Literature summary for 7.2.2.13 extracted from

Despa, S.; Bers, D.M.
Functional analysis of Na+/K+-ATPase isoform distribution in rat ventricular myocytes (2007), Am. J. Physiol. Cell Physiol., 293, C321-C327.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
sarcolemma	the functional density of the enzyme is significantly higher in t-tubules compared to external sarcolemma. Subunit isoform alpha2 is enriched in t-tubules, while isoform alpha1 is almost uniformly distributed between the t-tubules and external sarcolemma	Rattus norvegicus	42383	-
T-tubule	the functional density of the enzyme is significantly higher in t-tubules compared to external sarcolemma. Subunit isoform alpha2 is enriched in t-tubules, while isoform alpha1 is almost uniformly distributed between the t-tubules and external sarcolemma	Rattus norvegicus	30315	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
myocyte	ventricular myocyte. Subunit isoform alpha 2 accounts for 29.5% of the cation current, and the low-affinity subunit isoform alpha 1 accounts for 70.5% of current. The functional density of the enzyme is significantly higher in t-tubules compared to external sarcolemma. Subunit isoform alpha2 is enriched in t-tubules, while isoform alpha1 is almost uniformly distributed between the t-tubules and external sarcolemma	Rattus norvegicus	-

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Release 2023.1 (January 2023)