XB-FEAT-1012187 - Revision history

imported>Xenbase: /* nomenclature changes */

2019-08-28T15:56:30Z

nomenclature changes

← Older revision		Revision as of 15:56, 28 August 2019
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	This is the community wiki page for the gene ''kcnj2'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase		This is the community wiki page for the gene ''kcnj2'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase
	=nomenclature changes=		=nomenclature changes=
	01/15/2015 Human name has changed for Entrez Gene: 3759. From potassium inwardly-rectifying channel, subfamily J, member 2 to potassium channel, inwardly rectifying subfamily J, member 2		01/15/2015 Human name has changed for Entrez Gene: 3759. From potassium inwardly-rectifying channel, subfamily J, member 2 to potassium channel, inwardly rectifying subfamily J, member 2.

			08.23.2019
			Human name has changed for Entrez Gene: 3759. From potassium voltage-gated channel subfamily J member 2 to potassium inwardly rectifying channel subfamily J member 2

	=summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 =		=summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 =

imported>Xenbase: /* summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 */

2018-02-01T17:40:34Z

summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270

← Older revision		Revision as of 17:40, 1 February 2018
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	It is a 427 amino acid, two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers form a K+ channel that contributes to the potassium efﬂux that is critical for the repolarization of excitable cell membranes after an action potential, the so-called IK current. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242.		It is a 427 amino acid, two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers form a K+ channel that contributes to the potassium efﬂux that is critical for the repolarization of excitable cell membranes after an action potential, the so-called IK current. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242.

	It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); three PIP2 binding sites have been identiﬁed in the long C terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes;it is the effect of mutations on the QT interval and the U-wave that are thought to cause the cardiac arrhythmia.		It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); three PIP2 binding sites have been identiﬁed in the long C terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes; it is the effect of mutations on the QT interval and the U-wave that are thought to cause the cardiac arrhythmia.

	This symptom is the source of the synonym LQT for long Q-T interval (Hedley et al. 2009). Importantly, however,Kir2.1 also contributes to the resting potential (Vmem)~~o f~~ undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions ~~goway~~ beyond propagation of action potentials (Jongsma &Wilders, 2001).		This symptom is the source of the synonym LQT for long Q-T interval (Hedley et al. 2009). Importantly, however, Kir2.1 also contributes to the resting potential (Vmem) of undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions go way beyond propagation of action potentials (Jongsma &Wilders, 2001).

imported>Xenbase: /* summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 */

2018-02-01T17:39:40Z

summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270

← Older revision		Revision as of 17:39, 1 February 2018
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	Kir2.1 (NP000882.1), encoded in KCNJ2(NM000891.2), is the potassium, inwardly rectifying channel, subfamily J member 2a.		Kir2.1 (NP000882.1), encoded in KCNJ2(NM000891.2), is the potassium, inwardly rectifying channel, subfamily J member 2a.

	It is a 427 amino acid, two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers form a K+ channel that contributes to the potassium efﬂux that is critical for the repolarization of excitable cell membranes after an action potential, the so-called IK current. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242.		It is a 427 amino acid, two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers form a K+ channel that contributes to the potassium efﬂux that is critical for the repolarization of excitable cell membranes after an action potential, the so-called IK current. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242.

	It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); three PIP2 binding sites have been identiﬁed in the long C terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes;it is the effect of mutations on the QT interval and the U-wave that are thought to cause the cardiac arrhythmia.		It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); three PIP2 binding sites have been identiﬁed in the long C terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes;it is the effect of mutations on the QT interval and the U-wave that are thought to cause the cardiac arrhythmia.

	This symptom is the source of the synonym LQT for long Q-T interval (Hedley et al. 2009). Importantly, however,Kir2.1 also contributes to the resting potential (Vmem)o f undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions goway beyond propagation of action potentials (Jongsma &Wilders, 2001).		This symptom is the source of the synonym LQT for long Q-T interval (Hedley et al. 2009). Importantly, however,Kir2.1 also contributes to the resting potential (Vmem)o f undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions goway beyond propagation of action potentials (Jongsma &Wilders, 2001).

imported>Xenbase: /* summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 */

2018-02-01T17:39:19Z

summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270

← Older revision		Revision as of 17:39, 1 February 2018
Line 6:		Line 6:
	=summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 =		=summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 =

	Kir2.1 (NP000882.1), encoded in KCNJ2(NM000891.2), is the potassium, inwardly rectifying channel, subfamily J member 2a. It is a 427 amino acid,two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers ~~formaK~~+channel that contributes to the potassium ~~efﬂuxthat~~ is critical for the repolarization of excitable cell membranes after an action potential, the so-~~calledIKcurrent~~. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242. It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); ~~threePIP2binding~~ sites have ~~b een~~ identiﬁed in the ~~longC~~ terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes;it is the effect of mutations on the QT interval and ~~theU~~-wave that are thought to cause the cardiac arrhythmia.This symptom is the source of the synonym LQT for ~~longQ~~-T interval (Hedley et al. 2009). Importantly, however,Kir2.1 also contributes to the resting potential (Vmem)o f undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions goway beyond propagation of action potentials (Jongsma &Wilders, 2001).		Kir2.1 (NP000882.1), encoded in KCNJ2(NM000891.2), is the potassium, inwardly rectifying channel, subfamily J member 2a.

			It is a 427 amino acid, two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers form a K+ channel that contributes to the potassium efﬂux that is critical for the repolarization of excitable cell membranes after an action potential, the so-called IK current. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242.

			It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); three PIP2 binding sites have been identiﬁed in the long C terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes;it is the effect of mutations on the QT interval and the U-wave that are thought to cause the cardiac arrhythmia.

			This symptom is the source of the synonym LQT for long Q-T interval (Hedley et al. 2009). Importantly, however,Kir2.1 also contributes to the resting potential (Vmem)o f undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions goway beyond propagation of action potentials (Jongsma &Wilders, 2001).

imported>Xenbase: /* nomenclature changes */

2018-02-01T17:37:19Z

nomenclature changes

← Older revision		Revision as of 17:37, 1 February 2018
Line 3:		Line 3:
	=nomenclature changes=		=nomenclature changes=
	01/15/2015 Human name has changed for Entrez Gene: 3759. From potassium inwardly-rectifying channel, subfamily J, member 2 to potassium channel, inwardly rectifying subfamily J, member 2		01/15/2015 Human name has changed for Entrez Gene: 3759. From potassium inwardly-rectifying channel, subfamily J, member 2 to potassium channel, inwardly rectifying subfamily J, member 2

			=summary from Adams et al 2016. J Physiol 594.12 (2016) pp 3245–3270 =

			Kir2.1 (NP000882.1), encoded in KCNJ2(NM000891.2), is the potassium, inwardly rectifying channel, subfamily J member 2a. It is a 427 amino acid,two-pass, transmembrane protein, with both termini located in the cytoplasm. Kir2.1 homotetramers formaK+channel that contributes to the potassium efﬂuxthat is critical for the repolarization of excitable cell membranes after an action potential, the so-calledIKcurrent. Kir2.1 is negatively regulated (at membrane potentials positive to its equilibrium potential) by binding of spermine, spermidine and Mg2+(Yang et al. 1995), and by phosphorylation of Tyr242. It is positively regulated(at potentials negative to its equilibrium potential) by binding of phosphoinositol bisphosphate (PIP2); threePIP2binding sites have b een identiﬁed in the longC terminus of the protein, at amino acids 175–206,207–246 and 324–365 (Soom et al. 2001). Kir2.1 is critical for controlling the membrane voltage of cardiac myocytes;it is the effect of mutations on the QT interval and theU-wave that are thought to cause the cardiac arrhythmia.This symptom is the source of the synonym LQT for longQ-T interval (Hedley et al. 2009). Importantly, however,Kir2.1 also contributes to the resting potential (Vmem)o f undifferentiated embryonic cells, including those found in Xenopus embryos. Its effect on cellular functions goway beyond propagation of action potentials (Jongsma &Wilders, 2001).

imported>Christina: /* kcnj2 */

2015-01-21T16:01:33Z

kcnj2

← Older revision		Revision as of 16:01, 21 January 2015
Line 1:		Line 1:
	=kcnj2=		=kcnj2=
	This is the community wiki page for the gene ''kcnj2'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase		This is the community wiki page for the gene ''kcnj2'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase
			=nomenclature changes=
			01/15/2015 Human name has changed for Entrez Gene: 3759. From potassium inwardly-rectifying channel, subfamily J, member 2 to potassium channel, inwardly rectifying subfamily J, member 2

imported>Xenbase gene generator at 12:00, 10 February 2010

2010-02-10T12:00:00Z

New page

=kcnj2=
This is the community wiki page for the gene ''kcnj2'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase