Enzyme

Download
EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.319
Description:Type I protein arginine methyltransferase.
Cath: 3.20.20.150; 2.30.29.30; 3.40.50.150; 2.70.160.11;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.319
BRENDA Enzyme Link: BRENDA 2.1.1.319
KEGG Enzyme Link: KEGG2.1.1.319
BioCyc Enzyme Link: BioCyc 2.1.1.319
ExPASy Enzyme Link: ExPASy2.1.1.319
EC2PDB Enzyme Link: EC2PDB 2.1.1.319
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.319
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.319
IntEnz Enzyme Link: IntEnz 2.1.1.319
MEDLINE Enzyme Link: MEDLINE 2.1.1.319
MSA:

2.1.1.319;

Phylogenetic Tree:

2.1.1.319;

Uniprot:
M-CSA:
RHEA:48096 L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6].[*:7]-[S+;H0:8](-[*:9])-[CH3;+0:10]>>[*:1]-[N;H0;+0:2](-[CH3;+0:10])-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5].[*:7]-[S;H0;+0:8]-[*:9]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
RNA and protein interactions modulated by protein arginine methylation.Gary JD, Clarke S19989752719
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation.Tang J, Gary JD, Clarke S, Herschman HR1998 Jul 39642256
Automethylation of CARM1 allows coupling of transcription and mRNA splicing.Kuhn P, Chumanov R, Wang Y, Ge Y, Burgess RR, Xu W2011 Apr21138967
Enzymatic activity is required for the in vivo functions of CARM1.Kim D, Lee J, Cheng D, Li J, Carter C, Richie E, Bedford MT2010 Jan 819897492
Biochemical control of CARM1 enzymatic activity by phosphorylation.Feng Q, He B, Jung SY, Song Y, Qin J, Tsai SY, Tsai MJ, O'Malley BW2009 Dec 2519843527
Delineating Anopheles gambiae coactivator associated arginine methyltransferase 1 automethylation using top-down high resolution tandem mass spectrometry.Kuhn P, Xu Q, Cline E, Zhang D, Ge Y, Xu W2009 Jun19472346
Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4.Lakowski TM, Frankel A2009 Jun 2619405910
PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation.Hyllus D, Stein C, Schnabel K, Schiltz E, Imhof A, Dou Y, Hsieh J, Bauer UM2007 Dec 1518079182
Arginine methylation of the histone H3 tail impedes effector binding.Iberg AN, Espejo A, Cheng D, Kim D, Michaud-Levesque J, Richard S, Bedford MT2008 Feb 818077460
Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase.Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH2007 Oct 1717882261
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity.Frankel A, Yadav N, Lee J, Branscombe TL, Clarke S, Bedford MT2002 Feb 111724789
Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.Wang H, Huang ZQ, Xia L, Feng Q, Erdjument-Bromage H, Strahl BD, Briggs SD, Allis CD, Wong J, Tempst P, Zhang Y2001 Aug 311387442
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1.Schurter BT, Koh SS, Chen D, Bunick GJ, Harp JM, Hanson BL, Henschen-Edman A, Mackay DR, Stallcup MR, Aswad DW2001 May 1511341840
PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells.Tang J, Frankel A, Cook RJ, Kim S, Paik WK, Williams KR, Clarke S, Herschman HR2000 Mar 1710713084