PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24840043-1 2014 HLCS (holocarboxylase synthetase) is a nuclear protein that catalyses the binding of biotin to distinct lysine residues in chromatin proteins. Lysine 104-110 holocarboxylase synthetase Homo sapiens 0-4 24840043-1 2014 HLCS (holocarboxylase synthetase) is a nuclear protein that catalyses the binding of biotin to distinct lysine residues in chromatin proteins. Lysine 104-110 holocarboxylase synthetase Homo sapiens 6-32 24133061-4 2013 We used coimmunoprecipitation, mass spectrometry, and limited proteolysis assays to demonstrate that HSP72 interacts physically with the protein biotin ligase holocarboxylase synthetase (HLCS), leading to biotinylation of residues K112, K128 K348, K361, K415, and, probably, additional lysines. Lysine 286-293 holocarboxylase synthetase Homo sapiens 159-185 24133061-4 2013 We used coimmunoprecipitation, mass spectrometry, and limited proteolysis assays to demonstrate that HSP72 interacts physically with the protein biotin ligase holocarboxylase synthetase (HLCS), leading to biotinylation of residues K112, K128 K348, K361, K415, and, probably, additional lysines. Lysine 286-293 holocarboxylase synthetase Homo sapiens 187-191 23624957-1 2013 Holocarboxylase synthetase (HLCS) is a chromatin protein that facilitates the creation of histone H3 lysine 9-methylation (H3K9me) gene repression marks through physical interactions with the histone methyltransferase EHMT-1. Lysine 101-107 holocarboxylase synthetase Homo sapiens 0-26 23624957-1 2013 Holocarboxylase synthetase (HLCS) is a chromatin protein that facilitates the creation of histone H3 lysine 9-methylation (H3K9me) gene repression marks through physical interactions with the histone methyltransferase EHMT-1. Lysine 101-107 holocarboxylase synthetase Homo sapiens 28-32 23219734-1 2013 Holocarboxylase synthetase (HLCS) is part of a multiprotein gene repression complex and catalyzes the covalent binding of biotin to lysines (K) in histones H3 and H4, thereby creating rare gene repression marks such as K16-biotinylated histone H4 (H4K16bio). Lysine 132-139 holocarboxylase synthetase Homo sapiens 0-26 23219734-1 2013 Holocarboxylase synthetase (HLCS) is part of a multiprotein gene repression complex and catalyzes the covalent binding of biotin to lysines (K) in histones H3 and H4, thereby creating rare gene repression marks such as K16-biotinylated histone H4 (H4K16bio). Lysine 132-139 holocarboxylase synthetase Homo sapiens 28-32 22192339-1 2012 Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysine (K) residues in histones H3 and H4. Lysine 68-74 holocarboxylase synthetase Homo sapiens 0-26 22192339-1 2012 Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysine (K) residues in histones H3 and H4. Lysine 68-74 holocarboxylase synthetase Homo sapiens 28-31 20688500-1 2011 Holocarboxylase synthetase (HCS) mediates the binding of biotin to lysine (K) residues in histones H2A, H3 and H4; HCS knockdown disturbs gene regulation and decreases stress resistance and lifespan in eukaryotes. Lysine 67-73 holocarboxylase synthetase Homo sapiens 0-26 20688500-1 2011 Holocarboxylase synthetase (HCS) mediates the binding of biotin to lysine (K) residues in histones H2A, H3 and H4; HCS knockdown disturbs gene regulation and decreases stress resistance and lifespan in eukaryotes. Lysine 67-73 holocarboxylase synthetase Homo sapiens 28-31 20688500-1 2011 Holocarboxylase synthetase (HCS) mediates the binding of biotin to lysine (K) residues in histones H2A, H3 and H4; HCS knockdown disturbs gene regulation and decreases stress resistance and lifespan in eukaryotes. Lysine 67-73 holocarboxylase synthetase Homo sapiens 115-118 19812216-7 2009 We hypothesize that HCS binds specifically to genomic regions rich in methylated cytosines and catalyzes increased biotinylation of histone H4 at lysine-12. Lysine 146-152 holocarboxylase synthetase Homo sapiens 20-23 18845537-3 2008 This latter reaction is catalyzed by holocarboxylase synthetase (HCS) via synthesis of 5"-biotinyl-AMP (B-AMP) from biotin and ATP, followed by transfer of the biotin to a specific lysine residue of the apocarboxylase substrate. Lysine 181-187 holocarboxylase synthetase Homo sapiens 37-63 18845537-3 2008 This latter reaction is catalyzed by holocarboxylase synthetase (HCS) via synthesis of 5"-biotinyl-AMP (B-AMP) from biotin and ATP, followed by transfer of the biotin to a specific lysine residue of the apocarboxylase substrate. Lysine 181-187 holocarboxylase synthetase Homo sapiens 65-68 8420991-3 1993 Previously we have shown that the region around the biotinyl lysine of the 1.3 S subunit is critical for catalysis, that peptides in the amino-terminal region of 1.3 S are capable of forming complexes with 12 S and 5 S, and that amino acids in the carboxyl terminus of the 1.3 S subunit form part of the recognition site for holocarboxylase synthetase. Lysine 61-67 holocarboxylase synthetase Homo sapiens 325-351 21608095-1 2011 Biotin protein ligase (BPL) mediates the covalent attachment of biotin to a specific lysine residue of biotin carboxyl carrier protein (BCCP). Lysine 85-91 holocarboxylase synthetase Homo sapiens 0-21 21608095-1 2011 Biotin protein ligase (BPL) mediates the covalent attachment of biotin to a specific lysine residue of biotin carboxyl carrier protein (BCCP). Lysine 85-91 holocarboxylase synthetase Homo sapiens 23-26 19369050-2 2010 Biotinylation of lysine (K) residues in histones, mediated by holocarboxylase synthetase (HCS), is a novel diet-dependent mechanism to regulate chromatin structure and gene expression. Lysine 17-23 holocarboxylase synthetase Homo sapiens 62-88 19369050-2 2010 Biotinylation of lysine (K) residues in histones, mediated by holocarboxylase synthetase (HCS), is a novel diet-dependent mechanism to regulate chromatin structure and gene expression. Lysine 17-23 holocarboxylase synthetase Homo sapiens 90-93 20026029-1 2010 Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. Lysine 68-75 holocarboxylase synthetase Homo sapiens 0-26 20026029-1 2010 Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. Lysine 68-75 holocarboxylase synthetase Homo sapiens 28-31 20026029-2 2010 First, HCS catalyzes the synthesis of biotinyl-5"-AMP; second, the biotinyl moiety is ligated to lysine residues. Lysine 97-103 holocarboxylase synthetase Homo sapiens 7-10 20026029-6 2010 A potential target lysine in Syn67 was biotinylated by HCS only after arginine-to-glycine substitutions in Syn67 produced a histone-like peptide. Lysine 19-25 holocarboxylase synthetase Homo sapiens 55-58 19022951-4 2008 Here, we demonstrate that the covalent binding of the vitamin biotin to lysine-12 in histone H4 (H4K12bio) and lysine-9 in histone H2A (H2AK9bio), mediated by holocarboxylase synthetase (HCS), is an epigenetic mechanism to repress retrotransposon transcription in human and mouse cell lines and in primary cells from a human supplementation study. Lysine 72-78 holocarboxylase synthetase Homo sapiens 159-185 19022951-4 2008 Here, we demonstrate that the covalent binding of the vitamin biotin to lysine-12 in histone H4 (H4K12bio) and lysine-9 in histone H2A (H2AK9bio), mediated by holocarboxylase synthetase (HCS), is an epigenetic mechanism to repress retrotransposon transcription in human and mouse cell lines and in primary cells from a human supplementation study. Lysine 72-78 holocarboxylase synthetase Homo sapiens 187-190 18372281-1 2008 Biotin protein ligase (BPL) catalyzes the biotinylation of the biotin carboxyl carrier protein (BCCP) only at a special lysine residue. Lysine 120-126 holocarboxylase synthetase Homo sapiens 0-21 18372281-1 2008 Biotin protein ligase (BPL) catalyzes the biotinylation of the biotin carboxyl carrier protein (BCCP) only at a special lysine residue. Lysine 120-126 holocarboxylase synthetase Homo sapiens 23-26