PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32456215-0 2020 Regulation of a PRMT5/NF-kappaB Axis by Phosphorylation of PRMT5 at Serine 15 in Colorectal Cancer. Serine 68-74 protein arginine methyltransferase 5 Homo sapiens 16-21 33380261-3 2022 We found that phosphorylation at histone H4 Ser-1 site (H4S1) was inhibitory to activities of PRMT1 and PRMT5 in both monomethylating and dimethylating H4R3. Serine 44-47 protein arginine methyltransferase 5 Homo sapiens 104-109 32456215-4 2020 Here, we report a novel finding that PRMT5 is phosphorylated on serine 15 (S15) in response to interleukin-1beta (IL-1beta) stimulation. Serine 64-70 protein arginine methyltransferase 5 Homo sapiens 37-42 32456215-6 2020 Overexpression of the serine-to-alanine mutant of PRMT5 (S15A), in either HEK293 cells or CRC cells HT29, DLD1, and HCT116 attenuated NF-kappaB transactivation compared to WT-PRMT5, confirming that S15 phosphorylation is critical for the activation of NF-kappaB by PRMT5. Serine 22-28 protein arginine methyltransferase 5 Homo sapiens 50-55 32456215-6 2020 Overexpression of the serine-to-alanine mutant of PRMT5 (S15A), in either HEK293 cells or CRC cells HT29, DLD1, and HCT116 attenuated NF-kappaB transactivation compared to WT-PRMT5, confirming that S15 phosphorylation is critical for the activation of NF-kappaB by PRMT5. Serine 22-28 protein arginine methyltransferase 5 Homo sapiens 175-180 32456215-6 2020 Overexpression of the serine-to-alanine mutant of PRMT5 (S15A), in either HEK293 cells or CRC cells HT29, DLD1, and HCT116 attenuated NF-kappaB transactivation compared to WT-PRMT5, confirming that S15 phosphorylation is critical for the activation of NF-kappaB by PRMT5. Serine 22-28 protein arginine methyltransferase 5 Homo sapiens 175-180 32456215-0 2020 Regulation of a PRMT5/NF-kappaB Axis by Phosphorylation of PRMT5 at Serine 15 in Colorectal Cancer. Serine 68-74 protein arginine methyltransferase 5 Homo sapiens 59-64 31765670-4 2020 NDRG2/PP2A complex inhibited arginine methyltransferase activity of PRMT5 through dephosphorylation at Serine 335 (S335); however, in NDRG2low ATL-related cells, highly phosphorylated PRMT5 at S335 was mainly localized in cytoplasm with binding to HSP90A, resulting in enhancing arginine-methylation at the middle domain (R345 and R386). Serine 103-109 protein arginine methyltransferase 5 Homo sapiens 68-73 26912789-2 2016 We show that PRMT5 interacts with and methylates ASK1 at arginine residue 89 and thereby negatively regulates its activity by promoting the interaction between ASK1 and Akt and thus phosphorylating ASK1 at serine residue 83. Serine 206-212 protein arginine methyltransferase 5 Homo sapiens 13-18