PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27543355-9 2016 [3H]-GlySar and [3H]-l-His uptake receded to approximately 30% in the presence of His-Leu-LPV supporting the PepT1/PHT1 mediated uptake process. Histidine 21-26 solute carrier family 15 member 1 Homo sapiens 109-114 33952823-0 2021 Protonation State of a Histidine Residue in Human Oligopeptide Transporter 1 (hPEPT1) Regulates hPEPT1-Mediated Efflux Activity. Histidine 23-32 solute carrier family 15 member 1 Homo sapiens 78-84 33952823-0 2021 Protonation State of a Histidine Residue in Human Oligopeptide Transporter 1 (hPEPT1) Regulates hPEPT1-Mediated Efflux Activity. Histidine 23-32 solute carrier family 15 member 1 Homo sapiens 96-102 33952823-10 2021 These data indicate that the efflux process of hPEPT1 is also regulated in a pH-dependent manner by the protonation state of a histidine residue located at or near the substrate recognition site facing the extracellular space. Histidine 127-136 solute carrier family 15 member 1 Homo sapiens 47-53 27543355-9 2016 [3H]-GlySar and [3H]-l-His uptake receded to approximately 30% in the presence of His-Leu-LPV supporting the PepT1/PHT1 mediated uptake process. Histidine 23-26 solute carrier family 15 member 1 Homo sapiens 109-114 10362647-6 1999 A histidine residue modifier, diethyl pyrocarbonate, inhibited glycylsarcosine uptake by both transporters, although the inhibitory effect was greater on PEPT1. Histidine 2-11 solute carrier family 15 member 1 Homo sapiens 154-159 14567632-8 2003 Zinc inhibited the PEPT1 function, possibly by interacting with histidine residues of PEPT1 that are part of an H+-binding site. Histidine 64-73 solute carrier family 15 member 1 Homo sapiens 19-24 14567632-8 2003 Zinc inhibited the PEPT1 function, possibly by interacting with histidine residues of PEPT1 that are part of an H+-binding site. Histidine 64-73 solute carrier family 15 member 1 Homo sapiens 86-91 16651734-10 2006 Modification of carboxyl groups or hydroxyl groups had no significant influence on the pH-profile, whereas a chemical modification of histidine residue with diethylpyrocarbonate (DEPC) completely abolished the transport activity in CHO/hPEPT1 cells. Histidine 134-143 solute carrier family 15 member 1 Homo sapiens 236-242 16651734-12 2006 This protection was observed only in the presence of the substrate of hPEPT1, indicating that the histidine residue is located at the substrate recognition site. Histidine 98-107 solute carrier family 15 member 1 Homo sapiens 70-76 9003198-3 1997 In hPEPT1, these residues are His-57, His-121, and His-260. Histidine 30-33 solute carrier family 15 member 1 Homo sapiens 3-9 9003198-3 1997 In hPEPT1, these residues are His-57, His-121, and His-260. Histidine 38-41 solute carrier family 15 member 1 Homo sapiens 3-9 9003198-3 1997 In hPEPT1, these residues are His-57, His-121, and His-260. Histidine 38-41 solute carrier family 15 member 1 Homo sapiens 3-9 9003198-6 1997 His-57 in hPEPT1 and His-87 in hPEPT2 were found to be absolutely essential for catalytic activity because the corresponding mutants had no detectable peptide transport activity. Histidine 0-3 solute carrier family 15 member 1 Homo sapiens 10-16 9003198-7 1997 His-121 in hPEPT1 is not essential since mutation of this residue did not impair transport function. Histidine 0-3 solute carrier family 15 member 1 Homo sapiens 11-17 9003198-9 1997 The obligatory histidyl residue (His-57 in hPEPT1 and His-87 in hPEPT2) is located in an almost identical topological position in both transporters, near the extracellular surface of the second putative transmembrane domain. Histidine 33-36 solute carrier family 15 member 1 Homo sapiens 43-49 9003198-12 1997 The loss of transport function of hPEPT1 and hPEPT2, when His-57 in hPEPT1 and His-87 in hPEPT2 were mutated, was not due to alterations in protein expression because the expression levels of these mutants were similar to those of the respective wild type transporters in HeLa cells as assessed by immunoblot analysis. Histidine 58-61 solute carrier family 15 member 1 Homo sapiens 34-40 9003198-12 1997 The loss of transport function of hPEPT1 and hPEPT2, when His-57 in hPEPT1 and His-87 in hPEPT2 were mutated, was not due to alterations in protein expression because the expression levels of these mutants were similar to those of the respective wild type transporters in HeLa cells as assessed by immunoblot analysis. Histidine 58-61 solute carrier family 15 member 1 Homo sapiens 68-74 9003198-12 1997 The loss of transport function of hPEPT1 and hPEPT2, when His-57 in hPEPT1 and His-87 in hPEPT2 were mutated, was not due to alterations in protein expression because the expression levels of these mutants were similar to those of the respective wild type transporters in HeLa cells as assessed by immunoblot analysis. Histidine 79-82 solute carrier family 15 member 1 Homo sapiens 34-40 9003198-13 1997 Confocal analysis of immunofluorescence in X. laevis oocytes expressing the wild type and the three histidine mutants of hPEPT1 showed that the transporter protein is expressed exclusively in the plasma membrane and that the level of expression is comparable among the wild type and the three mutants. Histidine 100-109 solute carrier family 15 member 1 Homo sapiens 121-127 9003198-14 1997 These site-directed mutagenesis studies clearly show that His-57 in hPEPT1 and His-87 in hPEPT2 are the most critical histidyl residues necessary for the catalytic function of these transporters. Histidine 58-61 solute carrier family 15 member 1 Homo sapiens 68-74 8843163-6 1996 These findings suggest that both histidine 57 and histidine 121, which are conserved in the rat, rabbit and human PEPT1, are involved in substrate recognition of this molecule. Histidine 33-42 solute carrier family 15 member 1 Homo sapiens 114-119 8843163-6 1996 These findings suggest that both histidine 57 and histidine 121, which are conserved in the rat, rabbit and human PEPT1, are involved in substrate recognition of this molecule. Histidine 50-59 solute carrier family 15 member 1 Homo sapiens 114-119