ATP1B3: Difference between revisions

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{{Infobox_gene}}
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'''Sodium/potassium-transporting ATPase subunit beta-3''' is an [[enzyme]] that in humans is encoded by the ''ATP1B3'' [[gene]].<ref name="pmid8798450">{{cite journal | vauthors = Malik N, Canfield VA, Beckers MC, Gros P, Levenson R | title = Identification of the mammalian Na,K-ATPase 3 subunit | journal = J Biol Chem | volume = 271 | issue = 37 | pages = 22754–8 |date=Nov 1996 | pmid = 8798450 | pmc =  | doi =10.1074/jbc.271.37.22754  }}</ref><ref name="pmid9457675">{{cite journal | vauthors = Malik N, Canfield V, Sanchez-Watts G, Watts AG, Scherer S, Beatty BG, Gros P, Levenson R | title = Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene | journal = Mamm Genome | volume = 9 | issue = 2 | pages = 136–43 |date=Mar 1998 | pmid = 9457675 | pmc =  | doi =10.1007/s003359900704 }}</ref><ref name="entrez"/> ATP1B3 has also been designated as '''CD298''' ([[cluster of differentiation]] 298).
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATPase, Na+/K+ transporting, beta 3 polypeptide
| HGNCid = 806
| Symbol = ATP1B3
| AltSymbols =; ATPB-3; CD298; FLJ29027
| OMIM = 601867
| ECnumber =
| Homologene = 37510
| MGIid = 107788
  | Function = {{GNF_GO|id=GO:0005391 |text = sodium:potassium-exchanging ATPase activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005890 |text = sodium:potassium-exchanging ATPase complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 483
    | Hs_Ensembl = ENSG00000069849
    | Hs_RefseqProtein = XP_001133533
    | Hs_RefseqmRNA = XM_001133533
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 143078160
    | Hs_GenLoc_end = 143128072
    | Hs_Uniprot = P54709
    | Mm_EntrezGene = 11933
    | Mm_Ensembl = ENSMUSG00000032412
    | Mm_RefseqmRNA = NM_007502
    | Mm_RefseqProtein = NP_031528
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 96142036
    | Mm_GenLoc_end = 96173667
    | Mm_Uniprot = Q1WWL1
  }}
}}
'''ATPase, Na+/K+ transporting, beta 3 polypeptide''', also known as '''ATP1B3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP1B3 ATPase, Na+/K+ transporting, beta 3 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=483| accessdate = }}</ref> ATP1B3 has also been designated as '''CD298''' ([[cluster of differentiation]] 298).


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{{PBB Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes a beta 3 subunit. This gene encodes a beta 3 subunit. A pseudogene exists for this gene, and it is located on chromosome 2.<ref name="entrez">{{cite web | title = Entrez Gene: ATP1B3 ATPase, Na+/K+ transporting, beta 3 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=483| accessdate = }}</ref>
| summary_text = The protein encoded by this gene belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-[[Co-transport|coupled transport]] of a variety of organic and inorganic molecules, and for [[electrical excitability]] of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes a beta 3 subunit. A pseudogene exists for this gene, and it is located on chromosome 2.<ref name="entrez">{{cite web | title = Entrez Gene: ATP1B3 ATPase, Na+/K+ transporting, beta 3 polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=483| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Lingrel JB, Orlowski J, Shull MM, Price EM |title=Molecular genetics of Na,K-ATPase. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=38 |issue=  |pages= 37-89 |year= 1990 |pmid= 2158121 |doi=  }}
*{{cite journal  | vauthors=Lingrel JB, Orlowski J, Shull MM, Price EM |title=Molecular genetics of Na,K-ATPase |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=38 |issue=  |pages= 37–89 |year= 1990 |pmid= 2158121 |doi=10.1016/S0079-6603(08)60708-4  | series=Progress in Nucleic Acid Research and Molecular Biology  | isbn=978-0-12-540038-1 }}
*{{cite journal  | author=Jørgensen PL |title=Mechanism of the Na+, K+ pump. Protein structure and conformations of the pure (Na+ +K+)-ATPase. |journal=Biochim. Biophys. Acta |volume=694 |issue= 1 |pages= 27-68 |year= 1982 |pmid= 6289898 |doi=  }}
*{{cite journal  | author=Jørgensen PL |title=Mechanism of the Na+, K+ pump. Protein structure and conformations of the pure (Na+ +K+)-ATPase |journal=Biochim. Biophys. Acta |volume=694 |issue= 1 |pages= 27–68 |year= 1982 |pmid= 6289898 |doi=  10.1016/0304-4157(82)90013-2}}
*{{cite journal  | author=Malik N, Canfield VA, Beckers MC, ''et al.'' |title=Identification of the mammalian Na,K-ATPase 3 subunit. |journal=J. Biol. Chem. |volume=271 |issue= 37 |pages= 22754-8 |year= 1996 |pmid= 8798450 |doi=  }}
*{{cite journal  | vauthors=Chiampanichayakul S, Szekeres A, Khunkaewla P |title=Engagement of Na,K-ATPase beta3 subunit by a specific mAb suppresses T and B lymphocyte activation |journal=Int. Immunol. |volume=14 |issue= 12 |pages= 1407–14 |year= 2003 |pmid= 12456588 |doi=10.1093/intimm/dxf112 |display-authors=etal}}
*{{cite journal  | author=Malik N, Canfield V, Sanchez-Watts G, ''et al.'' |title=Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene. |journal=Mamm. Genome |volume=9 |issue= 2 |pages= 136-43 |year= 1998 |pmid= 9457675 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Chiampanichayakul S, Szekeres A, Khunkaewla P, ''et al.'' |title=Engagement of Na,K-ATPase beta3 subunit by a specific mAb suppresses T and B lymphocyte activation. |journal=Int. Immunol. |volume=14 |issue= 12 |pages= 1407-14 |year= 2003 |pmid= 12456588 |doi=  }}
*{{cite journal  | vauthors=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660–6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Chi A, Valencia JC, Hu ZZ |title=Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes |journal=J. Proteome Res. |volume=5 |issue= 11 |pages= 3135–44 |year= 2007 |pmid= 17081065 |doi= 10.1021/pr060363j |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Chiampanichayakul S, Khunkaewla P, Pata S, Kasinrerk W |title=Na, K ATPase beta3 subunit (CD298): association with alpha subunit and expression on peripheral blood cells |journal=Tissue Antigens |volume=68 |issue= 6 |pages= 509–17 |year= 2007 |pmid= 17176442 |doi= 10.1111/j.1399-0039.2006.00726.x }}
*{{cite journal  | author=Chi A, Valencia JC, Hu ZZ, ''et al.'' |title=Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. |journal=J. Proteome Res. |volume=5 |issue= 11 |pages= 3135-44 |year= 2007 |pmid= 17081065 |doi= 10.1021/pr060363j }}
*{{cite journal  | vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
*{{cite journal  | author=Chiampanichayakul S, Khunkaewla P, Pata S, Kasinrerk W |title=Na, K ATPase beta3 subunit (CD298): association with alpha subunit and expression on peripheral blood cells. |journal=Tissue Antigens |volume=68 |issue= 6 |pages= 509-17 |year= 2007 |pmid= 17176442 |doi= 10.1111/j.1399-0039.2006.00726.x }}
*{{cite journal  | vauthors=Aughey RJ, Murphy KT, Clark SA |title=Muscle Na+-K+-ATPase activity and isoform adaptations to intense interval exercise and training in well-trained athletes |journal=J. Appl. Physiol. |volume=103 |issue= 1 |pages= 39–47 |year= 2007 |pmid= 17446412 |doi= 10.1152/japplphysiol.00236.2006 |display-authors=etal}}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
*{{cite journal  | author=Aughey RJ, Murphy KT, Clark SA, ''et al.'' |title=Muscle Na+-K+-ATPase activity and isoform adaptations to intense interval exercise and training in well-trained athletes. |journal=J. Appl. Physiol. |volume=103 |issue= 1 |pages= 39-47 |year= 2007 |pmid= 17446412 |doi= 10.1152/japplphysiol.00236.2006 }}
}}
}}
{{refend}}
{{refend}}
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==External links==
==External links==
* {{MeshName|ATP1B3+protein,+human}}
* {{MeshName|ATP1B3+protein,+human}}
* {{UCSC gene info|ATP1B3}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{ATPases}}
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[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
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Latest revision as of 18:24, 29 August 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Wikidata
View/Edit Human

Sodium/potassium-transporting ATPase subunit beta-3 is an enzyme that in humans is encoded by the ATP1B3 gene.[1][2][3] ATP1B3 has also been designated as CD298 (cluster of differentiation 298).

The protein encoded by this gene belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes a beta 3 subunit. A pseudogene exists for this gene, and it is located on chromosome 2.[3]

References

  1. ↑ Malik N, Canfield VA, Beckers MC, Gros P, Levenson R (Nov 1996). "Identification of the mammalian Na,K-ATPase 3 subunit". J Biol Chem. 271 (37): 22754–8. doi:10.1074/jbc.271.37.22754. PMID 8798450.
  2. ↑ Malik N, Canfield V, Sanchez-Watts G, Watts AG, Scherer S, Beatty BG, Gros P, Levenson R (Mar 1998). "Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene". Mamm Genome. 9 (2): 136–43. doi:10.1007/s003359900704. PMID 9457675.
  3. ↑ 3.0 3.1 "Entrez Gene: ATP1B3 ATPase, Na+/K+ transporting, beta 3 polypeptide".

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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