PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27507651-1 2016 Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic. Lysine 85-88 PML nuclear body scaffold Homo sapiens 96-126 27903803-15 2017 We show that tight binding of IE1 to PML interferes with the de novo SUMOylation of a distinct lysine residue that is also the target of stress-mediated hyperSUMOylation of PML. Lysine 95-101 PML nuclear body scaffold Homo sapiens 37-40 27903803-15 2017 We show that tight binding of IE1 to PML interferes with the de novo SUMOylation of a distinct lysine residue that is also the target of stress-mediated hyperSUMOylation of PML. Lysine 95-101 PML nuclear body scaffold Homo sapiens 173-176 28250117-11 2017 Thus, this is the first report that the E3 ligase PML is capable of stimulating the SUMOylation of a viral protein which is supposed to serve as a cellular mechanism to compromise specific functions of IE1p72.IMPORTANCE The major immediate early proteins of human cytomegalovirus, termed IE1p72 and IE2p86, have previously been shown to undergo posttranslational modification by covalent coupling to SUMO moieties at specific lysine residues. Lysine 426-432 PML nuclear body scaffold Homo sapiens 50-53 27507651-1 2016 Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic. Lysine 85-88 PML nuclear body scaffold Homo sapiens 128-131 27507651-1 2016 Fasci et al proposed that a SENP1-mediated switch from SUMO2 to SUMO1 conjugation on Lys(65) in promyelocytic leukemia protein (PML) is required for arsenic-induced PML degradation, the basis for the antileukemic activity of arsenic. Lysine 85-88 PML nuclear body scaffold Homo sapiens 165-168 12759344-9 2003 Interestingly, PML mutants in which sumoylation at lysine 160 was inhibited displayed an increased association with MDM2, suggesting that sumoylation at this site may be a determinant of PML-MDM2 binding. Lysine 51-57 PML nuclear body scaffold Homo sapiens 15-18 27211601-5 2016 PolySUMO5 conjugation of PML at lysine 160 facilitates recruitment of PML-NB components, which enlarges PML-NBs. Lysine 32-38 PML nuclear body scaffold Homo sapiens 25-28 27211601-5 2016 PolySUMO5 conjugation of PML at lysine 160 facilitates recruitment of PML-NB components, which enlarges PML-NBs. Lysine 32-38 PML nuclear body scaffold Homo sapiens 70-73 27211601-5 2016 PolySUMO5 conjugation of PML at lysine 160 facilitates recruitment of PML-NB components, which enlarges PML-NBs. Lysine 32-38 PML nuclear body scaffold Homo sapiens 70-73 26060329-6 2015 On the basis of data obtained with mutational analysis and quantitative proteomics, we propose that the SUMO switch at Lys(65) of PML enhanced nuclear body formation, subsequent SUMO2 conjugation to Lys(160), and consequent RNF4-dependent ubiquitylation of PML. Lysine 119-122 PML nuclear body scaffold Homo sapiens 130-133 26060329-6 2015 On the basis of data obtained with mutational analysis and quantitative proteomics, we propose that the SUMO switch at Lys(65) of PML enhanced nuclear body formation, subsequent SUMO2 conjugation to Lys(160), and consequent RNF4-dependent ubiquitylation of PML. Lysine 119-122 PML nuclear body scaffold Homo sapiens 257-260 26060329-6 2015 On the basis of data obtained with mutational analysis and quantitative proteomics, we propose that the SUMO switch at Lys(65) of PML enhanced nuclear body formation, subsequent SUMO2 conjugation to Lys(160), and consequent RNF4-dependent ubiquitylation of PML. Lysine 199-202 PML nuclear body scaffold Homo sapiens 130-133 26060329-6 2015 On the basis of data obtained with mutational analysis and quantitative proteomics, we propose that the SUMO switch at Lys(65) of PML enhanced nuclear body formation, subsequent SUMO2 conjugation to Lys(160), and consequent RNF4-dependent ubiquitylation of PML. Lysine 199-202 PML nuclear body scaffold Homo sapiens 257-260 20205709-9 2010 We also demonstrate that SUMOylation of PML at Lysine positions K160 and/or K490 are required for nuclear body formation in vivo.We propose a model in which the isoform specific residence times of PML provide both, structural stability to function as a scaffold and flexibility to attract specific nuclear proteins for efficient biochemical reactions at the surface of nuclear bodies.MCS code: 92C37. Lysine 47-53 PML nuclear body scaffold Homo sapiens 40-43 20205709-9 2010 We also demonstrate that SUMOylation of PML at Lysine positions K160 and/or K490 are required for nuclear body formation in vivo.We propose a model in which the isoform specific residence times of PML provide both, structural stability to function as a scaffold and flexibility to attract specific nuclear proteins for efficient biochemical reactions at the surface of nuclear bodies.MCS code: 92C37. Lysine 47-53 PML nuclear body scaffold Homo sapiens 197-200 19553342-4 2009 In addition, we demonstrate that this disruption is largely dependent on both the integrity of a SUMO interaction motif in LANA2 and the lysine 160 from PML. Lysine 137-143 PML nuclear body scaffold Homo sapiens 153-156 18408733-3 2008 Here, we demonstrate that arsenic-induced PML SUMOylation triggers its Lys 48-linked polyubiquitination and proteasome-dependent degradation. Lysine 71-74 PML nuclear body scaffold Homo sapiens 42-45 25032863-3 2014 Here we demonstrate that acetylation of lysine 487 (K487) and SUMO1 conjugation of K490 at PML protein are mutually exclusive. Lysine 40-46 PML nuclear body scaffold Homo sapiens 91-94 23542129-0 2013 Dual roles for lysine 490 of promyelocytic leukemia protein in the transactivation of glucocorticoid receptor-interacting protein 1. Lysine 15-21 PML nuclear body scaffold Homo sapiens 29-59 23542129-5 2013 Three N-terminal sumoylation residues (Lys 65, 160, and 490) exhibited differential roles in the regulation of GRIP1 activity, and the sumoylation of Lys 490 acted as the primary nuclear localization signal of PML. Lysine 150-153 PML nuclear body scaffold Homo sapiens 210-213 20006587-4 2010 Deletion of a short lysine-rich domain that contains the major SUMO acceptor sites of CBP abrogated its ability to be SUMO modified, and prevented its association with endogenous SUMO-1/PML speckles in vivo. Lysine 20-26 PML nuclear body scaffold Homo sapiens 186-189 15748426-8 2005 As(2)O(3) binds ubiquitin like SUMO-1 through the lysine 160 of PML, resulting in the degradation of PML-RAR alpha. Lysine 50-56 PML nuclear body scaffold Homo sapiens 64-67 15748426-8 2005 As(2)O(3) binds ubiquitin like SUMO-1 through the lysine 160 of PML, resulting in the degradation of PML-RAR alpha. Lysine 50-56 PML nuclear body scaffold Homo sapiens 101-104 12759344-9 2003 Interestingly, PML mutants in which sumoylation at lysine 160 was inhibited displayed an increased association with MDM2, suggesting that sumoylation at this site may be a determinant of PML-MDM2 binding. Lysine 51-57 PML nuclear body scaffold Homo sapiens 187-190 12885887-0 2003 PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. Lysine 12-18 PML nuclear body scaffold Homo sapiens 0-3 12885887-0 2003 PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. Lysine 12-18 PML nuclear body scaffold Homo sapiens 58-61 12885887-11 2003 Using a transfection-based approach and a family of deletion and point mutations of PML, we found that efficient ICP0-induced PML degradation requires sequences within the C-terminal part of PML and lysine residue 160, one of the principal targets for SUMO-1 modification of the protein. Lysine 199-205 PML nuclear body scaffold Homo sapiens 84-87 12885887-11 2003 Using a transfection-based approach and a family of deletion and point mutations of PML, we found that efficient ICP0-induced PML degradation requires sequences within the C-terminal part of PML and lysine residue 160, one of the principal targets for SUMO-1 modification of the protein. Lysine 199-205 PML nuclear body scaffold Homo sapiens 126-129 12885887-11 2003 Using a transfection-based approach and a family of deletion and point mutations of PML, we found that efficient ICP0-induced PML degradation requires sequences within the C-terminal part of PML and lysine residue 160, one of the principal targets for SUMO-1 modification of the protein. Lysine 199-205 PML nuclear body scaffold Homo sapiens 126-129 9756909-7 1998 The PML mutant with Lys to Arg substitutions in all three sites is expressed normally, but cannot be sentrinized. Lysine 20-23 PML nuclear body scaffold Homo sapiens 4-7 9885291-5 1999 The precise molecular role for the SUMO-1 modification of PML is unclear, and the specific lysine residues within PML that are targeted for modification and the PML sub-domains necessary for mediating the modification in vivo are unknown. Lysine 91-97 PML nuclear body scaffold Homo sapiens 114-117 9885291-5 1999 The precise molecular role for the SUMO-1 modification of PML is unclear, and the specific lysine residues within PML that are targeted for modification and the PML sub-domains necessary for mediating the modification in vivo are unknown. Lysine 91-97 PML nuclear body scaffold Homo sapiens 114-117