PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22514282-2	2012	In vivo analysis has indicated that base J synthesis is initiated by the hydroxylation of thymidine by proteins (JBP1 and JBP2) homologous to the Fe(2+)/2-oxoglutarate (2-OG)-dependent dioxygenase superfamily where hydroxylation is driven by the oxidative decarboxylation of 2-OG, forming succinate and CO(2).	ammonium ferrous sulfate	146-152	protein arginine methyltransferase 5	Homo sapiens	113-117	
22514282-4	2012	We now demonstrate recombinant JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe(2+)-, 2-OG-, and O(2)-dependent manner.	ammonium ferrous sulfate	99-105	protein arginine methyltransferase 5	Homo sapiens	31-35	
22514282-5	2012	Under anaerobic conditions, the addition of Fe(2+) to JBP1/2-OG results in the formation of a broad absorption spectrum centered at 530 nm attributed to metal chelation of 2-OG bound to JBP, a spectroscopic signature of Fe(2+)/2-OG-dependent dioxygenases.	ammonium ferrous sulfate	44-50	protein arginine methyltransferase 5	Homo sapiens	54-63	
22514282-5	2012	Under anaerobic conditions, the addition of Fe(2+) to JBP1/2-OG results in the formation of a broad absorption spectrum centered at 530 nm attributed to metal chelation of 2-OG bound to JBP, a spectroscopic signature of Fe(2+)/2-OG-dependent dioxygenases.	ammonium ferrous sulfate	220-226	protein arginine methyltransferase 5	Homo sapiens	54-63	
22514282-6	2012	The N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity and mutation of residues involved in coordinating Fe(2+) inhibit iron binding and thymidine hydroxylation.	ammonium ferrous sulfate	134-140	protein arginine methyltransferase 5	Homo sapiens	47-51	
17389644-4	2007	We show that JBP1 belongs to the family of Fe(2+) and 2-oxoglutarate-dependent dioxygenases and that replacement of conserved residues putatively involved in Fe(2+) and 2-oxoglutarate-binding inactivates the ability of JBP1 to contribute to J synthesis without affecting its ability to bind to J-DNA.	ammonium ferrous sulfate	43-49	protein arginine methyltransferase 5	Homo sapiens	13-17	
17389644-4	2007	We show that JBP1 belongs to the family of Fe(2+) and 2-oxoglutarate-dependent dioxygenases and that replacement of conserved residues putatively involved in Fe(2+) and 2-oxoglutarate-binding inactivates the ability of JBP1 to contribute to J synthesis without affecting its ability to bind to J-DNA.	ammonium ferrous sulfate	158-164	protein arginine methyltransferase 5	Homo sapiens	13-17