| + |
CSNK2A1 | up-regulates 
phosphorylation
|
CFTR |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176619 |
Ser422 |
NNNNRKTsNGDDSLF |
Homo sapiens |
|
| pmid |
sentence |
| 21930781 |
Cftr possesses two ck2 phosphorylation sites (s422 and t1471)this is consistent with an important role for s422 phosphorylation in increasing cftr activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates 
phosphorylation
|
CFTR |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176623 |
Ser511 |
ENIIFGVsYDEYRYR |
Homo sapiens |
|
| pmid |
sentence |
| 21930781 |
Serine 511 has been previously implicated in the regulation of cftr by ck2, as the mutant s511d was found to be insensitive to tbb in xenopus oocytes but to have no major impact on the single-channel behavior of cftr |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176627 |
Thr1471 |
IAALKEEtEEEVQDT |
Homo sapiens |
|
| pmid |
sentence |
| 21930781 |
Cftr possesses two ck2 phosphorylation sites (s422 and t1471) the t1471 residue, previously described as a site for cftr phosphorylation by ck2 (25), seems to be critical for cftr turnover and processing. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | up-regulates
phosphorylation
|
CFTR |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18237 |
Ser660 |
FSAERRNsILTETLH |
Homo sapiens |
|
| pmid |
sentence |
| 1377674 |
Direct amino acid sequencing and peptide mapping of cf-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by pka and pkgcftr possesses a large cluster of strict dibasic consensus sites for phosphorylation by protein kinase a (pka) in the r-domain and an obligatory dependence on phosphorylation is a hallmark of cftr cl(-) channel function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72712 |
Ser660 |
FSAERRNsILTETLH |
Homo sapiens |
|
| pmid |
sentence |
| 10581361 |
Direct amino acid sequencing and peptide mapping of cf-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by pka and pkgcftr possesses a large cluster of strict dibasic consensus sites for phosphorylation by protein kinase a (pka) in the r-domain and an obligatory dependence on phosphorylation is a hallmark of cftr cl(-) channel function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72724 |
Ser795 |
TASTRKVsLAPQANL |
Homo sapiens |
|
| pmid |
sentence |
| 10581361 |
Direct amino acid sequencing and peptide mapping of cf-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by pka and pkgcftr possesses a large cluster of strict dibasic consensus sites for phosphorylation by protein kinase a (pka) in the r-domain and an obligatory dependence on phosphorylation is a hallmark of cftr cl(-) channel function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18249 |
Ser795 |
TASTRKVsLAPQANL |
Homo sapiens |
|
| pmid |
sentence |
| 1377674 |
Direct amino acid sequencing and peptide mapping of cf-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by pka and pkgcftr possesses a large cluster of strict dibasic consensus sites for phosphorylation by protein kinase a (pka) in the r-domain and an obligatory dependence on phosphorylation is a hallmark of cftr cl(-) channel function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18253 |
Ser813 |
DIYSRRLsQETGLEI |
Homo sapiens |
|
| pmid |
sentence |
| 1377674 |
Direct amino acid sequencing and peptide mapping of cf-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by pka and pkgcftr possesses a large cluster of strict dibasic consensus sites for phosphorylation by protein kinase a (pka) in the r-domain and an obligatory dependence on phosphorylation is a hallmark of cftr cl(-) channel function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72728 |
Ser813 |
DIYSRRLsQETGLEI |
Homo sapiens |
|
| pmid |
sentence |
| 10581361 |
Direct amino acid sequencing and peptide mapping of cf-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by pka and pkgcftr possesses a large cluster of strict dibasic consensus sites for phosphorylation by protein kinase a (pka) in the r-domain and an obligatory dependence on phosphorylation is a hallmark of cftr cl(-) channel function |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates
phosphorylation
|
CFTR |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21312 |
Ser660 |
FSAERRNsILTETLH |
Homo sapiens |
|
| pmid |
sentence |
| 1716180 |
Cftr, the protein associated with cystic fibrosis, is phosphorylated on serine residues in response to camp agonists. Serines 660, 737, 795, and 813 were identified as in vivo targets for phosphorylation by protein kinase a.mutagenesis of all four sites abolished the response. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21320 |
Ser795 |
TASTRKVsLAPQANL |
Homo sapiens |
|
| pmid |
sentence |
| 1716180 |
Cftr, the protein associated with cystic fibrosis, is phosphorylated on serine residues in response to camp agonists. Serines 660, 737, 795, and 813 were identified as in vivo targets for phosphorylation by protein kinase a.mutagenesis of all four sites abolished the response. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21324 |
Ser813 |
DIYSRRLsQETGLEI |
Homo sapiens |
|
| pmid |
sentence |
| 1716180 |
Cftr, the protein associated with cystic fibrosis, is phosphorylated on serine residues in response to camp agonists. Serines 660, 737, 795, and 813 were identified as in vivo targets for phosphorylation by protein kinase a.mutagenesis of all four sites abolished the response. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
CFTR |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250349 |
Ser660 |
FSAERRNsILTETLH |
in vitro |
|
| pmid |
sentence |
| 1377674 |
CFTR is phosphorylated directly by PKA and PKC in vivo. phosphorylation by PKA is necessary to allow ATP hydrolysis by CFTR and that ATP hydrolysis is necessary for channel opening. CF-2 was phosphorylated by PKA in vitro on serines 660,700, 737, 813 and most likely on both serines 768 and 795. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250348 |
Ser700 |
FGEKRKNsILNPINS |
in vitro |
|
| pmid |
sentence |
| 1377674 |
CFTR is phosphorylated directly by PKA and PKC in vivo. phosphorylation by PKA is necessary to allow ATP hydrolysis by CFTR and that ATP hydrolysis is necessary for channel opening. CF-2 was phosphorylated by PKA in vitro on serines 660,700, 737, 813 and most likely on both serines 768 and 795. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250351 |
Ser813 |
DIYSRRLsQETGLEI |
in vitro |
|
| pmid |
sentence |
| 1377674 |
CFTR is phosphorylated directly by PKA and PKC in vivo. phosphorylation by PKA is necessary to allow ATP hydrolysis by CFTR and that ATP hydrolysis is necessary for channel opening. CF-2 was phosphorylated by PKA in vitro on serines 660,700, 737, 813 and most likely on both serines 768 and 795. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCA | up-regulates activity
phosphorylation
|
CFTR |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248849 |
Ser686 |
WTETKKQsFKQTGEF |
in vitro |
|
| pmid |
sentence |
| 1377674 |
Direct amino acid sequencing and peptide mapping of CF-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by PKA and PKG, and serines 686 and 790 were phosphorylated by PKC. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248851 |
Ser790 |
IHRKTTAsTRKVSLA |
in vitro |
|
| pmid |
sentence |
| 1377674 |
Direct amino acid sequencing and peptide mapping of CF-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by PKA and PKG, and serines 686 and 790 were phosphorylated by PKC. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKG1 | up-regulates activity
phosphorylation
|
CFTR |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248850 |
Ser700 |
FGEKRKNsILNPINS |
in vitro |
|
| pmid |
sentence |
| 1377674 |
Direct amino acid sequencing and peptide mapping of CF-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by PKA and PKG, and serines 686 and 790 were phosphorylated by PKC. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates activity
phosphorylation
|
CFTR |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21316 |
Ser737 |
EPLERRLsLVPDSEQ |
Homo sapiens |
|
| pmid |
sentence |
| 19095655 |
AMPK phosphorylates CFTR in vitro at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18141 |
Ser768 |
EPLERRLsLVPDSEQ |
Homo sapiens |
|
| pmid |
sentence |
| 19095655 |
AMPK phosphorylates CFTR in vitro at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AMPK | down-regulates activity
phosphorylation
|
CFTR |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250350 |
Ser737 |
EPLERRLsLVPDSEQ |
Homo sapiens |
|
| pmid |
sentence |
| 19095655 |
AMPK phosphorylates CFTR¬†in vitro¬†at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.|Interestingly two of these sites, namely Ser737 and Ser768, have been identified as “inhibitory” R domain sites, i.e. when mutated to alanines they augment the open probability of CFTR relative to wild type|Our present results suggest that it might be AMPK rather than PKA that is phosphorylating Ser737 and Ser768 under baseline conditions |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72708 |
Ser768 |
LQARRRQsVLNLMTH |
Homo sapiens |
|
| pmid |
sentence |
| 19095655 |
AMPK phosphorylates CFTR¬†in vitro¬†at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.|Interestingly two of these sites, namely Ser737 and Ser768, have been identified as “inhibitory” R domain sites, i.e. when mutated to alanines they augment the open probability of CFTR relative to wild type|Our present results suggest that it might be AMPK rather than PKA that is phosphorylating Ser737 and Ser768 under baseline conditions |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | down-regulates activity
phosphorylation
|
CFTR |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259858 |
Ser737 |
EPLERRLsLVPDSEQ |
Homo sapiens |
|
| pmid |
sentence |
| 19095655 |
AMPK phosphorylates CFTR¬†in vitro¬†at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.|Interestingly two of these sites, namely Ser737 and Ser768, have been identified as “inhibitory” R domain sites, i.e. when mutated to alanines they augment the open probability of CFTR relative to wild type|Our present results suggest that it might be AMPK rather than PKA that is phosphorylating Ser737 and Ser768 under baseline conditions |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259867 |
Ser768 |
LQARRRQsVLNLMTH |
Homo sapiens |
|
| pmid |
sentence |
| 19095655 |
AMPK phosphorylates CFTR¬†in vitro¬†at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.|Interestingly two of these sites, namely Ser737 and Ser768, have been identified as “inhibitory” R domain sites, i.e. when mutated to alanines they augment the open probability of CFTR relative to wild type|Our present results suggest that it might be AMPK rather than PKA that is phosphorylating Ser737 and Ser768 under baseline conditions |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
glyburide | down-regulates activity
chemical inhibition
|
CFTR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258344 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 1281220 |
The sulfonylureas, tolbutamide and glibenclamide, inhibited whole-cell CFTR Cl- currents at half-maximal concentrations of approximately 150 and 20 microM, respectively. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ivacaftor | down-regulates
chemical inhibition
|
CFTR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193495 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tolbutamide | down-regulates activity
chemical inhibition
|
CFTR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258345 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 1281220 |
The sulfonylureas, tolbutamide and glibenclamide, inhibited whole-cell CFTR Cl- currents at half-maximal concentrations of approximately 150 and 20 microM, respectively. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
HSPA8 | down-regulates quantity
binding
|
CFTR |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271492 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21148293 |
JB12 cooperates with cytosolic Hsc70 and the ubiquitin ligase RMA1 to target CFTR and CFTRΔF508 for degradation. JB12 drives Hsc70 to associate with CFTR and the RMA1 E3 complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
polyubiquitination
|
CFTR |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272584 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11146634 |
Here we show that CHIP functions with Hsc70 to sense the folded state of CFTR and targets aberrant forms for proteasomal degradation by promoting their ubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXI1 | up-regulates quantity by expression 
transcriptional regulation
|
CFTR |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254176 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20972246 |
Results of transiently transfected vas deferens cells with either the -33G wild-type or the -33A variant CFTR directed luciferase reporter gene confirmed that the -33A variant, which alters the FOXI1 (Forkhead box I1) binding, significantly decreases the CFTR promoter activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK39 | down-regulates activity
phosphorylation
|
CFTR |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263134 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21317537 |
SPAK phosphorylates the transporters to reduce their surface expression and thus their activity and consequently inhibits ductal secretion to stabilize the resting state. PP1 reverses the effect of SPAK. Molecular analysis revealed that the WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264643 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Tissue: |
Pancreas |
| + |
GOPC | down-regulates
binding
|
CFTR |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111671 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11707463 |
Cal binds to cftr / cal affects insertion of cftr to the plasma membrane as well as its half-life in the plasma membrane. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF5 | down-regulates quantity by destabilization
ubiquitination
|
CFTR |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271494 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21148293 |
JB12 cooperates with cytosolic Hsc70 and the ubiquitin ligase RMA1 to target CFTR and CFTRΔF508 for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | up-regulates activity
dephosphorylation
|
CFTR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264646 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21317537 |
WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Pancreas |
3.0
CFTR
- 
- 