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Literature summary for 2.7.11.12 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

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(Commentary)

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/ Products (Substrates)

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

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

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

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 and Products (Substrate)

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

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

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

Expression

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

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