PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18617565-5	2008	Alanine substitution for the PKG phosphorylation candidate site at T69 but not at other sites (T14A, S28A, T193A, S321A) of TRPC6 similarly attenuated the inhibitory effects of SNAP and 8Br-cGMP.	Alanine	0-7	protein kinase cGMP-dependent 1	Homo sapiens	29-32	
23407708-4	2013	Serine to alanine substitutions at 3 of 6 putative cGKI phosphorylation sites (Ser691, Ser873, and Ser1112) in the BKCa alpha subunit individually reduced direct channel phosphorylation by 25-60% and blocked BKCa activation by either an NO donor or a membrane-permeable cGMP by 80-100%.	Alanine	10-17	protein kinase cGMP-dependent 1	Homo sapiens	51-55	
18635821-4	2008	Serine to alanine mutation of putative sites revealed that Ser64 is the main phosphorylation site for PKG.	Alanine	10-17	protein kinase cGMP-dependent 1	Homo sapiens	102-105	
17913921-5	2007	Mutation of Thr-276 in the fifth transmembrane domain (TM5) to alanine or aspartate prevented activation of wild-type hSERT through the PKG pathway and also blocked the inhibition of I425V activity by inhibitors of the pathway.	Alanine	63-70	protein kinase cGMP-dependent 1	Homo sapiens	136-139	
11309393-7	2001	Mutation of these four serines to alanine showed that cGKIbeta-dependent phosphorylation of Ser(696) is necessary to decrease calcium release from InsP(3)-sensitive stores.	Alanine	34-41	protein kinase cGMP-dependent 1	Homo sapiens	54-62	
17626895-10	2007	PKG-mediated inhibition of Ca(v)1.2 current was significantly reduced by coexpression of an alanine-substituted Ca(v)1.2 beta(2a) subunit (Ser(496)).	Alanine	92-99	protein kinase cGMP-dependent 1	Homo sapiens	0-3	
10615072-6	2000	Phosphorylation of H-Arg-Lys-Ile-Ser-Ala-Ser-Glu-Phe-Asp-Arg-Pro-Leu-Arg-OH (BPDEtide), a specific substrate for PKG, measured the activity of cGMP-dependent protein kinase (PKG).	Alanine	37-40	protein kinase cGMP-dependent 1	Homo sapiens	113-116	
10615072-6	2000	Phosphorylation of H-Arg-Lys-Ile-Ser-Ala-Ser-Glu-Phe-Asp-Arg-Pro-Leu-Arg-OH (BPDEtide), a specific substrate for PKG, measured the activity of cGMP-dependent protein kinase (PKG).	Alanine	37-40	protein kinase cGMP-dependent 1	Homo sapiens	174-177	
7819246-3	1995	Although the inhibitory peptide corresponding to this sequence (i.e., with an Ala at position 21) is a much more potent inhibitor of PKA than of PKG (approximately 250-fold), PKG actually exhibits a 60% higher kcat than does PKA with the (Ser21)PKI alpha(14-22) amide substrate peptide, with only a 20-fold higher Km value.	Alanine	78-81	protein kinase cGMP-dependent 1	Homo sapiens	145-148	
10196172-10	1999	A point mutation of cslo-alpha in which Ser-1072 (the only optimal consensus sequence for PKG phosphorylation) was replaced by Ala abolished the PKG effect on NPo in inside-out patches and the effect of SNP in cell attached patches.	Alanine	127-130	protein kinase cGMP-dependent 1	Homo sapiens	145-148