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Literature summary for 2.1.1.321 extracted from
- PRMT7 interacts with ASS1 and citrullinemia mutations disrupt the interaction (2017), J. Mol. Biol., 429, 2278-2289 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9NVM4 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | argininosuccinate synthetase (ASS1) specifically interacts with PRMT7 and that mutations in ASS1 at the interaction interface of PRMT7-ASS1 are detrimental. The interaction of PRMT7 with ASS1 implies that ASS1 might be a plausible substrate of PRMT7 | Homo sapiens | ? | - |
- |
 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PRMT7 | - |
Homo sapiens |
| protein arginine methyltransferase 7 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme (PRMT7) catalyzes the introduction of mono methylation marks at the arginine residues of substrate proteins. PRMT7 plays important roles in the regulation of gene expression, splicing, DNA damage, paternal imprinting, cancer and metastasis | Homo sapiens |
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