Structural highlights
Function
ANM1_RAT Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway.[1] [2] [3]
References
- ↑ Lim Y, Kwon YH, Won NH, Min BH, Park IS, Paik WK, Kim S. Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver. Biochim Biophys Acta. 2005 May 25;1723(1-3):240-7. Epub 2005 Mar 17. PMID:15837430 doi:10.1016/j.bbagen.2005.02.015
- ↑ Iwasaki H. Involvement of PRMT1 in hnRNPQ activation and internalization of insulin receptor. Biochem Biophys Res Commun. 2008 Jul 25;372(2):314-9. doi:, 10.1016/j.bbrc.2008.05.051. Epub 2008 May 19. PMID:18492485 doi:10.1016/j.bbrc.2008.05.051
- ↑ Zhang X, Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure. 2003 May;11(5):509-20. PMID:12737817
