PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9075934-2	1997	Using site-directed mutagenesis, residues on HLA-C that determine the locus specificity (alphaVal-76), allotype group specificity (a dimorphism alphaAsn-80/Lys-80), and affinity of NKIR binding (a second pair of dimorphisms, alphaAla-73, Asp-90 or alphaThr-73, Ala-90) have been identified.	Lysine	156-159	major histocompatibility complex, class I, C	Homo sapiens	45-50	
9459510-4	1998	Cw*1203 (Ser-Asn) and Cw*12042 (Asn-Lys) constitute the second known example of HLA-C alleles only differing at the KIR-related dimorphism of residues 77-80.	Lysine	36-39	major histocompatibility complex, class I, C	Homo sapiens	80-85	
9670929-3	1998	One soluble KIR2D, derived from an inhibitory receptor with a long cytoplasmic tail (KIR2DL1), bound to HLA-C allotypes containing asparagine 77 and lysine 80 in the heavy chain, as expected, since these allotypes inhibit lysis by NK cells expressing KIR2DL1.	Lysine	149-155	major histocompatibility complex, class I, C	Homo sapiens	104-109	
9271317-2	1997	The synthetic random copolymer of the amino acids, L-Glu, L-Lys, L-Ala and L-Tyr, termed GLAT, with promiscuous binding to multiple MHC class II alleles, reduces the incidence, onset and severity of disease in the BIO.D2 --> BALB/c model of lethal GVHD.	Lysine	58-63	major histocompatibility complex, class I, C	Homo sapiens	132-135	
8218246-4	1993	The presence of a C-terminal Lys in many of the peptides that are restricted to IEk suggests that this electrostatic interaction is widely used to bind peptides to this MHC molecule.	Lysine	29-32	major histocompatibility complex, class I, C	Homo sapiens	169-172	
26239392-2	2015	HLA-C*14:02:13 differs from HLA-C*14:02:01 by a silent G to A substitution at nucleotide position 400 in exon 2, where lysine at position 66 remains unchanged.	Lysine	119-125	major histocompatibility complex, class I, C	Homo sapiens	0-5	
6226585-2	1983	This correlation, and the large body of (largely) circumstantial but still quite convincing data, suggests that these Ly and Leu molecules play a very important role in T cell responses by actually interacting with monomorphic MHC class specific determinants.	Lysine	118-120	major histocompatibility complex, class I, C	Homo sapiens	227-230	
28122963-5	2017	By repairing the deletion, we resurrected 11 alleles of KIR2DP1F , the functional antecedent of KIR2DP1 We demonstrate how K44-KIR2DP1F with lysine 44 recognized C1+HLA-C, whereas T44-KIR2DP1F recognized C2+HLA-C.	Lysine	141-147	major histocompatibility complex, class I, C	Homo sapiens	165-170	
28122963-5	2017	By repairing the deletion, we resurrected 11 alleles of KIR2DP1F , the functional antecedent of KIR2DP1 We demonstrate how K44-KIR2DP1F with lysine 44 recognized C1+HLA-C, whereas T44-KIR2DP1F recognized C2+HLA-C.	Lysine	141-147	major histocompatibility complex, class I, C	Homo sapiens	207-212	
21541786-1	2011	Alternative lysine and methionine residues at position 44 in the D1 domain determine the specificities of human lineage III killer cell immunoglobulin-like receptors (KIR) for the C1 and C2 epitopes of HLA-C.	Lysine	12-18	major histocompatibility complex, class I, C	Homo sapiens	202-207	
25911107-0	2015	Histone Deacetylase 3 (HDAC3)-dependent Reversible Lysine Acetylation of Cardiac Myosin Heavy Chain Isoforms Modulates Their Enzymatic and Motor Activity.	Lysine	51-57	major histocompatibility complex, class I, C	Homo sapiens	81-99	
25911107-6	2015	Biomechanical studies revealed that lysine acetylation significantly decreased the Km for the actin-activated ATPase activity of MHC isoforms.	Lysine	36-42	major histocompatibility complex, class I, C	Homo sapiens	129-132	
20036705-8	2010	The genotype 2DL2+/HLA-C lys(80)+ was also more common in controls (IBD: p = 0.005; UC: p = 0.01; CD: p = NS); as well as 2DL1+/HLA-C Asn(80)+ (IBD: p = 0.026; UC: p = NS;CD: p = NS).	Lysine	25-28	major histocompatibility complex, class I, C	Homo sapiens	19-24	
20036705-8	2010	The genotype 2DL2+/HLA-C lys(80)+ was also more common in controls (IBD: p = 0.005; UC: p = 0.01; CD: p = NS); as well as 2DL1+/HLA-C Asn(80)+ (IBD: p = 0.026; UC: p = NS;CD: p = NS).	Lysine	25-28	major histocompatibility complex, class I, C	Homo sapiens	128-133	
21177250-0	2011	HDAC3-dependent reversible lysine acetylation of cardiac myosin heavy chain isoforms modulates their enzymatic and motor activity.	Lysine	27-33	major histocompatibility complex, class I, C	Homo sapiens	57-75	
18297378-8	2008	The genotype 2DS1+/HLA-C lys(80)+ was more common in subjects with AS.	Lysine	25-28	major histocompatibility complex, class I, C	Homo sapiens	19-24	
16720236-12	2006	CONCLUSION: When DTPA was conjugated to the epsilon NH2 group of the Lys(154) residue, MHC binding of the peptide was preserved and could still be recognized by cytotoxic T cells.	Lysine	69-72	major histocompatibility complex, class I, C	Homo sapiens	87-90	
16185272-5	2005	This permits classifying all HLA-C alleles into two functional groups: asparagine (N80) or lysine (K80) carrying alleles.	Lysine	91-97	major histocompatibility complex, class I, C	Homo sapiens	29-34	
15495159-0	2004	MHC class I-associated presentation of exogenous peptides is not only enhanced but also prolonged by linking with a C-terminal Lys-Asp-Glu-Leu endoplasmic reticulum retrieval signal.	Lysine	127-130	major histocompatibility complex, class I, C	Homo sapiens	0-3	
15495159-3	2004	In this study, we observed that exogenous peptides that were artificially fused with an endoplasmic reticulum (ER) retrieval signal, a C-terminal Lys-Asp-Glu-Leu sequence, could be efficiently presented by intracellular MHC class I molecules in a TAP- and proteasome-independent, but brefeldin A-sensitive manner.	Lysine	146-149	major histocompatibility complex, class I, C	Homo sapiens	220-223	
11777974-8	2002	The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts.	Lysine	10-12	major histocompatibility complex, class I, C	Homo sapiens	41-44	
11777974-8	2002	The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts.	Lysine	10-12	major histocompatibility complex, class I, C	Homo sapiens	161-164	
11777974-8	2002	The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts.	Lysine	67-69	major histocompatibility complex, class I, C	Homo sapiens	41-44	
11777974-8	2002	The three Ly-49C mutations that affected MHC binding correspond to Ly-49A residues that are in contact or close to H-2D(d) in the co-crystal, demonstrating that MHC class I binding by Ly-49C is dependent on residues in the same area as that used by Ly-49A for ligand contacts.	Lysine	67-69	major histocompatibility complex, class I, C	Homo sapiens	161-164