PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6418159-0 1983 Role of lysine residues in the binding of glyceraldehyde-3-phosphate dehydrogenase to human erythrocyte membranes. Lysine 8-14 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 42-82 18552833-5 2008 Here we show that nuclear GAPDH is acetylated at Lys 160 by the acetyltransferase p300/CREB binding protein (CBP) through direct protein interaction, which in turn stimulates the acetylation and catalytic activity of p300/CBP. Lysine 49-52 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-31 12493840-5 2003 Recently, the authors have shown that K191, K268, and K331, out of the 26 lysines present in glyceraldehyde-3-phosphate-dehydrogenase, are the reactive amine-donor sites forming cross-links with substance P, which bears the simplest Q(n) domain (n = 2). Lysine 74-81 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 93-133 11742130-9 2002 Here, we report that of the 26 lysines present in GAPDH, K191, K268, and K331 were the only amino-donor residues modified by tissue transglutaminase. Lysine 31-38 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 50-55 15048777-1 2004 Brownian dynamics simulations of computer models of GAPDH mutants interacting with F-actin emphasized the electrostatic nature of such interactions, and confirmed the importance of four previously identified lysine residues on the GAPDH structure in these interactions. Lysine 208-214 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 52-57 15048777-1 2004 Brownian dynamics simulations of computer models of GAPDH mutants interacting with F-actin emphasized the electrostatic nature of such interactions, and confirmed the importance of four previously identified lysine residues on the GAPDH structure in these interactions. Lysine 208-214 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 231-236 14196563-0 1964 SPECIFIC ACETYLATION OF A LYSINE RESIDUE DURING THE HYDROLYTIC ACTION OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE. Lysine 26-32 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 73-113 5087618-0 1971 Identification of lysines reactive with pyridoxal 5"-phosphate in glyceraldehyde-3-phosphate dehydrogenase. Lysine 18-25 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 66-106 5880873-0 1965 Amino acid sequence around a reactive lysine in glyceraldehyde 3-phosphate dehydrogenase. Lysine 38-44 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 48-88 25416785-4 2015 DJ-1 deglycates cysteines, arginines, and lysines (the three major glycated amino acids) of serum albumin, glyceraldehyde-3-phosphate dehydrogenase, aldolase, and aspartate aminotransferase and thus reactivates these proteins. Lysine 42-49 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 107-147 30659183-7 2019 Upon LPS stimulation, GAPDH undergoes malonylation on lysine 213, leading to its dissociation from TNFalpha mRNA, promoting translation. Lysine 54-60 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 22-27 28258188-4 2017 Several proteomics studies have identified 4 lysine residues in critical regions of mammalian GAPDH that are altered by multiple post-translational modifications. Lysine 45-51 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 94-99 22847419-4 2012 The Rossmann fold containing NAD(+) binding region on GAPDH is responsible for the interaction with TERC, whereas a lysine residue in the GAPDH catalytic domain is required for inhibiting telomerase activity and disrupting telomere maintenance. Lysine 116-122 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 54-59 22847419-4 2012 The Rossmann fold containing NAD(+) binding region on GAPDH is responsible for the interaction with TERC, whereas a lysine residue in the GAPDH catalytic domain is required for inhibiting telomerase activity and disrupting telomere maintenance. Lysine 116-122 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 138-143 24912753-6 2014 At low concentrations of homocysteine thiolactone, modification of GAPDH leads not only to prevention of spontaneous inactivation but also increases thermal stability of this enzyme on heating to 80 C. A moderate reduction of the activity of GAPDH observed in case of its crosslinking with 50-fold excess of homocysteine thiolactone per lysine is probably caused by hindered substrate diffusion. Lysine 337-343 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 67-72 24912753-6 2014 At low concentrations of homocysteine thiolactone, modification of GAPDH leads not only to prevention of spontaneous inactivation but also increases thermal stability of this enzyme on heating to 80 C. A moderate reduction of the activity of GAPDH observed in case of its crosslinking with 50-fold excess of homocysteine thiolactone per lysine is probably caused by hindered substrate diffusion. Lysine 337-343 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 242-247 24362262-0 2014 Glyceraldehyde-3-phosphate dehydrogenase is activated by lysine 254 acetylation in response to glucose signal. Lysine 57-63 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-40 24362262-3 2014 Here, we report that acetylation at lysine 254 (K254) increases GAPDH activity in response to glucose. Lysine 36-42 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 64-69 20601085-3 2010 The GAPDH-Siah interaction depends on the integrity of lysine 227 in human GAPDH, being the mutant K227A unable to associate with Siah. Lysine 55-61 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 4-9 20601085-3 2010 The GAPDH-Siah interaction depends on the integrity of lysine 227 in human GAPDH, being the mutant K227A unable to associate with Siah. Lysine 55-61 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 75-80 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 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 77-82 20601085-10 2010 Finally, we identified Lys 227 as a third GAPDH residue whose acetylation is needed for its transport from cytoplasm to the nucleus. Lysine 23-26 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 42-47 20601085-11 2010 Thus, results reported here indicate that nuclear translocation of GAPDH is mediated by acetylation of three specific Lys residues (117, 227 and 251 in human cells). Lysine 118-121 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 67-72 20177150-6 2010 The nuclear export induced by the re-addition of serum or growth factors was prevented by LY 294002 and SH-5, inhibitors of phosphoinositide 3-kinase (PI3K) and Akt/protein kinase B, respectively, suggesting an involvement of the PI3K signaling pathway in the nuclear export of GAPDH. Lysine 90-92 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 278-283