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Aliases ATP1B3, ATPB-3, CD298, ATPase Na+/K+ transporting subunit beta 3
External IDs MGI: 107788 HomoloGene: 37510 GeneCards: ATP1B3
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 3: 141.88 – 141.93 Mb Chr 9: 96.33 – 96.36 Mb
PubMed search [1] [2]
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Sodium/potassium-transporting ATPase subunit beta-3 is an enzyme that in humans is encoded by the ATP1B3 gene.[3][4][5] ATP1B3 has also been designated as CD298 (cluster of differentiation 298).

The protein encoded by this gene belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes a beta 3 subunit. A pseudogene exists for this gene, and it is located on chromosome 2.[5]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Malik N, Canfield VA, Beckers MC, Gros P, Levenson R (Nov 1996). "Identification of the mammalian Na,K-ATPase 3 subunit". J Biol Chem. 271 (37): 22754–8. doi:10.1074/jbc.271.37.22754. PMID 8798450. 
  4. ^ Malik N, Canfield V, Sanchez-Watts G, Watts AG, Scherer S, Beatty BG, Gros P, Levenson R (Mar 1998). "Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene". Mamm Genome. 9 (2): 136–43. doi:10.1007/s003359900704. PMID 9457675. 
  5. ^ a b "Entrez Gene: ATP1B3 ATPase, Na+/K+ transporting, beta 3 polypeptide". 

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.