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Information on EC 2.1.1.320 - type II protein arginine methyltransferase and Organism(s) Rattus norvegicus and UniProt Accession D4A0E8

for references in articles please use BRENDA:EC2.1.1.320
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EC Tree
IUBMB Comments
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
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Rattus norvegicus
UNIPROT: D4A0E8
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
prmt5, prmt7, protein arginine methyltransferase 5, prmt9, type ii protein arginine methyltransferase, prmt-5, prmt-9, jak-binding protein 1, janus kinase-binding protein 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PRMT5
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-
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PRMT9
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega'-dimethyl-L-arginine-forming)
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PRMT5 expression gradually increases throughout postnatal brain development, coinciding with the period of active myelination
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
D4A0E8_RAT
637
0
72695
TrEMBL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, J.; Vogel, G.; Yu, Z.; Almazan, G.; Richard, S.
Type II arginine methyltransferase PRMT5 regulates gene expression of inhibitors of differentiation/DNA binding Id2 and Id4 during glial cell differentiation
J. Biol. Chem.
286
44424-44432
2011
Mus musculus, Rattus norvegicus (D4A0E8)
Manually annotated by BRENDA team