PRMT5 Products

Description

Arginine methylation is an irreversible post translational modification linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These proteins include nuclear proteins (Histone 2A, 3, 4), IL enhancer binding factor, nuclear factors (NF45, 90, ILF3, Nucleolin, STAT1, Poly(A) binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src-adaptor Sam68), apoptosis proteins (FADD, ICE-like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions.

Bioinformatics

Entrez	10419 Human 27374 Mouse 364382 Rat
Uniprot	AAF04502 Human AAH25979 Human AAH25979.1 Human NM_006109 Human NP_006100 Human NP_006100.2 Human O14744 Human
Product By Gene ID	10419
Alternate Names	EC 2.1.1.- EC 2.1.1.125 Histone-arginine N-methyltransferase PRMT5 HMT1 hnRNP methyltransferase-like 5,72 kDa ICln-binding protein HRMT1L5 IBP72 Jak-binding protein 1 JBP1 protein arginine methyltransferase 5 protein arginine N-methyltransferase 5 Shk1 kinase-binding protein 1 homolog skb1 (S. pombe) homolog SKB1 homolog (S. pombe) SKB1 SKB1HsSKB1 homolog

Research Areas for PRMT5

Find related products by research area and learn more about each of the different research areas below.

Cell Cycle and Replication
Chromatin Research
Circadian Rhythm