PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25855960-3 2015 Here, we show that PCAF can directly acetylate cytoplasmic GLI1 protein at lysine 518, preventing its nuclear translocation and promoter occupancy, and consequently suppressing Hedgehog (Hh) signaling in HCC. Lysine 75-81 lysine acetyltransferase 2B Homo sapiens 19-23 29555684-7 2018 A series of biochemical analyses disclosed that the host lysine acetyltransferases GCN5 and PCAF acetylate NP in vitro MS experiments identified three lysine residues as acetylation targets in the host cells and suggested that Lys-31 and Lys-90 are acetylated by PCAF and GCN5, respectively. Lysine 57-63 lysine acetyltransferase 2B Homo sapiens 92-96 29555684-7 2018 A series of biochemical analyses disclosed that the host lysine acetyltransferases GCN5 and PCAF acetylate NP in vitro MS experiments identified three lysine residues as acetylation targets in the host cells and suggested that Lys-31 and Lys-90 are acetylated by PCAF and GCN5, respectively. Lysine 57-63 lysine acetyltransferase 2B Homo sapiens 263-267 29555684-7 2018 A series of biochemical analyses disclosed that the host lysine acetyltransferases GCN5 and PCAF acetylate NP in vitro MS experiments identified three lysine residues as acetylation targets in the host cells and suggested that Lys-31 and Lys-90 are acetylated by PCAF and GCN5, respectively. Lysine 227-230 lysine acetyltransferase 2B Homo sapiens 92-96 29555684-7 2018 A series of biochemical analyses disclosed that the host lysine acetyltransferases GCN5 and PCAF acetylate NP in vitro MS experiments identified three lysine residues as acetylation targets in the host cells and suggested that Lys-31 and Lys-90 are acetylated by PCAF and GCN5, respectively. Lysine 227-230 lysine acetyltransferase 2B Homo sapiens 263-267 29555684-7 2018 A series of biochemical analyses disclosed that the host lysine acetyltransferases GCN5 and PCAF acetylate NP in vitro MS experiments identified three lysine residues as acetylation targets in the host cells and suggested that Lys-31 and Lys-90 are acetylated by PCAF and GCN5, respectively. Lysine 238-241 lysine acetyltransferase 2B Homo sapiens 92-96 26802082-7 2016 Pharmacological inhibition of KAT2B by anacardic acid in NCM460 cells reduced the levels of histone H4 lysine 5 acetylation [H4K5ac] and interleukin-10 [IL-10] in a dose-dependent manner. Lysine 103-109 lysine acetyltransferase 2B Homo sapiens 30-35 25800736-4 2015 We identified that PCAF interacts with and acetylates EZH2 mainly at lysine 348 (K348). Lysine 69-75 lysine acetyltransferase 2B Homo sapiens 19-23 30833716-7 2019 Deletions or point mutations identified several lysine residues in different delta-catenin domains involved in PCAF-mediated delta-catenin downregulation. Lysine 48-54 lysine acetyltransferase 2B Homo sapiens 111-115 29440709-6 2018 We demonstrated that lysine 830 of BRCA1 is a preferential acetylation site by pCAF and tested its function in embryonic stem (ES) cells by changing lysine 830 to arginine using a transcription activator-like effector nuclease (TALEN) system. Lysine 21-27 lysine acetyltransferase 2B Homo sapiens 79-83 24732800-6 2014 Here we found that activation was dependent on the histone H3 lysine 9 (H3K9) demethylase activity of LSD1, which removes repressive methyl marks from dimethylated H3K9 (H3K9Me2), to facilitate subsequent H3K9 acetylation by the NeuroD1-associated histone acetyltransferase, P300/CBP-associated factor (PCAF). Lysine 62-68 lysine acetyltransferase 2B Homo sapiens 275-301 24732800-6 2014 Here we found that activation was dependent on the histone H3 lysine 9 (H3K9) demethylase activity of LSD1, which removes repressive methyl marks from dimethylated H3K9 (H3K9Me2), to facilitate subsequent H3K9 acetylation by the NeuroD1-associated histone acetyltransferase, P300/CBP-associated factor (PCAF). Lysine 62-68 lysine acetyltransferase 2B Homo sapiens 303-307 24686445-4 2014 Here we show through systematic epigenetic studies that the histone acetyltransferase p300/CBP-associated factor (PCAF) promotes acetylation of histone 3 Lys 9 at the promoters of established key regeneration-associated genes following a peripheral but not a central axonal injury. Lysine 154-157 lysine acetyltransferase 2B Homo sapiens 114-118 22547391-5 2012 PCAF associates with p27 through its catalytic domain and acetylates p27 at lysine 100. Lysine 76-82 lysine acetyltransferase 2B Homo sapiens 0-4 24037888-10 2013 CONCLUSIONS: These observations demonstrate that 1) HOXA10 associates with and is acetylated by PCAF at lysines K338 and K339 in Ishikawa cells and 2) HOXA10-PCAF association impairs embryo implantation by inhibiting ITGB3 protein expression in endometrial epithelial cells. Lysine 104-111 lysine acetyltransferase 2B Homo sapiens 96-100 24037888-10 2013 CONCLUSIONS: These observations demonstrate that 1) HOXA10 associates with and is acetylated by PCAF at lysines K338 and K339 in Ishikawa cells and 2) HOXA10-PCAF association impairs embryo implantation by inhibiting ITGB3 protein expression in endometrial epithelial cells. Lysine 104-111 lysine acetyltransferase 2B Homo sapiens 158-162 23932781-4 2013 Acetylation at these three lysine residues is stimulated by P300/calcium-binding protein (CBP)-associated factor (PCAF) acetyltransferase under high glucose and increases ACLY stability by blocking its ubiquitylation and degradation. Lysine 27-33 lysine acetyltransferase 2B Homo sapiens 114-118 24832227-8 2012 This improved characterization of Tat.PCAF bromodomain binding may help in defining the structural determinants of other protein interactions involving lysine acetylation. Lysine 152-158 lysine acetyltransferase 2B Homo sapiens 38-42 23760262-1 2013 PCAF and GCN5 acetylate cyclin A at specific lysine residues targeting it for degradation at mitosis. Lysine 45-51 lysine acetyltransferase 2B Homo sapiens 0-4 19773423-9 2009 Moreover, we also observed that PCAF acetylates cdk2 at lysine 33. Lysine 56-62 lysine acetyltransferase 2B Homo sapiens 32-36 20601085-8 2010 By spot mapping analysis we first identified Lys 117 and 251 as the putative GAPDH residues that could be acetylated by PCAF. Lysine 45-48 lysine acetyltransferase 2B Homo sapiens 120-124 22207202-7 2012 Here, we use mutagenesis to show that a lysine residue at position 34 within AD1 of E12/E47 is acetylated by CBP/p300 and PCAF. Lysine 40-46 lysine acetyltransferase 2B Homo sapiens 122-126 21416054-3 2011 Mass spectrometry and immunoprecipitations determined that p300 and/or PCAF promoted KLF8 acetylation at K67, K93, and K95 and this acetylation was abolished in lysine-to-arginine (R) mutants. Lysine 161-167 lysine acetyltransferase 2B Homo sapiens 71-75 20363750-9 2010 Thus, acetylation of EVI1 at Lys(564) by P/CAF enhances the DNA binding capacity of EVI1 and thereby contributes to the activation of GATA2. Lysine 29-32 lysine acetyltransferase 2B Homo sapiens 41-46 18400184-4 2008 Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. Lysine 247-254 lysine acetyltransferase 2B Homo sapiens 153-179 19483727-2 2009 Here, we report that the acetyltransferase P/CAF directly interacts with cyclin A that as a consequence becomes acetylated at lysines 54, 68, 95 and 112. Lysine 126-133 lysine acetyltransferase 2B Homo sapiens 25-48 19351588-0 2009 Multiple lysine methylation of PCAF by Set9 methyltransferase. Lysine 9-15 lysine acetyltransferase 2B Homo sapiens 31-35 19351588-6 2009 Further methyltransferase assays focusing on the six lysine residues showed that K78 and K89 are preferentially methylated in full-length PCAF in vitro. Lysine 53-59 lysine acetyltransferase 2B Homo sapiens 138-142 18250157-3 2008 Here we show that cellular GCN5 and P/CAF, members of the GCN5-related N-acetyltransferase family of histone acetyltransferases, regulate CDK9 function by specifically acetylating the catalytic core of the enzyme and, in particular, a lysine that is essential for ATP coordination and the phosphotransfer reaction. Lysine 235-241 lysine acetyltransferase 2B Homo sapiens 36-41 19015268-4 2009 Intramolecular acetylation targets five lysines within the nuclear localization signal at the P/CAF C terminus. Lysine 40-47 lysine acetyltransferase 2B Homo sapiens 94-99 18400184-4 2008 Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. Lysine 247-254 lysine acetyltransferase 2B Homo sapiens 181-185 18400184-4 2008 Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. Lysine 247-253 lysine acetyltransferase 2B Homo sapiens 153-179 18400184-4 2008 Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. Lysine 247-253 lysine acetyltransferase 2B Homo sapiens 181-185 17301242-4 2007 Here, we show that C/EBPbeta is acetylated by GCN5 and PCAF within a cluster of lysine residues between amino acids 98-102 and that this acetylation is strongly induced by glucocorticoid treatment. Lysine 80-86 lysine acetyltransferase 2B Homo sapiens 55-59 17884818-5 2007 An in vivo acetylation assay using 293T cells revealed that Fli1 is mainly acetylated by the histone acetyltransferase activity of p300/CBP-associated factor (PCAF) at lysine 380. Lysine 168-174 lysine acetyltransferase 2B Homo sapiens 131-157 17884818-5 2007 An in vivo acetylation assay using 293T cells revealed that Fli1 is mainly acetylated by the histone acetyltransferase activity of p300/CBP-associated factor (PCAF) at lysine 380. Lysine 168-174 lysine acetyltransferase 2B Homo sapiens 159-163 17884818-11 2007 These results indicate that PCAF-dependent acetylation of lysine 380 abrogates repressor function of Fli1 with respect to collagen gene expression. Lysine 58-64 lysine acetyltransferase 2B Homo sapiens 28-32 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-3 2007 It turned out that five lysine residues in HMGA1a, i.e., Lys-14, Lys-64, Lys-66, Lys-70, and Lys-73, could be acetylated by both p300 and PCAF. Lysine 24-30 lysine acetyltransferase 2B Homo sapiens 138-142 17627840-3 2007 It turned out that five lysine residues in HMGA1a, i.e., Lys-14, Lys-64, Lys-66, Lys-70, and Lys-73, could be acetylated by both p300 and PCAF. Lysine 57-60 lysine acetyltransferase 2B Homo sapiens 138-142 17627840-3 2007 It turned out that five lysine residues in HMGA1a, i.e., Lys-14, Lys-64, Lys-66, Lys-70, and Lys-73, could be acetylated by both p300 and PCAF. Lysine 65-68 lysine acetyltransferase 2B Homo sapiens 138-142 17627840-3 2007 It turned out that five lysine residues in HMGA1a, i.e., Lys-14, Lys-64, Lys-66, Lys-70, and Lys-73, could be acetylated by both p300 and PCAF. Lysine 65-68 lysine acetyltransferase 2B Homo sapiens 138-142 17627840-3 2007 It turned out that five lysine residues in HMGA1a, i.e., Lys-14, Lys-64, Lys-66, Lys-70, and Lys-73, could be acetylated by both p300 and PCAF. Lysine 65-68 lysine acetyltransferase 2B Homo sapiens 138-142 17627840-3 2007 It turned out that five lysine residues in HMGA1a, i.e., Lys-14, Lys-64, Lys-66, Lys-70, and Lys-73, could be acetylated by both p300 and PCAF. Lysine 65-68 lysine acetyltransferase 2B Homo sapiens 138-142 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 166-169 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 166-169 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 266-270 17627840-5 2007 Quantification results revealed that p300 and PCAF exhibited different site preferences for the acetylation; the preference of p300 acetylation followed the order of Lys-64 approximately Lys-70 > Lys-66 > Lys-14 approximately Lys73, whereas the selectivity of PCAF acetylation followed the sequence of Lys-70 approximately Lys-73 > Lys-64 approximately Lys-66 > Lys-14. Lysine 187-190 lysine acetyltransferase 2B Homo sapiens 46-50 14661947-3 2003 Interestingly, the Gcn5/PCAF HAT family has a remarkable ability to acetylate lysine residues within diverse cognate sites such as those found around lysines 14, 8, and 320 of histones H3, H4, and p53, respectively. Lysine 78-84 lysine acetyltransferase 2B Homo sapiens 24-28 16135803-6 2005 Association of p73 with Tat prevented the acetylation of Tat on lysine 28 by PCAF. Lysine 64-70 lysine acetyltransferase 2B Homo sapiens 77-81 14661947-6 2003 In contrast, while the histone H3 complex shows extensive interactions with tGcn5 and peptide residues N-terminal to the target lysine, the corresponding residues in histone H4 and p53 are disordered, suggesting that the N-terminal substrate region plays an important role in the enhanced affinity of the Gcn5/PCAF HAT proteins for histone H3. Lysine 128-134 lysine acetyltransferase 2B Homo sapiens 310-314 14661947-3 2003 Interestingly, the Gcn5/PCAF HAT family has a remarkable ability to acetylate lysine residues within diverse cognate sites such as those found around lysines 14, 8, and 320 of histones H3, H4, and p53, respectively. Lysine 150-157 lysine acetyltransferase 2B Homo sapiens 24-28 14661947-5 2003 A comparison of these structures with tGcn5 bound to histone H3 reveals that the Gcn5/PCAF HATs can accommodate divergent substrates by utilizing analogous interactions with the lysine target and two C-terminal residues with a related chemical nature, suggesting that these interactions play a general role in Gcn5/PCAF substrate binding selectivity. Lysine 178-184 lysine acetyltransferase 2B Homo sapiens 86-90 12758070-4 2003 We found that CBP and PCAF acetylated KLF13 at specific lysine residues in the zinc finger domain of KLF13. Lysine 56-62 lysine acetyltransferase 2B Homo sapiens 22-26 12888487-6 2003 The intramolecular acetylation targets five lysines (416-442) at the P/CAF C-terminus, which are in the nuclear localisation signal (NLS). Lysine 44-51 lysine acetyltransferase 2B Homo sapiens 69-74 11514574-9 2001 Consistent with a recent report, we show that nuclear localization of CIITA is enhanced by lysine 144, an in vitro target of pCAF-mediated HAT. Lysine 91-97 lysine acetyltransferase 2B Homo sapiens 125-129 12419806-3 2003 Here, we show that the p65 subunit of NF-kappaB is acetylated by both p300 and PCAF on lysines 122 and 123. Lysine 87-94 lysine acetyltransferase 2B Homo sapiens 79-83 12374802-7 2002 However, a mutant that cannot be acetylated by PCAF due to a change in the surrounding amino acid context of lysine 92 showed increased DNA binding and activity compared with wild type IRF7. Lysine 109-115 lysine acetyltransferase 2B Homo sapiens 47-51 11931765-0 2002 Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain. Lysine 20-26 lysine acetyltransferase 2B Homo sapiens 63-67 11931765-2 2002 Tat transactivation activity is dependent on lysine acetylation and its association with nuclear histone acetyltransferases p300/CBP (CREB binding protein) and p300/CBP-associated factor (PCAF). Lysine 45-51 lysine acetyltransferase 2B Homo sapiens 160-186 11931765-2 2002 Tat transactivation activity is dependent on lysine acetylation and its association with nuclear histone acetyltransferases p300/CBP (CREB binding protein) and p300/CBP-associated factor (PCAF). Lysine 45-51 lysine acetyltransferase 2B Homo sapiens 188-192 11931765-3 2002 Here, we show that the bromodomain of PCAF binds specifically to HIV-1 Tat acetylated at lysine 50 and that this interaction competes effectively against HIV-1 TAR RNA binding to the lysine-acetylated Tat. Lysine 89-95 lysine acetyltransferase 2B Homo sapiens 38-42 11931765-3 2002 Here, we show that the bromodomain of PCAF binds specifically to HIV-1 Tat acetylated at lysine 50 and that this interaction competes effectively against HIV-1 TAR RNA binding to the lysine-acetylated Tat. Lysine 183-189 lysine acetyltransferase 2B Homo sapiens 38-42 11931765-4 2002 The three-dimensional solution structure of the PCAF bromodomain in complex with a lysine 50-acetylated Tat peptide together with biochemical analyses provides the structural basis for the specificity of this molecular recognition and reveals insights into the differences in ligand selectivity of bromodomains. Lysine 83-89 lysine acetyltransferase 2B Homo sapiens 48-52 12486002-4 2002 It has recently been shown that acetylation at a single lysine, residue 50, regulated the association of Tat with PCAF. Lysine 56-62 lysine acetyltransferase 2B Homo sapiens 114-118 12486002-8 2002 Thus, differential lysine acetylation of Tat coordinates the interactions with its co-activators, cyclin T1 and PCAF. Lysine 19-25 lysine acetyltransferase 2B Homo sapiens 112-116 11486036-5 2001 YY1 was acetylated in two regions: both p300 and PCAF acetylated the central glycine-lysine-rich domain of residues 170 to 200, and PCAF also acetylated YY1 at the C-terminal DNA-binding zinc finger domain. Lysine 85-91 lysine acetyltransferase 2B Homo sapiens 49-53 11486036-5 2001 YY1 was acetylated in two regions: both p300 and PCAF acetylated the central glycine-lysine-rich domain of residues 170 to 200, and PCAF also acetylated YY1 at the C-terminal DNA-binding zinc finger domain. Lysine 85-91 lysine acetyltransferase 2B Homo sapiens 132-136 10944526-4 2000 In vitro, MyoD is acetylated both by CBP/p300 and by PCAF on two lysines located at the boundary of the DNA binding domain. Lysine 65-72 lysine acetyltransferase 2B Homo sapiens 53-57 11509661-3 2001 We previously showed that the CtBP-binding motif in E1A is flanked by a Lys residue and suggested that acetylation of this residue by the p300/CBP-associated factor P/CAF disrupts the CtBP interaction. Lysine 72-75 lysine acetyltransferase 2B Homo sapiens 138-170 11118214-4 2000 P/CAF-mediated acetylation, which mapped to a lysine-rich motif in the loop region, increased TAL1 binding to DNA while selectively inhibiting its interaction with the transcriptional co-repressor mSin3A. Lysine 46-52 lysine acetyltransferase 2B Homo sapiens 0-5 9744860-4 1998 p300 acetylates Lys-382 in the carboxy-terminal region of p53, whereas PCAF acetylates Lys-320 in the nuclear localization signal. Lysine 87-90 lysine acetyltransferase 2B Homo sapiens 71-75 11046145-4 2000 Interestingly, CBP and PCAF acetylate CIITA at lysine residues within a nuclear localization signal. Lysine 47-53 lysine acetyltransferase 2B Homo sapiens 23-27 11046145-6 2000 The shuttling behavior and activity of the protein are regulated by acetylation: overexpression of PCAF or inhibition of cellular deacetylases by trichostatin A increases the nuclear accumulation of CIITA in a manner determined by the presence of the acetylation target lysines. Lysine 270-277 lysine acetyltransferase 2B Homo sapiens 99-103 10891493-6 2000 PCAF binds to the E1B 55-kDa protein and to a region near the C terminus of p53 encompassing Lys-320, the specific PCAF acetylation site. Lysine 93-96 lysine acetyltransferase 2B Homo sapiens 0-4 10891493-6 2000 PCAF binds to the E1B 55-kDa protein and to a region near the C terminus of p53 encompassing Lys-320, the specific PCAF acetylation site. Lysine 93-96 lysine acetyltransferase 2B Homo sapiens 115-119 10852958-7 2000 Acetylation of CDP/cut by PCAF is directed at conserved lysine residues near the homeodomain region and regulates CDP/cut function. Lysine 56-62 lysine acetyltransferase 2B Homo sapiens 26-30 9891054-5 1999 In this study, we demonstrate that PCAF also acetylates p53 in vitro at a lysine residue distinct from that acetylated by p300 and thereby increases p53"s ability to bind to its cognate DNA site. Lysine 74-80 lysine acetyltransferase 2B Homo sapiens 35-39 9891054-6 1999 We have generated antibodies to acetylated p53 peptides at either of the two lysine residues that are targeted by PCAF or p300 and have demonstrated that these antibodies are highly specific for both acetylation and the particular site. Lysine 77-83 lysine acetyltransferase 2B Homo sapiens 114-118 9880483-4 1999 PCAF primarily acetylates lysine 14 of H3 but also less efficiently acetylates lysine 8 of H4. Lysine 26-32 lysine acetyltransferase 2B Homo sapiens 0-4 9880483-4 1999 PCAF primarily acetylates lysine 14 of H3 but also less efficiently acetylates lysine 8 of H4. Lysine 79-85 lysine acetyltransferase 2B Homo sapiens 0-4 10777508-6 2000 PCAF-catalyzed acetylation of the substrate H3-20 was shown to be specific for Lys-14, analogous to its behavior with the full-length histone H3 protein. Lysine 79-82 lysine acetyltransferase 2B Homo sapiens 0-4 10619020-4 1999 Here, we provide a molecular explanation of this phenomenon and report that MyoD is directly acetylated by PCAF at evolutionarily conserved lysines. Lysine 140-147 lysine acetyltransferase 2B Homo sapiens 107-111 10207070-3 1999 Using mass spectrum sequence analysis, we identified the lysine at position 2 as the predominant site acetylated by PCAF. Lysine 57-63 lysine acetyltransferase 2B Homo sapiens 116-120 10207070-4 1999 Lysine 2 is a prominent acetylation site in vivo, suggesting that this PCAF-mediated acetylation is physiologically relevant. Lysine 0-6 lysine acetyltransferase 2B Homo sapiens 71-75 9809067-2 1998 We show that CBP and P/CAF acetylate HMG I(Y), the essential architectural component required for enhanceosome assembly, at distinct lysine residues, causing distinct effects on transcription. Lysine 133-139 lysine acetyltransferase 2B Homo sapiens 21-26 34555274-0 2021 P300/CBP-associated factor (PCAF)-mediated acetylation of Fascin at lysine 471 inhibits its actin-bundling activity and tumor metastasis in esophageal cancer. Lysine 68-74 lysine acetyltransferase 2B Homo sapiens 0-26 34555274-0 2021 P300/CBP-associated factor (PCAF)-mediated acetylation of Fascin at lysine 471 inhibits its actin-bundling activity and tumor metastasis in esophageal cancer. Lysine 68-74 lysine acetyltransferase 2B Homo sapiens 28-32 34555274-10 2021 RESULTS: Fascin directly interacted and colocalized with PCAF in the cytoplasm and was acetylated at lysine 471 (K471) by PCAF. Lysine 101-107 lysine acetyltransferase 2B Homo sapiens 122-126