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Literature summary for 2.1.1.319 extracted from
- A novel splicing isoform of protein arginine methyltransferase 1 (PRMT1) that lacks the dimerization arm and correlates with cellular malignancy (2018), J. Cell. Biochem., 119, 2110-2123 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q99873 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PRMT1 | - |
Homo sapiens |
| protein arginine methyltransferase 1 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | a splicing isoform is characterized which does not affect the amino-terminus of the protein like the seven known isoforms, but rather lacks exons 8 and 9 which encode the dimerization arm of the enzyme that is essential for enzymatic activity. Consequently, the isoform does not form catalytically active oligomers with the other endogenous PRMT1 isoforms. This isoform is found in a variety of cell lines, but is increased in cell lines of cancer origin or after expression of the EMT-inducing transcriptional repressor Snail1. The novel isoform could act as a modulator of PRMT1 activity in cancer cells by acting as a competitive inhibitor that shields substrates from access to active PRMT1 oligomers | Homo sapiens |
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Release 2023.1 (January 2023)
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