PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23542169-7	2014	In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha.	Proline	198-205	hypoxia inducible factor 1 subunit alpha	Homo sapiens	80-90	
23542169-7	2014	In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha.	Proline	198-205	hypoxia inducible factor 1 subunit alpha	Homo sapiens	159-169	
23542169-7	2014	In addition, RUNX3 directly interacted with the C-terminal activation domain of HIF-1alpha and prolyl hydroxylase (PHD) 2 and enhanced the interaction between HIF-1alpha and PHD2, which potentiated proline hydroxylation and promoted the degradation of HIF-1alpha.	Proline	198-205	hypoxia inducible factor 1 subunit alpha	Homo sapiens	159-169	
23542169-9	2014	Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2.	Proline	98-105	hypoxia inducible factor 1 subunit alpha	Homo sapiens	62-72	
23542169-9	2014	Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2.	Proline	98-105	hypoxia inducible factor 1 subunit alpha	Homo sapiens	123-133	
23542169-9	2014	Taken together, these results suggest that RUNX3 destabilizes HIF-1alpha protein by promoting the proline hydroxylation of HIF-1alpha through binding to HIF-1alpha/PHD2.	Proline	98-105	hypoxia inducible factor 1 subunit alpha	Homo sapiens	123-133