AT1B1_HUMAN
ID AT1B1_HUMAN Reviewed; 303 AA.
AC P05026; Q5TGZ3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=ATP1B1; Synonyms=ATP1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3008098; DOI=10.1093/nar/14.7.2833;
RA Kawakami K., Nojima H., Ohta T., Nagano K.;
RT "Molecular cloning and sequence analysis of human Na,K-ATPase beta-
RT subunit.";
RL Nucleic Acids Res. 14:2833-2844(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2559024; DOI=10.1016/0888-7543(89)90008-6;
RA Lane L.K., Shull M.M., Whitmer K.R., Lingrel J.B.;
RT "Characterization of two genes for the human Na,K-ATPase beta subunit.";
RL Genomics 5:445-453(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retinal pigment epithelium;
RX PubMed=7536695; DOI=10.1016/0378-1119(94)00812-7;
RA Ruiz A., Bhat S.P., Bok D.;
RT "Characterization and quantification of full-length and truncated Na,K-
RT ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal
RT pigment epithelium.";
RL Gene 155:179-184(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-72.
RC TISSUE=Sperm;
RX PubMed=2555225; DOI=10.1016/0014-5793(89)81591-1;
RA Ushkaryov Y.A., Monastyrskaya G.S., Broude N.E., Nikiforova N.N.,
RA Bessarab B.A., Orlova M.Y., Petrukhin K.E., Modyanov N.N., Sverdlov E.D.;
RT "Human Na(+), K(+)-ATPase genes. Beta subunit gene family contains at least
RT one gene and one pseudogene.";
RL FEBS Lett. 257:439-442(1989).
RN [8]
RP GLYCOSYLATION AT ASN-158; ASN-193 AND ASN-265.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [9]
RP FUNCTION IN ADHESION, AND DOMAIN IMMUNOGLOBULIN-LIKE.
RX PubMed=19694409; DOI=10.1021/bi900868e;
RA Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E.,
RA Karlish S.J.;
RT "A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase
RT resembles cell adhesion molecules.";
RL Biochemistry 48:8684-8691(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158; ASN-193 AND ASN-265.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH MLC1.
RX PubMed=22328087; DOI=10.1093/hmg/dds032;
RA Lanciotti A., Brignone M.S., Molinari P., Visentin S., De Nuccio C.,
RA Macchia G., Aiello C., Bertini E., Aloisi F., Petrucci T.C., Ambrosini E.;
RT "Megalencephalic leukoencephalopathy with subcortical cysts protein 1
RT functionally cooperates with the TRPV4 cation channel to activate the
RT response of astrocytes to osmotic stress: dysregulation by pathological
RT mutations.";
RL Hum. Mol. Genet. 21:2166-2180(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH KIRREL3.
RX PubMed=25902260; DOI=10.1371/journal.pone.0123106;
RA Liu Y.F., Sowell S.M., Luo Y., Chaubey A., Cameron R.S., Kim H.G.,
RA Srivastava A.K.;
RT "Autism and intellectual disability-associated KIRREL3 interacts with
RT neuronal proteins MAP1B and MYO16 with potential roles in
RT neurodevelopment.";
RL PLoS ONE 10:E0123106-E0123106(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TRAF3 AND TRAF6.
RX PubMed=34011520; DOI=10.4049/jimmunol.2001262;
RA Cao W., Guo Y., Cheng Z., Xu G., Zuo Q., Nie L., Huang Y., Liu S., Zhu Y.;
RT "Inducible ATP1B1 Upregulates Antiviral Innate Immune Responses by the
RT Ubiquitination of TRAF3 and TRAF6.";
RL J. Immunol. 206:2668-2681(2021).
CC -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC which catalyzes the hydrolysis of ATP coupled with the exchange of
CC Na(+) and K(+) ions across the plasma membrane. The beta subunit
CC regulates, through assembly of alpha/beta heterodimers, the number of
CC sodium pumps transported to the plasma membrane (PubMed:19694409).
CC Plays a role in innate immunity by enhancing virus-triggered induction
CC of interferons (IFNs) and interferon stimulated genes (ISGs).
CC Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well
CC as the phosphorylation of TAK1 and TBK1 (PubMed:34011520).
CC {ECO:0000269|PubMed:19694409, ECO:0000269|PubMed:34011520}.
CC -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000269|PubMed:19694409}.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. Interacts with catalytic subunit ATP12A
CC (By similarity). Interacts with regulatory subunit FXYD1 (By
CC similarity). Interacts with regulatory subunit FXYD3 (By similarity).
CC Interacts with NKAIN1, NKAIN2 and NKAIN4 (By similarity). Interacts
CC with MLC1 (PubMed:22328087). Part of a complex containing MLC1, TRPV4,
CC AQP4 and HEPACAM (PubMed:22328087). Interacts with KIRREL3
CC (PubMed:25902260). Interacts with OBSCN (via protein kinase domain 1)
CC (By similarity). Interacts with TRAF3 and TRAF6 (PubMed:34011520).
CC {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094,
CC ECO:0000269|PubMed:22328087, ECO:0000269|PubMed:25902260,
CC ECO:0000269|PubMed:34011520}.
CC -!- INTERACTION:
CC P05026; P30556: AGTR1; NbExp=2; IntAct=EBI-714630, EBI-6623016;
CC P05026; P05067: APP; NbExp=3; IntAct=EBI-714630, EBI-77613;
CC P05026; P05023: ATP1A1; NbExp=2; IntAct=EBI-714630, EBI-358778;
CC P05026; Q8IZU9: KIRREL3; NbExp=4; IntAct=EBI-714630, EBI-16427312;
CC P05026; P02730: SLC4A1; NbExp=8; IntAct=EBI-714630, EBI-7576138;
CC P05026; PRO_0000033087 [P61278]: SST; NbExp=2; IntAct=EBI-714630, EBI-26451163;
CC P05026; O76024: WFS1; NbExp=6; IntAct=EBI-714630, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34011520};
CC Single-pass type II membrane protein {ECO:0000255}. Apical cell
CC membrane {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane
CC protein {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the
CC intercalated disk and sarcolemma in cardiomyocytes. Localizes in long
CC striations at the level of Z and M lines.
CC {ECO:0000250|UniProtKB:P14094}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05026-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05026-2; Sequence=VSP_000349;
CC -!- TISSUE SPECIFICITY: Found in most tissues.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- PTM: Glutathionylated (By similarity). N-glycosylated (By similarity).
CC {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X03747; CAA27385.1; -; mRNA.
DR EMBL; M25160; AAA36352.1; -; Genomic_DNA.
DR EMBL; M25161; AAA36352.1; JOINED; Genomic_DNA.
DR EMBL; U16799; AAC50132.1; -; mRNA.
DR EMBL; BT009787; AAP88789.1; -; mRNA.
DR EMBL; AL031726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000006; AAH00006.1; -; mRNA.
DR EMBL; X17161; CAA35040.1; -; Genomic_DNA.
DR CCDS; CCDS1276.1; -. [P05026-1]
DR PIR; A23764; PWHUNB.
DR RefSeq; NP_001668.1; NM_001677.3. [P05026-1]
DR AlphaFoldDB; P05026; -.
DR SMR; P05026; -.
DR BioGRID; 106971; 147.
DR ComplexPortal; CPX-125; Sodium:potassium-exchanging ATPase complex.
DR CORUM; P05026; -.
DR IntAct; P05026; 34.
DR MINT; P05026; -.
DR STRING; 9606.ENSP00000356790; -.
DR BindingDB; P05026; -.
DR ChEMBL; CHEMBL2095186; -.
DR DrugBank; DB09020; Bisacodyl.
DR DrugBank; DB09479; Rubidium Rb-82.
DR DrugBank; DB16690; Tegoprazan.
DR DrugCentral; P05026; -.
DR TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
DR GlyConnect; 1757; 21 N-Linked glycans (3 sites).
DR GlyGen; P05026; 3 sites, 18 N-linked glycans (3 sites).
DR iPTMnet; P05026; -.
DR MetOSite; P05026; -.
DR PhosphoSitePlus; P05026; -.
DR SwissPalm; P05026; -.
DR BioMuta; ATP1B1; -.
DR DMDM; 114392; -.
DR CPTAC; CPTAC-27; -.
DR CPTAC; CPTAC-28; -.
DR EPD; P05026; -.
DR jPOST; P05026; -.
DR MassIVE; P05026; -.
DR MaxQB; P05026; -.
DR PaxDb; P05026; -.
DR PeptideAtlas; P05026; -.
DR PRIDE; P05026; -.
DR ProteomicsDB; 51770; -. [P05026-1]
DR ProteomicsDB; 51771; -. [P05026-2]
DR Antibodypedia; 2485; 333 antibodies from 37 providers.
DR DNASU; 481; -.
DR Ensembl; ENST00000367815.9; ENSP00000356789.3; ENSG00000143153.14. [P05026-1]
DR Ensembl; ENST00000367816.5; ENSP00000356790.1; ENSG00000143153.14. [P05026-1]
DR Ensembl; ENST00000689522.1; ENSP00000509039.1; ENSG00000143153.14. [P05026-1]
DR Ensembl; ENST00000690184.1; ENSP00000509517.1; ENSG00000143153.14. [P05026-1]
DR GeneID; 481; -.
DR KEGG; hsa:481; -.
DR MANE-Select; ENST00000367815.9; ENSP00000356789.3; NM_001677.4; NP_001668.1.
DR UCSC; uc001gfr.2; human. [P05026-1]
DR CTD; 481; -.
DR DisGeNET; 481; -.
DR GeneCards; ATP1B1; -.
DR HGNC; HGNC:804; ATP1B1.
DR HPA; ENSG00000143153; Tissue enhanced (brain, kidney).
DR MalaCards; ATP1B1; -.
DR MIM; 182330; gene.
DR neXtProt; NX_P05026; -.
DR OpenTargets; ENSG00000143153; -.
DR PharmGKB; PA66; -.
DR VEuPathDB; HostDB:ENSG00000143153; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_2_0_1; -.
DR InParanoid; P05026; -.
DR OMA; ECKAYGQ; -.
DR PhylomeDB; P05026; -.
DR TreeFam; TF314618; -.
DR PathwayCommons; P05026; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P05026; -.
DR SIGNOR; P05026; -.
DR BioGRID-ORCS; 481; 13 hits in 1086 CRISPR screens.
DR ChiTaRS; ATP1B1; human.
DR GeneWiki; ATP1B1; -.
DR GenomeRNAi; 481; -.
DR Pharos; P05026; Tclin.
DR PRO; PR:P05026; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P05026; protein.
DR Bgee; ENSG00000143153; Expressed in substantia nigra pars compacta and 206 other tissues.
DR ExpressionAtlas; P05026; baseline and differential.
DR Genevisible; P05026; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0031090; C:organelle membrane; IGI:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0036126; C:sperm flagellum; IDA:ARUK-UCL.
DR GO; GO:0030315; C:T-tubule; IGI:ARUK-UCL.
DR GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; ISS:BHF-UCL.
DR GO; GO:0098655; P:cation transmembrane transport; IGI:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; TAS:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:1903281; P:positive regulation of calcium:sodium antiporter activity; ISS:BHF-UCL.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IDA:ARUK-UCL.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0044861; P:protein transport into plasma membrane raft; TAS:BHF-UCL.
DR GO; GO:1902600; P:proton transmembrane transport; IC:ComplexPortal.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISS:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0055119; P:relaxation of cardiac muscle; ISS:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IGI:ARUK-UCL.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR015565; Na/K_ATPase_sub_beta_chordates.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR PANTHER; PTHR11523:SF10; PTHR11523:SF10; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glutathionylation; Glycoprotein; Immunity; Innate immunity; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219097"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 191..303
FT /note="immunoglobulin-like"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07340"
FT MOD_RES 101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14094"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT DISULFID 213..276
FT /evidence="ECO:0000250"
FT VAR_SEQ 300..303
FT /note="EVKS -> KF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7536695"
FT /id="VSP_000349"
SQ SEQUENCE 303 AA; 35061 MW; 107D3C04394F2D11 CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISEFKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEA YVLNIVRFLE KYKDSAQRDD
MIFEDCGDVP SEPKERGDFN HERGERKVCR FKLEWLGNCS GLNDETYGYK EGKPCIIIKL
NRVLGFKPKP PKNESLETYP VMKYNPNVLP VQCTGKRDED KDKVGNVEYF GLGNSPGFPL
QYYPYYGKLL QPKYLQPLLA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE
VKS
