Crystallization (Comment) | Organism |
---|---|
- |
Caenorhabditis elegans |
- |
Trypanosoma brucei brucei |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | entirely localized to the cytoplasmic fraction in mouse embryo fibroblasts | Mus musculus | 5737 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | - |
? | |
S-adenosyl-L-methionine + [histone H4R3]-L-arginine | Homo sapiens | - |
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine | - |
? | |
S-adenosyl-L-methionine + [histone H4R3]-L-arginine | Mus musculus | - |
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Caenorhabditis elegans | Q9XW42 | - |
- |
Homo sapiens | Q9NVM4 | - |
- |
Mus musculus | Q922X9 | - |
- |
Trypanosoma brucei brucei | Q582G4 | - |
- |
Trypanosoma brucei brucei 927 | Q582G4 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | embryonic | Mus musculus | - |
HEK-293T cell | - |
Homo sapiens | - |
MCF-7 cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
S-adenosyl-L-methionine + [histone H4R3]-L-arginine | - |
Homo sapiens | S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine | - |
? | |
S-adenosyl-L-methionine + [histone H4R3]-L-arginine | - |
Mus musculus | S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine | - |
? | |
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
PRMT7 | - |
Homo sapiens |
PRMT7 | - |
Mus musculus |
PRMT7 | - |
Caenorhabditis elegans |
PRMT7 | - |
Trypanosoma brucei brucei |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
10 | 25 | - |
Homo sapiens |
10 | 25 | - |
Mus musculus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
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 |
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 | Comment | Organism |
---|---|---|
malfunction | defects in muscle stem cells (satellite cells) and immune cells are found in mouse Prmt7 homozygous knockout | Mus musculus |
malfunction | defects in muscle stem cells (satellite cells) and immune cells are found in mouse Prmt7 homozygous knockouts | Mus musculus |
malfunction | humans lacking PRMT7 are characterized by significant intellectual developmental delays, hypotonia, and facial dysmorphisms | Homo sapiens |
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 |
metabolism | overexpression of the PRMT7 gene is correlated with cancer metastasis in humans | Homo sapiens |
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 |