PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29787766-6 2018 The H112N mutant was found to be dimeric, but devoid of catalytic activity, due to the loss of the catalytically essential histidine; nevertheless, it exhibited high affinity to AMP and a HINT1 inhibitor. Histidine 123-132 histidine triad nucleotide binding protein 1 Homo sapiens 188-193 30772266-3 2019 We hypothesize that the enzyme responsible for (d)NMPS catabolism could be Hint1, an enzyme that belongs to the histidine triad (HIT) superfamily and is present in all organisms. Histidine 112-121 histidine triad nucleotide binding protein 1 Homo sapiens 75-80 30622225-1 2019 Histidine triad nucleotide-binding protein (HINT) is a member of the histidine triad (HIT) superfamily, which has hydrolase activity owing to a histidine triad motif. Histidine 69-78 histidine triad nucleotide binding protein 1 Homo sapiens 0-42 30622225-1 2019 Histidine triad nucleotide-binding protein (HINT) is a member of the histidine triad (HIT) superfamily, which has hydrolase activity owing to a histidine triad motif. Histidine 69-78 histidine triad nucleotide binding protein 1 Homo sapiens 44-48 30622225-1 2019 Histidine triad nucleotide-binding protein (HINT) is a member of the histidine triad (HIT) superfamily, which has hydrolase activity owing to a histidine triad motif. Histidine 144-153 histidine triad nucleotide binding protein 1 Homo sapiens 0-42 30622225-1 2019 Histidine triad nucleotide-binding protein (HINT) is a member of the histidine triad (HIT) superfamily, which has hydrolase activity owing to a histidine triad motif. Histidine 144-153 histidine triad nucleotide binding protein 1 Homo sapiens 44-48 29125116-1 2017 The histidine triad nucleotide binding protein1(HINT1),which belongs to the histidine triad(HIT) enzyme superfamily,exerts its enzymic activities as hydrolase or transferase. Histidine 4-13 histidine triad nucleotide binding protein 1 Homo sapiens 48-53 28984882-1 2017 As a member of the histidine triad (HIT) protein superfamily, human histidine triad nucleotide binding protein 1 (hHint1) serves as an efficient enzyme in the hydrolysis of phosphoramidate. Histidine 19-28 histidine triad nucleotide binding protein 1 Homo sapiens 68-112 28984882-1 2017 As a member of the histidine triad (HIT) protein superfamily, human histidine triad nucleotide binding protein 1 (hHint1) serves as an efficient enzyme in the hydrolysis of phosphoramidate. Histidine 19-28 histidine triad nucleotide binding protein 1 Homo sapiens 114-120 28739258-3 2017 The role of metal ions in regulating postsynaptic transmission is well known, and the active site of hHint1 contains multiple histidines. Histidine 126-136 histidine triad nucleotide binding protein 1 Homo sapiens 101-107 28691797-3 2017 The active site of hHint1 comprises an ensemble of strictly conserved histidines, including nucleophilic His112. Histidine 70-80 histidine triad nucleotide binding protein 1 Homo sapiens 19-25 19081673-1 2009 The Hint1 protein, a member of the histidine triad (HIT) family, is highly conserved in diverse species and ubiquitously expressed in mammalian tissues. Histidine 35-44 histidine triad nucleotide binding protein 1 Homo sapiens 4-9 25976113-3 2016 In the present study, we used affinity purification to identify PsGPA1-interacting proteins, including PsHint1, a histidine triad (HIT) domain-containing protein orthologous to human HIT nucleotide-binding protein 1 (HINT1). Histidine 114-123 histidine triad nucleotide binding protein 1 Homo sapiens 183-215 20940308-3 2010 We suggest that the enzyme responsible for nucleoside 5"-O-monophosphorothioate ((d)NMPS) metabolism could be histidine triad nucleotide-binding protein 1 (Hint-1), a phosphoramidase belonging to the histidine triad (HIT) superfamily that is present in all forms of life. Histidine 110-119 histidine triad nucleotide binding protein 1 Homo sapiens 156-162 29214080-2 2017 As a member of the histidine triad (HIT) enzyme superfamily, HINT1 is distributed in almost every organ and has both enzymatic and nonenzymatic activity. Histidine 19-28 histidine triad nucleotide binding protein 1 Homo sapiens 61-66 25176218-1 2014 Histidine triad nucleotide-binding protein 1 (HINT1) is a member of a superfamily of histidine triad proteins named by the conserved nucleotide-binding motif histidine-x-histidine-x-histidine-xx, in which x represents hydrophobic amino acid. Histidine 85-94 histidine triad nucleotide binding protein 1 Homo sapiens 0-44 25176218-1 2014 Histidine triad nucleotide-binding protein 1 (HINT1) is a member of a superfamily of histidine triad proteins named by the conserved nucleotide-binding motif histidine-x-histidine-x-histidine-xx, in which x represents hydrophobic amino acid. Histidine 85-94 histidine triad nucleotide binding protein 1 Homo sapiens 46-51 25176218-1 2014 Histidine triad nucleotide-binding protein 1 (HINT1) is a member of a superfamily of histidine triad proteins named by the conserved nucleotide-binding motif histidine-x-histidine-x-histidine-xx, in which x represents hydrophobic amino acid. Histidine 158-167 histidine triad nucleotide binding protein 1 Homo sapiens 0-44 25176218-1 2014 Histidine triad nucleotide-binding protein 1 (HINT1) is a member of a superfamily of histidine triad proteins named by the conserved nucleotide-binding motif histidine-x-histidine-x-histidine-xx, in which x represents hydrophobic amino acid. Histidine 158-167 histidine triad nucleotide binding protein 1 Homo sapiens 46-51 23666425-8 2013 This NO acts on the RGSZ2 zinc finger, providing the zinc ions that are required for PKC/Raf-1 cysteine-rich domains to simultaneously bind to the histidines present in the HINT1 homodimer. Histidine 147-157 histidine triad nucleotide binding protein 1 Homo sapiens 173-178 19720079-1 2010 Histidine triad nucleotide binding protein (HINT) represents the most ancient and widespread branches in the histidine triad superfamily. Histidine 109-118 histidine triad nucleotide binding protein 1 Homo sapiens 44-48 15790557-3 2005 Disease-associated mutations in Aprataxin target a histidine triad domain that is similar to Hint, a universally conserved AMP-lysine hydrolase, or truncate the protein NH2-terminal to a zinc finger. Histidine 51-60 histidine triad nucleotide binding protein 1 Homo sapiens 93-97 19206287-1 2008 We have demonstrated that nanostructures, and in particular nanorings incorporating a homodimeric enzyme, can be prepared by chemically induced self-assembly of dihydrofolate reductase (DHFR)-histidine triad nucleotide binding 1 (Hint1) fusion proteins. Histidine 192-201 histidine triad nucleotide binding protein 1 Homo sapiens 230-235 17870088-15 2007 Taken together, these results imply that while Hint3 and Hint1 prefer aminoacyl-adenylates as substrates and catalytically interact with aminoacyl-tRNA synthetases, the significant differences in phosphoramidase activity, oligomeric state, and cellular localization suggest that Hint3s should be placed in a distinct branch of the histidine triad superfamily. Histidine 331-340 histidine triad nucleotide binding protein 1 Homo sapiens 57-62 17510397-1 2007 There is accumulating evidence that histidine triad (HIT) nucleotide-binding protein 1 (HINT1), a member of the evolutionary highly conserved HIT protein super family, is a novel tumor suppressor. Histidine 36-45 histidine triad nucleotide binding protein 1 Homo sapiens 88-93 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 53-62 histidine triad nucleotide binding protein 1 Homo sapiens 161-165 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 53-62 histidine triad nucleotide binding protein 1 Homo sapiens 186-191 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 142-145 histidine triad nucleotide binding protein 1 Homo sapiens 83-87 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 142-145 histidine triad nucleotide binding protein 1 Homo sapiens 161-165 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 142-145 histidine triad nucleotide binding protein 1 Homo sapiens 186-191 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 169-172 histidine triad nucleotide binding protein 1 Homo sapiens 83-87 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 169-172 histidine triad nucleotide binding protein 1 Homo sapiens 186-191 16014379-2 2005 In this study, Hint1/PKCI, a member of the evolutionary conserved family of histidine triad proteins, was characterised as a new interaction partner of Pontin and Reptin. Histidine 76-85 histidine triad nucleotide binding protein 1 Homo sapiens 15-20 18596417-7 2008 Here, we summarize these findings with special emphasis on the histidine triad proteins Hint1 and Fhit and their repressive activity on the beta-catenin signaling function. Histidine 63-72 histidine triad nucleotide binding protein 1 Homo sapiens 88-93 17158446-7 2007 Site-directed mutagenesis studies of the active site histidine triad revealed that Hint labeling could be abolished by substitution of either His-101 of E. coli hinT or His-112 of human Hint1 by either alanine or glycine. Histidine 53-62 histidine triad nucleotide binding protein 1 Homo sapiens 83-87 16186798-1 2006 The HINT1 protein, a member of the histidine triad (HIT) family, is highly conserved in diverse species and ubiquitously expressed in mammalian tissues. Histidine 35-44 histidine triad nucleotide binding protein 1 Homo sapiens 4-9 15256063-7 2004 Hint/PKCI-1, which is the only other characterized human histidine triad (HIT) nucleotide-binding protein in addition to tumor-suppressor gene FHIT, might be involved in lung carcinogenesis. Histidine 57-66 histidine triad nucleotide binding protein 1 Homo sapiens 0-4 15256063-7 2004 Hint/PKCI-1, which is the only other characterized human histidine triad (HIT) nucleotide-binding protein in addition to tumor-suppressor gene FHIT, might be involved in lung carcinogenesis. Histidine 57-66 histidine triad nucleotide binding protein 1 Homo sapiens 5-11 10958787-2 2000 Here, we report a novel interaction between Cdk7 and a histidine triad (HIT) family protein, Hint/PKCI-1. Histidine 55-64 histidine triad nucleotide binding protein 1 Homo sapiens 93-97 10958787-2 2000 Here, we report a novel interaction between Cdk7 and a histidine triad (HIT) family protein, Hint/PKCI-1. Histidine 55-64 histidine triad nucleotide binding protein 1 Homo sapiens 98-104 10958787-6 2000 The physical and genetic interactions of Hint and Hnt1 with Cdk7 and Kin28 suggest a role for this class of histidine triad proteins in the regulation of Cdk7 and Kin28 functions. Histidine 108-117 histidine triad nucleotide binding protein 1 Homo sapiens 41-45