| + |
PRKG2 | down-regulates activity 
phosphorylation
|
PLCB3 |
0.508 |
| 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 |
0.348 |
| 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 |
0.508 |
| 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 |
0.276 |
| 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 | 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
- 
- 