PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15536085-9	2005	Most interestingly, pH 9-10, which neutralizes the Lys groups of beta-LG, not only reduced its immunoreactivity but also its binding to palmitic acid implicating a role of Lys-69.	Lysine	51-54	beta-lactoglobulin	Bos taurus	65-72	
15536085-9	2005	Most interestingly, pH 9-10, which neutralizes the Lys groups of beta-LG, not only reduced its immunoreactivity but also its binding to palmitic acid implicating a role of Lys-69.	Lysine	172-175	beta-lactoglobulin	Bos taurus	65-72	
10888497-4	2000	Structural analysis using monoclonal antibodies indicated that the conformation around (15)Val-(29)Ile (beta-sheet region) in beta-LG-GlcN and beta-LG-CPO had changed but that in beta-LG-CHS was maintained, whereas the conformation around (125)Thr-(135)Lys (alpha-helix region) in the conjugates had changed.	Lysine	253-256	beta-lactoglobulin	Bos taurus	126-133	
14748079-0	2004	Transglutaminase-mediated modification of glutamine and lysine residues in native bovine beta-lactoglobulin.	Lysine	56-62	beta-lactoglobulin	Bos taurus	89-107	
14748079-6	2004	MTGase-mediated BLG crosslinking is hampered by the low reactivity of the lysines and enzymatic deamidation of the glutamines prevails.	Lysine	74-81	beta-lactoglobulin	Bos taurus	16-19	
10888497-4	2000	Structural analysis using monoclonal antibodies indicated that the conformation around (15)Val-(29)Ile (beta-sheet region) in beta-LG-GlcN and beta-LG-CPO had changed but that in beta-LG-CHS was maintained, whereas the conformation around (125)Thr-(135)Lys (alpha-helix region) in the conjugates had changed.	Lysine	253-256	beta-lactoglobulin	Bos taurus	143-150	
10888497-4	2000	Structural analysis using monoclonal antibodies indicated that the conformation around (15)Val-(29)Ile (beta-sheet region) in beta-LG-GlcN and beta-LG-CPO had changed but that in beta-LG-CHS was maintained, whereas the conformation around (125)Thr-(135)Lys (alpha-helix region) in the conjugates had changed.	Lysine	253-256	beta-lactoglobulin	Bos taurus	143-150	
21920659-4	2011	In the present study, citraconylation was employed to neutralize the charges on accessible lysine residues of beta-lg and different approaches such as turbidimetry, thermodynamic analysis, extrinsic fluorimetry and theoretical studies have been successfully used to compare the different behaviors of the native and modified proteins.	Lysine	91-97	beta-lactoglobulin	Bos taurus	110-117	
9240451-3	1997	Identification of lactosylated sites by trypsinolysis and Tandem MS indicate that, although the glycosylation reaction was non-specific and potentially involved all the reactive sites (alpha- and epsilon-amino groups), beta-LG appeared to have at least two populations of lysine with the distinct ability to react with lactose.	Lysine	272-278	beta-lactoglobulin	Bos taurus	219-226	
23129483-2	2013	Lactostatin (Ile-Ile-Ala-Glu-Lys), derived from beta-lactoglobulin in cow"s milk, is a bioactive peptide with hypocholesterolemic activity higher than sitosterol, a known anti-hypercholesterolemic drug.	Lysine	29-32	beta-lactoglobulin	Bos taurus	48-66	
18634071-1	1997	The major component of the whey fraction of bovine milk, beta-lactoglobulin (betaLG), has been transformed by grafting polyethylene glycol chains either on the thiol group (free and after reduction of the S-S bridges) of the cysteine residues, or on the amino group of the lysine residues and/or of the N-terminal amino acid.	Lysine	273-279	beta-lactoglobulin	Bos taurus	57-75	
26281976-4	2015	We describe here the expression in the yeast Pichia pastoris of a mutant bovine beta-LG, in which lysine at position 69, in the main epitopes of the protein, was changed into asparagine (Lys69Asn).	Lysine	98-104	beta-lactoglobulin	Bos taurus	80-87	
20875748-0	2011	Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified beta-lactoglobulin: Relevance towards anti-HIV binding.	Lysine	70-76	beta-lactoglobulin	Bos taurus	86-104	
20875748-4	2011	In this article, interactions between lysine modified bovine beta-lactoglobulin (beta-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process.	Lysine	38-44	beta-lactoglobulin	Bos taurus	61-79	
20875748-4	2011	In this article, interactions between lysine modified bovine beta-lactoglobulin (beta-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process.	Lysine	38-44	beta-lactoglobulin	Bos taurus	81-88	
20875748-5	2011	Lysine residues of beta-lg were modified by acetylation and succinylation.	Lysine	0-6	beta-lactoglobulin	Bos taurus	19-26