PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16103119-4	2005	Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon.	Tyrosine	33-42	mitogen-activated protein kinase 1	Mus musculus	172-175	
16103119-4	2005	Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon.	Tyrosine	44-47	mitogen-activated protein kinase 1	Mus musculus	172-175	
16103119-4	2005	Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon.	Tyrosine	54-57	mitogen-activated protein kinase 1	Mus musculus	172-175	
16103119-4	2005	Furthermore, we identified three tyrosines (Tyr-1175, Tyr-1265, and Tyr-1294) within the kinase domain that play critical but overlapping roles in controlling constitutive Erk activation by mRon.	Tyrosine	54-57	mitogen-activated protein kinase 1	Mus musculus	172-175	
16103119-5	2005	Phenylalanine mutations at these three tyrosines results in a receptor that fails to constitutively activate the Erk pathway but retains the ability to induce Erk phosphorylation in response to ligand stimulation.	Tyrosine	39-48	mitogen-activated protein kinase 1	Mus musculus	113-116	
16103119-5	2005	Phenylalanine mutations at these three tyrosines results in a receptor that fails to constitutively activate the Erk pathway but retains the ability to induce Erk phosphorylation in response to ligand stimulation.	Tyrosine	39-48	mitogen-activated protein kinase 1	Mus musculus	159-162