Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
31776 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
Sodium/potassium-transporting ATPase subunit beta-3 
Protein Synonyms/Alias
Sodium/potassium-dependent ATPase subunit beta-3;ATPB-3 CD_antigen=CD298; 
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. We isolated a full-length cDNA encoding a novel 278 amino acid beta subunit of Na,K-ATPase from a mouse retinal cDNA library. The highest sequence identity was to known beta 3 isoforms, identifying the protein as the mouse beta 3 subunit of Na,K-ATPase. Two transcripts, 1.75 kb and 2.1 kb, probably arise from use of alternative poly(A) addition signals. PMID: [9003452] 

2. Endogenous regeneration and repair mechanisms are responsible for replacing dead and damaged cells to maintain or enhance tissue and organ function, and one of the best examples of endogenous repair mechanisms involves skeletal muscle. Although the molecular mechanisms that regulate the differentiation of satellite cells and myoblasts toward myofibers are not fully understood, cell surface proteins that sense and respond to their environment play an important role. The cell surface capturing technology was used here to uncover the cell surface N-linked glycoprotein subproteome of myoblasts and to identify potential markers of myoblast differentiation. 128 bona fide cell surface-exposed N-linked glycoproteins, including 117 transmembrane, four glycosylphosphatidylinositol-anchored, five extracellular matrix, and two membrane-associated proteins were identified from mouse C2C12 myoblasts. The data set revealed 36 cluster of differentiation-annotated proteins and confirmed the occupancy for 235 N-linked glycosylation sites. The identification of the N-glycosylation sites on the extracellular domain of the proteins allowed for the determination of the orientation of the identified proteins within the plasma membrane. One glycoprotein transmembrane orientation was found to be inconsistent with Swiss-Prot annotations, whereas ambiguous annotations for 14 other proteins were resolved. Several of the identified N-linked glycoproteins, including aquaporin-1 and beta-sarcoglycan, were found in validation experiments to change in overall abundance as the myoblasts differentiate toward myotubes. Therefore, the strategy and data presented shed new light on the complexity of the myoblast cell surface subproteome and reveal new targets for the clinically important characterization of cell intermediates during myoblast differentiation into myotubes. PMID: [19656770] 

3. Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement. We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge. We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage. A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means. PMID: [19349973] 

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This is the non-catalytic component of the activeenzyme, which catalyzes the hydrolysis of ATP coupled with theexchange of Na(+) and K(+) ions across the plasma membrane. Theexact function of the beta-3 subunit is not known. 
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Subcellular Location
Membrane; Single-pass type II membraneprotein. Melanosome (By similarity). 
Tissue Specificity
Widely expressed. 
Gene Ontology
GO IDGO termEvidence
GO:0005901 C:caveola IEA:Compara.
GO:0005737 C:cytoplasm IDA:MGI.
GO:0042470 C:melanosome IEA:UniProtKB-SubCell.
GO:0005890 C:sodium:potassium-exchanging ATPase complex IEA:Compara.
GO:0005391 F:sodium:potassium-exchanging ATPase activity IEA:Compara.
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IPR000402;    ATPase_P-typ_cation-exchng_bsu.
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PF00287;    Na_K-ATPase;    1.
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PS00390;    ATPASE_NA_K_BETA_1;    1.
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Created Date
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    278       Sodium/potassium-transporting ATPase
                             subunit beta-3.
TOPO_DOM      1     35       Cytoplasmic (Potential).
TRANSMEM     36     56       Helical; Signal-anchor for type II
                             membrane protein; (Potential).
TOPO_DOM     57    278       Extracellular (Potential).
CARBOHYD    124    124       N-linked (GlcNAc...).
CARBOHYD    197    197       N-linked (GlcNAc...).
DISULFID    128    144       By similarity.
DISULFID    154    170       By similarity.
DISULFID    191    249       By similarity.
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Nucleotide Sequence
Length: 1842 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 278 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
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