PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15105418-1	2004	The regulatory domains of novel protein kinases C (PKC) contain two C1 domains (C1A and C1B), which have been identified as the interaction site for sn-1,2-diacylglycerol (DAG) and phorbol ester, and a C2 domain that may be involved in interaction with lipids and/or proteins.	Phorbol Esters	181-194	endogenous retrovirus group K member 1	Homo sapiens	80-91	
15105418-4	2004	Isothermal titration calorimetry and surface plasmon resonance measurements showed that isolated C1A and C1B domains of PKCdelta have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	166-179	endogenous retrovirus group K member 1	Homo sapiens	97-100	
15105418-4	2004	Isothermal titration calorimetry and surface plasmon resonance measurements showed that isolated C1A and C1B domains of PKCdelta have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	166-179	endogenous retrovirus group K member 1	Homo sapiens	190-193	
15105418-4	2004	Isothermal titration calorimetry and surface plasmon resonance measurements showed that isolated C1A and C1B domains of PKCdelta have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	270-283	endogenous retrovirus group K member 1	Homo sapiens	97-100	
15105418-4	2004	Isothermal titration calorimetry and surface plasmon resonance measurements showed that isolated C1A and C1B domains of PKCdelta have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	270-283	endogenous retrovirus group K member 1	Homo sapiens	190-193	
14503869-2	2003	Novel and conventional protein kinase C isozymes contain a tandem repeat of C1 domains, the C1A and C1B, which each contain a binding pocket for phorbol esters/diacylglycerol.	Phorbol Esters	145-159	endogenous retrovirus group K member 1	Homo sapiens	92-103	
12954613-1	2003	The regulatory domains of conventional and novel protein kinases C (PKC) have two C1 domains (C1A and C1B) that have been identified as the interaction site for diacylglycerol (DAG) and phorbol ester.	Phorbol Esters	186-199	endogenous retrovirus group K member 1	Homo sapiens	94-105	
12954613-3	2003	In this study, we measured the affinity of isolated C1A and C1B domains of two conventional PKCs, PKCalpha and PKCgamma, for soluble and membrane-incorporated DAG and phorbol ester by isothermal calorimetry and surface plasmon resonance.	Phorbol Esters	167-180	endogenous retrovirus group K member 1	Homo sapiens	52-55	
12954613-4	2003	The C1A and C1B domains of PKCalpha have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	73-86	endogenous retrovirus group K member 1	Homo sapiens	4-7	
12954613-4	2003	The C1A and C1B domains of PKCalpha have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	73-86	endogenous retrovirus group K member 1	Homo sapiens	97-100	
12954613-4	2003	The C1A and C1B domains of PKCalpha have opposite affinities for DAG and phorbol ester; i.e. the C1A domain with high affinity for DAG and the C1B domain with high affinity for phorbol ester.	Phorbol Esters	177-190	endogenous retrovirus group K member 1	Homo sapiens	4-7	
12954613-5	2003	In contrast, the C1A and C1b domains of PKCgamma have comparably high affinities for both DAG and phorbol ester.	Phorbol Esters	98-111	endogenous retrovirus group K member 1	Homo sapiens	17-20	
14503869-6	2003	The increased potency of dimeric phorbol esters is reduced if either the C1A or C1B domains are mutated so that they are unable to bind PMA, if one moiety of the dimer contains a nonfunctional phorbol, or if the binding to the isolated C1B domain is measured.	Phorbol Esters	33-47	endogenous retrovirus group K member 1	Homo sapiens	73-76	
29317197-0	2018	Structural determinants of phorbol ester binding activity of the C1a and C1b domains of protein kinase C theta.	Phorbol Esters	27-40	endogenous retrovirus group K member 1	Homo sapiens	65-68	
15769752-3	2005	The regulatory domains of novel PKC contain a C2 domain and a tandem repeat of C1 domains (C1A and C1B), which have been identified as the interaction site for DAG and phorbol ester.	Phorbol Esters	168-181	endogenous retrovirus group K member 1	Homo sapiens	91-102	
15769752-4	2005	Isothermal titration calorimetry and surface plasmon resonance measurements showed that isolated C1A and C1B domains of PKCepsilon have comparably high affinities for DAG and phorbol ester.	Phorbol Esters	175-188	endogenous retrovirus group K member 1	Homo sapiens	97-100	
9041654-2	1997	These domains were first discovered as the loci of phorbol ester and diacylglycerol binding to conventional protein kinase C isozymes, which contain 2 C1 domains (C1A and C1B) in their N-terminal regulatory regions.	Phorbol Esters	51-64	endogenous retrovirus group K member 1	Homo sapiens	163-174	
15927450-2	2005	The regulatory region of PKD contains a tandem repeat of C1 domains designated C1a and C1b that bind diacylglycerol and phorbol esters, and are important membrane targeting modules.	Phorbol Esters	120-134	endogenous retrovirus group K member 1	Homo sapiens	79-82	
15927450-5	2005	Meanwhile, mutations in C1a of truncated C1ab of PKD3 lead to the loss of binding affinity, while these mutations in C1b have little impact, indicating that C1a is responsible for most of the phorbol ester-binding activities of PKD3.	Phorbol Esters	192-205	endogenous retrovirus group K member 1	Homo sapiens	41-44	
15927450-11	2005	Taken together, our results indicate that both C1a and the kinase activity of PKD3 are necessary for the phorbol ester-induced plasma membrane translocation of PKD3.	Phorbol Esters	105-118	endogenous retrovirus group K member 1	Homo sapiens	47-50	
15975900-4	2005	C1a/C1b, in particular C1b, is required for phorbol ester binding and gastrin-stimulated PKD2 activation, but it has no inhibitory effect on the catalytic activity.	Phorbol Esters	44-57	endogenous retrovirus group K member 1	Homo sapiens	0-3