| + |
PRKG2 | down-regulates activity 
phosphorylation
|
PLCB3 |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249078 |
Ser1105 |
LDRKRHNsISEAKMR |
Rattus norvegicus |
|
| 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-249080 |
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 |
| + |
PRKG2 |
phosphorylation
|
LASP1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249197 |
Ser146 |
MEPERRDsQDGSSYR |
Homo sapiens |
|
| pmid |
sentence |
| 12571245 |
Recombinant human LASP was phosphorylated by cGMP- and cAMP-dependent protein kinase (cAK) in vitro. Cotransfection of PtK-2 cells with LASP and cGK confirmed phosphorylation of LASP in vivo. 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 |
| + |
PRKG2 | up-regulates 
phosphorylation
|
PTS |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71751 |
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 |
| + |
PRKG2 | down-regulates activity
phosphorylation
|
PDGFRB |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277577 |
Ser254 |
WTYPRKEsGRLVEPV |
Homo sapiens |
AGS Cell |
| pmid |
sentence |
| 35066967 |
Secretory PKG II inhibited PDGF‐BB ‐induced PDGFRβ activation via phosphorylating its Ser254. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277401 |
Ser712 |
SDKRRPPsAELYSNA |
Homo sapiens |
Gastric Cancer Cell |
| pmid |
sentence |
| 29935031 |
PKG II inhibited PDGFRβ activation in gastric cancer via phosphorylating Ser712 of this RTK. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKG2 | down-regulates activity
phosphorylation
|
CTH |
0.246 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275800 |
Ser377 |
SDTLIRLsVGLEDEE |
|
|
| pmid |
sentence |
| 25900831 |
CO stimulated protein kinase G (PKG)-dependent phosphorylation of Ser(377) of CSE, inhibiting the production of H2S. |
|
| Publications: |
1 |
| + |
PRKG2 | up-regulates activity
phosphorylation
|
PTPN6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276288 |
Ser553 |
KNAHAKAsRTSSKHK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21177494 |
PKGII directly phosphorylated and stimulated SHP-1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276286 |
Ser556 |
HAKASRTsSKHKEDV |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21177494 |
PKGII directly phosphorylated and stimulated SHP-1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276287 |
Ser557 |
AKASRTSsKHKEDVY |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21177494 |
PKGII directly phosphorylated and stimulated SHP-1 activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKG2 | down-regulates activity
phosphorylation
|
HCN2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263185 |
Ser668 |
DRIGKKNsILLHKVQ |
Mus musculus |
Brain |
| pmid |
sentence |
| 21347269 |
Here, we show for the first time that in the HCN2 channel cGMP can also exert an inhibitory effect on gating via cGMP-dependent protein kinase II (cGKII)-mediated phosphorylation.We identify the proximal C-terminus of HCN2 as binding region of cGKII and show that cGKII phosphorylates HCN2 at a specific serine residue (S641) in the C-terminal end of the CNBD. The cGKII shifts the voltage-dependence of HCN2 activation to 2-5 mV more negative voltages and, hence, counteracts the stimulatory effect of cGMP on gating. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKG2 | down-regulates
phosphorylation
|
HSPB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186796 |
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-186943 |
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-186947 |
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 |
| + |
PRKG2 | up-regulates activity
phosphorylation
|
GRIA1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278427 |
Ser863 |
TSTLPRNsGAGASSG |
Homo sapiens |
|
| pmid |
sentence |
| 18728399 |
In cultured hippocampal neurons, activation of cGKII induces an accumulation of GluR1 on the cellular plasma membrane at extrasynaptic sites, and blockage of cGKII activity prevents the surface increase of GluR1, and also the increase in mEPSC frequency and amplitude, that follows a chemical form of LTP (chemLTP).|In this complex, cGKII phosphorylates GluR1 at serine 845 (S845), a site known to be phosphorylated also by PKA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG2 | down-regulates activity
phosphorylation
|
EGFR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277589 |
Thr430 |
LEIIRGRtKQHGQFS |
in vitro |
|
| pmid |
sentence |
| 35226996 |
Recombinant PKG II inhibited the epidermal growth factor (EGF)-induced activation of the EGF receptor via phosphorylating the T406 of the extracellular domain and blocked EGF-triggered proliferation of various cancer cells. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PRKG2
- 
- 