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Literature summary for 2.1.1.319 extracted from
- Comparative monomethylarginine proteomics suggests that protein arginine methyltransferase 1 (PRMT1) is a significant contributor to arginine monomethylation in Toxoplasma gondii (2017), Mol. Cell. Proteomics, 16, 567-580 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Toxoplasma gondii | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | identification of TgPRMT1 substrates. A number of candidate PRMT1 substrates are identified in this study. A significant proportion of candidate TgPRMT1 substrates localize to the nucleus | Toxoplasma gondii | ? | - |
- |
 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PRMT1 | - |
Toxoplasma gondii |
| protein arginine methyltransferase 1 | - |
Toxoplasma gondii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme (PRMT1) is important for cell division and growth. The enzyme (PRMT1) is a significant contributor to arginine monomethylation in Toxoplasma gondii | Toxoplasma gondii |
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