Sodium/potassium-transporting ATPase subunit beta-1


NameSodium/potassium-transporting ATPase subunit beta-1
SynonymsATP1B Sodium/potassium-dependent ATPase subunit beta-1
Gene NameATP1B1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0008762|Sodium/potassium-transporting ATPase subunit beta-1
MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLT
ISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIVRFLEKYKDSAQRDD
MIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLNDETYGYKEGKPCIIIKL
NRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKVGNVEYFGLGNSPGFPL
QYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIE
VKS
Number of residues303
Molecular Weight35061.07
Theoretical pINone
GO Classification
Functions
    sodium
    ATPase binding
    ATPase activator activity
    MHC class II protein complex binding
Processes
    establishment or maintenance of transmembrane electrochemical gradient
    protein stabilization
    potassium ion import across plasma membrane
    transmembrane transport
    cell communication by electrical coupling involved in cardiac conduction
    sodium ion export from cell
    leukocyte migration
    positive regulation of ATPase activity
    potassium ion import
    ATP metabolic process
    ion transmembrane transport
    regulation of cardiac muscle contraction by calcium ion signaling
    cellular calcium ion homeostasis
    positive regulation of defense response to virus by host
    response to hypoxia
    positive regulation of sodium ion export from cell
    relaxation of cardiac muscle
    xenophagy
    cellular potassium ion homeostasis
    cell adhesion
    positive regulation of potassium ion import
    membrane repolarization during cardiac muscle cell action potential
    blood coagulation
    regulation of gene expression
    positive regulation of potassium ion transmembrane transporter activity
    cardiac muscle contraction
    mitophagy in response to mitochondrial depolarization
    protein localization to plasma membrane
    positive regulation of calcium
    cellular sodium ion homeostasis
    protein transport into plasma membrane raft
    ATP hydrolysis coupled transmembrane transport
    membrane repolarization
Components
    caveola
    intracellular
    membrane
    extracellular vesicle
    intercalated disc
    basolateral plasma membrane
    sarcolemma
    plasma membrane
    sodium
    extracellular exosome
    myelin sheath
    apical plasma membrane
General FunctionSodium:potassium-exchanging atpase activity
Specific FunctionThis is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.Involved in cell adhesion and establishing epithelial cell polarity.
Transmembrane Regions35-62
GenBank Protein ID
UniProtKB IDP05026
UniProtKB Entry NameAT1B1_HUMAN
Cellular LocationCell membrane
Gene sequence
>lcl|BSEQ0019662|Sodium/potassium-transporting ATPase subunit beta-1 (ATP1B1)
ATGGCCCGCGGGAAAGCCAAGGAGGAGGGCAGCTGGAAGAAATTCATCTGGAACTCAGAG
AAGAAGGAGTTTCTGGGCAGGACCGGTGGCAGTTGGTTTAAGATCCTTCTATTCTACGTA
ATATTTTATGGCTGCCTGGCTGGCATCTTCATCGGAACCATCCAAGTGATGCTGCTCACC
ATCAGTGAATTTAAGCCCACATATCAGGACCGAGTGGCCCCGCCAGGATTAACACAGATT
CCTCAGATCCAGAAGACTGAAATTTCCTTTCGTCCTAATGATCCCAAGAGCTATGAGGCA
TATGTACTGAACATAGTTAGGTTCCTGGAAAAGTACAAAGATTCAGCCCAGAGGGATGAC
ATGATTTTTGAAGATTGTGGCGATGTGCCCAGTGAACCGAAAGAACGAGGAGACTTTAAT
CATGAACGAGGAGAGCGAAAGGTCTGCAGATTCAAGCTTGAATGGCTGGGAAATTGCTCT
GGATTAAATGATGAAACTTATGGCTACAAAGAGGGCAAACCGTGCATTATTATAAAGCTC
AACCGAGTTCTAGGCTTCAAACCTAAGCCTCCCAAGAATGAGTCCTTGGAGACTTACCCA
GTGATGAAGTATAACCCAAATGTCCTTCCCGTTCAGTGCACTGGCAAGCGAGATGAAGAT
AAGGATAAAGTTGGAAATGTGGAGTATTTTGGACTGGGCAACTCCCCTGGTTTTCCTCTG
CAGTATTATCCGTACTATGGCAAACTCCTGCAGCCCAAATACCTGCAGCCCCTGCTGGCC
GTACAGTTCACCAATCTTACCATGGACACTGAAATTCGCATAGAGTGTAAGGCGTACGGT
GAGAACATTGGGTACAGTGAGAAAGACCGTTTTCAGGGACGTTTTGATGTAAAAATTGAA
GTTAAGAGCTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:804
Chromosome Location1
LocusNone
References
  1. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22.[24275569 ]
  2. Kawakami K, Nojima H, Ohta T, Nagano K: Molecular cloning and sequence analysis of human Na,K-ATPase beta-subunit. Nucleic Acids Res. 1986 Apr 11;14(7):2833-44.[3008098 ]
  3. Lane LK, Shull MM, Whitmer KR, Lingrel JB: Characterization of two genes for the human Na,K-ATPase beta subunit. Genomics. 1989 Oct;5(3):445-53.[2559024 ]
  4. Ruiz A, Bhat SP, Bok D: 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. 1995 Apr 3;155(2):179-84.[7536695 ]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21.[16710414 ]
  6. Ushkaryov YuA, Monastyrskaya GS, Broude NE, Nikiforova NN, Bessarab DA, Orlova MYu, Petrukhin KE, Modyanov NN, Sverdlov ED: Human Na+,K+-ATPase genes. Beta-subunit gene family contains at least one gene and one pseudogene. FEBS Lett. 1989 Nov 6;257(2):439-42.[2555225 ]
  7. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18.[12754519 ]
  8. Bab-Dinitz E, Albeck S, Peleg Y, Brumfeld V, Gottschalk KE, Karlish SJ: A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase resembles cell adhesion molecules. Biochemistry. 2009 Sep 15;48(36):8684-91. doi: 10.1021/bi900868e.[19694409 ]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012.[19159218 ]
  10. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. doi: 10.1038/nbt.1532. Epub 2009 Apr 6.[19349973 ]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17.[21269460 ]
  12. Lanciotti A, Brignone MS, Molinari P, Visentin S, De Nuccio C, Macchia G, Aiello C, Bertini E, Aloisi F, Petrucci TC, Ambrosini E: Megalencephalic leukoencephalopathy with subcortical cysts protein 1 functionally cooperates with the TRPV4 cation channel to activate the response of astrocytes to osmotic stress: dysregulation by pathological mutations. Hum Mol Genet. 2012 May 15;21(10):2166-80. doi: 10.1093/hmg/dds032. Epub 2012 Feb 9.[22328087 ]
  13. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7.[15489334 ]

Related FRC


FRCD ID Name Exact Mass Structure



Tetrachloroethylene




165.822



Endrin




380.895



1,1,1-Trichloroethane




133.396



1,1,2,2-Tetrachloroethane




167.838



1,1-Dichloroethane




98.954



Hexachlorocyclopentadiene




272.755



Mirex




545.51



Vanadyl sulfate




165.013



Butenolide




141.126



Chloroform




119.369



Clofenotane




354.476



Trichloroethylene




131.38



Dieldrin




380.895



Chlordane




409.758



Hexachlorobutadiene




260.744



Toxaphene




411.774



Heptachlor




373.3



3,3'-Dichlorobenzidine




253.126



Pentachlorophenol




266.323



Methoxychlor




345.644



1,1-Dichloroethene




96.938



1,2-Dichloroethane




98.954



2,4,6-Trichlorophenol




197.439



Hexachlorobenzene




284.766



Ethylbenzene




106.168



Chlorobenzene




112.556



1,2,3-Trichlorobenzene




181.44



Lead-210




209.984



Chlorpyrifos




350.575



Chlordecone




490.609



Dicofol




370.475



1,4-Dichlorobenzene




146.998



1,2-Dichlorobenzene




146.998



Vanadium




50.941



1,2,4-Trichlorobenzene




181.44



Tetraethyl lead




323.448



Methiochlor




377.766



Chlorbenzylate




325.185



1,3,5-Trichlorobenzene




181.44



Telodrin




411.73



Isodrin




364.896



Plumbane




211.232



Oleandrin




576.727



Patulin




154.121



Rubratoxin B




518.515



Rubratoxin A




520.531



Asteltoxin




418.486