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Literature summary for 2.1.1.319 extracted from

  • Tang, J.; Kao, P.N.; Herschman, H.R.
    Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3 (2000), J. Biol. Chem., 275, 19866-19876.
    View publication on PubMed
Search for more literature for 2.1.1.319

Activating Compound

Activating Compound Comment Organism Structure
interleukin enhancer-binding factor ILF3 isoform PRMT1 and ILF3 coprecipitate in immunoprecipitation assays and can be isolated together in pull-down experiments. ILF3 is a robust substrate for methylation by PRMT1 and can modulate PRMT1 activity in in vitro methylation assays. The COOH-terminal region of ILF3, rich in arginine, glycine, and serine, is responsible for the strong interaction between PRMT1 and ILF3 and is the site of ILF3 methylation by PRMT1 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus isoform PRMT1 and interleukin enhancer-binding factor ILF3 colocalize in the nucleus Homo sapiens 5634
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q99873 isoform PRMT1
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Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [interleukin enhancer-binding factor ILF3]-L-arginine
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 Homo sapiens S-adenosyl-L-homocysteine + [interleukin enhancer-binding factor ILF3]-Nomega-methyl-L-arginine the COOH-terminal region of ILF3, rich in arginine, glycine, and serine, is responsible for the strong interaction between PRMT1 and ILF3 and is the site of ILF3 methylation by PRMT1 ?
S-adenosyl-L-methionine + [interleukin enhancer-binding factor ILF3]-Nomega-methyl-L-arginine
-
 Homo sapiens S-adenosyl-L-homocysteine + [interleukin enhancer-binding factor ILF3]-Nomega,Nomega-dimethyl-L-arginine the COOH-terminal region of ILF3, rich in arginine, glycine, and serine, is responsible for the strong interaction between PRMT1 and ILF3 and is the site of ILF3 methylation by PRMT1 ?

Synonyms

Synonyms Comment Organism
PRMT1
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 Homo sapiens