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Sodium/potassium-transporting ATPase subunit beta-1 (Sodium/potassium-dependent ATPase subunit beta-1)

 AT1B1_HUMAN             Reviewed;         303 AA.
P05026; Q5TGZ3;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 182.
RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
Name=ATP1B1; Synonyms=ATP1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3008098; DOI=10.1093/nar/14.7.2833;
Kawakami K., Nojima H., Ohta T., Nagano K.;
"Molecular cloning and sequence analysis of human Na,K-ATPase beta-
subunit.";
Nucleic Acids Res. 14:2833-2844(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2559024; DOI=10.1016/0888-7543(89)90008-6;
Lane L.K., Shull M.M., Whitmer K.R., Lingrel J.B.;
"Characterization of two genes for the human Na,K-ATPase beta
subunit.";
Genomics 5:445-453(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Retinal pigment epithelium;
PubMed=7536695; DOI=10.1016/0378-1119(94)00812-7;
Ruiz A., Bhat S.P., 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 155:179-184(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-72.
TISSUE=Sperm;
PubMed=2555225; DOI=10.1016/0014-5793(89)81591-1;
Ushkaryov Y.A., Monastyrskaya G.S., Broude N.E., Nikiforova N.N.,
Bessarab B.A., Orlova M.Y., Petrukhin K.E., Modyanov N.N.,
Sverdlov E.D.;
"Human Na(+), K(+)-ATPase genes. Beta subunit gene family contains at
least one gene and one pseudogene.";
FEBS Lett. 257:439-442(1989).
[8]
GLYCOSYLATION AT ASN-158; ASN-193 AND ASN-265.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[9]
FUNCTION IN ADHESION, AND DOMAIN IMMUNOGLOBULIN-LIKE.
PubMed=19694409; DOI=10.1021/bi900868e;
Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E.,
Karlish S.J.;
"A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase
resembles cell adhesion molecules.";
Biochemistry 48:8684-8691(2009).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158; ASN-193 AND ASN-265.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
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. 8:651-661(2009).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH MLC1.
PubMed=22328087; DOI=10.1093/hmg/dds032;
Lanciotti A., Brignone M.S., Molinari P., Visentin S., De Nuccio C.,
Macchia G., Aiello C., Bertini E., Aloisi F., Petrucci T.C.,
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. 21:2166-2180(2012).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[15]
INTERACTION WITH KIRREL3.
PubMed=25902260; DOI=10.1371/journal.pone.0123106;
Liu Y.F., Sowell S.M., Luo Y., Chaubey A., Cameron R.S., Kim H.G.,
Srivastava A.K.;
"Autism and intellectual disability-associated KIRREL3 interacts with
neuronal proteins MAP1B and MYO16 with potential roles in
neurodevelopment.";
PLoS ONE 10:E0123106-E0123106(2015).
-!- FUNCTION: This 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. {ECO:0000269|PubMed:19694409}.
-!- FUNCTION: Involved in cell adhesion and establishing epithelial
cell polarity. {ECO:0000269|PubMed:19694409}.
-!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
catalytic alpha subunit, an auxiliary non-catalytic beta subunit
and an additional regulatory subunit. Interacts with regulatory
subunit FXYD1 (By similarity). Interacts with regulatory subunit
FXYD3 (By similarity). Interacts with NKAIN1, NKAIN2 and NKAIN4
(By similarity). Interacts with MLC1 (PubMed:22328087). Part of a
complex containing MLC1, TRPV4, AQP4 and HEPACAM
(PubMed:22328087). Interacts with KIRREL3 (PubMed:25902260).
Interacts with OBSCN (via protein kinase domain 1) (By
similarity). {ECO:0000250|UniProtKB:P07340,
ECO:0000250|UniProtKB:P14094, ECO:0000269|PubMed:22328087,
ECO:0000269|PubMed:25902260}.
-!- INTERACTION:
P02730:SLC4A1; NbExp=8; IntAct=EBI-714630, EBI-7576138;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass
type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the
intercalated disk and sarcolemma in cardiomyocytes. Localizes in
long striations at the level of Z and M lines.
{ECO:0000250|UniProtKB:P14094}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P05026-1; Sequence=Displayed;
Name=2;
IsoId=P05026-2; Sequence=VSP_000349;
-!- TISSUE SPECIFICITY: Found in most tissues.
-!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like
domain and mediates cell adhesion properties. {ECO:0000250}.
-!- PTM: Glutathionylated. {ECO:0000250|UniProtKB:P14094}.
-!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta
family. {ECO:0000305}.
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EMBL; X03747; CAA27385.1; -; mRNA.
EMBL; M25160; AAA36352.1; -; Genomic_DNA.
EMBL; M25161; AAA36352.1; JOINED; Genomic_DNA.
EMBL; U16799; AAC50132.1; -; mRNA.
EMBL; BT009787; AAP88789.1; -; mRNA.
EMBL; AL031726; CAI18888.1; -; Genomic_DNA.
EMBL; BC000006; AAH00006.1; -; mRNA.
EMBL; X17161; CAA35040.1; -; Genomic_DNA.
CCDS; CCDS1276.1; -. [P05026-1]
PIR; A23764; PWHUNB.
RefSeq; NP_001668.1; NM_001677.3. [P05026-1]
UniGene; Hs.291196; -.
ProteinModelPortal; P05026; -.
BioGrid; 106971; 73.
IntAct; P05026; 15.
MINT; MINT-5000887; -.
STRING; 9606.ENSP00000356789; -.
ChEMBL; CHEMBL2095186; -.
DrugBank; DB09479; Rubidium chloride Rb-82.
TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P05026; -.
PhosphoSitePlus; P05026; -.
SwissPalm; P05026; -.
BioMuta; ATP1B1; -.
DMDM; 114392; -.
EPD; P05026; -.
MaxQB; P05026; -.
PaxDb; P05026; -.
PeptideAtlas; P05026; -.
PRIDE; P05026; -.
DNASU; 481; -.
Ensembl; ENST00000367815; ENSP00000356789; ENSG00000143153. [P05026-1]
Ensembl; ENST00000367816; ENSP00000356790; ENSG00000143153. [P05026-1]
GeneID; 481; -.
KEGG; hsa:481; -.
UCSC; uc001gfr.2; human. [P05026-1]
CTD; 481; -.
DisGeNET; 481; -.
EuPathDB; HostDB:ENSG00000143153.12; -.
GeneCards; ATP1B1; -.
H-InvDB; HIX0001311; -.
HGNC; HGNC:804; ATP1B1.
HPA; HPA012911; -.
MIM; 182330; gene.
neXtProt; NX_P05026; -.
OpenTargets; ENSG00000143153; -.
PharmGKB; PA66; -.
eggNOG; KOG3927; Eukaryota.
eggNOG; ENOG411150A; LUCA.
GeneTree; ENSGT00550000074530; -.
HOGENOM; HOG000039248; -.
HOVERGEN; HBG050603; -.
InParanoid; P05026; -.
KO; K01540; -.
OMA; TELRIEC; -.
OrthoDB; EOG091G0DJ4; -.
PhylomeDB; P05026; -.
TreeFam; TF314618; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP1B1; human.
GeneWiki; ATP1B1; -.
GenomeRNAi; 481; -.
PRO; PR:P05026; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143153; -.
CleanEx; HS_ATP1B1; -.
ExpressionAtlas; P05026; baseline and differential.
Genevisible; P05026; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IEA:Ensembl.
GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; ISS:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:BHF-UCL.
GO; GO:1903281; P:positive regulation of calcium:sodium antiporter activity; ISS:BHF-UCL.
GO; GO:1903288; P:positive regulation of potassium ion import; IDA:BHF-UCL.
GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:1903278; P:positive regulation of sodium ion export from cell; IDA:BHF-UCL.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0044861; P:protein transport into plasma membrane raft; TAS:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISS:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; ISS:BHF-UCL.
GO; GO:0055119; P:relaxation of cardiac muscle; ISS:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0036376; P:sodium ion export from cell; IDA:BHF-UCL.
InterPro; IPR000402; Na/K_ATPase_sub_beta.
InterPro; IPR015565; Na/K_ATPase_sub_beta_chordates.
PANTHER; PTHR11523; PTHR11523; 1.
PANTHER; PTHR11523:SF10; PTHR11523:SF10; 1.
Pfam; PF00287; Na_K-ATPase; 1.
TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glutathionylation; Glycoprotein; Ion transport;
Membrane; Phosphoprotein; Potassium; Potassium transport;
Reference proteome; Signal-anchor; Sodium; Sodium transport;
Sodium/potassium transport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 303 Sodium/potassium-transporting ATPase
subunit beta-1.
/FTId=PRO_0000219097.
TOPO_DOM 1 34 Cytoplasmic. {ECO:0000255}.
TRANSMEM 35 62 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 63 303 Extracellular. {ECO:0000255}.
REGION 191 303 immunoglobulin-like.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:P07340}.
MOD_RES 101 101 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14094}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
DISULFID 126 149 {ECO:0000250}.
DISULFID 159 175 {ECO:0000250}.
DISULFID 213 276 {ECO:0000250}.
VAR_SEQ 300 303 EVKS -> KF (in isoform 2).
{ECO:0000303|PubMed:7536695}.
/FTId=VSP_000349.
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


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Genprice Inc, Invoices and accounting
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