ATP12A

ATP12A

ATPase, H+/K+ transporting, nongastric, alpha polypeptide, also known as ATP12A, is a human gene.cite web | title = Entrez Gene: ATP12A ATPase, H+/K+ transporting, nongastric, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=479| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene belongs to the family of P-type cation transport ATPases. This gene encodes a catalytic subunit of the ouabain-sensitive H+/K+ -ATPase that catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. It is also responsible for potassium absorption in various tissues.cite web | title = Entrez Gene: ATP12A ATPase, H+/K+ transporting, nongastric, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=479| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Modyanov NN, Petrukhin KE, Sverdlov VE, "et al." |title=The family of human Na,K-ATPase genes. ATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase. |journal=FEBS Lett. |volume=278 |issue= 1 |pages= 91–4 |year= 1991 |pmid= 1847115 |doi=
*cite journal | author=Yang-Feng TL, Schneider JW, Lindgren V, "et al." |title=Chromosomal localization of human Na+, K+-ATPase alpha- and beta-subunit genes. |journal=Genomics |volume=2 |issue= 2 |pages= 128–38 |year= 1988 |pmid= 2842249 |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=Grishin AV, Sverdlov VE, Kostina MB, Modyanov NN |title=Cloning and characterization of the entire cDNA encoded by ATP1AL1--a member of the human Na,K/H,K-ATPase gene family. |journal=FEBS Lett. |volume=349 |issue= 1 |pages= 144–50 |year= 1994 |pmid= 8045293 |doi=
*cite journal | author=Sverdlov VE, Kostina MB, Modyanov NN |title=Genomic organization of the human ATP1AL1 gene encoding a ouabain-sensitive H,K-ATPase. |journal=Genomics |volume=32 |issue= 3 |pages= 317–27 |year= 1997 |pmid= 8838794 |doi= 10.1006/geno.1996.0125
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Pestov NB, Romanova LG, Korneenko TV, "et al." |title=Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian genes encoding the catalytic alpha subunit. |journal=FEBS Lett. |volume=440 |issue= 3 |pages= 320–4 |year= 1999 |pmid= 9872395 |doi=
*cite journal | author=Pestov NB, Korneenko TV, Adams G, "et al." |title=Nongastric H-K-ATPase in rodent prostate: lobe-specific expression and apical localization. |journal=Am. J. Physiol., Cell Physiol. |volume=282 |issue= 4 |pages= C907–16 |year= 2002 |pmid= 11880279 |doi= 10.1152/ajpcell.00258.2001
*cite journal | author=Reinhardt J, Kosch M, Lerner M, "et al." |title=Stimulation of protein kinase C pathway mediates endocytosis of human nongastric H+-K+-ATPase, ATP1AL1. |journal=Am. J. Physiol. Renal Physiol. |volume=283 |issue= 2 |pages= F335–43 |year= 2002 |pmid= 12110518 |doi= 10.1152/ajprenal.00226.2001
*cite journal | author=Takahashi Y, Sakai H, Kuragari M, "et al." |title=Expression of ATP1AL1, a non-gastric proton pump, in human colorectum. |journal=Jpn. J. Physiol. |volume=52 |issue= 3 |pages= 317–21 |year= 2003 |pmid= 12230809 |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=Li J, Codina J, Petroske E, "et al." |title=The carboxy terminus of the colonic H(+), K(+)-ATPase alpha-subunit is required for stable beta subunit assembly and function. |journal=Kidney Int. |volume=65 |issue= 4 |pages= 1301–10 |year= 2004 |pmid= 15086469 |doi= 10.1111/j.1523-1755.2004.00507.x
*cite journal | author=Johansson M, Jansson T, Pestov NB, Powell TL |title=Non-gastric H+/K+ ATPase is present in the microvillous membrane of the human placental syncytiotrophoblast. |journal=Placenta |volume=25 |issue= 6 |pages= 505–11 |year= 2004 |pmid= 15135233 |doi= 10.1016/j.placenta.2003.11.008
*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

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


Wikimedia Foundation. 2010.

Игры ⚽ Нужно решить контрольную?

Look at other dictionaries:

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

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

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

  • 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

  • Kinesin — Animation of kinesin walking on a microtubule The kinesin dimer attaches to, and mo …   Wikipedia

Share the article and excerpts

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