PRMT3 involved in several pathways and played different roles in them. We selected most pathways PRMT3 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with PRMT3 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name |
Pathway Related Protein |
PRMT3 has several biochemical functions, for example, histone-arginine N-methyltransferase activity, metal ion binding, methyltransferase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by PRMT3 itself. We selected most functions PRMT3 had, and list some proteins which have the same functions with PRMT3. You can find most of the proteins on our site.
| Function |
Related Protein |
| histone-arginine N-methyltransferase activity |
PRMT8; PRMT3; PRMT7; PRMT5; PRMT6; PRMT2; CARM1 |
| metal ion binding |
ZNF654; ZFP473; VDRB; FOXP3; PRKCZ; WT1B; ZNF483; ZNF710A; POGZ; ERCC5 |
| methyltransferase activity |
SETD1B; PRDM12; MLL5; SETDB1B; PMT; C2orf56; EHMT1B; PRDM13; PRMT8B; FAM86 |
| protein binding |
WAS; BATF; VMP1; KIAA1279; CYP2S1; CC10; ZBTB49; OCA2; JAM3; CDK5R1 |
| protein-arginine N-methyltransferase activity |
CARM1; METTL21A; RNMTL1B; FBXO11; TRMT10B; PRMT1; METTL8; PRDM13; PRMT3; DIMT1 |
| protein-arginine omega-N asymmetric methyltransferase activity |
CARM1; PRMT7; PRMT3; PRMT8; PRMT6; PRMT2; PRMT1; PRMT8B |
PRMT3 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PRMT3 here. Most of them are supplied by our site. Hope this information will be useful for your research of PRMT3.
SCN5A; HNRNPK; RASSF2; PPARD; serS; HNRNPD; Ranbp2
Kim, C; Lim, Y; et al. Regulation of post-translational protein arginine methylation during HeLa cell cycle. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS 1800:977-985(2010).
Trojer, P; Dangl, M; et al. Histone methyltransferases in Aspergillus nidulans: Evidence for a novel enzyme with a unique substrate specificity. BIOCHEMISTRY 43:10834-10843(2004).
