PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 32500264-3 2020 Here, we identified HP1a-interacting domains in the somatic cells of Drosophila ovaries using a DamID-seq approach and compared them with insertion sites of transposable elements (TEs) revealed by genome sequencing. damid 96-101 Suppressor of variegation 205 Drosophila melanogaster 20-24 27579368-2 2016 Targeting of HP1 proteins to specific chromatin locales is mediated, at least in part, by the HP1 chromodomain, which binds to histone H3 methylated at lysine 9 that marks condensed regions of the genome. Lysine 152-158 Suppressor of variegation 205 Drosophila melanogaster 13-16 27579368-2 2016 Targeting of HP1 proteins to specific chromatin locales is mediated, at least in part, by the HP1 chromodomain, which binds to histone H3 methylated at lysine 9 that marks condensed regions of the genome. Lysine 152-158 Suppressor of variegation 205 Drosophila melanogaster 94-97 27579368-6 2016 These findings help elucidate important functional roles of reversible posttranslational modifications of proteins in the HP1 family, in this case, regulating the targeting of a ciliate HP1 to chromatin regions marked with methylated H3 lysine 27. Lysine 237-243 Suppressor of variegation 205 Drosophila melanogaster 122-125 27579368-6 2016 These findings help elucidate important functional roles of reversible posttranslational modifications of proteins in the HP1 family, in this case, regulating the targeting of a ciliate HP1 to chromatin regions marked with methylated H3 lysine 27. Lysine 237-243 Suppressor of variegation 205 Drosophila melanogaster 186-189 25860864-8 2015 Further analysis of muscle-specific knockdown of heterochromatin protein 1a revealed that the excessive gammaH2AX accumulation in thoracic and leg muscles induces accelerated degeneration and decreases longevity. gammah2ax 104-113 Suppressor of variegation 205 Drosophila melanogaster 49-75 27425411-7 2016 Thus, Piwi-piRISCs require both H1 and HP1a to repress TEs, and the silencing is correlated with the chromatin state rather than H3K9me3 marks. TES 55-58 Suppressor of variegation 205 Drosophila melanogaster 39-43 22052799-0 2011 Tuning HP1alpha chromodomain selectivity for di- and trimethyllysine. di- and trimethyllysine 45-68 Suppressor of variegation 205 Drosophila melanogaster 7-15 24555990-2 2014 Mechanistic studies implicate HP1 family proteins as "hub proteins," able to interact with a variety of chromosomal proteins through the chromo-shadow domain (CSD), as well as to recognize key histone modification sites [primarily histone H3 di/trimethyl Lys9 (H3K9me2/3)] through the chromodomain (CD). Cadmium 299-301 Suppressor of variegation 205 Drosophila melanogaster 30-33 23611785-1 2013 Heterochromatin protein 1 (HP1) is an epigenetic gene silencing protein that is regulated by lysine 9 methylation of histone H3. Lysine 93-99 Suppressor of variegation 205 Drosophila melanogaster 0-25 23611785-1 2013 Heterochromatin protein 1 (HP1) is an epigenetic gene silencing protein that is regulated by lysine 9 methylation of histone H3. Lysine 93-99 Suppressor of variegation 205 Drosophila melanogaster 27-30 23519136-5 2013 Here, we hypothesize that chromatin landscape changes induced by ecdysone surges direct the HDAC1- or HP1a-containing Fru complex to distinct targets, thereby allowing them to switch the neuronal sexual fate in the brain. Ecdysone 65-73 Suppressor of variegation 205 Drosophila melanogaster 102-106 25790265-1 2015 Methylated lysine 9 on the histone 3 (H3) tail recruits heterochromatin protein 1 from Drosophila (dHP1) via its chromodomain and results in gene silencing. Lysine 11-17 Suppressor of variegation 205 Drosophila melanogaster 56-81 25790265-1 2015 Methylated lysine 9 on the histone 3 (H3) tail recruits heterochromatin protein 1 from Drosophila (dHP1) via its chromodomain and results in gene silencing. Lysine 11-17 Suppressor of variegation 205 Drosophila melanogaster 99-103 25790265-2 2015 The dHP1 chromodomain binds H3 K9Me3 with an aromatic cage surrounding the trimethyllysine. h3 k9me3 28-36 Suppressor of variegation 205 Drosophila melanogaster 4-8 25790265-2 2015 The dHP1 chromodomain binds H3 K9Me3 with an aromatic cage surrounding the trimethyllysine. trimethyllysine 75-90 Suppressor of variegation 205 Drosophila melanogaster 4-8 23793104-9 2013 Examining a panel of amino acid substitutions in the HP1a CSD, we find that Leu-165 in HP1a interacts with HP2 but not PIWI, supporting the conclusion that different sites in the binding surface provide discrimination for partner selection. Leucine 76-79 Suppressor of variegation 205 Drosophila melanogaster 53-57 23793104-9 2013 Examining a panel of amino acid substitutions in the HP1a CSD, we find that Leu-165 in HP1a interacts with HP2 but not PIWI, supporting the conclusion that different sites in the binding surface provide discrimination for partner selection. Leucine 76-79 Suppressor of variegation 205 Drosophila melanogaster 87-91 23166515-1 2012 Heterochromatin protein 1 (HP1) proteins, recognized readers of the heterochromatin mark methylation of histone H3 lysine 9 (H3K9me), are important regulators of heterochromatin-mediated gene silencing and chromosome structure. Lysine 115-121 Suppressor of variegation 205 Drosophila melanogaster 0-25 23166515-1 2012 Heterochromatin protein 1 (HP1) proteins, recognized readers of the heterochromatin mark methylation of histone H3 lysine 9 (H3K9me), are important regulators of heterochromatin-mediated gene silencing and chromosome structure. Lysine 115-121 Suppressor of variegation 205 Drosophila melanogaster 27-30 22052799-6 2011 The selectivity of HP1alpha chromodomain for H3K9Me(3) over H3K9Me(2) was investigated by mutating E52 to remove or weaken the hydrogen bond to K9Me(2) while maintaining affinity for K9Me(3,) including E52F, E52I, E52V, E52D, an E52Q. Hydrogen 129-137 Suppressor of variegation 205 Drosophila melanogaster 19-27 20962594-4 2011 HP1 contains a chromodomain that binds to di- and- tri-methylated lysine 9 of histone H3. Lysine 66-72 Suppressor of variegation 205 Drosophila melanogaster 0-3 21472955-11 2011 Glutamic acid substitution at these sites destabilizes HP1a dimers, but improves the interaction with both binding partners. Glutamic Acid 0-13 Suppressor of variegation 205 Drosophila melanogaster 55-59 21472955-12 2011 Our studies underscore the importance of CSD dimerization and cooperation with the CTE in forming distinct complexes of HP1a. 1,1,1-trifluoro-2-chloroethane 83-86 Suppressor of variegation 205 Drosophila melanogaster 120-124 19189944-1 2009 Methylation of histone H3 lysine 9 (H3K9) is a key feature of silent chromatin and plays an important role in stabilizing the interaction of heterochromatin protein 1 (HP1) with chromatin. Lysine 26-32 Suppressor of variegation 205 Drosophila melanogaster 141-166 19798443-3 2009 According to the model, histone methyltransferase enzymes (HMTases) methylate the histone H3 at lysine 9 (H3K9me), creating selective binding sites for itself and the chromodomain of HP1a. Lysine 96-102 Suppressor of variegation 205 Drosophila melanogaster 183-187 20435908-4 2010 To gain insights into this question, we have studied the function of heterochromatin protein 1 (HP1), which is a reader of repressive methylation at histone H3 lysine 9, in genome-wide organization of replication. HS 3 157-159 Suppressor of variegation 205 Drosophila melanogaster 69-94 20435908-4 2010 To gain insights into this question, we have studied the function of heterochromatin protein 1 (HP1), which is a reader of repressive methylation at histone H3 lysine 9, in genome-wide organization of replication. HS 3 157-159 Suppressor of variegation 205 Drosophila melanogaster 96-99 20435908-4 2010 To gain insights into this question, we have studied the function of heterochromatin protein 1 (HP1), which is a reader of repressive methylation at histone H3 lysine 9, in genome-wide organization of replication. Lysine 160-166 Suppressor of variegation 205 Drosophila melanogaster 69-94 20435908-4 2010 To gain insights into this question, we have studied the function of heterochromatin protein 1 (HP1), which is a reader of repressive methylation at histone H3 lysine 9, in genome-wide organization of replication. Lysine 160-166 Suppressor of variegation 205 Drosophila melanogaster 96-99 19189944-1 2009 Methylation of histone H3 lysine 9 (H3K9) is a key feature of silent chromatin and plays an important role in stabilizing the interaction of heterochromatin protein 1 (HP1) with chromatin. Lysine 26-32 Suppressor of variegation 205 Drosophila melanogaster 168-171 19061644-0 2008 Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase. HS 3 46-48 Suppressor of variegation 205 Drosophila melanogaster 0-26 19061644-0 2008 Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase. Lysine 49-55 Suppressor of variegation 205 Drosophila melanogaster 0-26 17652514-2 2007 Whereas suppressor of variegation 3-9 [SU(VAR)3-9], a histone methyltransferase, is mainly responsible for lysine 9 of histone H3 (H3K9) methylation of the chromocenter and consequent binding of the heterochromatin-protein HP1, the enzyme for painting of the fourth chromosome by H3K9 methylation has been elusive. Lysine 107-113 Suppressor of variegation 205 Drosophila melanogaster 223-226 12897054-0 2003 Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. N(2)-methyl-L-lysine 53-66 Suppressor of variegation 205 Drosophila melanogaster 103-106 17335352-7 2007 HP1 target genes are also marked by the histone variant H3.3 and dimethylated histone 3 lysine 4 (H3K4me2), which are both typical of active chromatin. Lysine 88-94 Suppressor of variegation 205 Drosophila melanogaster 0-3 15630020-6 2005 The results suggest an ordered cascade of events leading to the establishment of heterochromatin and requiring the recruitment of the histone H2Av variant followed by H4 Lys 12 acetylation as necessary steps before H3 Lys 9 methylation and HP1 recruitment can take place. Lysine 170-173 Suppressor of variegation 205 Drosophila melanogaster 240-243 12826664-1 2003 Association of the highly conserved heterochromatin protein, HP1, with the specialized chromatin of centromeres and telomeres requires binding to a specific histone H3 modification of methylation on lysine 9. Lysine 199-205 Suppressor of variegation 205 Drosophila melanogaster 61-64 15215206-4 2004 HP1 associates with centric heterochromatin through an interaction with methylated lysine 9 of histone H3, a modification generated by SU(VAR)3-9. Lysine 83-89 Suppressor of variegation 205 Drosophila melanogaster 0-3 12897054-3 2003 In Drosophila S2 cells, and on polytene chromosomes, methyl-Lys 27 and Pc are both excluded from areas that are enriched in methyl-Lys 9 and HP1. Lysine 60-63 Suppressor of variegation 205 Drosophila melanogaster 141-144 11121421-9 2001 Serine-to-alanine and serine-to-glutamate substitutions at consensus protein kinase motifs resulted in reduction or loss of silencing activity of mutant HP1 in transgenic flies. Serine 0-6 Suppressor of variegation 205 Drosophila melanogaster 153-156 12642487-3 2003 HP1 associates with centric regions through an interaction with methylated lysine nine of histone H3, a modification generated by the histone methyltransferase SU(VAR)3-9. Lysine 75-81 Suppressor of variegation 205 Drosophila melanogaster 0-3 12151603-4 2002 Recently, one mechanism of HP1 chromosome association was revealed; the amino-terminal chromo domain of HP1 interacts with methylated lysine nine of histone H3, consistent with the histone code hypothesis. Lysine 134-140 Suppressor of variegation 205 Drosophila melanogaster 27-30 12151603-4 2002 Recently, one mechanism of HP1 chromosome association was revealed; the amino-terminal chromo domain of HP1 interacts with methylated lysine nine of histone H3, consistent with the histone code hypothesis. Lysine 134-140 Suppressor of variegation 205 Drosophila melanogaster 104-107 12130537-2 2002 In fission yeast, conserved heterochromatin-specific modifications of the histone H3 tail, involving deacetylation of Lys 9 and Lys 14 and subsequent methylation of Lys 9, promote the recruitment of a heterochromatin protein, Swi6, a homolog of the Drosophila heterochromatin protein 1. Lysine 118-121 Suppressor of variegation 205 Drosophila melanogaster 260-285 12130537-2 2002 In fission yeast, conserved heterochromatin-specific modifications of the histone H3 tail, involving deacetylation of Lys 9 and Lys 14 and subsequent methylation of Lys 9, promote the recruitment of a heterochromatin protein, Swi6, a homolog of the Drosophila heterochromatin protein 1. Lysine 128-131 Suppressor of variegation 205 Drosophila melanogaster 260-285 12130537-2 2002 In fission yeast, conserved heterochromatin-specific modifications of the histone H3 tail, involving deacetylation of Lys 9 and Lys 14 and subsequent methylation of Lys 9, promote the recruitment of a heterochromatin protein, Swi6, a homolog of the Drosophila heterochromatin protein 1. Lysine 128-131 Suppressor of variegation 205 Drosophila melanogaster 260-285 11121421-9 2001 Serine-to-alanine and serine-to-glutamate substitutions at consensus protein kinase motifs resulted in reduction or loss of silencing activity of mutant HP1 in transgenic flies. Alanine 10-17 Suppressor of variegation 205 Drosophila melanogaster 153-156 11121421-9 2001 Serine-to-alanine and serine-to-glutamate substitutions at consensus protein kinase motifs resulted in reduction or loss of silencing activity of mutant HP1 in transgenic flies. Serine 22-28 Suppressor of variegation 205 Drosophila melanogaster 153-156 11121421-9 2001 Serine-to-alanine and serine-to-glutamate substitutions at consensus protein kinase motifs resulted in reduction or loss of silencing activity of mutant HP1 in transgenic flies. Glutamic Acid 32-41 Suppressor of variegation 205 Drosophila melanogaster 153-156 10329715-4 1999 We report here that HP1 is phosphorylated by casein kinase II in vivo at three serine residues located at the N and C termini of the protein. Serine 79-85 Suppressor of variegation 205 Drosophila melanogaster 20-23 10329715-5 1999 Alanine substitution mutations in the casein kinase II target phosphorylation sites dramatically reduce the heterochromatin binding activity of HP1, whereas glutamate substitution mutations, which mimic the charge contributions of phosphorylated serine, have apparently wild-type binding activity. Alanine 0-7 Suppressor of variegation 205 Drosophila melanogaster 144-147 10329715-5 1999 Alanine substitution mutations in the casein kinase II target phosphorylation sites dramatically reduce the heterochromatin binding activity of HP1, whereas glutamate substitution mutations, which mimic the charge contributions of phosphorylated serine, have apparently wild-type binding activity. Serine 246-252 Suppressor of variegation 205 Drosophila melanogaster 144-147 34866135-0 2021 HP1a-mediated heterochromatin formation inhibits high dietary sugar-induced tumor progression. Sugars 62-67 Suppressor of variegation 205 Drosophila melanogaster 0-4 7615662-5 1995 We find an enrichment of heterochromatin protein 1 in the intensely DAPI-staining regions near the apical surface of nuclear cycle 10 embryos. DAPI 68-72 Suppressor of variegation 205 Drosophila melanogaster 25-50 34203110-4 2021 Recent experiments have shown that the HP1a sequence of Drosophila melanogaster can undergo liquid-liquid phase separation under both in vitro and in vivo conditions, induced by changes of the monovalent salt concentration. Salts 204-208 Suppressor of variegation 205 Drosophila melanogaster 39-43 34203110-5 2021 While the phase separation of HP1a is thought to be the mechanism underlying chromatin compartmentalization, the molecular level mechanistic picture of salt-driven phase separation of HP1a has remained poorly understood. Salts 152-156 Suppressor of variegation 205 Drosophila melanogaster 184-188 34203110-6 2021 The disordered hinge region of HP1a is seen as the driver of salt-induced condensation because of its charge enriched sequence and post-translational modifications. Salts 61-65 Suppressor of variegation 205 Drosophila melanogaster 31-35 34203110-7 2021 Here, we set out to decipher the mechanisms of salt-induced condensation of HP1a through a systematic study of salt-dependent conformations of single chains and fuzzy dimers of disordered HP1a hinge sequences. Salts 47-51 Suppressor of variegation 205 Drosophila melanogaster 76-80 34203110-7 2021 Here, we set out to decipher the mechanisms of salt-induced condensation of HP1a through a systematic study of salt-dependent conformations of single chains and fuzzy dimers of disordered HP1a hinge sequences. Salts 47-51 Suppressor of variegation 205 Drosophila melanogaster 188-192 34203110-7 2021 Here, we set out to decipher the mechanisms of salt-induced condensation of HP1a through a systematic study of salt-dependent conformations of single chains and fuzzy dimers of disordered HP1a hinge sequences. Salts 111-115 Suppressor of variegation 205 Drosophila melanogaster 76-80 34203110-10 2021 Furthermore, we find that salt-induced changes in the ensemble of conformations of HP1a disordered hinge sequence fine-tune the inter-chain vs. self-chain interactions in ways that favor fuzzy dimer formation under low salt conditions in the agreement with condensation trends seen in experiments. Salts 26-30 Suppressor of variegation 205 Drosophila melanogaster 83-87 34203110-10 2021 Furthermore, we find that salt-induced changes in the ensemble of conformations of HP1a disordered hinge sequence fine-tune the inter-chain vs. self-chain interactions in ways that favor fuzzy dimer formation under low salt conditions in the agreement with condensation trends seen in experiments. Salts 219-223 Suppressor of variegation 205 Drosophila melanogaster 83-87