PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21525134-2 2011 Importantly, 24-h BUO reduces the abundance of the collecting duct water channel aquaporin-2 (AQP2) and AQP2 phosphorylated at serine 256 (AQP2pS256). Serine 127-133 aquaporin 2 Rattus norvegicus 104-108 27488997-13 2016 Serine-264 of AQP2 is a phosphorylation site that is regulated by both PP1/PP2A and PP2B. Serine 0-6 aquaporin 2 Rattus norvegicus 14-18 26074997-7 2015 Importantly, the protein expression of AQP2 and AQP2 phosphorylated at serine 256 (pS256-AQP2) was downregulated after administration of QL and Valsartan to CHF rats. Serine 71-77 aquaporin 2 Rattus norvegicus 39-43 26074997-7 2015 Importantly, the protein expression of AQP2 and AQP2 phosphorylated at serine 256 (pS256-AQP2) was downregulated after administration of QL and Valsartan to CHF rats. Serine 71-77 aquaporin 2 Rattus norvegicus 48-52 26074997-7 2015 Importantly, the protein expression of AQP2 and AQP2 phosphorylated at serine 256 (pS256-AQP2) was downregulated after administration of QL and Valsartan to CHF rats. Serine 71-77 aquaporin 2 Rattus norvegicus 48-52 21511701-5 2011 The effect of simvastatin was independent of protein kinase A activation and phosphorylation at AQP2-Ser(256), a critical event involved in vasopressin (VP)-regulated AQP2 trafficking. Serine 101-104 aquaporin 2 Rattus norvegicus 96-100 18843259-0 2009 Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells. Serine 0-6 aquaporin 2 Rattus norvegicus 26-37 19209902-2 2009 Phosphorylation of Ser-256 at AQP2"s cytoplasmic COOH-terminus is well-accepted as a critical step for translocation. Serine 19-22 aquaporin 2 Rattus norvegicus 30-34 19209902-8 2009 These proteins were found to bind less to the Ser-256-phosphorylated AQP2 than to the nonphosphorylated form. Serine 46-49 aquaporin 2 Rattus norvegicus 69-73 19209902-12 2009 These results suggest that phosphorylation of AQP2 at Ser-256 may regulate AQP2 trafficking in part by mediating differential binding of hsp70 family proteins to the COOH-terminal tail. Serine 54-57 aquaporin 2 Rattus norvegicus 46-50 19209902-12 2009 These results suggest that phosphorylation of AQP2 at Ser-256 may regulate AQP2 trafficking in part by mediating differential binding of hsp70 family proteins to the COOH-terminal tail. Serine 54-57 aquaporin 2 Rattus norvegicus 75-79 18843259-2 2009 We recently identified a novel form of aquaporin-2 that is phosphorylated at serine-269 (pS269-AQP2). Serine 77-83 aquaporin 2 Rattus norvegicus 39-50 18843259-2 2009 We recently identified a novel form of aquaporin-2 that is phosphorylated at serine-269 (pS269-AQP2). Serine 77-83 aquaporin 2 Rattus norvegicus 95-99 18664568-5 2008 AQP2 mutants that mimic the Ser(256)-phosphorylated and -nonphosphorylated state accumulated at the cell surface and TGN, respectively. Serine 28-31 aquaporin 2 Rattus norvegicus 0-4 18596208-10 2008 The content of serine 256-phosphorylated AQP2 was greater in DRM than in non-DRM fractions. Serine 15-21 aquaporin 2 Rattus norvegicus 41-45 18029369-5 2008 RESULTS: We demonstrated that the protein expression of renal AQP2, Ser-256 phosphorylated AQP2, AQP3, beta- and gamma-ENaC (but not alpha-ENaC) increased consistently with an increased AVP response. Serine 68-71 aquaporin 2 Rattus norvegicus 91-95 18606813-2 2008 Using mass spectrometry, we previously demonstrated four phosphorylated serines (Ser256, Ser261, Ser264, and Ser269) in the carboxyl-terminal tail of rat AQP2. Serine 72-79 aquaporin 2 Rattus norvegicus 154-158 18606813-8 2008 Immunogold electron microscopy localized Ser(P)269-AQP2 solely in the apical plasma membrane of rat collecting duct cells, in contrast to the other three phospho-forms (found in both apical plasma membrane and intracellular vesicles). Serine 41-44 aquaporin 2 Rattus norvegicus 51-55 9321919-8 1997 Furthermore, substitution of the mercury-sensitive cysteine for a serine results in an impaired routing of human and rat AQP2. Serine 66-72 aquaporin 2 Rattus norvegicus 121-125 12388409-3 2002 Semiquantitative immunoblotting revealed a significant reduction in the abundance of inner medullary AQP2 (52 +/- 6% of control levels), consistent with previous studies, and of AQP2, which is phosphorylated at the PKA phosphorylation consensus site serine 256 (p-AQP2; 36 +/- 8%). Serine 250-256 aquaporin 2 Rattus norvegicus 178-182 11249863-3 2001 Semiquantitative immunoblotting revealed a significant increase in inner medullary AQP2 (201 +/- 12% of control rats, P < 0.05) and phosphorylated (Ser(256)) AQP2 (p-AQP2) abundance (299 +/- 32%) in DM rats. Serine 151-154 aquaporin 2 Rattus norvegicus 161-165 10710543-3 2000 Using a phosphorylation state-specific AQP2 antibody, we demonstrated that AVP stimulates AQP2 phosphorylation at the Ser(256) protein kinase A consensus site in a time- and dose-dependent manner. Serine 118-121 aquaporin 2 Rattus norvegicus 39-43 10710543-3 2000 Using a phosphorylation state-specific AQP2 antibody, we demonstrated that AVP stimulates AQP2 phosphorylation at the Ser(256) protein kinase A consensus site in a time- and dose-dependent manner. Serine 118-121 aquaporin 2 Rattus norvegicus 90-94 10710544-1 2000 Vasopression-induced phosphorylation of serine 256 of the aquaporin-2 (AQP2) water channel triggers translocation of the protein from cystolic reservoir vesicles to the apical membrane of collecting duct principal cells. Serine 40-46 aquaporin 2 Rattus norvegicus 58-69 10710544-1 2000 Vasopression-induced phosphorylation of serine 256 of the aquaporin-2 (AQP2) water channel triggers translocation of the protein from cystolic reservoir vesicles to the apical membrane of collecting duct principal cells. Serine 40-46 aquaporin 2 Rattus norvegicus 71-75 10644653-1 2000 Phosphorylation of Ser(256), in a PKA consensus site, in AQP2 (p-AQP2) appears to be critically involved in the vasopressin-induced trafficking of AQP2. Serine 19-22 aquaporin 2 Rattus norvegicus 57-61 10644653-1 2000 Phosphorylation of Ser(256), in a PKA consensus site, in AQP2 (p-AQP2) appears to be critically involved in the vasopressin-induced trafficking of AQP2. Serine 19-22 aquaporin 2 Rattus norvegicus 63-69 10644653-1 2000 Phosphorylation of Ser(256), in a PKA consensus site, in AQP2 (p-AQP2) appears to be critically involved in the vasopressin-induced trafficking of AQP2. Serine 19-22 aquaporin 2 Rattus norvegicus 65-69 10644653-2 2000 In the present study, affinity-purified antibodies that selectively recognize AQP2 phosphorylated at Ser(256) were developed. Serine 101-104 aquaporin 2 Rattus norvegicus 78-82 10644653-11 2000 Thus the results demonstrate that AQP2 phosphorylated in Ser(256) is present in the apical plasma membrane and in intracellular vesicles and that both the intracellular distribution/trafficking, as well as the abundance of p-AQP2, are regulated via V(2) receptors by altering phosphorylation and/or dephosphorylation of Ser(256) in AQP2. Serine 57-60 aquaporin 2 Rattus norvegicus 34-38 10644653-11 2000 Thus the results demonstrate that AQP2 phosphorylated in Ser(256) is present in the apical plasma membrane and in intracellular vesicles and that both the intracellular distribution/trafficking, as well as the abundance of p-AQP2, are regulated via V(2) receptors by altering phosphorylation and/or dephosphorylation of Ser(256) in AQP2. Serine 320-323 aquaporin 2 Rattus norvegicus 34-38 10644653-11 2000 Thus the results demonstrate that AQP2 phosphorylated in Ser(256) is present in the apical plasma membrane and in intracellular vesicles and that both the intracellular distribution/trafficking, as well as the abundance of p-AQP2, are regulated via V(2) receptors by altering phosphorylation and/or dephosphorylation of Ser(256) in AQP2. Serine 320-323 aquaporin 2 Rattus norvegicus 223-229 17636261-5 2007 The direct interaction of AQP2 with hsc70 is partially inhibited by ATP, and the Ser-256 residue in the AQP2 C terminus is important for this direct interaction. Serine 81-84 aquaporin 2 Rattus norvegicus 26-30 17636261-5 2007 The direct interaction of AQP2 with hsc70 is partially inhibited by ATP, and the Ser-256 residue in the AQP2 C terminus is important for this direct interaction. Serine 81-84 aquaporin 2 Rattus norvegicus 104-108 16985212-0 2007 Dynamics of aquaporin-2 serine-261 phosphorylation in response to short-term vasopressin treatment in collecting duct. Serine 24-30 aquaporin 2 Rattus norvegicus 12-23 16985212-1 2007 We recently identified a novel phosphorylation site, serine-261 (pS261), in the COOH-terminus of the vasopressin-regulated water channel, aquaporin-2 (AQP2). Serine 53-59 aquaporin 2 Rattus norvegicus 138-149 16985212-1 2007 We recently identified a novel phosphorylation site, serine-261 (pS261), in the COOH-terminus of the vasopressin-regulated water channel, aquaporin-2 (AQP2). Serine 53-59 aquaporin 2 Rattus norvegicus 151-155 15644488-2 2005 The paradigm for vasopressin-receptor signaling involves cAMP-mediated protein kinase A activation, which results in the functionally critical phosphorylation of AQP2 on amino acid serine 256. Serine 181-187 aquaporin 2 Rattus norvegicus 162-166 15585668-8 2005 Semiquantitative immunoblotting revealed significantly decreased expression of medullary aquaporin-2 (AQP2) and AQP2 phosphorylated in the PKA phosphorylation consensus site Ser-256 (p-AQP2) in response to DDAVP and candesartan cotreatment compared with DDAVP treatment alone. Serine 174-177 aquaporin 2 Rattus norvegicus 112-116 15585668-8 2005 Semiquantitative immunoblotting revealed significantly decreased expression of medullary aquaporin-2 (AQP2) and AQP2 phosphorylated in the PKA phosphorylation consensus site Ser-256 (p-AQP2) in response to DDAVP and candesartan cotreatment compared with DDAVP treatment alone. Serine 174-177 aquaporin 2 Rattus norvegicus 112-116 15010357-7 2004 However, substantial amounts of PKA-mediated serine 256 phosphorylated aquaporin-2 were still present after 4 h of ZP120C treatment. Serine 45-51 aquaporin 2 Rattus norvegicus 71-82 12388409-3 2002 Semiquantitative immunoblotting revealed a significant reduction in the abundance of inner medullary AQP2 (52 +/- 6% of control levels), consistent with previous studies, and of AQP2, which is phosphorylated at the PKA phosphorylation consensus site serine 256 (p-AQP2; 36 +/- 8%). Serine 250-256 aquaporin 2 Rattus norvegicus 178-182 10919858-3 2000 In addition, the levels of AQP2 phosphorylated in the protein kinase A (PKA) consensus site (Ser(256) of AQP2) was reduced to 3 +/- 1% of control levels. Serine 93-96 aquaporin 2 Rattus norvegicus 27-31 10919858-3 2000 In addition, the levels of AQP2 phosphorylated in the protein kinase A (PKA) consensus site (Ser(256) of AQP2) was reduced to 3 +/- 1% of control levels. Serine 93-96 aquaporin 2 Rattus norvegicus 105-109 33843270-12 2021 The vasopressin-like action on the kidney appears to accelerate AQP2 transcription and dephosphorylate AQP2 at serine 261. Serine 111-117 aquaporin 2 Rattus norvegicus 103-107 33255239-7 2020 ADM significantly decreased aquaporin-2 (AQP2) phosphorylation at Serine 256 (pS256) and increased it at Serine 261 (pS261). Serine 66-72 aquaporin 2 Rattus norvegicus 28-39 33255239-7 2020 ADM significantly decreased aquaporin-2 (AQP2) phosphorylation at Serine 256 (pS256) and increased it at Serine 261 (pS261). Serine 66-72 aquaporin 2 Rattus norvegicus 41-45 8621414-2 1996 AQP-2 possesses a single consensus cAMP-dependent protein kinase A (PKA) phosphorylation site (Ser-256) hypothesized to regulate channel Pf(Kuwahara, M., Fushimi, K., Terada, Y., Bai, L., Sasaki, S., and Marumo, F. (1995) J. Biol. Serine 95-98 aquaporin 2 Rattus norvegicus 0-5 29357442-8 2018 Urinary exosomal release of either the Ser-256- or Ser-269-phosphorylated form of AQP2, both of which are involved in apical trafficking of AQP2, was positively correlated with that of total AQP2. Serine 39-42 aquaporin 2 Rattus norvegicus 140-144 29357442-8 2018 Urinary exosomal release of either the Ser-256- or Ser-269-phosphorylated form of AQP2, both of which are involved in apical trafficking of AQP2, was positively correlated with that of total AQP2. Serine 39-42 aquaporin 2 Rattus norvegicus 140-144 29357442-8 2018 Urinary exosomal release of either the Ser-256- or Ser-269-phosphorylated form of AQP2, both of which are involved in apical trafficking of AQP2, was positively correlated with that of total AQP2. Serine 51-54 aquaporin 2 Rattus norvegicus 82-86 29357442-8 2018 Urinary exosomal release of either the Ser-256- or Ser-269-phosphorylated form of AQP2, both of which are involved in apical trafficking of AQP2, was positively correlated with that of total AQP2. Serine 51-54 aquaporin 2 Rattus norvegicus 140-144 29357442-8 2018 Urinary exosomal release of either the Ser-256- or Ser-269-phosphorylated form of AQP2, both of which are involved in apical trafficking of AQP2, was positively correlated with that of total AQP2. Serine 51-54 aquaporin 2 Rattus norvegicus 140-144