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Literature summary extracted from

  • Jain, K.; Clarke, S.G.
    PRMT7 as a unique member of the protein arginine methyltransferase family A review (2019), Arch. Biochem. Biophys., 665, 36-45 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.321
-
 Caenorhabditis elegans
2.1.1.321
-
 Trypanosoma brucei brucei

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.321 NaCl sodium chloride strongly inhibits the activity of the human enzyme. Half maximal activity is seen at about 25 mM with a peptide substrate based on histone H2B and about 200 mM for the GST-GAR protein substrate Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.321 cytoplasm entirely localized to the cytoplasmic fraction in mouse embryo fibroblasts Mus musculus 5737
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.321 S-adenosyl-L-methionine + [histone H4R17]-L-arginine Homo sapiens crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3 S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R17]-L-arginine Mus musculus crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3 S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R3]-L-arginine Homo sapiens
-
 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R3]-L-arginine Mus musculus
-
 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.321 Caenorhabditis elegans Q9XW42
-
-
2.1.1.321 Homo sapiens Q9NVM4
-
-
2.1.1.321 Mus musculus Q922X9
-
-
2.1.1.321 Trypanosoma brucei brucei Q582G4
-
-
2.1.1.321 Trypanosoma brucei brucei 927 Q582G4
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.321 fibroblast embryonic Mus musculus
-
2.1.1.321 HEK-293T cell
-
 Homo sapiens
-
2.1.1.321 MCF-7 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.321 2 S-adenosyl-L-methionine + [protein]-L-arginine the enzyme has a strong preference for RXR motifs surrounded by basic amino acids Homo sapiens 2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
-
 ?
2.1.1.321 2 S-adenosyl-L-methionine + [protein]-L-arginine the enzyme has a strong preference for RXR motifs surrounded by basic amino acids Mus musculus 2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R17]-L-arginine crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3 Homo sapiens S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R17]-L-arginine crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3 Mus musculus S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
-
 Homo sapiens S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
-
 Mus musculus S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [protein]-L-arginine substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues Homo sapiens S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
-
 ?
2.1.1.321 S-adenosyl-L-methionine + [protein]-L-arginine substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues Mus musculus S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.321 PRMT7
-
 Homo sapiens
2.1.1.321 PRMT7
-
 Mus musculus
2.1.1.321 PRMT7
-
 Caenorhabditis elegans
2.1.1.321 PRMT7
-
 Trypanosoma brucei brucei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.321 10 25
-
 Homo sapiens
2.1.1.321 10 25
-
 Mus musculus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.1.321 10 37 the enzyme is most active from 10°C to 25°C with less than 10% of the optimal activity at 37°C in vitro Homo sapiens
2.1.1.321 10 37 the enzyme is most active from 10°C to 25°C with less than 10% of the optimal activity at 37°C in vitro Mus musculus

General Information

EC Number General Information Comment Organism
2.1.1.321 malfunction defects in muscle stem cells (satellite cells) and immune cells are found in mouse Prmt7 homozygous knockout Mus musculus
2.1.1.321 malfunction defects in muscle stem cells (satellite cells) and immune cells are found in mouse Prmt7 homozygous knockouts Mus musculus
2.1.1.321 malfunction humans lacking PRMT7 are characterized by significant intellectual developmental delays, hypotonia, and facial dysmorphisms Homo sapiens
2.1.1.321 malfunction humans lacking PRMT7 are characterized by significant intellectual developmental delays, hypotonia, and facial dysmorphisms. The overexpression of the PRMT7 gene is correlated with cancer metastasis in humans Homo sapiens
2.1.1.321 metabolism overexpression of the PRMT7 gene is correlated with cancer metastasis in humans Homo sapiens
2.1.1.321 physiological function in human cell lines PRMT7 expression and subsequent methylation of histone H4R3 leads to repression of DNA damage repair genes such as APEX2, POLD1, and POLD2. The enzyme (PRMT7) is involved in regulation of the DNA repair machinery of the cell Homo sapiens