PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12460119-8	2003	Experiments with individual C1 domains showed that treatment with carbachol or phorbol 12,13-dibutyrate elicited translocation of PKC alpha C1a, PKC epsilon C1a and PKC epsilon C1b, whereas PKC alpha C1b was largely insensitive to these agents.	Phorbol 12,13-Dibutyrate	79-103	endogenous retrovirus group K member 1	Homo sapiens	140-143	
11504643-1	2001	Conventional and novel protein kinase C (PKC) isozymes contain two cysteine-rich C1 domains (C1A and C1B), both of which are candidate phorbol-12,13-dibutyrate (PDBu) binding sites.	Phorbol 12,13-Dibutyrate	135-159	endogenous retrovirus group K member 1	Homo sapiens	93-104	
11504643-1	2001	Conventional and novel protein kinase C (PKC) isozymes contain two cysteine-rich C1 domains (C1A and C1B), both of which are candidate phorbol-12,13-dibutyrate (PDBu) binding sites.	Phorbol 12,13-Dibutyrate	161-165	endogenous retrovirus group K member 1	Homo sapiens	93-104