Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Mus musculus | |
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Homo sapiens | |
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Rattus norvegicus | |
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Sus scrofa | |
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Bos taurus | |
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Oryctolagus cuniculus | |
cGMP | PKG-I is activated by the NO/sGC/cGMP system | Ovis aries |
Cloned (Comment) | Organism |
---|---|
human PKG-Ialpha and PKG-Ibeta are generated by alternative splicing of a single gene, dissection of the human PKG-I proximal core promoter reveal the presence of regulatory regions involved in basal PKG-I transcription. Regulatory domain I corresponds to high-affinity Sp1 transcription factor recognition sites and binds Sp1 and Sp3, but not Sp2, the regulatory domain II binds USF1/2 and other transcription factors | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? | |
additional information | Homo sapiens | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? | |
additional information | Rattus norvegicus | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? | |
additional information | Sus scrofa | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? | |
additional information | Bos taurus | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? | |
additional information | Oryctolagus cuniculus | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? | |
additional information | Ovis aries | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
isozymes PKG-Ialpha and PKG-Ibeta | - |
Homo sapiens | - |
isozymes PKG-Ialpha and PKG-Ibeta | - |
Mus musculus | - |
isozymes PKG-Ialpha and PKG-Ibeta | - |
Oryctolagus cuniculus | - |
isozymes PKG-Ialpha and PKG-Ibeta | - |
Ovis aries | - |
PKG-Ialpha and PKG-Ibeta | - |
Rattus norvegicus | - |
isozymes PKG-Ialpha and PKG-Ibeta | - |
Sus scrofa | - |
isozymes PKG-Ialpha and PKG-Ibeta | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Mus musculus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Homo sapiens |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Rattus norvegicus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Sus scrofa |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Bos taurus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Oryctolagus cuniculus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Ovis aries |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Mus musculus |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Homo sapiens |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Rattus norvegicus |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Sus scrofa |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Bos taurus |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Oryctolagus cuniculus |
phosphoprotein | PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded | Ovis aries |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
aorta | - |
Homo sapiens | - |
aorta | - |
Bos taurus | - |
aorta | - |
Ovis aries | - |
aorta | aortic homogenate, neointima | Mus musculus | - |
aorta | aortic homogenate, neointima | Rattus norvegicus | - |
blood platelet | platelets express very high levels of PKG-Ibeta isoform, not PKG-Ialpha | Homo sapiens | - |
cardiomyocyte | - |
Rattus norvegicus | - |
cardiomyocyte | PKG-Ialpha | Homo sapiens | - |
carotid artery | - |
Mus musculus | - |
carotid artery | - |
Rattus norvegicus | - |
carotid artery | - |
Oryctolagus cuniculus | - |
coronary artery | - |
Sus scrofa | - |
Corpus cavernosum smooth muscle | - |
Rattus norvegicus | - |
endothelial cell | PKG-Ibeta | Homo sapiens | - |
fetus | - |
Ovis aries | - |
kidney | - |
Ovis aries | - |
lung | - |
Sus scrofa | - |
additional information | PKG-I expression is reduced or even lost in many primary cultured and passaged cells, e.g. vascular smooth muscle cells and endothelial cells | Homo sapiens | - |
additional information | PKG-I expression is reduced or even lost in many primary cultured and passaged cells, e.g. vascular smooth muscle cells and endothelial cells | Rattus norvegicus | - |
pulmonary artery | - |
Sus scrofa | - |
pulmonary artery | - |
Ovis aries | - |
pulmonary vein | of fetus | Ovis aries | - |
urinary bladder | - |
Oryctolagus cuniculus | - |
vascular smooth muscle cell | both PKG-Ialpha and PKG-Ibeta | Mus musculus | - |
vascular smooth muscle cell | both PKG-Ialpha and PKG-Ibeta | Homo sapiens | - |
vascular smooth muscle cell | both PKG-Ialpha and PKG-Ibeta | Sus scrofa | - |
vascular smooth muscle cell | both PKG-Ialpha and PKG-Ibeta | Bos taurus | - |
vascular smooth muscle cell | from normal/hypertensive fetal lambs | Ovis aries | - |
vascular smooth muscle cell | from old and young rat aorta | Rattus norvegicus | - |
vascular smooth muscle cell | neointimal | Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Mus musculus | ? | - |
? | |
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Homo sapiens | ? | - |
? | |
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Rattus norvegicus | ? | - |
? | |
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Sus scrofa | ? | - |
? | |
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Bos taurus | ? | - |
? | |
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Oryctolagus cuniculus | ? | - |
? | |
additional information | PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins | Ovis aries | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PKG-I | - |
Mus musculus |
PKG-I | - |
Homo sapiens |
PKG-I | - |
Rattus norvegicus |
PKG-I | - |
Sus scrofa |
PKG-I | - |
Bos taurus |
PKG-I | - |
Oryctolagus cuniculus |
PKG-I | - |
Ovis aries |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mus musculus | |
ATP | - |
Homo sapiens | |
ATP | - |
Rattus norvegicus | |
ATP | - |
Sus scrofa | |
ATP | - |
Bos taurus | |
ATP | - |
Oryctolagus cuniculus | |
ATP | - |
Ovis aries |
Organism | Comment | Expression |
---|---|---|
Mus musculus | down-regulation of PKG-Ialpha protein occurs after chronic activation in murine aortic smooth muscle cells by the cGMP analogue in normoxic conditions | down |
Homo sapiens | PKG-I expression is suppressed by mitogenes, e.g. platelet-derived growth factor-BB, angiotenssin II, TGF-beta and TNF-alpha. RhoA and Rac1 have opposing effects on PKG-I expression, with RhoA suppressing and Rac1 activating its promoter. RhoA regulation of the PKG-Iapha promoter is mediated, at least in part, through binding of KLF4 to Sp1 consensus sites in the proximal promoter, which is located within the two Sp1 sites, overview | down |
Homo sapiens | overexpression of USF1/2 increased PKG-I promoter activity RhoA and Rac1 have opposing effects on PKG-I expression, with RhoA suppressing and Rac1 activating its promoter | up |
General Information | Comment | Organism |
---|---|---|
malfunction | accumulation of poly-ubiquitinated PKG-I induced by hypoxia is not affected by the endogenous activation of PKG-I by a cGMP analogue, or by the endogenous inhibition of PKG-I activity via a cell-permeable inhibitor | Homo sapiens |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Mus musculus |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Homo sapiens |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Rattus norvegicus |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Sus scrofa |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Bos taurus |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Oryctolagus cuniculus |
metabolism | molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview | Ovis aries |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Mus musculus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Homo sapiens |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Rattus norvegicus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Sus scrofa |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Bos taurus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Oryctolagus cuniculus |
additional information | the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform | Ovis aries |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction | Mus musculus |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction | Rattus norvegicus |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction | Sus scrofa |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction | Bos taurus |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction | Oryctolagus cuniculus |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction | Ovis aries |
physiological function | PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction. PKG-I expression is controlled by RhoA and Rac1 activities. RhoA and Rac1 have opposing effects on PKG-I expression, with RhoA suppressing and Rac1 activating its promoter. RhoA regulation of the PKG-Ialpha promoter is mediated, at least in part, through binding of KLF4 to Sp1 consensus sites in the proximal promoter, which is located within the two Sp1 sites | Homo sapiens |