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Literature summary extracted from

  • Sellak, H.; Choi, C.S.; Dey, N.B.; Lincoln, T.M.
    Transcriptional and post-transcriptional regulation of cGMP-dependent protein kinase (PKG-I): pathophysiological significance (2013), Cardiovasc. Res., 97, 200-207.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Mus musculus
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Homo sapiens
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Rattus norvegicus
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Sus scrofa
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Bos taurus
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Oryctolagus cuniculus
2.7.11.12 cGMP PKG-I is activated by the NO/sGC/cGMP system Ovis aries

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.12 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.12 additional information Mus musculus PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?
2.7.11.12 additional information Homo sapiens PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?
2.7.11.12 additional information Rattus norvegicus PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?
2.7.11.12 additional information Sus scrofa PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?
2.7.11.12 additional information Bos taurus PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?
2.7.11.12 additional information Oryctolagus cuniculus PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?
2.7.11.12 additional information Ovis aries PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.12 Bos taurus
-
isozymes PKG-Ialpha and PKG-Ibeta
-
2.7.11.12 Homo sapiens
-
isozymes PKG-Ialpha and PKG-Ibeta
-
2.7.11.12 Mus musculus
-
isozymes PKG-Ialpha and PKG-Ibeta
-
2.7.11.12 Oryctolagus cuniculus
-
isozymes PKG-Ialpha and PKG-Ibeta
-
2.7.11.12 Ovis aries
-
PKG-Ialpha and PKG-Ibeta
-
2.7.11.12 Rattus norvegicus
-
isozymes PKG-Ialpha and PKG-Ibeta
-
2.7.11.12 Sus scrofa
-
isozymes PKG-Ialpha and PKG-Ibeta
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Mus musculus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Homo sapiens
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Rattus norvegicus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Sus scrofa
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Bos taurus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Oryctolagus cuniculus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Ovis aries
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Mus musculus
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Homo sapiens
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Rattus norvegicus
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Sus scrofa
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Bos taurus
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Oryctolagus cuniculus
2.7.11.12 phosphoprotein PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded Ovis aries

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.12 aorta
-
Homo sapiens
-
2.7.11.12 aorta
-
Bos taurus
-
2.7.11.12 aorta
-
Ovis aries
-
2.7.11.12 aorta aortic homogenate, neointima Mus musculus
-
2.7.11.12 aorta aortic homogenate, neointima Rattus norvegicus
-
2.7.11.12 blood platelet platelets express very high levels of PKG-Ibeta isoform, not PKG-Ialpha Homo sapiens
-
2.7.11.12 cardiomyocyte
-
Rattus norvegicus
-
2.7.11.12 cardiomyocyte PKG-Ialpha Homo sapiens
-
2.7.11.12 carotid artery
-
Mus musculus
-
2.7.11.12 carotid artery
-
Rattus norvegicus
-
2.7.11.12 carotid artery
-
Oryctolagus cuniculus
-
2.7.11.12 coronary artery
-
Sus scrofa
-
2.7.11.12 Corpus cavernosum smooth muscle
-
Rattus norvegicus
-
2.7.11.12 endothelial cell PKG-Ibeta Homo sapiens
-
2.7.11.12 fetus
-
Ovis aries
-
2.7.11.12 kidney
-
Ovis aries
-
2.7.11.12 lung
-
Sus scrofa
-
2.7.11.12 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
-
2.7.11.12 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
-
2.7.11.12 pulmonary artery
-
Sus scrofa
-
2.7.11.12 pulmonary artery
-
Ovis aries
-
2.7.11.12 pulmonary vein of fetus Ovis aries
-
2.7.11.12 urinary bladder
-
Oryctolagus cuniculus
-
2.7.11.12 vascular smooth muscle cell both PKG-Ialpha and PKG-Ibeta Mus musculus
-
2.7.11.12 vascular smooth muscle cell both PKG-Ialpha and PKG-Ibeta Homo sapiens
-
2.7.11.12 vascular smooth muscle cell both PKG-Ialpha and PKG-Ibeta Sus scrofa
-
2.7.11.12 vascular smooth muscle cell both PKG-Ialpha and PKG-Ibeta Bos taurus
-
2.7.11.12 vascular smooth muscle cell from normal/hypertensive fetal lambs Ovis aries
-
2.7.11.12 vascular smooth muscle cell from old and young rat aorta Rattus norvegicus
-
2.7.11.12 vascular smooth muscle cell neointimal Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Mus musculus ?
-
?
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Homo sapiens ?
-
?
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Rattus norvegicus ?
-
?
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Sus scrofa ?
-
?
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Bos taurus ?
-
?
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Oryctolagus cuniculus ?
-
?
2.7.11.12 additional information PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins Ovis aries ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.12 PKG-I
-
Mus musculus
2.7.11.12 PKG-I
-
Homo sapiens
2.7.11.12 PKG-I
-
Rattus norvegicus
2.7.11.12 PKG-I
-
Sus scrofa
2.7.11.12 PKG-I
-
Bos taurus
2.7.11.12 PKG-I
-
Oryctolagus cuniculus
2.7.11.12 PKG-I
-
Ovis aries

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.12 ATP
-
Mus musculus
2.7.11.12 ATP
-
Homo sapiens
2.7.11.12 ATP
-
Rattus norvegicus
2.7.11.12 ATP
-
Sus scrofa
2.7.11.12 ATP
-
Bos taurus
2.7.11.12 ATP
-
Oryctolagus cuniculus
2.7.11.12 ATP
-
Ovis aries

Expression

EC Number Organism Comment Expression
2.7.11.12 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
2.7.11.12 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
2.7.11.12 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

EC Number General Information Comment Organism
2.7.11.12 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
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Mus musculus
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Homo sapiens
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Rattus norvegicus
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Sus scrofa
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Bos taurus
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Oryctolagus cuniculus
2.7.11.12 metabolism molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview Ovis aries
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Mus musculus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Homo sapiens
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Rattus norvegicus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Sus scrofa
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Bos taurus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Oryctolagus cuniculus
2.7.11.12 additional information the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform Ovis aries
2.7.11.12 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
2.7.11.12 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
2.7.11.12 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
2.7.11.12 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
2.7.11.12 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
2.7.11.12 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
2.7.11.12 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