ATP2B1

ATP2B1

ATPase, Ca++ transporting, plasma membrane 1, also known as ATP2B1, is a human gene.cite web | title = Entrez Gene: ATP2B1 ATPase, Ca++ transporting, plasma membrane 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=490| 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 1. Alternatively spliced transcript variants encoding different isoforms have been identified.cite web | title = Entrez Gene: ATP2B1 ATPase, Ca++ transporting, plasma membrane 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=490| 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=Kessler F, Falchetto R, Heim R, "et al." |title=Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump. |journal=Biochemistry |volume=31 |issue= 47 |pages= 11785–92 |year= 1992 |pmid= 1332771 |doi=
*cite journal | author=Olson S, Wang MG, Carafoli E, "et al." |title=Localization of two genes encoding plasma membrane Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and 12q21-23. |journal=Genomics |volume=9 |issue= 4 |pages= 629–41 |year= 1991 |pmid= 1674727 |doi=
*cite journal | author=Wang KK, Wright LC, Machan CL, "et al." |title=Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes. |journal=J. Biol. Chem. |volume=266 |issue= 14 |pages= 9078–85 |year= 1991 |pmid= 1827443 |doi=
*cite journal | author=Strehler EE, Strehler-Page MA, Vogel G, Carafoli E |title=mRNAs for plasma membrane calcium pump isoforms differing in their regulatory domain are generated by alternative splicing that involves two internal donor sites in a single exon. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 18 |pages= 6908–12 |year= 1989 |pmid= 2528729 |doi=
*cite journal | author=James PH, Pruschy M, Vorherr TE, "et al." |title=Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump. |journal=Biochemistry |volume=28 |issue= 10 |pages= 4253–8 |year= 1989 |pmid= 2548572 |doi=
*cite journal | author=Verma AK, Filoteo AG, Stanford DR, "et al." |title=Complete primary structure of a human plasma membrane Ca2+ pump. |journal=J. Biol. Chem. |volume=263 |issue= 28 |pages= 14152–9 |year= 1988 |pmid= 2844759 |doi=
*cite journal | author=Howard A, Legon S, Walters JR |title=Human and rat intestinal plasma membrane calcium pump isoforms. |journal=Am. J. Physiol. |volume=265 |issue= 5 Pt 1 |pages= G917–25 |year= 1993 |pmid= 7694502 |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=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=Kumar R, Haugen JD, Penniston JT |title=Molecular cloning of a plasma membrane calcium pump from human osteoblasts. |journal=J. Bone Miner. Res. |volume=8 |issue= 4 |pages= 505–13 |year= 1993 |pmid= 8386431 |doi=
*cite journal | author=Hilfiker H, Strehler-Page MA, Stauffer TP, "et al." |title=Structure of the gene encoding the human plasma membrane calcium pump isoform 1. |journal=J. Biol. Chem. |volume=268 |issue= 26 |pages= 19717–25 |year= 1993 |pmid= 8396145 |doi=
*cite journal | author=Andersson B, Wentland MA, Ricafrente JY, "et al." |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138
*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=Benkwitz C, Kubisch C, Kraft K, Neyses L |title=Investigation of the Met-267 Arg exchange in isoform 1 of the human plasma membrane calcium pump in patients with essential hypertension by the amplification-created restriction site technique. |journal=J. Mol. Med. |volume=75 |issue= 1 |pages= 62–6 |year= 1997 |pmid= 9020386 |doi=
*cite journal | author=Yu W, Andersson B, Worley KC, "et al." |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=
*cite journal | author=Elshorst B, Hennig M, Försterling H, "et al." |title=NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. |journal=Biochemistry |volume=38 |issue= 38 |pages= 12320–32 |year= 1999 |pmid= 10493800 |doi=

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


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

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”