PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15550676-1	2005	Human UMP/CMP kinase (cytidylate kinase; EC 2.7.4.14) is responsible for phosphorylation of CMP, UMP, and deoxycytidine monophosphate (dCMP) and also plays an important role in the activation of pyrimidine analogs, some of which are clinically useful anticancer or antiviral drugs.	Deoxycytidine Monophosphate	106-133	cmp	Drosophila melanogaster	10-13	
15550676-1	2005	Human UMP/CMP kinase (cytidylate kinase; EC 2.7.4.14) is responsible for phosphorylation of CMP, UMP, and deoxycytidine monophosphate (dCMP) and also plays an important role in the activation of pyrimidine analogs, some of which are clinically useful anticancer or antiviral drugs.	Deoxycytidine Monophosphate	135-139	cmp	Drosophila melanogaster	10-13	
15550676-2	2005	Previous kinetic data using recombinant or highly purified human UMP/CMP kinase showed that dCMP, as well as pyrimidine analog monophosphates, were much poorer substrates than CMP or UMP for this enzyme.	Deoxycytidine Monophosphate	92-96	cmp	Drosophila melanogaster	69-72	
15550676-4	2005	Here, we reevaluated the optimal reaction conditions for human recombinant human UMP/CMP kinase to phosphorylate dCMP and CMP (referred as dCMPK and CMPK activities).	Deoxycytidine Monophosphate	113-117	cmp	Drosophila melanogaster	85-88	
15550676-9	2005	The data suggest that the active sites of human UMP/CMP kinase for dCMP and for CMP cannot be identical.	Deoxycytidine Monophosphate	67-71	cmp	Drosophila melanogaster	52-55	
15550676-10	2005	Furthermore, enzyme inhibition studies demonstrated that CMP could inhibit dCMP phosphorylation in a noncompetitive manner, with Ki values much higher than its own Km values.	Deoxycytidine Monophosphate	75-79	cmp	Drosophila melanogaster	57-60