PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20108989-6	2010	The branched, 40 kDa PEG chain of peginterferon-alpha-2a is covalently attached via stable amide bonds to lysine residues of interferon-alpha-2a, and circulates as an intact molecule.	Lysine	106-112	interferon alpha 2	Homo sapiens	37-56	
18020402-3	2008	It is possible to extend the circulating half-life of IFN-alpha2 by random modification of lysine residues in the protein with polyethylene glycol (PEG); however, such preparations have heterogeneous structures and low specific activities, and may not provide optimal therapeutic benefits to patients.	Lysine	91-97	interferon alpha 2	Homo sapiens	54-64	
18937499-5	2008	In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1.	Lysine	47-50	interferon alpha 2	Homo sapiens	35-45	
18937499-5	2008	In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1.	Lysine	47-50	interferon alpha 2	Homo sapiens	54-64	
18937499-5	2008	In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1.	Lysine	47-50	interferon alpha 2	Homo sapiens	54-64	
18937499-5	2008	In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1.	Lysine	47-50	interferon alpha 2	Homo sapiens	54-64	
9758677-1	1998	Palmitoyl derivatives of interferon alpha2b (p-IFNalpha) were prepared by covalent attachment of the fatty acid to lysine residues in the protein through a reaction with N-hydroxysuccinimide palmitate ester.	Lysine	115-121	interferon alpha 2	Homo sapiens	25-43	
15656592-3	2005	Previous studies showed that it is possible to extend the circulating half-life of IFN-alpha2 by modifying lysine residues of the protein with amine-reactive poly(ethylene glycol) (PEG) reagents.	Lysine	107-113	interferon alpha 2	Homo sapiens	83-93	
15656592-4	2005	However, amine-PEGylated IFN-alpha2 comprises a heterogeneous product mixture with low specific activity due to the large number and critical locations of lysine residues in IFN-alpha2.	Lysine	155-161	interferon alpha 2	Homo sapiens	25-35	
15656592-4	2005	However, amine-PEGylated IFN-alpha2 comprises a heterogeneous product mixture with low specific activity due to the large number and critical locations of lysine residues in IFN-alpha2.	Lysine	155-161	interferon alpha 2	Homo sapiens	174-184	
15646642-7	2004	Interferon alpha-2a is monopegylated at four major positional lysine (Lys) residues.	Lysine	62-68	interferon alpha 2	Homo sapiens	0-19	
15646642-7	2004	Interferon alpha-2a is monopegylated at four major positional lysine (Lys) residues.	Lysine	70-73	interferon alpha 2	Homo sapiens	0-19	
9085937-2	1997	Thus, the mature IFN-alpha2a protein product is characterized by a lysine residue at position 23 (AAA) and a histidine at position 34 (CAA), IFN-alpha2b has an arginine at position 23 (AGA) and histidine at position 34 (CAT), and IFN-alpha2c has arginine residues at both positions 23 (AGA) and 34 (CGT).	Lysine	67-73	interferon alpha 2	Homo sapiens	17-27	
1692865-4	1990	Although a corresponding sequence of amino acids in the IFN-beta molecule was localized to the region 134-139 and shows only a 66% homology with the assumed IFN-alpha 2 binding site, lysine at position 132 in IFN-alpha 2 and at position 134 in IFN-beta seems to be crucial for establishment of the common epitope.	Lysine	183-189	interferon alpha 2	Homo sapiens	157-168	
1692865-4	1990	Although a corresponding sequence of amino acids in the IFN-beta molecule was localized to the region 134-139 and shows only a 66% homology with the assumed IFN-alpha 2 binding site, lysine at position 132 in IFN-alpha 2 and at position 134 in IFN-beta seems to be crucial for establishment of the common epitope.	Lysine	183-189	interferon alpha 2	Homo sapiens	209-220	
2077397-3	1990	An IFN-alpha analogue in which arginine and lysine residues 121 and 122 were replaced by 2 leucines was generated by site-directed in vitro mutagenesis of the IFN-alpha 4 gene; at equivalent concentrations of antiviral activity, this analogue was 10-fold less effective in NK stimulation.	Lysine	44-50	interferon alpha 2	Homo sapiens	3-12	
34497374-4	2021	In this study, we report that IFN-alpha2b enhances the histone deacetylase 3 (HDAC3)-mediated de-2-hydroxyisobutyrylation of histone H4 lysine 8 (H4K8) on HBV cccDNA minichromosome to restrict the cccDNA transcription in liver.	Lysine	136-142	interferon alpha 2	Homo sapiens	30-41