Sequence of ANM1_RAT
EC Number:2.1.1.319
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
Other sequences found for EC No. 2.1.1.319
General information:
Sequence
0 MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN
60 SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV
120 VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL HARDKWLAPD GLIFPDRATL
180 YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY
240 TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY
300 MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1028715
Lin W.-J.,Gary J.D.,Yang M.C.,Clarke S.,Herschman H.R.
The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase.
J. Biol. Chem.
271
15034-15044
1996
1028716
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1028717
Lim Y.,Kwon Y.H.,Won N.H.,Min B.H.,Park I.S.,Paik W.K.,Kim S.
Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver.
Biochim. Biophys. Acta
1723
240-247
2005
1028718
Iwasaki H.
Involvement of PRMT1 in hnRNPQ activation and internalization of insulin receptor.
Biochem. Biophys. Res. Commun.
372
314-319
2008
1028719
Lakowski T.M.,Frankel A.
Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4.
Biochem. J.
421
253-261
2009
1028720
Cho J.H.,Lee M.K.,Yoon K.W.,Lee J.,Cho S.G.,Choi E.J.
Arginine methylation-dependent regulation of ASK1 signaling by PRMT1.
Cell Death Differ.
19
859-870
2012
1028721
Zhang X.,Cheng X.
Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides.
Structure
11
509-520
2003
