Literature summary for 2.1.1.320 extracted from

Gonsalvez, G.B.; Tian, L.; Ospina, J.K.; Boisvert, F.M.; Lamond, A.I.; Matera, A.G.
Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins (2007), J. Cell Biol., 178, 733-740.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O14744	isoform PRMT5	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HeLa cell	-	Homo sapiens	-

General Information

General Information	Comment	Organism
physiological function	knockdown of isoform PRMT5 results in a reduction in symmetric dimethyl arginine modifcation of the SM protein set of small nuclear ribonucleoproteins. A similar effect is observed when cells are treated with siRNAs targeting methylosome protein MEP50. Isoform PRMT7, EC 2.1.1.321, knockdown also causes a reduction in Sm protein symmetric dimethylarginine modification. Double depletion of both PRMT5 and PRMT7 does not disrupt the modification to a greater extent than either single depletion alone. PRMT7 is not able to restore symmetric dimethylarginine modification of the Sm proteins in cells that are depleted of PRMT5. Cytoplasmic small nuclear ribonucleoprotein assembly requires the activities of both PRMT5 and PRMT7, and Sm protein symmetric dimethylarginine modification is primarily required for cytoplasmic small nuclear ribonucleoprotein assembly	Homo sapiens

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Release 2023.1 (January 2023)