Sodium/potassium-transporting ATPase subunit beta-2 (ATP1B2)
The protein contains 290 amino acids for an estimated molecular weight of 33367 Da.
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 exact function of the beta-2 subunit is not known.', 'Mediates cell adhesion of neurons and astrocytes, and promotes neurite outgrowth. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs34745087 | |
| dbSNP:rs2227866 |
Biological Process
Cell communication by electrical coupling involved in cardiac conduction
Cell-substrate adhesion
Cellular potassium ion homeostasis
Cellular sodium ion homeostasis
Ion transmembrane transport
Lateral ventricle development
Leukocyte migration
Membrane repolarization
Motor behavior
Negative regulation of glial cell migration
Neuronal-glial interaction involved in hindbrain glial-mediated radial cell migration
Photoreceptor cell maintenance
Plasma membrane bounded cell projection organization
Positive regulation of ATPase activity
Positive regulation of neuron projection development
Positive regulation of potassium ion import across plasma membrane
Positive regulation of potassium ion transmembrane transporter activity
Positive regulation of sodium ion export across plasma membrane
Potassium ion import across plasma membrane
Protein stabilization
Regulation of cardiac conduction
Retina homeostasis
Sodium ion export across plasma membrane
Third ventricle development
Transport across blood-brain barrier
Cellular Component
Apical plasma membrane
Astrocyte end-foot
Astrocyte projection
Cell body membrane
Cell periphery
Cell projection membrane
Cytoplasm
External side of plasma membrane
Lateral plasma membrane
Membrane
Neuron to neuron synapse
Obsolete cell
Photoreceptor inner segment
Plasma membrane
Sodium:potassium-exchanging ATPase complex
The reference OMIM entry for this protein is 182331
Atpase, na+/k+ transporting, beta-2 polypeptide; atp1b2
Na,k-atpase beta-2 polypeptide
Adhesion molecule on glia; amog
DESCRIPTION
The Na+/K+ ATPase is a plasma membrane pump with numerous physiologic functions. It maintains ionic homeostasis that is critical for cell survival, differentiation, and apoptosis. The Na+/K+ ATPase holoenzyme consists of a catalytic alpha subunit (see 182310), a beta subunit, and a modulatory gamma subunit (FXYD2; 601814). Beta subunits, such as ATP1B2, are responsible for formation and structural integrity of the Na+/K+ ATPase holoenzyme (summary by Li et al., 2011).CLONING
Martin-Vasallo et al. (1989) isolated cDNA clones from rat brain and human liver encoding a putative isoform of the Na,K-ATPase beta subunit, termed beta-2. The rat cDNA encodes a deduced protein of 290 amino acids with a molecular mass of 33.4 kD. The protein sequence shows 98% sequence identity to the human counterpart. Gloor et al. (1990) found that the sequence of mouse Amog (adhesion molecular on glia) is 97% identical to the rat Na,K-ATPase beta-2 subunit identified by Martin-Vasallo et al. (1989). Mouse Amog is an integral membrane glycoprotein with a molecular mass of 45-50 kD that is expressed by glial cells and mediates granule neuron migration along Bergmann glial cells in the developing cerebellum. The cDNA sequence of the mouse gene was shown by Pagliusi et al. (1989) to have structural similarity to the beta-1 subunit of Na,K-ATPase (ATP1B1; 182330). Like ATP1B1, AMOG is molecularly associated with the alpha subunit and influences its catalytic activity.MAPPING
In the mouse, Malo et al. (1990) mapped the beta-2 subunit of sodium-potassium-ATPase to chromosome 11 in a segment that is conserved on the pericentromeric region of human chromosome 17. Thus, Malo et al. (1990) speculated that the human ATP1B2 gene is on the proximal short arm or pericentric area of chromosome 17. By somatic cell hybrid analysis, Hsieh et al. (1990) demonstrated that the gene is indeed located on human chromosome 17 and confirmed the assignment to mouse chromosome 11. By study of recombinant inbred strains, Hsieh et al. (1990) placed the Amog locus close to the genes for zinc finger protein-3 (194480) and the asialoglycoprotein receptor (108360, 108361) in a region of mouse chromosome 11 that is homologous to human 17p. Gross (2014) mapped the ATP1B2 gene to chromosome 17p13.1 based on an alignment of the ATP1B2 sequence (GenBank GENBANK AF007876) with the genomic sequence (GRCh37). ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 182331 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).