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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 2.1.1.320

Accepted Name
Type II protein arginine methyltransferase.
Reaction catalysed
2 S-adenosyl-L-methionine + [protein]-L-arginine <=> 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine
Comment(s)
  • The enzyme catalyzes 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, EC 2.1.1.321 and EC 2.1.1.322.
  • Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.
Cross-references
BRENDA2.1.1.320
EC2PDB2.1.1.320
ExplorEnz2.1.1.320
PRIAM enzyme-specific profiles2.1.1.320
KEGG Ligand Database for Enzyme Nomenclature2.1.1.320
IUBMB Enzyme Nomenclature2.1.1.320
IntEnz2.1.1.320
MEDLINEFind literature relating to 2.1.1.320
MetaCyc2.1.1.320
UniProtKB/Swiss-Prot
A7YW45, ANM5_BOVIN;  P46580, ANM5_CAEEL;  Q54KI3, ANM5_DICDI;  
O14744, ANM5_HUMAN;  Q4R5M3, ANM5_MACFA;  Q8CIG8, ANM5_MOUSE;  
A2X0Q3, ANM5_ORYSI;  Q6YXZ7, ANM5_ORYSJ;  Q5R698, ANM5_PONAB;  
Q6NUA1, ANM5_XENLA;  Q6P2P2, ANM9_HUMAN;  Q3U3W5, ANM9_MOUSE;  
A0JMU5, ANM9_XENLA;  P38274, HSL7_YEAST;  Q2KHV5, NDUF7_BOVIN;  
Q09644, NDUF7_CAEEL;  Q08BY0, NDUF7_DANRE;  Q54S83, NDUF7_DICDI;  
Q9VGR2, NDUF7_DROME;  Q7L592, NDUF7_HUMAN;  Q9CWG8, NDUF7_MOUSE;  
Q5XI79, NDUF7_RAT;  O14138, NDUF7_SCHPO;  Q6GQ37, NDUF7_XENLA;  
Q5BKM6, NDUF7_XENTR;  P36052, NDUF7_YEAST;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
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