PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15921168-0	2005	Hb Kurosaki [alpha7(A5)Lys -->Glu (AAG --> GAG)]: an alpha2-globin gene mutation found in Thailand.	Glutamic Acid	30-33	N-methylpurine DNA glycosylase	Homo sapiens	35-38	
26719496-5	2016	The guanine-to-adenine change causes substitution of the normal glutamic acid codon (GAG) with a mutant lysine codon (AAG) at position 312 (E312 K mutation).	Glutamic Acid	64-77	N-methylpurine DNA glycosylase	Homo sapiens	118-121	
19876867-6	2009	We found a deletion of AAG at position 595-597 of TP53 (exon 6), resulting in the deletion of Glu 199 in the protein and a genomic polymorphism of TP73, identified as an A-to-G change, at position E8/+15 at intron 8 (IVS8-15A>G).	Glutamic Acid	94-97	N-methylpurine DNA glycosylase	Homo sapiens	23-26	
19500310-1	2009	Human leukocyte antigen (HLA)-DRB1*1611 has one nucleotide change at codon 14 (GAG-->AAG) from DRB1*160201, resulting in a coding change from Glu to Lys.	Glutamic Acid	145-148	N-methylpurine DNA glycosylase	Homo sapiens	88-91	
15921168-1	2005	Hb Kurosaki [alpha 7(A5)Lys --> Glu (AAG --> GAG)], has been found for the first time in Thailand.	Glutamic Acid	32-35	N-methylpurine DNA glycosylase	Homo sapiens	37-40	
10660595-2	2000	Although Asp was identified as the active site residue in various DNA glycosylases based on the crystal structure, Glu-125 in human MPG (Glu-145 in mouse MPG) was recently proposed to be the catalytic residue.	Glutamic Acid	115-118	N-methylpurine DNA glycosylase	Homo sapiens	132-135	
11380459-5	2001	Band 3 Cape Town is defined by a GAG-->AAG point mutation at codon 90, substituting a glutamic acid with a lysine in the cytoplasmic domain of the molecule, while band 3 Prague III is a codon 870 CGG-->TGG point mutation, replacing an arginine with a tryptophan in the transmembrane region of band 3. mRNA is transcribed from both mutant alleles, implying that mutant proteins are synthesized, but are either degraded prior to membrane incorporation or insertion is impaired.	Glutamic Acid	89-102	N-methylpurine DNA glycosylase	Homo sapiens	42-45	
10660595-2	2000	Although Asp was identified as the active site residue in various DNA glycosylases based on the crystal structure, Glu-125 in human MPG (Glu-145 in mouse MPG) was recently proposed to be the catalytic residue.	Glutamic Acid	137-140	N-methylpurine DNA glycosylase	Homo sapiens	132-135	
9398839-3	1997	Two mutations, a C-->T substitution that changes the Arg 257 (CGA) to a stop codon (TGA) and an A-->G substitution that changes the Lys 83 (AAG) to a Glu codon (GAG), were found in this novel gene in Swiss and Finnish APECED patients.	Glutamic Acid	156-159	N-methylpurine DNA glycosylase	Homo sapiens	146-149	
7635945-4	1995	DNA sequence analysis of the mutant apoE gene revealed a single-point mutation that resulted in the substitution of glutamic acid (GAG) for lysine (AAG) at residue 146 in the proposed receptor-binding domain of apoE.	Glutamic Acid	116-129	N-methylpurine DNA glycosylase	Homo sapiens	148-151	
7912945-11	1994	The results showed a point mutation in the PrP gene at codon 200; GAG to AAG (Glu-->Lys).	Glutamic Acid	78-81	N-methylpurine DNA glycosylase	Homo sapiens	73-76	
1364220-4	1992	Sequence analysis of the amplified product revealed a GAG > AAG transversion at codon 26, which resulted in an amino acid substitution of lysine for glutamic acid.	Glutamic Acid	152-165	N-methylpurine DNA glycosylase	Homo sapiens	63-66	
1356443-2	1992	Sequence analysis of the DNA of the proband that was amplified by PCR and subcloned, revealed a single substitution of one lysine (AAG) for one glutamic acid (GAG) at position 146, thereby adding two negatively charged units to apo E3.	Glutamic Acid	144-157	N-methylpurine DNA glycosylase	Homo sapiens	131-134	
1520883-3	1992	In all individuals, we found a single-base substitution in codon 56 of one band 3 allele changing lysine to glutamic acid (AAG----GAG) which, in some of them, was linked with an additional mutation in cdb3.	Glutamic Acid	108-121	N-methylpurine DNA glycosylase	Homo sapiens	123-126	
1674745-7	1991	A second G to A substitution at amino acid 13 led to the exchange of lysine (AAG) for glutamic acid (GAG), thereby adding 2 positive charge units to the protein and producing the apoE-5 variant.	Glutamic Acid	86-99	N-methylpurine DNA glycosylase	Homo sapiens	77-80	
1685643-3	1991	This mutation at codon 200 changes glutamic acid coded by GAG to lysine coded by AAG.	Glutamic Acid	35-48	N-methylpurine DNA glycosylase	Homo sapiens	81-84	
1973689-8	1990	In the apoA-IV-3 allele we identified a single G to A substitution that converts the glutamic acid (GAG) at position 230 of the mature protein to a lysine (AAG), thus adding 2 positive charge units to the apoA-IV-1 isoprotein (pI 4.97) and forming the more basic apoA-IV-3 isoprotein (pI 5.08).	Glutamic Acid	85-98	N-methylpurine DNA glycosylase	Homo sapiens	156-159	
31450984-4	2019	Identification of abnormal hemoglobin (Hb) using direct DNA sequencing showed a genetic defect causing a delta-globin gene missense mutation at codon 43 (GAG>AAG) causing a glutamic acid to lysine substitution corresponding to Hb A2-Melbourne.	Glutamic Acid	176-189	N-methylpurine DNA glycosylase	Homo sapiens	161-164