Literature summary for 2.1.1.319 extracted from

Berberich, H.; Terwesten, F.; Rakow, S.; Sahu, P.; Bouchard, C.; Meixner, M.; Philipsen, S.; Kolb, P.; Bauer, U.M.
Identification and insilico structural analysis of Gallus gallus protein arginine methyltransferase 4 (PRMT4) (2017), FEBS open bio, 7, 1909-1923 .

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 S-adenosyl-L-methionine + [histone H3R17]-L-arginine	Gallus gallus	-	2 S-adenosyl-L-homocysteine + [histone H3R17]-Nomega,Nomega-dimethyl-L-arginine	-	?

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	A0A2D3I4C6	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
macrophage	-	Gallus gallus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 S-adenosyl-L-methionine + [histone H3R17]-L-arginine	-	Gallus gallus	2 S-adenosyl-L-homocysteine + [histone H3R17]-Nomega,Nomega-dimethyl-L-arginine	-	?

Synonyms

Synonyms	Comment	Organism
PRMT4	-	Gallus gallus
protein arginine methyltransferase 4	-	Gallus gallus

General Information

General Information	Comment	Organism
physiological function	protein arginine methyltransferase 4 (PRMT4) is an essential epigenetic regulator of fundamental and conserved processes during vertebrate development, such as pluripotency and differentiation	Gallus gallus

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Release 2023.1 (January 2023)