| + |
PRKG1 |
phosphorylation
|
CRIP2 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249038 |
Ser104 |
RAEERKAsGPPKGPS |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10681529 |
Cyclic GMP kinase I phosphorylated CRP2 at Ser-104, because the mutation to Ala completely prevented the in vivo phosphorylation. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKG1 |
phosphorylation
|
GKAP1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249037 |
Ser106 |
SNPVQKDsREENWQE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10671526 |
Although both cGK-Ialpha and -Ibeta, but not cAMP-dependent protein kinase, phosphorylated GKAP42 in vitro, GKAP42 was a good substrate only for cGK-Ialpha in intact cells, suggesting that the association with kinase protein is required for the phosphorylation in vivo. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKG1 | down-regulates activity 
phosphorylation
|
PLCB3 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249077 |
Ser1105 |
LDRKRHNsISEAKMR |
Rattus norvegicus |
Smooth Muscle Cell |
| pmid |
sentence |
| 11278298 |
PKG can directly phosphorylate PLC-beta2 and PLC-beta3 in vitro with purified proteins and in vivo with metabolic labeling. Phosphorylation of PLC-beta leads to the inhibition of G-protein-activated PLC-beta3 activity by 50-70% in COS-7 cell transfection assays. By using phosphopeptide mapping and site-directed mutagenesis, we further identified two key phosphorylation sites for the regulation of PLC-beta3 by PKG (Ser(26) and Ser(1105)). Mutation at these two sites (S26A and S1105A) of PLC-beta3 completely blocked the phosphorylation of PLC-beta3 protein catalyzed by PKG. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249079 |
Ser26 |
VETLRRGsKFIKWDE |
Rattus norvegicus |
Smooth Muscle Cell |
| pmid |
sentence |
| 11278298 |
PKG can directly phosphorylate PLC-beta2 and PLC-beta3 in vitro with purified proteins and in vivo with metabolic labeling. Phosphorylation of PLC-beta leads to the inhibition of G-protein-activated PLC-beta3 activity by 50-70% in COS-7 cell transfection assays. By using phosphopeptide mapping and site-directed mutagenesis, we further identified two key phosphorylation sites for the regulation of PLC-beta3 by PKG (Ser(26) and Ser(1105)). Mutation at these two sites (S26A and S1105A) of PLC-beta3 completely blocked the phosphorylation of PLC-beta3 protein catalyzed by PKG. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PRKG1 | up-regulates 
phosphorylation
|
FHOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170094 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
| pmid |
sentence |
| 21106951 |
Pkgi also directly phosphorylates fhod1, and studies with wild-type and mutant fhod1-derived peptides identify ser-1131 in the fhod1 c terminus as the unique pkgi phosphorylation site in fhod1. phosphorylation of three conserved residues within the dad domain activates fhod1 while binding to rac regulates fhod1 subcellular localization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123646 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
| pmid |
sentence |
| 15051728 |
Pkgi also directly phosphorylates fhod1, and studies with wild-type and mutant fhod1-derived peptides identify ser-1131 in the fhod1 c terminus as the unique pkgi phosphorylation site in fhod1. phosphorylation of three conserved residues within the dad domain activates fhod1 while binding to rac regulates fhod1 subcellular localization |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
PRKG1 |
phosphorylation
|
CREB1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249076 |
Ser133 |
EILSRRPsYRKILND |
in vitro |
|
| pmid |
sentence |
| 11175347 |
G-kinase phosphorylated GST-CREB, albeit less efficiently than A-kinase, but GST was not phosphorylated by either kinase (Figure 5a). GST-CREB purified from bacteria was similarly phosphorylated by G-kinase, whereas GST-CREB containing a serine 133 to alanine mutation was not (Figure 5b). These results demonstrate that G-kinase can directly phosphorylate CREB on serine 133. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKG1 | down-regulates
phosphorylation
|
LASP1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97946 |
Ser146 |
MEPERRDsQDGSSYR |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12571245 |
Studies with human lasp mutants identified serine 146 as a specific phosphorylation site for cgk and cak in vivo. Lasp is an actin-binding protein, and the phospho-lasp-mimicking mutant s146d showed reduced binding affinity for f-actin in cosedimentation experiments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates
phosphorylation
|
VASP |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120347 |
Ser157 |
EHIERRVsNAGGPPA |
Homo sapiens |
|
| pmid |
sentence |
| 14679200 |
Vasodilator-stimulated phosphoprotein activation of serum-response element-dependent transcription occurs downstream of rhoa and is inhibited by cgmp-dependent protein kinase phosphorylationg-kinase phosphorylation of vasp on ser(239) at the carboxyl-terminal end of the g-actin binding site, with some contribution by phosphorylation of ser(157) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120351 |
Ser239 |
GAKLRKVsKQEEASG |
Homo sapiens |
|
| pmid |
sentence |
| 14679200 |
Vasodilator-stimulated phosphoprotein activation of serum-response element-dependent transcription occurs downstream of rhoa and is inhibited by cgmp-dependent protein kinase phosphorylation. G-kinase phosphorylation of vasp on ser(239) at the carboxyl-terminal end of the g-actin binding site, with some contribution by phosphorylation of ser(157) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98139 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
|
| pmid |
sentence |
| 12576312 |
Vasodilator-stimulated phosphoprotein activation of serum-response element-dependent transcription occurs downstream of rhoa and is inhibited by cgmp-dependent protein kinase phosphorylation. Three phosphorylation sites have been identified in vasp: ser157, ser239, and thr278, all of which can be phosphorylated by either pka or pkg in vitro |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKG1 |
phosphorylation
|
ITPR1 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248916 |
Ser1764 |
RPSGRREsLTSFGNG |
Rattus norvegicus |
Vascular Smooth Muscle Cell |
| pmid |
sentence |
| 8132598 |
Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic GMP-dependent protein kinase. | The synthetic peptide corresponding to serine 1755 (GRRESLTSFG) was phosphorylated with aKm in the range of 30-40 microM by both kinases. The kinetic analysis revealed that this peptide substrate is the best substrate described for cGMP kinase to date. Vascular smooth muscle cells prelabeled with [32P]orthophosphate and treated with atrial natriuretic peptide or sodium nitroprusside to elevate cGMP also resulted in increased labeling of the IP3 receptor. Phosphorylation of IP3 receptor by cGMP kinase may regulate the function of IP3 receptor in vascular smooth muscle cells and contribute to the effect of cGMP to regulate intracellular calcium levels. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKG1 | up-regulates
phosphorylation
|
PTS |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71680 |
Ser19 |
AQVSRRIsFSASHRL |
Homo sapiens |
|
| pmid |
sentence |
| 10531334 |
Upon expression in cos-1 cells, ptps-s19a was stable but not phosphorylated and had a reduced activity of approximately 33% in comparison to wild-type ptps. Addition of cgmp stimulated phosphotransferase activity 2-fold. Extracts from transfected cos-1 cells overexpressing cgkii stimulated ser(19) phosphorylation more than 100-fold.In assays with purified enzymes, wild-type but not ptps-s19a was a specific substrate for the cgmp-dependent protein kinase (cgk) type i and ii. Upon expression in cos-1 cells, ptps-s19a was stable but not phosphorylated and had a reduced activity of approximately 33% in comparison to wild-type ptps |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
PRKG1 | down-regulates activity
phosphorylation
|
SF1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249018 |
Ser20 |
PSKKRKRsRWNQDTM |
Rattus norvegicus |
Neuronal Cell Line |
| pmid |
sentence |
| 10449420 |
PKG phosphorylates SF1 at Ser20, which inhibits the SF1-U2AF65 interaction leading to a block of pre-spliceosome assembly. Mutation of Ser20 to Ala or Thr also inhibits the interaction with U2AF65, indicating that Ser20 is essential for binding. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKG1 | up-regulates
phosphorylation
|
TNNI3 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134640 |
Ser23 |
PAPIRRRsSNYRAYA |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134644 |
Ser24 |
APIRRRSsNYRAYAT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKG1 | down-regulates
phosphorylation
|
TRPC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142953 |
Ser251 |
KNDYRKLsMQCKDFV |
Homo sapiens |
|
| pmid |
sentence |
| 16331690 |
There are two known phosphorylation-mediated inactivation mechanisms for trpc3 channels. Protein kinase g (pkg) inactivates trpc3 by direct phosphorylation on thr-11 and ser-263 of the trpc3 proteins, and protein kinase c (pkc) inactivates trpc3 by phosphorylation on ser-712. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122978 |
Ser251 |
KNDYRKLsMQCKDFV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14983059 |
There are two known phosphorylation-mediated inactivation mechanisms for trpc3 channels. Protein kinase g (pkg) inactivates trpc3 by direct phosphorylation on thr-11 and ser-263 of the trpc3 proteins, and protein kinase c (pkc) inactivates trpc3 by phosphorylation on ser-712. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142961 |
Ser263 |
KNDYRKLsMQCKDFV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16331690 |
The present study demonstrates that human trpc3 expressed in hek293 cells forms store-operated ca2+ influx channels, the activity of which is inhibited by pkg. The inhibition is due to a direct phosphorylation of pkg on trpc3 channels at position t11 and s263. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142964 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16331690 |
The present study demonstrates that human trpc3 expressed in hek293 cells forms store-operated ca2+ influx channels, the activity of which is inhibited by pkg. The inhibition is due to a direct phosphorylation of pkg on trpc3 channels at position t11 and s263. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PRKG1 |
phosphorylation
|
RYR1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248918 |
Ser2843 |
KKKTRKIsQSAQTYD |
in vitro |
|
| pmid |
sentence |
| 8380342 |
Automated Edman sequence analysis of the major phosphopeptide obtained from PK-A and PK-G phosphorylation and one phosphopeptide obtained from PK-CaM phosphorylation yielded the sequence KISQTAQTYDPR (residues 28412852) with serine 2843 as phosphorylation site |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKG1 | down-regulates
phosphorylation
|
HRH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124360 |
Ser398 |
WKRLRSHsRQYVSGL |
Homo sapiens |
|
| pmid |
sentence |
| 15107581 |
A specific pkg inhibitor inhibits h1r downregulation in cho cells (37). However, direct activation of pkg in these cells does not cause h1r down-regulation, indicating that more studies are required to clarify the role of pkg in h1r down-regulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66019 |
Ser398 |
WKRLRSHsRQYVSGL |
Homo sapiens |
|
| pmid |
sentence |
| 10101032 |
Ser396 and ser398 are also potential phosphorylation sites for capk, cgmp-dependent protein kinase, and camk ii. Elevation of intracellular camp content has been shown to attenuate histamine-induced accumulation of ip in c6 glioma cells (peakman and hill, 1994) and in ddt1 mf-2 smooth muscle cells (sipma et al., 1995 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
PRKG1 | up-regulates
phosphorylation
|
GTF2I |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89849 |
Ser412 |
GIPFRRPsTYGIPRL |
Homo sapiens |
|
| pmid |
sentence |
| 12082086 |
G-kinase phosphorylated tfii-i in vitro and in vivo on ser(371) and ser(743) outside of the interaction domain. G-kinase strongly enhanced tfii-i transactivation of a serum-response element-containing promoter in cos7 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89853 |
Ser784 |
GVPFRRPsTFGIPRL |
Homo sapiens |
|
| pmid |
sentence |
| 12082086 |
G-kinase phosphorylated tfii-i in vitro and in vivo on ser(371) and ser(743) outside of the interaction domain. G-kinase strongly enhanced tfii-i transactivation of a serum-response element-containing promoter in cos7 cells |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PRKG1 | up-regulates activity
phosphorylation
|
RGS2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249240 |
Ser46 |
KDWKTRLsYFLQNSS |
in vitro |
|
| pmid |
sentence |
| 14608379 |
Thus, PKGI-alpha binds to, phosphorylates and activates RGS-2, attenuating receptor-mediated vascular contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249241 |
Ser64 |
KPKTGKKsKQQAFIK |
in vitro |
|
| pmid |
sentence |
| 14608379 |
Thus, PKGI-alpha binds to, phosphorylates and activates RGS-2, attenuating receptor-mediated vascular contraction. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKG1 | up-regulates
phosphorylation
|
PRKG1 |
0.22 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89839 |
Ser65 |
TTRAQGIsAEPQTYR |
Homo sapiens |
|
| pmid |
sentence |
| 12080049 |
Serines 64 and 79 are homologous residues that are juxtaposed to the autoinhibitory pseudosubstrate site in cgmp-dependent protein kinase type ialpha and type ibeta (pkg-ialpha and pkg-ibeta), respectively. Autophosphorylation of this residue is associated with activation of type i pkgs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | up-regulates
phosphorylation
|
CFTR |
0.2 |
| 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-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-72716 |
Ser737 |
EPLERRLsLVPDSEQ |
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-18241 |
Ser737 |
EPLERRLsLVPDSEQ |
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-72720 |
Ser768 |
LQARRRQsVLNLMTH |
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-18245 |
Ser768 |
LQARRRQsVLNLMTH |
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-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-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-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 |
|
| 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 |
|
| Publications: |
10 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | up-regulates activity
phosphorylation
|
CFTR |
0.2 |
| 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 |
| + |
PRKG1 | down-regulates
phosphorylation
|
HSPB1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186784 |
Ser78 |
PAYSRALsRQLSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186788 |
Ser82 |
RALSRQLsSGVSEIR |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186792 |
Thr143 |
RCFTRKYtLPPGVDP |
Homo sapiens |
|
| pmid |
sentence |
| 19593530 |
Purified pkg isoforms ia, ib, and ii all caused incorporation of phosphate in recombinant hsp27 at ser-78, ser-82, and thr-143, but not ser-15.These Studies indicate that hsp27 is a genuine substrate for pkg and that pkg may mediate inhibition of platelet aggregation through phosphorylation of hsp27 and subsequent prevent of actin polymerization |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates
phosphorylation
|
TRPC3 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142957 |
Thr11 |
SPSLRRMtVMREKGR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16331690 |
The present study demonstrates that human trpc3 expressed in hek293 cells forms store-operated ca2+ influx channels, the activity of which is inhibited by pkg. The inhibition is due to a direct phosphorylation of pkg on trpc3 channels at position t11 and s263. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates
phosphorylation
|
SRF |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188185 |
Thr159 |
DNKLRRYtTFSKRKT |
Homo sapiens |
|
| pmid |
sentence |
| 19778940 |
This residue conforms to a highly conserved consensus camp-dependent protein kinase (pka) site, and in vitro and in vivo labeling studies demonstrated that it was phosphorylated by pka. Results from gel shift and chromatin immunoprecipitation assays demonstrated that t159 phosphorylation inhibited srf binding to smc-specific carg elements. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
PRKG1 | up-regulates
phosphorylation
|
SLC6A4 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158186 |
Thr276 |
SIWKGVKtSGKVVWV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17913921 |
These results are consistent with the hypothesis that pkg phosphorylates hsert at thr-276 and increases its activity by modifying the substrate permeation pathway formed, in part, by tm5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | up-regulates
phosphorylation
|
PRKG1 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98803 |
Thr59 |
THIGPRTtRAQGISA |
Homo sapiens |
|
| pmid |
sentence |
| 12609995 |
Antibodies generated against phosphorylated threonine 58 were used to demonstrate phosphorylation in response to pma treatment of the cells with kinetics similar to vasodilator-stimulated phosphoprotein phosphorylation. A phospho-mimetic mutation at this site (t58e) generated a partially activated pkg that was more sensitive to cgmp levels. A phospho- mutation (t58a) revealed that this residue is important but not sufficient for pkg activation by pkc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
PRKG1
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