+ |
PKC | up-regulates activity
phosphorylation
|
KCNJ1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275990 |
Ser201 |
FSKNAVIsKRGGKLC |
in vitro |
|
pmid |
sentence |
12221079 |
We conclude that ROMK1 is a substrate of PKC and that serine residues 4 and 201 are the two main PKC phosphorylation sites that are essential for the expression of ROMK1 in the cell surface. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275989 |
Ser4 |
sSRNVFDT |
in vitro |
|
pmid |
sentence |
12221079 |
We conclude that ROMK1 is a substrate of PKC and that serine residues 4 and 201 are the two main PKC phosphorylation sites that are essential for the expression of ROMK1 in the cell surface. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PRKCA | down-regulates activity
phosphorylation
|
KCNJ1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276389 |
Thr193 |
KKRAKTItFSKNAVI |
in vitro |
|
pmid |
sentence |
22139477 |
The giant patch clamp together with site direct mutagenesis revealed that Thr-193 is the phosphorylation site on PKC that regulates the pH(i) sensitivity of ROMK1 channels. Mutation of PKC-induced phosphorylation sites (T193A) decreases the pH(i) sensitivity and increases the interaction of channel-PIP(2). |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
SRC | down-regulates
phosphorylation
|
KCNJ1 |
0.318 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97803 |
Tyr337 |
SKTKEGKyRVDFHNF |
Homo sapiens |
|
pmid |
sentence |
12556363 |
Inhibition of c-src with herbimycin a significantly decreased the tyrosine phosphorylation level of romk1... tyrosine dephosphorylation enhances the exocytosis of romk1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92513 |
Tyr337 |
SKTKEGKyRVDFHNF |
Homo sapiens |
|
pmid |
sentence |
12217858 |
Addition of active c-src and [32p]atp to the purified romk1 protein resulted in the phosphorylation of the romk1 protein. However, c-src did not phosphorylate r1y337a in which tyrosine residue 337 was mutated to alanine. Furthermore, phosphopeptide mapping identified two phosphopeptides from the trypsin-digested romk1 protein. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCD | up-regulates activity
|
KCNJ1 |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248943 |
|
|
Homo sapiens |
|
pmid |
sentence |
8621594 |
To determine whether this channel is a substrate for PKA, ROMK tagged with the hemagglutinin epitope was transiently transfected into HEK293 cells. In vitro labeling of immunoprecipitated proteins from transfected cells showed that ROMK could be phosphorylated by PKA. | Taken together, these results provide strong evidence that direct phosphorylation of the channel polypeptide by PKA is involved in channel regulation and PKA-dependent phosphorylation is essential for ROMK channel activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |