PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20371672-7	2010	Furthermore, SFK activity contributed to endogenous tyrosine phosphorylation of PKG-Ialpha in OV2008 and A2780cp cells.	Tyrosine	52-60	protein kinase cGMP-dependent 1	Homo sapiens	80-83	
25586176-8	2015	These data indicated that TNF-alpha-induced repression of GKAP42 via cGK-Ialpha caused reduction of insulin-induced IRS-1 tyrosine phosphorylation at least in part.	Tyrosine	122-130	protein kinase cGMP-dependent 1	Homo sapiens	69-79	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	218-226	protein kinase cGMP-dependent 1	Homo sapiens	119-122	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	91-99	protein kinase cGMP-dependent 1	Homo sapiens	53-56	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	91-99	protein kinase cGMP-dependent 1	Homo sapiens	119-122	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	91-99	protein kinase cGMP-dependent 1	Homo sapiens	119-122	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	91-99	protein kinase cGMP-dependent 1	Homo sapiens	119-122	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	218-226	protein kinase cGMP-dependent 1	Homo sapiens	53-56	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	218-226	protein kinase cGMP-dependent 1	Homo sapiens	119-122	
20371672-8	2010	In vitro coincubation of recombinant human c-Src and PKG-Ialpha resulted in c-Src-mediated tyrosine phosphorylation of PKG-Ialpha and enhanced c-Src autophosphorylation/activation, suggesting that human c-Src directly tyrosine phosphorylates PKG-Ialpha and the c-Src/PKG-Ialpha interaction enhances Src kinase activity.	Tyrosine	218-226	protein kinase cGMP-dependent 1	Homo sapiens	119-122	
19487814-5	2009	Activation of eNOS in Cav1-/- lungs led to the impairment of PKG activity through tyrosine nitration.	Tyrosine	82-90	protein kinase cGMP-dependent 1	Homo sapiens	61-64	
19487814-8	2009	Together, these data show that loss of caveolin-1 leads to hyperactive eNOS and subsequent tyrosine nitration-dependent impairment of PKG activity, which results in PH.	Tyrosine	91-99	protein kinase cGMP-dependent 1	Homo sapiens	134-137	
9675253-3	1998	The kinase activity of cGK is elevated approximately 4-fold (relative to autophosphorylated cGK) or 10-fold (relative to unphosphorylated cGK) upon tyrosine phosphorylation by Src.	Tyrosine	148-156	protein kinase cGMP-dependent 1	Homo sapiens	23-26	
9675253-3	1998	The kinase activity of cGK is elevated approximately 4-fold (relative to autophosphorylated cGK) or 10-fold (relative to unphosphorylated cGK) upon tyrosine phosphorylation by Src.	Tyrosine	148-156	protein kinase cGMP-dependent 1	Homo sapiens	92-95	
9675253-3	1998	The kinase activity of cGK is elevated approximately 4-fold (relative to autophosphorylated cGK) or 10-fold (relative to unphosphorylated cGK) upon tyrosine phosphorylation by Src.	Tyrosine	148-156	protein kinase cGMP-dependent 1	Homo sapiens	92-95	
31519182-14	2019	PKA/PKG pathways inhibited EB-induced platelet aggregation and Akt phosphorylation but, surprisingly, enhanced Syk and LAT/PLCgamma2 tyrosine phosphorylation.	Tyrosine	133-141	protein kinase cGMP-dependent 1	Homo sapiens	4-7	
17616649-3	2007	Hypoxia decreased the relaxation response to 8-bromo-cGMP, PKG protein expression, and kinase activity and increased tyrosine nitration in PKG.	Tyrosine	117-125	protein kinase cGMP-dependent 1	Homo sapiens	139-142