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

BRENDA support

2.1.1.321: type III protein arginine methyltransferase

This is an abbreviated version!
For detailed information about type III protein arginine methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.321

Reaction

S-adenosyl-L-methionine
+
[protein]-L-arginine
=
S-adenosyl-L-homocysteine
+
[protein]-Nomega-methyl-L-arginine

Synonyms

EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, PRMT-7, PRMT7, protein arginine methyltransferase 7

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.321 type III protein arginine methyltransferase

Disease

Disease on EC 2.1.1.321 - type III protein arginine methyltransferase

Please use the Disease Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Automethylation of protein arginine methyltransferase 7 and its impact on breast cancer progression.
PRMT7 contributes to the metastasis phenotype in human non-small-cell lung cancer cells possibly through the interaction with HSPA5 and EEF2.
Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression.
Carcinoma, Hepatocellular
S-adenosylmethionine:protein methyltransferases in hepatomas.
Neoplasm Metastasis
Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions.
PRMT7 contributes to the metastasis phenotype in human non-small-cell lung cancer cells possibly through the interaction with HSPA5 and EEF2.
Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site.
Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.