Primary Information |
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| BoMiProt ID | Bomi8317 |
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| Protein Name | Protein arginine N-methyltransferase 5 |
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| Organism | Bos taurus |
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| Uniprot ID | A7YW45 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001098844.1 |
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| Aminoacid Length | 637 |
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| Molecular Weight | 72629 |
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| FASTA Sequence |
Download |
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| Gene Name | PRMT5 |
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| Gene ID | 515594 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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. |
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| 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. |
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| PTMs | Acetylation,Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | (1-12) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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. |
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| Bibliography | 1.Kim, H., & Ronai, Z. A. (2020). PRMT5 function and targeting in cancer. Cell stress, 4(8), 199–215. https://doi.org/10.15698/cst2020.08.228 |
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