ATP2B3

ATP2B3

ATPase, Ca++ transporting, plasma membrane 3, also known as ATP2B3, is a human gene.cite web | title = Entrez Gene: ATP2B3 ATPase, Ca++ transporting, plasma membrane 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=492| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 3. Alternatively spliced transcript variants encoding different isoforms have been identified.cite web | title = Entrez Gene: ATP2B3 ATPase, Ca++ transporting, plasma membrane 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=492| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Møller JV, Juul B, le Maire M |title=Structural organization, ion transport, and energy transduction of P-type ATPases. |journal=Biochim. Biophys. Acta |volume=1286 |issue= 1 |pages= 1–51 |year= 1996 |pmid= 8634322 |doi=
*cite journal | author=Strehler EE, Zacharias DA |title=Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. |journal=Physiol. Rev. |volume=81 |issue= 1 |pages= 21–50 |year= 2001 |pmid= 11152753 |doi=
*cite journal | author=Strehler EE, Treiman M |title=Calcium pumps of plasma membrane and cell interior. |journal=Curr. Mol. Med. |volume=4 |issue= 3 |pages= 323–35 |year= 2004 |pmid= 15101689 |doi=
*cite journal | author=Brandt P, Neve RL, Kammesheidt A, "et al." |title=Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels. |journal=J. Biol. Chem. |volume=267 |issue= 7 |pages= 4376–85 |year= 1992 |pmid= 1531651 |doi=
*cite journal | author=Stauffer TP, Hilfiker H, Carafoli E, Strehler EE |title=Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. |journal=J. Biol. Chem. |volume=269 |issue= 50 |pages= 32022 |year= 1995 |pmid= 7989379 |doi=
*cite journal | author=Wang MG, Yi H, Hilfiker H, "et al." |title=Localization of two genes encoding plasma membrane Ca2+ ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26-->p25 and Xq28, respectively. |journal=Cytogenet. Cell Genet. |volume=67 |issue= 1 |pages= 41–5 |year= 1994 |pmid= 8187550 |doi=
*cite journal | author=Stauffer TP, Hilfiker H, Carafoli E, Strehler EE |title=Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25993–6003 |year= 1994 |pmid= 8245032 |doi=
*cite journal | author=Brown BJ, Hilfiker H, DeMarco SJ, "et al." |title=Primary structure of human plasma membrane Ca(2+)-ATPase isoform 3. |journal=Biochim. Biophys. Acta |volume=1283 |issue= 1 |pages= 10–3 |year= 1996 |pmid= 8765088 |doi=
*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=Mallon AM, Platzer M, Bate R, "et al." |title=Comparative genome sequence analysis of the Bpa/Str region in mouse and Man. |journal=Genome Res. |volume=10 |issue= 6 |pages= 758–75 |year= 2000 |pmid= 10854409 |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=Moreau R, Daoud G, Masse A, "et al." |title=Expression and role of calcium-ATPase pump and sodium-calcium exchanger in differentiated trophoblasts from human term placenta. |journal=Mol. Reprod. Dev. |volume=65 |issue= 3 |pages= 283–8 |year= 2004 |pmid= 12784250 |doi= 10.1002/mrd.10303
*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=Martin R, Harvey NC, Crozier SR, "et al." |title=Placental calcium transporter (PMCA3) gene expression predicts intrauterine bone mineral accrual. |journal=Bone |volume=40 |issue= 5 |pages= 1203–8 |year= 2007 |pmid= 17336174 |doi= 10.1016/j.bone.2006.12.060

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


Wikimedia Foundation. 2010.

Игры ⚽ Поможем сделать НИР

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”