ATP1B1

Protein-coding gene in the species Homo sapiens
ATP1B1
Identifiers
AliasesATP1B1, ATP1B, ATPase Na+/K+ transporting subunit beta 1
External IDsOMIM: 182330; MGI: 88108; HomoloGene: 37509; GeneCards: ATP1B1; OMA:ATP1B1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ATP1B1
Genomic location for ATP1B1
Band1q24.2Start169,105,697 bp[1]
End169,310,992 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for ATP1B1
Genomic location for ATP1B1
Band1 H2.2|1 71.75 cMStart164,264,678 bp[2]
End164,285,924 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Pars compacta

  • lateral nuclear group of thalamus

  • renal medulla

  • pars reticulata

  • pons

  • Epithelium of choroid plexus

  • superior vestibular nucleus

  • external globus pallidus

  • Brodmann area 23

  • postcentral gyrus
Top expressed in
  • olfactory tubercle

  • medial vestibular nucleus

  • lateral septal nucleus

  • left colon

  • amygdala

  • nucleus accumbens

  • subiculum

  • medial dorsal nucleus

  • cerebellar vermis

  • prefrontal cortex
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • ATPase binding
  • potassium ion binding
  • sodium ion binding
  • P-type sodium:potassium-exchanging transporter activity
  • ATPase activity
  • protein C-terminus binding
  • protein binding
  • MHC class II protein complex binding
  • ATPase activator activity
  • ATP binding
  • protein kinase binding
Cellular component
  • extracellular vesicle
  • integral component of membrane
  • membrane
  • intercalated disc
  • myelin sheath
  • plasma membrane
  • intracellular anatomical structure
  • sodium:potassium-exchanging ATPase complex
  • basolateral plasma membrane
  • apical plasma membrane
  • caveola
  • sarcolemma
  • extracellular exosome
Biological process
  • regulation of cardiac conduction
  • regulation of cardiac muscle contraction by calcium ion signaling
  • response to hypoxia
  • positive regulation of ATP-dependent activity
  • cardiac muscle contraction
  • positive regulation of sodium ion export across plasma membrane
  • sodium ion transport
  • cellular sodium ion homeostasis
  • sodium ion export across plasma membrane
  • metal ion transport
  • cell communication by electrical coupling involved in cardiac conduction
  • protein stabilization
  • positive regulation of potassium ion import across plasma membrane
  • cellular calcium ion homeostasis
  • ion transport
  • cellular potassium ion homeostasis
  • potassium ion transport
  • membrane repolarization
  • ion transmembrane transport
  • ATP metabolic process
  • cell adhesion
  • regulation of gene expression
  • positive regulation of calcium:sodium antiporter activity
  • protein localization to plasma membrane
  • membrane repolarization during cardiac muscle cell action potential
  • relaxation of cardiac muscle
  • regulation of calcium ion transmembrane transport
  • leukocyte migration
  • positive regulation of potassium ion transmembrane transporter activity
  • protein transport into plasma membrane raft
  • potassium ion import across plasma membrane
  • establishment or maintenance of transmembrane electrochemical gradient
  • transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

481

11931

Ensembl

ENSG00000143153

ENSMUSG00000026576

UniProt

P05026

P14094

RefSeq (mRNA)

NM_001677
NM_001001787

NM_009721

RefSeq (protein)

NP_001668

NP_033851

Location (UCSC)Chr 1: 169.11 – 169.31 MbChr 1: 164.26 – 164.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Sodium/potassium-transporting ATPase subunit beta-1 is an enzyme that in humans is encoded by the ATP1B1 gene.[5]

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 1 subunit. Alternatively spliced transcript variants encoding different isoforms have been identified.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143153 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026576 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: ATP1B1 ATPase, Na+/K+ transporting, beta 1 polypeptide".

Further reading

  • Lingrel JB, Orlowski J, Shull MM, Price EM (1990). "Molecular genetics of Na,K-ATPase". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 38: 37–89. doi:10.1016/S0079-6603(08)60708-4. ISBN 978-0-12-540038-1. PMID 2158121.
  • Oakey RJ, Watson ML, Seldin MF (1993). "Construction of a physical map on mouse and human chromosome 1: comparison of 13 Mb of mouse and 11 Mb of human DNA". Hum. Mol. Genet. 1 (8): 613–20. doi:10.1093/hmg/1.8.613. PMID 1301170.
  • Martin-Vasallo P, Dackowski W, Emanuel JR, Levenson R (1989). "Identification of a putative isoform of the Na,K-ATPase beta subunit. Primary structure and tissue-specific expression". J. Biol. Chem. 264 (8): 4613–8. doi:10.1016/S0021-9258(18)83787-5. PMID 2538450.
  • Ushkaryov YuA, Monastyrskaya GS, Broude NE, et al. (1990). "Human Na+,K+-ATPase genes. Beta-subunit gene family contains at least one gene and one pseudogene". FEBS Lett. 257 (2): 439–42. doi:10.1016/0014-5793(89)81591-1. PMID 2555225. S2CID 13623201.
  • Lane LK, Shull MM, Whitmer KR, Lingrel JB (1990). "Characterization of two genes for the human Na,K-ATPase beta subunit". Genomics. 5 (3): 445–53. doi:10.1016/0888-7543(89)90008-6. PMID 2559024.
  • Yang-Feng TL, Schneider JW, Lindgren V, et al. (1988). "Chromosomal localization of human Na+, K+-ATPase alpha- and beta-subunit genes". Genomics. 2 (2): 128–38. doi:10.1016/0888-7543(88)90094-8. PMID 2842249.
  • Sverdlov ED, Broude NE, Sverdlov VE, et al. (1987). "Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism". FEBS Lett. 221 (1): 129–33. doi:10.1016/0014-5793(87)80366-6. PMID 2887455. S2CID 32756405.
  • Kawakami K, Nojima H, Ohta T, Nagano K (1986). "Molecular cloning and sequence analysis of human Na,K-ATPase beta-subunit". Nucleic Acids Res. 14 (7): 2833–44. doi:10.1093/nar/14.7.2833. PMC 339706. PMID 3008098.
  • Coca-Prados M, Fernández-Cabezudo MJ, Sánchez-Torres J, et al. (1996). "Cell-specific expression of the human Na+,K+-ATPase beta 2 subunit isoform in the nonpigmented ciliary epithelium". Invest. Ophthalmol. Vis. Sci. 36 (13): 2717–28. PMID 7499094.
  • Ruiz A, Bhat SP, Bok D (1995). "Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium". Gene. 155 (2): 179–84. doi:10.1016/0378-1119(94)00812-7. PMID 7536695.
  • Mobasheri A, Oukrif D, Dawodu SP, et al. (2001). "Isoforms of Na+, K+-ATPase in human prostate; specificity of expression and apical membrane polarization". Histol. Histopathol. 16 (1): 141–54. PMID 11193188.
  • Gamaleĭ IA, Polozov IuS, Aksenov ND, et al. (2001). "[Cell cycle and formation of active form of oxygen in rodent fibroblasts]". Tsitologiia. 43 (6): 602–12. PMID 11534180.
  • Béguin P, Crambert G, Monnet-Tschudi F, et al. (2002). "FXYD7 is a brain-specific regulator of Na,K-ATPase α1–β isozymes". EMBO J. 21 (13): 3264–73. doi:10.1093/emboj/cdf330. PMC 125393. PMID 12093728.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Zhang H, Li XJ, Martin DB, Aebersold R (2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nat. Biotechnol. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519. S2CID 581283.
  • Fuller W, Eaton P, Bell JR, Shattock MJ (2004). "Ischemia-induced phosphorylation of phospholemman directly activates rat cardiac Na/K-ATPase". FASEB J. 18 (1): 197–9. doi:10.1096/fj.03-0213fje. PMID 14597563. S2CID 41768501.
  • Li J, Codina J, Petroske E, et al. (2004). "The carboxy terminus of the colonic H+, K+-ATPase alpha-subunit is required for stable beta subunit assembly and function". Kidney Int. 65 (4): 1301–10. doi:10.1111/j.1523-1755.2004.00507.x. PMID 15086469.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wickham L, Benjannet S, Marcinkiewicz E, et al. (2005). "Beta-amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furin". J. Neurochem. 92 (1): 93–102. doi:10.1111/j.1471-4159.2004.02840.x. PMID 15606899.

External links

  • v
  • t
  • e
3.6.13.6.23.6.3-4: ATPase
3.6.3
Cu++ (3.6.3.4)
Ca+ (3.6.3.8)
Na+/K+ (3.6.3.9)
H+/K+ (3.6.3.10)
  • ATP4A
Other P-type ATPase
3.6.4
3.6.5: GTPase
3.6.5.1: Heterotrimeric G protein
3.6.5.2: Small GTPase > Ras superfamily
3.6.5.3: Protein-synthesizing GTPase
3.6.5.5-6: Polymerization motors


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