Search by BoMiProt ID - Bomi8317

Primary Information

BoMiProt ID Bomi8317
Protein Name Protein arginine N-methyltransferase 5
Organism Bos taurus
Uniprot IDA7YW45
Milk FractionExosomes
Ref Sequence ID NP_001098844.1
Aminoacid Length 637
Molecular Weight 72629
FASTA Sequence Download
Gene Name PRMT5
Gene ID 515594
Protein Existence Status reviewed

Secondary Information

Protein Function Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties.
Biochemical Properties The C-terminal catalytic domain of PRMT5 consists of two domains, the Rossam fold and β-barrel domains, required for binding cofactor (the methyl donor, SAM/AdoMet) and substrate, respectively. The structural restraints of substrate binding dictate preferential methylation of glycine-rich sequences, which allow conformational freedom of polypeptide chain to form a sharp β-turn.
PTMs Acetylation,Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions (1-12)
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Phosphorylated by JAK2.A threonine residue within the PRMT5 C-terminal tail is phosphorylated by Akt/SGK, an activity that serves as a switch to control PRMT5 targeting to the plasma membrane via choice of differential interacting partners, a PDZ domain protein or 14-3-3, depending on phosphorylation status.ROCK (RhoA-activated kinase) and MP (myosin phosphatase), respectively, phosphorylate and dephosphorylate PRMT5 threonine 80, to modulate PRMT5 activity, thereby pointing to a tumor suppressor role of MP in HCC.LKB1, a kinase with tumor suppressor function, phosphorylates multiple threonines (T132, 139 and 144) in the PRMT5 TIM-barrel domains required for MEP50, pICln and RIOK1 interaction, suppressing PRMT5 enzymatic activity .PRMT5 itself is arginine-methylated by CARM1 (PRMT4) in the erythroleukemia cells Lys-562, which is essential for PRMT5 methyltransferase activity to repress human γ-globin expression.
Bibliography 1.Kim, H., & Ronai, Z. A. (2020). PRMT5 function and targeting in cancer. Cell stress, 4(8), 199–215.