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| genesymbol | type | description | chr. | startpos | endpos | synonyms | |
| ATP1B1 | protein-coding | ATPase Na+/K+ transporting subunit beta 1 | 1 | 169075947 | 169101960 | MGC1798, ATP1B | |
| links | NCBI ENSEMBL SwissProt GeneCards STRING PubMed create primers for all transcripts | ||||||
| KEGG pathways | Cardiac muscle contraction, Aldosterone-regulated sodium reabsorption, Proximal tubule bicarbonate reclamation, Salivary secretion, Gastric acid secretion | ||||||
| PFAM | Sodium / potassium ATPase beta chain | ||||||
| InterPro domains | Sodium/potassium-transporting ATPase subunit beta, Sodium/potassium-transporting ATPase subunit beta, chordates | ||||||
| paralogs | ATP1B2 (37%), ATP1B3 (34%), ATP4B (28%), ATP1B4 (32%) | ||||||
| OMIM | ATPase, Na+/K+ TRANSPORTING, BETA-1 POLYPEPTIDE; ATP1B1 text: CLONING From HeLa cells, Kawakami et al. (1986) isolated a cDNA clone that covered the entire coding region of the beta subunit of Na,K-ATPase. Remarkably, 61% homology to the amino acid sequence of the Torpedo (electric ray) counterpart was demonstrated. - Pseudogenes Lane et al. (1989) isolated clones for a processed pseudogene designated ATP1BL1. Whether this is the same as the ATP1BL1 gene mapped to chromosome 4 by Yang-Feng et al. (1988) was not certain. GENE STRUCTURE Lane et al. (1989) found that the ATP1B gene spans about 26.7 kb of genomic DNA and includes 24 kb of intron sequence. The complete message is encoded by 6 exons ranging in size from 81 to 1,427 bp. MAPPING Yang-Feng et al. (1988) assigned the ATP1B gene to 1q by Southern analysis of DNA from rodent/human somatic cell hybrids. In the course of construction of a physical map of human 1q23-q25, Oakey et al. (1992) mapped ATP1B near the middle of this segment. The corresponding gene in the mouse is located on chromosome 1 (Kent et al., 1987). By linkage studies in interspecific backcrosses of Mus spretus and Mus musculus domesticus, Seldin (1989) also demonstrated that the homologous gene is located on mouse chromosome 1. BIOCHEMICAL FEATURES - Crystal Structure Morth et al. (2007) presented the x-ray crystal structure at 3.5-angstrom resolution of the pig renal sodium/potassium ATPase (Na+,K(+)-ATPase) with 2 rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the alpha subunit (see ATP1A1, 182310). Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K(+)-ATPase are homologous to those binding calcium in the calcium-ion ATPase of sarcoendoplasmic reticulum (SERCA1; 108730). The beta and gamma (ATP1G1; 601814) subunits specific to the Na+,K(+)-ATPase are associated with transmembrane helices alpha-M7/alpha-M10, and alpha-M9, respectively. The gamma subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential. Crystal structures of the potassium-bound form of the Na+/K(+)-ATPase pump revealed an intimate docking of the alpha-subunit carboxy terminus at the transmembrane domain (e.g., Morth et al., 2007). Poulsen et al. (2010) showed that this element is a key regulator of a theretofore unrecognized ion pathway. Models of P-type ATPases operated with a single ion conduit through the pump, but the data of Poulsen et al. (2010) suggested an additional pathway in the Na+/K(+)-ATPase between the ion-binding sites and the cytoplasm. The C-terminal pathway allows a cytoplasmic proton to enter and stabilize site III when empty in the potassium-bound state, and when potassium is released the proton will also return to the cytoplasm, thus allowing an overall asymmetric stoichiometry of the transported ions. The C terminus controls the gate to the pathway. Its structure is crucial for pump function, as demonstrated by at least 8 mutations in the region that cause severe neurologic diseases. This novel model for ion transport by the Na+/K(+)-ATPase was established by electrophysiologic studies of C-terminal mutations in familial hemiplegic migraine (602481) and was further substantiated by molecular dynamics simulations. Poulsen et al. (2010) considered a similar ion regulation likely to apply to the H+/K(+)-ATPase and the Ca(2+)-ATPase. GENE FUNCTION Using yeast 2-hybrid analysis, Zatyka et al. (2008) found that the C-terminal domain of WFS1 (606201) bound the C-terminal domain of ATP1B1. The interaction was confirmed by reciprocal coimmunoprecipitation analysis of proteins expressed in transfected COS-7 cells and endogenous proteins in human and mouse cell lines. Fibroblasts from Wolfram syndrome (222300) patients with 2 different WFS1 mutations showed reduced ATP1B1 levels. Conversely, knockdown of Atp1b1 expression in a mouse insulinoma cell line led to reduced Wfs1 expression. Zatyka et al. (2008) concluded that interaction with WFS1 may be important for ATP1B1 maturation in the endoplasmic reticulum and that loss of this interaction may contribute to the pathology seen in Wolfram syndrome. MOLECULAR GENETICS Chang et al. (2007) reported genomewide linkage and candidate gene-based association studies that demonstrated a replicated linkage peak for blood pressure regulation on human chromosome 1q23-q32, homologous to mouse and rat quantitative trait loci (QTLs) for blood pressure. The region contained at least 3 genes associated with blood pressure level in multiple samples: ATP1B1, RGS5 (603276), and SELE (131210). Individual variants in these 3 genes accounted for 2- to 5-mm Hg differences in mean systolic blood pressure, and the cumulative effect reached 8 to 10 mm Hg. Because the associated alleles in these genes are relatively common (frequency more than 5%), these 3 genes are important contributors to elevated blood pressure in the population at large. Chang et al. (2007) viewed the probable relationship between each of these genes and blood pressure regulation. See report at OMIM's website. |
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| transcripts | ENST00000367816: 2608 bases (protein_coding) ENST00000367815: 1883 bases (protein_coding) ENST00000499679: 1738 bases (protein_coding) ENST00000367813: 1382 bases (protein_coding) ENST00000494797: 718 bases (protein_coding) |
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| GeneOntology |
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| If you feel that GeneDistiller has helped you in your research, please cite the following publication: Seelow D, Schwarz JM, Schuelke M. GeneDistiller--distilling candidate genes from linkage intervals. PLoS ONE. 2008;3(12):e3874. Epub 2008 Dec 5. |
| entity | last update (YYYY-MM-DD) |
| Disease Ontology | 2020-06-29 |
| Ensembl 84 (GRCh73) | 2016-06-14 |
| Ensembl:Entrez | 2021-10-28 |
| Entrez gene history | 2021-10-28 |
| Entrez gene positions | 2021-10-28 |
| Entrez gene RIFS | 2021-10-28 |
| Entrez genes | 2021-10-28 |
| Entrez gene synonyms | 2021-10-28 |
| HPO:Genes | 2015-12-22 |
| HPO:OMIM | 2015-12-22 |
| HPO:OrphaNet | 2015-12-22 |
| Human Phenotype Ontology | 2015-12-22 |
| OMIM | 2015-08-25 |