PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
31734465-1	2020	BACKGROUND: Asymmetric arginine dimethylation of histone H4R3 to H4R3me2a by protein arginine methyltransferase 1 (PRMT1) has been implicated to play a key role in gene activation throughout vertebrates.	h4r3me2s	65-73	protein arginine methyltransferase 1	Xenopus tropicalis	115-120
31868234-6	2020	We demonstrate that as the CYP24A1 gene promoter remains transcriptionally silent, there is enrichment of H4R3me2s together with its "writing" enzyme PRMT5 and decreased abundance of the istone H3 and H4 acetylation, H3R17me2a, and H4R3me2a marks as well as of their corresponding "writers."	h4r3me2s	106-114	cytochrome P450 family 24 subfamily A member 1	Homo sapiens	27-34
31868234-6	2020	We demonstrate that as the CYP24A1 gene promoter remains transcriptionally silent, there is enrichment of H4R3me2s together with its "writing" enzyme PRMT5 and decreased abundance of the istone H3 and H4 acetylation, H3R17me2a, and H4R3me2a marks as well as of their corresponding "writers."	h4r3me2s	217-226	cytochrome P450 family 24 subfamily A member 1	Homo sapiens	27-34
31868234-6	2020	We demonstrate that as the CYP24A1 gene promoter remains transcriptionally silent, there is enrichment of H4R3me2s together with its "writing" enzyme PRMT5 and decreased abundance of the istone H3 and H4 acetylation, H3R17me2a, and H4R3me2a marks as well as of their corresponding "writers."	h4r3me2s	232-240	cytochrome P450 family 24 subfamily A member 1	Homo sapiens	27-34
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	168-177	vitamin D receptor	Homo sapiens	0-3
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	168-177	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	4-9
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	168-177	coactivator associated arginine methyltransferase 1	Homo sapiens	118-123
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	168-177	protein arginine methyltransferase 1	Homo sapiens	128-133
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	182-190	vitamin D receptor	Homo sapiens	0-3
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	182-190	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	4-9
31868234-8	2020	VDR/SRC-1 binding occurs concomitant with the release of PRMT5 and the recruitment of the arginine methyltransferases CARM1 and PRMT1 to catalyze the deposition of the H3R17me2a and H4R3me2a marks, respectively.	h4r3me2s	182-190	coactivator associated arginine methyltransferase 1	Homo sapiens	118-123
31734465-5	2020	RESULTS: We observed that PRMT1 knockout had no apparent effect on embryogenesis because normally feeding tadpoles were formed, despite the reduced asymmetric H4R3 di-methylation (H4R3me2a) due to the knockout.	h4r3me2s	180-188	protein arginine methyltransferase 1	Xenopus tropicalis	26-31
31848151-5	2020	Deletion of Prmt1 in adult beta cells resulted in the immediate loss of histone H4 arginine 3 asymmetric di-methylation (H4R3me2a) and the subsequent loss of beta cell identity.	h4r3me2s	121-129	protein arginine methyltransferase 1	Homo sapiens	12-17
31574302-4	2020	We found that the accumulation of Hsl7-mediated H4R3me2s is maintained by the histone deacetylase Rpd3 during transcriptional repression and that the low level of H4R3me2s is required for proper asymmetric cell growth during cell division.	h4r3me2s	48-56	histone deacetylase 1	Homo sapiens	98-102
31813251-3	2020	In this study, we observed that PRMT1 and its specific epigenetic marker, asymmetric di-methylated histone 4 arginine 3 (H4R3Me2a), were highly expressed in cultured renal interstitial fibroblasts.	h4r3me2s	121-129	protein arginine N-methyltransferase 1	Mus musculus	32-37
32042864-3	2019	PRMT5 is the main type II enzyme that catalyzes symmetric dimethylarginine of histone proteins to induce gene silencing by generating repressive histone marks, including H2AR3me2s, H3R8me2s, and H4R3me2s.	h4r3me2s	170-189	protein arginine methyltransferase 5	Homo sapiens	0-5
32042864-3	2019	PRMT5 is the main type II enzyme that catalyzes symmetric dimethylarginine of histone proteins to induce gene silencing by generating repressive histone marks, including H2AR3me2s, H3R8me2s, and H4R3me2s.	h4r3me2s	195-203	protein arginine methyltransferase 5	Homo sapiens	0-5
31848151-7	2020	ChIP-seq and ATAC-seq analyses revealed that PRMT1-dependent H4R3me2a increases chromatin accessibility at the binding sites for CTCF and beta cell transcription factors.	h4r3me2s	61-69	protein arginine methyltransferase 1	Homo sapiens	45-50
31848151-7	2020	ChIP-seq and ATAC-seq analyses revealed that PRMT1-dependent H4R3me2a increases chromatin accessibility at the binding sites for CTCF and beta cell transcription factors.	h4r3me2s	61-69	CCCTC-binding factor	Homo sapiens	129-133