PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1390707-3	1992	When H1 and the basic N-terminal tails of the core histones are dissociated from the DNA by treating nuclei with 0.4 and 0.8 M NaCl, the two tyrosines which are adjacent to the basic regions of H2B and H3 become accessible as well.	Tyrosine	141-150	H2B clustered histone 21	Homo sapiens	194-197	
1390707-5	1992	When the H2A-H2B dimers are dissociated from the chromatin by raising the NaCl concentration to 1.2 M, three to four tyrosines located in the structured regions of H2B and H4 are exposed, suggesting that these tyrosine residues may be located at the dimer-tetramer interface.	Tyrosine	117-126	H2B clustered histone 21	Homo sapiens	13-16	
1390707-5	1992	When the H2A-H2B dimers are dissociated from the chromatin by raising the NaCl concentration to 1.2 M, three to four tyrosines located in the structured regions of H2B and H4 are exposed, suggesting that these tyrosine residues may be located at the dimer-tetramer interface.	Tyrosine	117-126	H2B clustered histone 21	Homo sapiens	164-167	
1390707-5	1992	When the H2A-H2B dimers are dissociated from the chromatin by raising the NaCl concentration to 1.2 M, three to four tyrosines located in the structured regions of H2B and H4 are exposed, suggesting that these tyrosine residues may be located at the dimer-tetramer interface.	Tyrosine	117-125	H2B clustered histone 21	Homo sapiens	13-16	
1390707-5	1992	When the H2A-H2B dimers are dissociated from the chromatin by raising the NaCl concentration to 1.2 M, three to four tyrosines located in the structured regions of H2B and H4 are exposed, suggesting that these tyrosine residues may be located at the dimer-tetramer interface.	Tyrosine	117-125	H2B clustered histone 21	Homo sapiens	164-167	
29290954-2	2017	Previously, we uncovered that WEE1 phosphorylates histone H2B at tyrosine 37 (pY37-H2B) to negatively regulate global histone transcriptional output.	Tyrosine	65-73	H2B clustered histone 21	Homo sapiens	58-61	
29290954-2	2017	Previously, we uncovered that WEE1 phosphorylates histone H2B at tyrosine 37 (pY37-H2B) to negatively regulate global histone transcriptional output.	Tyrosine	65-73	H2B clustered histone 21	Homo sapiens	83-86	
26536630-8	2016	The results showed that peroxynitrite-mediated nitration and oxidation in H2B histone exhibited hyperchromicity, decrease of tyrosine fluorescence accompanied by increase in ANS-binding specific fluorescence, loss of beta-sheet structure, appearance of new peak in FT-IR, increase in melting temperature and also loss of alpha-helix to produce a partially folded structure in comparison to intrinsically disordered structure of native H2B histone.	Tyrosine	125-133	H2B clustered histone 21	Homo sapiens	74-77	
4027221-2	1985	Sequence analysis of the peptides isolated from the H2A-H2B dimer formed in solution and in nuclei demonstrated that both dimers are produced through the covalent linkage of Tyr-40 of H2B and Pro-26 of H2A.	Tyrosine	174-177	H2B clustered histone 21	Homo sapiens	56-59	
4027221-2	1985	Sequence analysis of the peptides isolated from the H2A-H2B dimer formed in solution and in nuclei demonstrated that both dimers are produced through the covalent linkage of Tyr-40 of H2B and Pro-26 of H2A.	Tyrosine	174-177	H2B clustered histone 21	Homo sapiens	184-187	
4027221-4	1985	We conclude that the precise juxtaposition of Tyr-40 of H2B and Pro-26 of H2A in this region of the H2A/H2B contact site is not altered upon interaction of these histones with H3 and H4 (tetramer), DNA, or other chromosomal components during nucleosome assembly.	Tyrosine	46-49	H2B clustered histone 21	Homo sapiens	56-59	
4027221-4	1985	We conclude that the precise juxtaposition of Tyr-40 of H2B and Pro-26 of H2A in this region of the H2A/H2B contact site is not altered upon interaction of these histones with H3 and H4 (tetramer), DNA, or other chromosomal components during nucleosome assembly.	Tyrosine	46-49	H2B clustered histone 21	Homo sapiens	104-107	
4027222-3	1985	Tyrosines-83 and -121 of H2B were iodinated, both when the histone was free in solution and when it was associated with H2A, while tyrosines-37, -40, and -42 of H2B were not iodinated under either condition.	Tyrosine	0-9	H2B clustered histone 21	Homo sapiens	25-28	
6706950-5	1984	We show that tyrosines 37, 40, and 42 of H2B are protected from iodination in intact core particles, as expected since these tyrosines lie within the H2B-H2A binding site.	Tyrosine	13-22	H2B clustered histone 21	Homo sapiens	41-44	
6706950-5	1984	We show that tyrosines 37, 40, and 42 of H2B are protected from iodination in intact core particles, as expected since these tyrosines lie within the H2B-H2A binding site.	Tyrosine	13-22	H2B clustered histone 21	Homo sapiens	150-153	
6706950-5	1984	We show that tyrosines 37, 40, and 42 of H2B are protected from iodination in intact core particles, as expected since these tyrosines lie within the H2B-H2A binding site.	Tyrosine	125-134	H2B clustered histone 21	Homo sapiens	41-44	
6706950-6	1984	Yet iodination of these tyrosines in denatured H2B does not interfere with nucleosome assembly.	Tyrosine	24-33	H2B clustered histone 21	Homo sapiens	47-50	
6706950-8	1984	In contrast, iodination of tyrosines 83 and 121 of H2B, as well as iodination of the tyrosines of H2A, increases the stability of the histone octamer core.	Tyrosine	27-36	H2B clustered histone 21	Homo sapiens	51-54	
15632282-4	2005	To provide insights into how histone variants may impact the thermodynamics of the nucleosome, the stability of the heterodimer between the H2A.Z variant and H2B was determined by urea-induced denaturation, monitored by far-UV circular dichroism, intrinsic Tyr fluorescence intensity, and anisotropy.	Tyrosine	257-260	H2B clustered histone 21	Homo sapiens	158-161