PRMT1

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title: "PRMT1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["genes-mutated-in-mice"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/genes-mutated-in-mice" source: "https://en.wikipedia.org/wiki/PRMT1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene. The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4.

Function

PRMT1 gene encodes for the protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4 in eukaryotic cells. Specifically altering histone H4 in eukaryotes gives it the ability to remodel chromatin acting as a post-translational modifier.

Through regulation of gene expression, arginine methyltransferases control the cell cycle and death of eukaryotic cells.

Reaction pathway

While all PRMT enzymes catalyze the methylation of arginine residues in proteins, PRMT1 is unique in that is catalyzes the formation of asymmetric dimethylarginine as opposed to the PRMT2 that catalyzes the formation of symmetric dimethylarginine. Individual PRMT utilize S-adenosyl-L-methionine (SAM) as the methyl donor and catalyze methyl group transfer to the ω-nitrogen of an arginine residue.

Clinical significance

In humans, these enzymes regulate gene expression and hence are involved in pathogenesis of many human diseases. Using enzyme inhibitors for arginine methyltransferase 1, studies were able to demonstrate the enzyme's potential as an early catalyst of various cancers.

Interactions

PRMT1 has been shown to interact with:

• BTG1,
• BTG2,
• DHX9,
• FUS,
• HNRNPR,
• HNRPK,
• IFNAR1,
• ILF3,
• KHDRBS1, and
• SUPT5H.

References

References

1. (June 1998). "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)". Genomics.
2. "Entrez Gene: PRMT1 protein arginine methyltransferase 1".
3. (2016-01-01). "Epi-Informatics". Academic Press.
4. (September 2008). "Kinetic mechanism of protein arginine methyltransferase 1". Biochemistry.
5. (2015-01-01). "Epigenetic Technological Applications". Academic Press.
6. (August 2020). "Epigenetics in atherosclerosis: key features and therapeutic implications". Expert Opinion on Therapeutic Targets.
7. (June 1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase". J. Biol. Chem..
8. (January 2002). "Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects". Genes Cells.
9. (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". J. Biol. Chem..
10. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell.
11. (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy". Biochim. Biophys. Acta.
12. (January 1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J..
13. (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep..
14. (June 2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3". J. Biol. Chem..
15. (January 2003). "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1". Mol. Biol. Cell.
16. (April 2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell.

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