EC 2.1.1.319 - Type I protein arginine methyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.319

Names

Accepted name:
type I protein arginine methyltransferase
Other names:
PRMT1 (gene name)
PRMT2 (gene name)
PRMT3 (gene name)
PRMT4 (gene name)
PRMT6 (gene name)
PRMT8 (gene name)
RMT1 (gene name)
CARM1 (gene name)
Systematic name:
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω-dimethyl-L-arginine-forming)

Reaction

Comments:

This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues [1]. PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells [2]. cf. EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0035242
UniProtKB/Swiss-Prot: (51) [show] [UniProt]

References

  1. Gary, J. D., Clarke, S.
    RNA and protein interactions modulated by protein arginine methylation.
    Prog. Nucleic Acid Res. Mol. Biol. 61: 65-131 (1998). [PMID: 9752719]
  2. Tang, J., Gary, J. D., Clarke, S., Herschman, H. R.
    PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation.
    J. Biol. Chem. 273: 16935-16945 (1998). [PMID: 9642256]
  3. Tang, J., Frankel, A., Cook, R. J., Kim, S., Paik, W. K., Williams, K. R., Clarke, S., Herschman, H. R.
    PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells.
    J. Biol. Chem. 275: 7723-7730 (2000). [PMID: 10713084]
  4. Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S., Bedford, M. T.
    The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity.
    J. Biol. Chem. 277: 3537-3543 (2002). [PMID: 11724789]

[EC 2.1.1.319 created 2015]