PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25146482-4	2015	However, HLA-B*44:05 (identical to B*44:02 except for tyrosine 116) can efficiently load peptides in the absence of tapasin.	Tyrosine	54-62	major histocompatibility complex, class I, B	Homo sapiens	9-14	
26811146-8	2016	In this regard, HLA-B*27 bound efficiently peptides with aliphatic, aromatic (including tyrosine), and basic C-terminal residues while Mamu-B*08 preferred peptides with leucine and phenylalanine in this position.	Tyrosine	88-96	major histocompatibility complex, class I, B	Homo sapiens	16-21	
33258295-1	2021	HLA-B*55:71 has one nucleotide change from HLA-B*55:02:01:01 where Histidine (3) is changed to Tyrosine.	Tyrosine	95-103	major histocompatibility complex, class I, B	Homo sapiens	0-5	
33258295-1	2021	HLA-B*55:71 has one nucleotide change from HLA-B*55:02:01:01 where Histidine (3) is changed to Tyrosine.	Tyrosine	95-103	major histocompatibility complex, class I, B	Homo sapiens	43-48	
27723268-7	2017	RESULTS: By expressing HLA-B*27:05, 06-like, and 09 alleles on a restrictive rat transporter associated with antigen processing background, we demonstrate that a tyrosine expressed at p116, either alone or together with an aspartic acid residue at p114, inhibited HLA-B27 dimerization and increased the assembly rate.	Tyrosine	162-170	major histocompatibility complex, class I, B	Homo sapiens	23-28	
27723268-7	2017	RESULTS: By expressing HLA-B*27:05, 06-like, and 09 alleles on a restrictive rat transporter associated with antigen processing background, we demonstrate that a tyrosine expressed at p116, either alone or together with an aspartic acid residue at p114, inhibited HLA-B27 dimerization and increased the assembly rate.	Tyrosine	162-170	major histocompatibility complex, class I, B	Homo sapiens	264-271	
12022472-3	2002	In contrast, natural killer receptors lack the Ca++ and sugar-binding amino acids but conserve homologous cysteines in the form of C-type lectin, and possess an immunoreceptor tyrosine-based inhibitory motif in the cytoplasmic region which inhibits killer activity when they recognize the self major histocompatibility (MHC) class I molecule.	Tyrosine	176-184	major histocompatibility complex, class I, B	Homo sapiens	294-341	
21968657-10	2012	CONCLUSION: Our results show that STAT-1 tyrosine 701 is constitutively highly phosphorylated in the HLA-B27-expressing monocyte/macrophage cell line.	Tyrosine	41-49	major histocompatibility complex, class I, B	Homo sapiens	101-108	
21968657-11	2012	Since phosphorylation of tyrosine 701 on STAT-1 is sufficient to induce interferon (IFN)-dependent genes, constitutive activity of this phosphorylation site may lead to the overexpression of IFN-dependent genes, as well as other STAT-1-dependent genes, in HLA-B27 monocyte/macrophages.	Tyrosine	25-33	major histocompatibility complex, class I, B	Homo sapiens	256-263	
18647362-4	2008	In HLA-B*4455, an nt exchange occurred in codon 9 of HLA-B*44020101, resulting in a change of the amino acid coding from tyrosine to histidine.	Tyrosine	121-129	major histocompatibility complex, class I, B	Homo sapiens	3-8	
20641675-11	2004	A synthetic peptide (Arg-Glu-Asn-Leu-Arg-Ile-Ala-Leu-Arg-Tyr, B2702-p) corresponding to residues 75-84 of HLA-B2702 was shown to bind specifically to VCAM-1 (9).	Tyrosine	57-60	major histocompatibility complex, class I, B	Homo sapiens	106-111	
16101835-2	2005	This allele shows a sequence identical to that of HLA-B*5601 except for two nucleotide substitutions that cause a change from TTA to TAC at codon 116 and an amino acidic change from Leucine to Tyrosine in the mature protein.	Tyrosine	193-201	major histocompatibility complex, class I, B	Homo sapiens	50-55	
14989719-4	2004	The sequence of B*5809 is identical to that of HLA-B*5801, except for a point mutation at position 583 in exon 3, where a T is substituted by a C. This change leads to an amino acidic substitution from Tyr (TAC) to His (CAC) at codon 171.	Tyrosine	202-205	major histocompatibility complex, class I, B	Homo sapiens	47-52	
23799076-8	2013	In contrast, competitive titration assays revealed that the Tyr to Phe substitution at P8 reduced T cell recognition by 50-130 fold despite intact peptide binding to HLA-B(*)35:01.	Tyrosine	60-63	major histocompatibility complex, class I, B	Homo sapiens	166-171	
20518835-3	2010	HLA-B*5728N, differs from HLA-B*5701 because of a nucleotide substitution at position 420 (C->G) resulting in a coding change from Tyrosine to a stop codon.	Tyrosine	134-142	major histocompatibility complex, class I, B	Homo sapiens	0-5	
20518835-3	2010	HLA-B*5728N, differs from HLA-B*5701 because of a nucleotide substitution at position 420 (C->G) resulting in a coding change from Tyrosine to a stop codon.	Tyrosine	134-142	major histocompatibility complex, class I, B	Homo sapiens	26-31	
18647362-4	2008	In HLA-B*4455, an nt exchange occurred in codon 9 of HLA-B*44020101, resulting in a change of the amino acid coding from tyrosine to histidine.	Tyrosine	121-129	major histocompatibility complex, class I, B	Homo sapiens	53-58	
18194362-2	2008	This allele is identical to the HLA-B*570101 allele except for two point mutations in exon 3 at codon 138 (ACG-->ACC) with no amino acid change [persisting threonine (T)] and at codon 171 (TAC-->CAC), resulting in an amino acid change from tyrosine (Y) to histidine (H).	Tyrosine	246-254	major histocompatibility complex, class I, B	Homo sapiens	32-37	
10395699-5	1999	In this report we show that ligation of class I molecules with Abs to distinct HLA-A locus and HLA-B locus molecules results in increased tyrosine phosphorylation of intracellular proteins and induction of fibroblast growth factor receptor expression on endothelial and smooth muscle cells.	Tyrosine	138-146	major histocompatibility complex, class I, B	Homo sapiens	95-100	
9435344-1	1998	HLA-B*3501 and -B*5101 molecules, which belong to the HLA-B5 cross-reactive group, bind peptides carrying similar anchor residues at P2 and the C-terminus, but differences are observed in the preference for a Tyr residue at the C-terminus and the affinity of peptides.	Tyrosine	209-212	major histocompatibility complex, class I, B	Homo sapiens	0-5	
11490536-11	1998	Therefore a Tyr C-terminal anchor correlates with the HLA-B27 F-pocket composition rather than with susceptibility to SA.	Tyrosine	12-15	major histocompatibility complex, class I, B	Homo sapiens	54-61	
9586638-4	1998	MHC I modulation relies on a tyrosine-based sorting signal located in the cytoplasmic domain of HLA-A and -B heavy chains.	Tyrosine	29-37	major histocompatibility complex, class I, B	Homo sapiens	96-108	
9098927-9	1997	This suggests that the ability of HLA-B27 to present peptides with C-terminal Tyr might be critical for its association to spondyloarthropathy.	Tyrosine	78-81	major histocompatibility complex, class I, B	Homo sapiens	34-41	
7878657-4	1994	The motif was found to be essentially identical for HLA-B*4402 and -B*4403, with a strong predominance for Glu at position 2, Tyr or Phe at positions 9 and 10 and hydrophobic residues, especially Met, at position 3.	Tyrosine	126-129	major histocompatibility complex, class I, B	Homo sapiens	52-57	
9382929-0	1997	HLA-B*2707 peptide motif: Tyr C-terminal anchor is not shared by all disease-associated subtypes.	Tyrosine	26-29	major histocompatibility complex, class I, B	Homo sapiens	0-5	
7751638-2	1995	According to the peptide motif of HLA-B*3501, aliphatic hydrophobic (Leu, Ile, and Met) or aromatic residues (Tyr and Phe) specify the main anchor at the C terminus, and position 2 renders an auxiliary anchor for proline.	Tyrosine	110-113	major histocompatibility complex, class I, B	Homo sapiens	34-39	
8671633-2	1996	In common for all these peptides is the core sequence NH2-Ser-Arg-Tyr-Trp-Ala-Ile-Arg-Thr-Arg-COOH, NP383-391, known as an antigenic peptide specific for the HLA-B27 class I antigen.	Tyrosine	66-69	major histocompatibility complex, class I, B	Homo sapiens	158-165	
8624811-2	1996	Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket.	Tyrosine	116-124	major histocompatibility complex, class I, B	Homo sapiens	68-73	
8428632-1	1993	Peptides eluted from the native MHC class I molecule, Kd, are generally nonamers that display a strong preference for Tyr in position 2.	Tyrosine	118-121	major histocompatibility complex, class I, B	Homo sapiens	32-52	
8155602-2	1994	Both sequences were consistent with previously reported motifs of HLA-B*3501 binding peptides which carry proline at position 2 and tyrosine at position 9 as anchor residues.	Tyrosine	132-140	major histocompatibility complex, class I, B	Homo sapiens	66-71	
8155602-7	1994	These results indicate that two anchor residues, proline at position 2 and tyrosine at position 9 are critical in binding of peptides to HLA-B*3501 molecules.	Tyrosine	75-83	major histocompatibility complex, class I, B	Homo sapiens	137-142	
2126195-10	1990	Further studies showed that the tryptophan residue influenced the association of the gag peptide with HLA B27, because the affinity of the gag peptide for B27 was strongly increased after replacing this residue with a leucine or a tyrosine.	Tyrosine	231-239	major histocompatibility complex, class I, B	Homo sapiens	102-109