PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23933260-1 2013 Chromatin posttranslational modifications (PTMs), including monoubiquitylation of histone H2B on lysine 120 (H2Bub1), play a major role in regulating genome functions. Lysine 97-103 H2B clustered histone 21 Homo sapiens 90-93 20442396-0 2010 A modified "cross-talk" between histone H2B Lys-120 ubiquitination and H3 Lys-79 methylation. Lysine 44-47 H2B clustered histone 21 Homo sapiens 40-43 22252316-1 2012 Ubiquitylation of H2B on lysine 120 (H2Bub) is associated with active transcriptional elongation. Lysine 25-31 H2B clustered histone 21 Homo sapiens 18-21 23417674-5 2013 Likewise, the point mutation of lysine 123 (ubiquitylation site) to arginine of H2B (H2B-K123R) also lowers the association of RNA polymerase II with GAL1, consistent with the role of H2B ubiquitylation in promoting RNA polymerase II association. Lysine 32-38 H2B clustered histone 21 Homo sapiens 80-83 23417674-5 2013 Likewise, the point mutation of lysine 123 (ubiquitylation site) to arginine of H2B (H2B-K123R) also lowers the association of RNA polymerase II with GAL1, consistent with the role of H2B ubiquitylation in promoting RNA polymerase II association. Lysine 32-38 H2B clustered histone 21 Homo sapiens 85-90 23417674-5 2013 Likewise, the point mutation of lysine 123 (ubiquitylation site) to arginine of H2B (H2B-K123R) also lowers the association of RNA polymerase II with GAL1, consistent with the role of H2B ubiquitylation in promoting RNA polymerase II association. Lysine 32-38 H2B clustered histone 21 Homo sapiens 85-88 22549955-1 2012 Monoubiquitination of histone H2B on Lys 123 (H2BK123ub) is a transient histone modification considered to be essential for establishing H3K4 and H3K79 trimethylation by Set1/COMPASS and Dot1, respectively. Lysine 37-40 H2B clustered histone 21 Homo sapiens 30-33 22244335-1 2012 Histone H2B ubiquitylation is a transcription-dependent modification that not only regulates nucleosome dynamics but also controls the trimethylation of histone H3 on lysine 4 by promoting ubiquitylation of Swd2, a component of both the histone methyltransferase COMPASS complex and the cleavage and polyadenylation factor(CPF). Lysine 167-173 H2B clustered histone 21 Homo sapiens 8-11 21739721-0 2011 An acetylation-mono-ubiquitination switch on lysine 120 of H2B. Lysine 45-51 H2B clustered histone 21 Homo sapiens 59-62 21739721-3 2011 Lysine 120 of H2B is modified by two PTMs: ubiquitination, which is required for further trans-tail H3 methylations and elongation, and acetylation, whose role is less clear. Lysine 0-6 H2B clustered histone 21 Homo sapiens 14-17 21739721-9 2011 Our data point at acetylation of Lysine 120 of H2B as an early mark of poised or active state and establish a temporal sequence between acetylation and mono-ubiquitination of this H2B residue. Lysine 33-39 H2B clustered histone 21 Homo sapiens 47-50 20442396-0 2010 A modified "cross-talk" between histone H2B Lys-120 ubiquitination and H3 Lys-79 methylation. Lysine 74-77 H2B clustered histone 21 Homo sapiens 40-43 20442396-6 2010 We found that H2B ubiquitination is inversely correlated with H3 Lys-79 methylation. Lysine 65-68 H2B clustered histone 21 Homo sapiens 14-17 20442396-7 2010 Therefore, we propose that a catalytic and inhibitory loop mechanism may better describe the cross-talk relationship between H2B ubiquitination and H3 Lys-79 methylation. Lysine 151-154 H2B clustered histone 21 Homo sapiens 125-128 20086098-7 2010 The immunopurified BAF250b E3 ubiquitin ligase was found to target histone H2B at lysine 120 for monoubiquitination in vitro. Lysine 82-88 H2B clustered histone 21 Homo sapiens 75-78 16319397-9 2006 The main histone H2B variant, H2BA, was acetylated at Lys-12, -15, and -20. Lysine 54-57 H2B clustered histone 21 Homo sapiens 17-20 19923226-4 2010 Disruption of Lge1 abolished ubiquitylation of histone H2B on lysine 123 and H3 methylation on lysines 4 and 79 and resulted in significant sensitivity to 6-azauracil and mycophenolic acid. Lysine 62-68 H2B clustered histone 21 Homo sapiens 55-58 19923226-4 2010 Disruption of Lge1 abolished ubiquitylation of histone H2B on lysine 123 and H3 methylation on lysines 4 and 79 and resulted in significant sensitivity to 6-azauracil and mycophenolic acid. Lysine 95-102 H2B clustered histone 21 Homo sapiens 55-58 18449190-3 2008 One such modification, ubiquitylation of histone H2B (uH2B) on lysine 120 (K120) in humans, and lysine 123 in yeast, has been correlated with enhanced methylation of lysine 79 (K79) of histone H3 (refs 5-8), by K79-specific methyltransferase Dot1 (KMT4). Lysine 63-69 H2B clustered histone 21 Homo sapiens 49-52 17643376-2 2007 We previously studied histone H2B ubiquitylation on lysine 123 and subsequent deubiquitylation by SAGA-associated Ubp8. Lysine 52-58 H2B clustered histone 21 Homo sapiens 30-33 15528187-5 2005 Lge1p is a nuclear protein that has been found to play a role in ubiquitination of histone H2B at Lys(123). Lysine 98-101 H2B clustered histone 21 Homo sapiens 91-94 14563679-3 2003 Substitution of the H2B ubiquitylation site at Lys 123 (K123) lowered transcription of certain genes regulated by the acetylation complex SAGA. Lysine 47-50 H2B clustered histone 21 Homo sapiens 20-23 14563679-8 2003 In addition, disruption of either ubiquitylation or Ubp8-mediated deubiquitylation of H2B resulted in altered levels of gene-associated H3 Lys 4 methylation and Lys 36 methylation, which have both been linked to transcription. Lysine 139-142 H2B clustered histone 21 Homo sapiens 86-89 14563679-8 2003 In addition, disruption of either ubiquitylation or Ubp8-mediated deubiquitylation of H2B resulted in altered levels of gene-associated H3 Lys 4 methylation and Lys 36 methylation, which have both been linked to transcription. Lysine 161-164 H2B clustered histone 21 Homo sapiens 86-89 1753964-3 1991 H2B can be linked to DNA via its N-terminal tail and via several lysines contained within residues 24-34. Lysine 65-72 H2B clustered histone 21 Homo sapiens 0-3 33796843-3 2021 Here, we found that histone H2B is mainly degraded through the proteasome-mediated pathway, and the lysine-120 site of H2B is essential for its K48-linked polyubiquitination and degradation. Lysine 100-106 H2B clustered histone 21 Homo sapiens 28-31 32341358-3 2020 Here we show that RNF40, a histone H2B lysine 120 E3 ubiquitin-protein ligase, is specifically required for early reprogramming during induced pluripotency. Lysine 39-45 H2B clustered histone 21 Homo sapiens 35-38 34290256-4 2021 Among these are RNF20 and RNF40, which form a complex that monoubiquitinates H2B on lysine 120. Lysine 84-90 H2B clustered histone 21 Homo sapiens 77-80 35074526-5 2022 Mechanism study suggests that ECL covalently modifies a previously undisclosed lysine 46 (K46) in H2B, and recruits E3 ubiquitin ligase RNF20 to promote H2Bub1 at K120. Lysine 79-85 H2B clustered histone 21 Homo sapiens 98-101 196686-4 1977 The purified enzyme displays high specificity for the lysine-rich histones (H1, H2b, H2a). Lysine 54-60 H2B clustered histone 21 Homo sapiens 80-83 861226-3 1977 For lysine-rich histones (H1 and H2B) it has been found that the main characteristics which governs the interaction with DNA are located in the very lysine-rich part of the molecules, i.e. in the C-H1 and N-H2B segments. Lysine 4-10 H2B clustered histone 21 Homo sapiens 33-36 861226-3 1977 For lysine-rich histones (H1 and H2B) it has been found that the main characteristics which governs the interaction with DNA are located in the very lysine-rich part of the molecules, i.e. in the C-H1 and N-H2B segments. Lysine 149-155 H2B clustered histone 21 Homo sapiens 33-36 6845437-2 1983 Moderately lysine-rich histones H2A and H2B were found to be more susceptible to acetylation than arginine-rich H3 and H4. Lysine 11-17 H2B clustered histone 21 Homo sapiens 40-43 33070155-7 2020 We demonstrate that RNF40-driven H2B monoubiquitination is essential for transcriptional activation of RHO/ROCK/LIMK pathway components and proper actin-cytoskeleton dynamics through a trans-histone crosstalk with histone 3 lysine 4 trimethylation (H3K4me3). Lysine 224-230 H2B clustered histone 21 Homo sapiens 33-36 31485071-5 2019 H3K4 methylation is stimulated by mono-ubiquitination of histone H2B on lysine 120 (H2BK120ub1), a prevalent histone H2B mark that disrupts chromatin compaction and favours open chromatin structures, but the underlying mechanism remains unknown10-12. Lysine 72-78 H2B clustered histone 21 Homo sapiens 65-68 31267712-1 2019 Monoubiquitination of histone H2B on lysine 120 (H2Bub1) is an epigenetic mark generally associated with transcriptional activation, yet the global functions of H2Bub1 remain poorly understood. Lysine 37-43 H2B clustered histone 21 Homo sapiens 30-33 30942468-6 2019 In addition, deletion mutants without RING domain or C-terminus of TRAIP diminished the ability to induce H2B monoubiquitination at lysine 120. Lysine 132-138 H2B clustered histone 21 Homo sapiens 106-109 30791110-7 2019 By disrupting an evolutionarily conserved Cullin4A-damage-specific DNA binding protein 1-RING type of E3 ligase, CRL4WDR70 , through its H-box, we show that HBx inhibits H2B monoubiquitylation at lysine 120 at double-strand breaks, thus reducing the efficiency of long-range resection. Lysine 196-202 H2B clustered histone 21 Homo sapiens 170-173 30510186-0 2018 MacroH2A1 chromatin specification requires its docking domain and acetylation of H2B lysine 20. Lysine 85-91 H2B clustered histone 21 Homo sapiens 81-84 26759222-6 2016 H2B regained acetylation on multiple lysine residues, phosphorylation on Thr19, and methylation on Lys23 and Lys43 in the DU-145 cells after sodium butyrate treatment. Lysine 37-43 H2B clustered histone 21 Homo sapiens 0-3 29507117-5 2018 SMU1, by acting as a substrate recognition module, binds to H2B and mediates monoubiquitylation at the lysine (K) residue K120 through CRL7SMU1 E3 ligase complex. Lysine 103-109 H2B clustered histone 21 Homo sapiens 60-63 26830124-1 2016 Ubiquitylation of histone H2B at lysine 120 (H2B-Ub), a post-translational modification first discovered in 1980, plays a critical role in diverse nuclear processes including the regulation of transcription and DNA damage repair. Lysine 33-39 H2B clustered histone 21 Homo sapiens 26-29 26830124-1 2016 Ubiquitylation of histone H2B at lysine 120 (H2B-Ub), a post-translational modification first discovered in 1980, plays a critical role in diverse nuclear processes including the regulation of transcription and DNA damage repair. Lysine 33-39 H2B clustered histone 21 Homo sapiens 45-48 26830124-2 2016 Herein, we use a suite of protein chemistry methods to explore how H2B-Ub stimulates hDot1L-mediated methylation of histone H3 on lysine 79 (H3K79me). Lysine 130-136 H2B clustered histone 21 Homo sapiens 67-70 26709619-3 2016 Our results show that a lysine-containing part of this H2B tail that is subject to post-translational modification is engulfed by the enlarged DNA minor groove imposed by the lesion. Lysine 24-30 H2B clustered histone 21 Homo sapiens 55-58 26330467-3 2015 Here, we analyze differential histone modifications between WT and MED23(-/-) (KO) cells and identify H2B mono-ubiquitination at lysine 120 (H2Bub) as a MED23-dependent histone modification. Lysine 129-135 H2B clustered histone 21 Homo sapiens 102-105 26240340-1 2015 Ubiquitylation of histone H2B at lysine 120 (H2B-Ub) plays a critical role in transcriptional elongation, chromatin conformation, as well as the regulation of specific histone H3 methylations. Lysine 33-39 H2B clustered histone 21 Homo sapiens 26-29 26240340-1 2015 Ubiquitylation of histone H2B at lysine 120 (H2B-Ub) plays a critical role in transcriptional elongation, chromatin conformation, as well as the regulation of specific histone H3 methylations. Lysine 33-39 H2B clustered histone 21 Homo sapiens 45-48 25063569-3 2014 In eukaryotic organisms, a single Ub is attached to specific lysine residues of histones H2A and H2B in a modification that, unlike many other forms of ubiquitination in the cell, does not signal degradation. Lysine 61-67 H2B clustered histone 21 Homo sapiens 97-100 24526689-2 2014 Mono-ubiquitination of H2B in the histone tail (at Lys-123 in yeast or Lys-120 in humans) is a conserved modification that has been implicated in the regulation of transcription, replication, and DNA repair processes. Lysine 51-54 H2B clustered histone 21 Homo sapiens 23-26 24526689-2 2014 Mono-ubiquitination of H2B in the histone tail (at Lys-123 in yeast or Lys-120 in humans) is a conserved modification that has been implicated in the regulation of transcription, replication, and DNA repair processes. Lysine 71-74 H2B clustered histone 21 Homo sapiens 23-26 24339737-0 2013 The oncogenic polycomb histone methyltransferase EZH2 methylates lysine 120 on histone H2B and competes ubiquitination. Lysine 65-71 H2B clustered histone 21 Homo sapiens 87-90 24339737-3 2013 In the present study, we demonstrated that EZH2 has the function to monomethylate lysine 120 on histone H2B (H2BK120). Lysine 82-88 H2B clustered histone 21 Homo sapiens 104-107 24339737-3 2013 In the present study, we demonstrated that EZH2 has the function to monomethylate lysine 120 on histone H2B (H2BK120). Lysine 82-88 H2B clustered histone 21 Homo sapiens 109-116