ATP1A4

ATP1A4

ATPase, Na+/K+ transporting, alpha 4 polypeptide, also known as ATP1A4, is a human gene.cite web | title = Entrez Gene: ATP1A4 ATPase, Na+/K+ transporting, alpha 4 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=480| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene belongs to the family of P-type cation transport ATPases, 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 catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 4 subunit. Alternatively spliced transcript variants encoding different isoforms have been identified.cite web | title = Entrez Gene: ATP1A4 ATPase, Na+/K+ transporting, alpha 4 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=480| accessdate = ]

References

Further reading

PBB_Further_reading
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 | author=Buetow KH, Nishimura D, Nakamura Y, "et al." |title=A detailed multipoint gene map of chromosome 1q. |journal=Genomics |volume=8 |issue= 1 |pages= 13–21 |year= 1991 |pmid= 1981991 |doi=
*cite journal | author=Sverdlov ED, Broude NE, Sverdlov VE, "et al." |title=Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism. |journal=FEBS Lett. |volume=221 |issue= 1 |pages= 129–33 |year= 1987 |pmid= 2887455 |doi=
*cite journal | author=Shull MM, Lingrel JB |title=Multiple genes encode the human Na+,K+-ATPase catalytic subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 12 |pages= 4039–43 |year= 1987 |pmid= 3035563 |doi=
*cite journal | author=Sverdlov ED, Monastyrskaya GS, Broude NE, "et al." |title=The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. |journal=FEBS Lett. |volume=217 |issue= 2 |pages= 275–8 |year= 1987 |pmid= 3036582 |doi=
*cite journal | author=Shamraj OI, Lingrel JB |title=A putative fourth Na+,K(+)-ATPase alpha-subunit gene is expressed in testis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 26 |pages= 12952–6 |year= 1995 |pmid= 7809153 |doi=
*cite journal | author=Woo AL, James PF, Lingrel JB |title=Characterization of the fourth alpha isoform of the Na, K-ATPase. |journal=J. Membr. Biol. |volume=169 |issue= 1 |pages= 39–44 |year= 1999 |pmid= 10227850 |doi=
*cite journal | author=Woo AL, James PF, Lingrel JB |title=Sperm motility is dependent on a unique isoform of the Na, K-ATPase. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20693–9 |year= 2000 |pmid= 10764792 |doi= 10.1074/jbc. M002323200
*cite journal | author=Woo AL, James PF, Lingrel JB |title=Roles of the Na, K-ATPase alpha4 isoform and the Na+/H+ exchanger in sperm motility. |journal=Mol. Reprod. Dev. |volume=62 |issue= 3 |pages= 348–56 |year= 2003 |pmid= 12112599 |doi= 10.1002/mrd.90002
*cite journal | author=Keryanov S, Gardner KL |title=Physical mapping and characterization of the human Na, K-ATPase isoform, ATP1A4. |journal=Gene |volume=292 |issue= 1-2 |pages= 151–66 |year= 2002 |pmid= 12119109 |doi=
*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 | author=Lingrel J, Moseley A, Dostanic I, "et al." |title=Functional roles of the alpha isoforms of the Na, K-ATPase. |journal=Ann. N. Y. Acad. Sci. |volume=986 |issue= |pages= 354–9 |year= 2003 |pmid= 12763850 |doi=
*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 | 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 | author=Hlivko JT, Chakraborty S, Hlivko TJ, "et al." |title=The human Na, K-ATPase alpha 4 isoform is an ouabain-sensitive alpha isoform that is expressed in sperm. |journal=Mol. Reprod. Dev. |volume=73 |issue= 1 |pages= 101–15 |year= 2006 |pmid= 16175638 |doi= 10.1002/mrd.20383
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727
*cite journal | author=Rodova M, Nguyen AN, Blanco G |title=The transcription factor CREMtau and cAMP regulate promoter activity of the Na, K-ATPase alpha4 isoform. |journal=Mol. Reprod. Dev. |volume=73 |issue= 11 |pages= 1435–47 |year= 2006 |pmid= 16894555 |doi= 10.1002/mrd.20518

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать реферат

Look at other dictionaries:

  • P-type ATPase — Calcium ATPase, E2 Pi state Identifiers Symbol E1 E2 ATPase Pfam …   Wikipedia

  • Na+/K+-ATPase — Flow of ions. Alpha and beta units …   Wikipedia

  • ATP7A — ATPase, Cu++ transporting, alpha polypeptide PDB rendering based on 1aw0 …   Wikipedia

  • ATPase — ATPases are a class of enzymes that catalyze the decomposition of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and a free phosphate ion. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses… …   Wikipedia

  • ATP synthase — Molecular model of ATP synthase by X ray diffraction method ATP synthase (EC 3.6.3.14) is an important enzyme that provides energy for the cell to use through the synthesis of adenosine triphosphate (ATP). ATP is the most commonly used energy… …   Wikipedia

  • Na⁺/K⁺-ATPase — [ thumb|200px|Sodium potassium pump, E2 Pi state. Calculated hydrocarbon boundaries of the lipid bilayer are shown as blue (intracellular) and red (extracellular) planes] Na+/K+ ATPase (also known as the Na+/K+ pump, sodium potassium pump, or… …   Wikipedia

  • Small GTPase — Small GTPases are a family of hydrolase enzymes that can bind and hydrolyze guanosine triphosphate (GTP). They are a form of G proteins found in the cytosol which are homologous to the alpha subunit of heterotrimeric G proteins, but unlike the… …   Wikipedia

  • Helicase — Structure of E. coli helicase RuvA Helicases are a class of enzymes vital to all living organisms. They are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two annealed nucleic acid strands (i.e.,… …   Wikipedia

  • Myosin — Part of the myosin II structure. Atoms in the heavy chain are colored red on the left hand side, and atoms in the light chains are colored orange and yellow. Myosins comprise a family of ATP dependent motor proteins and are best known for their… …   Wikipedia

  • Membrane transport protein — A membrane transport protein (or simply transporter) is a membrane protein[1] involved in the movement of ions, small molecules, or macromolecules, such as another protein across a biological membrane. Transport proteins are integral membrane… …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”