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P05026 (AT1B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit beta-1
Alternative name(s):
Sodium/potassium-dependent ATPase subunit beta-1
Gene names
Name:ATP1B1
Synonyms:ATP1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9

Involved in cell adhesion and establishing epithelial cell polarity. Ref.9

Subunit structure

Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with NKAIN1, NKAIN2 and NKAIN4 By similarity. Interacts with MLC1. Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM. Ref.13

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Tissue specificity

Found in most tissues.

Domain

The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties By similarity. Ref.9

Sequence similarities

Belongs to the X(+)/potassium ATPases subunit beta family.

Ontologies

Keywords
   Biological processCell adhesion
Ion transport
Potassium transport
Sodium transport
Sodium/potassium transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandPotassium
Sodium
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

ion transmembrane transport

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Traceable author statement Ref.2. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

plasma membrane

Traceable author statement. Source: Reactome

sodium:potassium-exchanging ATPase complex

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functionMHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

sodium:potassium-exchanging ATPase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05026-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05026-2)

The sequence of this isoform differs from the canonical sequence as follows:
     300-303: EVKS → KF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Sodium/potassium-transporting ATPase subunit beta-1
PRO_0000219097

Regions

Topological domain1 – 3434Cytoplasmic Potential
Transmembrane35 – 6228Helical; Signal-anchor for type II membrane protein; Potential
Topological domain63 – 303241Extracellular Potential
Region191 – 303113immunoglobulin-like

Amino acid modifications

Modified residue1011Phosphotyrosine By similarity
Glycosylation1581N-linked (GlcNAc...) Ref.8 Ref.10
Glycosylation1931N-linked (GlcNAc...) Ref.8 Ref.10
Glycosylation2651N-linked (GlcNAc...) Ref.8 Ref.10 Ref.11
Disulfide bond126 ↔ 149 By similarity
Disulfide bond159 ↔ 175 By similarity
Disulfide bond213 ↔ 276 By similarity

Natural variations

Alternative sequence300 – 3034EVKS → KF in isoform 2.
VSP_000349

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 107D3C04394F2D11

FASTA30335,061
        10         20         30         40         50         60 
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT 

        70         80         90        100        110        120 
ISEFKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEA YVLNIVRFLE KYKDSAQRDD 

       130        140        150        160        170        180 
MIFEDCGDVP SEPKERGDFN HERGERKVCR FKLEWLGNCS GLNDETYGYK EGKPCIIIKL 

       190        200        210        220        230        240 
NRVLGFKPKP PKNESLETYP VMKYNPNVLP VQCTGKRDED KDKVGNVEYF GLGNSPGFPL 

       250        260        270        280        290        300 
QYYPYYGKLL QPKYLQPLLA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE 


VKS 

« Hide

Isoform 2 [UniParc].

Checksum: 670C194F2D114F67
Show »

FASTA30134,893

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of human Na,K-ATPase beta-subunit."
Kawakami K., Nojima H., Ohta T., Nagano K.
Nucleic Acids Res. 14:2833-2844(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of two genes for the human Na,K-ATPase beta subunit."
Lane L.K., Shull M.M., Whitmer K.R., Lingrel J.B.
Genomics 5:445-453(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium."
Ruiz A., Bhat S.P., Bok D.
Gene 155:179-184(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Retinal pigment epithelium.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[7]"Human Na(+), K(+)-ATPase genes. Beta subunit gene family contains at least one gene and one pseudogene."
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.
FEBS Lett. 257:439-442(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-72.
Tissue: Sperm.
[8]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-158; ASN-193 AND ASN-265.
[9]"A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase resembles cell adhesion molecules."
Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E., Karlish S.J.
Biochemistry 48:8684-8691(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ADHESION, DOMAIN IMMUNOGLOBULIN-LIKE.
[10]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158; ASN-193 AND ASN-265.
Tissue: Liver.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
Tissue: Leukemic T-cell.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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."
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.
Hum. Mol. Genet. 21:2166-2180(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLC1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03747 mRNA. Translation: CAA27385.1.
M25160, M25161 Genomic DNA. Translation: AAA36352.1.
U16799 mRNA. Translation: AAC50132.1.
BT009787 mRNA. Translation: AAP88789.1.
AL031726 Genomic DNA. Translation: CAI18888.1.
BC000006 mRNA. Translation: AAH00006.1.
X17161 Genomic DNA. Translation: CAA35040.1.
CCDSCCDS1276.1. [P05026-1]
PIRPWHUNB. A23764.
RefSeqNP_001668.1. NM_001677.3. [P05026-1]
UniGeneHs.291196.

3D structure databases

ProteinModelPortalP05026.
SMRP05026. Positions 1-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106971. 24 interactions.
IntActP05026. 10 interactions.
MINTMINT-5000887.
STRING9606.ENSP00000356789.

Chemistry

BindingDBP05026.
ChEMBLCHEMBL2095186.

Protein family/group databases

TCDB3.A.3.1.1. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP05026.

Polymorphism databases

DMDM114392.

Proteomic databases

MaxQBP05026.
PaxDbP05026.
PRIDEP05026.

Protocols and materials databases

DNASU481.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367815; ENSP00000356789; ENSG00000143153. [P05026-1]
ENST00000367816; ENSP00000356790; ENSG00000143153. [P05026-1]
GeneID481.
KEGGhsa:481.
UCSCuc001gfr.1. human. [P05026-1]

Organism-specific databases

CTD481.
GeneCardsGC01P169074.
H-InvDBHIX0001311.
HGNCHGNC:804. ATP1B1.
HPAHPA012911.
MIM182330. gene.
neXtProtNX_P05026.
PharmGKBPA66.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313139.
HOGENOMHOG000039248.
HOVERGENHBG050603.
InParanoidP05026.
KOK01540.
OMAGFKPKPP.
OrthoDBEOG7M6D85.
PhylomeDBP05026.
TreeFamTF314618.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP05026.
BgeeP05026.
CleanExHS_ATP1B1.
GenevestigatorP05026.

Family and domain databases

InterProIPR000402. Na/K_ATPase_sub_beta.
IPR015565. Na/K_ATPase_sub_beta_chordates.
[Graphical view]
PANTHERPTHR11523. PTHR11523. 1 hit.
PTHR11523:SF10. PTHR11523:SF10. 1 hit.
PfamPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP1B1. human.
GeneWikiATP1B1.
GenomeRNAi481.
NextBio1995.
PROP05026.
SOURCESearch...

Entry information

Entry nameAT1B1_HUMAN
AccessionPrimary (citable) accession number: P05026
Secondary accession number(s): Q5TGZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM