptide, modified Rps25a/Rps25b-derived peptide | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + APKQQLSKY | synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide | Mus musculus | ? | - |
? | |
S-adenosyl-L-methionine + APKQQLSKY | synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide | Homo sapiens | ? | - |
? | |
S-adenosyl-L-methionine + PPKQQLSKY | synthetic peptide, Rps25a/Rps25b-derived peptide | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + PPKQQLSKY | synthetic peptide, yeast protein Rps25a/Rps25b-derived peptide | Mus musculus | ? | - |
? | |
S-adenosyl-L-methionine + PPKQQLSKY | synthetic peptide, yeast protein Rps25a/Rps25b-derived peptide | Homo sapiens | ? | - |
? | |
S-adenosyl-L-methionine + Rpl12ab | methylation of Rpl12ab at the N-terminal proline residue | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + Rps25a | - |
Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + Rps25a | Rps25a and Rps25b differ only at position 104, a threonine residue is present in the former and an alanine residue in the latter | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + Rps25b | - |
Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + Rps25b | Rps25a and Rps25b differ only at position 104, a threonine residue is present in the former and an alanine residue in the latter | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + SPKQQLSKY | synthetic peptide, modified Rps25a/Rps25b-derived peptide | Saccharomyces cerevisiae | ? | - |
? | |
S-adenosyl-L-methionine + SPKQQLSKY | synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide | Mus musculus | ? | - |
? | |
S-adenosyl-L-methionine + SPKQQLSKY | synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme is a seven beta-strand methyltransferase | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
METT11B | - |
Mus musculus |
METTL11A | - |
Mus musculus |
METTL11A | - |
Homo sapiens |
Ntm1 | - |
Saccharomyces cerevisiae |
NTMT1 | - |
Homo sapiens |
YBR261C/Tae1 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Mus musculus |
22 | - |
assay at room temperature | Saccharomyces cerevisiae |
22 | - |
assay at room temperature | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Mus musculus |
7 | - |
assay at | Saccharomyces cerevisiae |
7 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Mus musculus | |
S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae | |
S-adenosyl-L-methionine | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | loss of the Saccharomyces cerevisiae ORF YBR261c/TAE results in the loss of the N-terminal methylation of both Rpl12ab and Rps25a/Rps25b | Saccharomyces cerevisiae |
physiological function | protein X-Pro-Lys N-terminal methylation reactions catalyzed by the enzyme may be widespread in nature | Homo sapiens |
physiological function | the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b, the YBR261C/TAE1 product is necessary for the formation of the dimethylproline residue in each of these ribosomal proteins. Protein X-Pro-Lys N-terminal methylation reactions catalyzed by the enzyme may be widespread in nature | Saccharomyces cerevisiae |