Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.319 extracted from

  • Cha, B.; Park, Y.; Hwang, B.N.; Kim, S.Y.; Jho, E.H.
    Protein arginine methyltransferase 1 methylates Smurf2 (2015), Mol. Cells, 38, 723-728.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.319

Cloned(Commentary)

Cloned (Comment) Organism
-
 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [Smurf2]-L-arginine Smurf2, i.e. a member of the HECT domain E3 ligase family. Smurf2, not Smurf1, is methylated by PRMT1. Among the type I PRMT family, only PRMT1 shows activity for Smurf2. Methylation sites are located within amino acid region 224-298 of Smurf2 Mus musculus S-adenosyl-L-homocysteine + [Smurf2]-Nomega-methyl-L-arginine
-
 ?
S-adenosyl-L-methionine + [Smurf2]-Nomega-methyl-L-arginine Smurf2, i.e. a member of the HECT domain E3 ligase family. Smurf2, not Smurf1, is methylated by PRMT1. Among the type I PRMT family, only PRMT1 shows activity for Smurf2. Methylation sites are located within amino acid region 224-298 of Smurf2 Mus musculus S-adenosyl-L-homocysteine + [Smurf2]-Nomega,Nomega-dimethyl-L-arginine
-
 ?

General Information

General Information Comment Organism
physiological function knockdown of isoform PRMT1 results in increased Smurf2 expression as well as inhibition of TGF-beta-mediated reporter activity Mus musculus