ATP5F1

ATP5F1

ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1, also known as ATP5F1, is a human gene.cite web | title = Entrez Gene: ATP5F1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=515| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the b subunit of the proton channel.cite web | title = Entrez Gene: ATP5F1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=515| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Higuti T, Tsurumi C, Osaka F, "et al." |title=Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 3 |pages= 1014–20 |year= 1991 |pmid= 1831354 |doi=
*cite journal | author=Gay NJ, Walker JE |title=Two genes encoding the bovine mitochondrial ATP synthase proteolipid specify precursors with different import sequences and are expressed in a tissue-specific manner. |journal=EMBO J. |volume=4 |issue= 13A |pages= 3519–24 |year= 1986 |pmid= 2868890 |doi=
*cite journal | author=Farrell LB, Nagley P |title=Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex. |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue= 3 |pages= 1257–64 |year= 1987 |pmid= 2883974 |doi=
*cite journal | author=Houstĕk J, Andersson U, Tvrdík P, "et al." |title=The expression of subunit c correlates with and thus may limit the biosynthesis of the mitochondrial F0F1-ATPase in brown adipose tissue. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7689–94 |year= 1995 |pmid= 7706317 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Elston T, Wang H, Oster G |title=Energy transduction in ATP synthase. |journal=Nature |volume=391 |issue= 6666 |pages= 510–3 |year= 1998 |pmid= 9461222 |doi= 10.1038/35185
*cite journal | author=Wang H, Oster G |title=Energy transduction in the F1 motor of ATP synthase. |journal=Nature |volume=396 |issue= 6708 |pages= 279–82 |year= 1998 |pmid= 9834036 |doi= 10.1038/24409
*cite journal | author=Jia L, Young MF, Powell J, "et al." |title=Gene expression profile of human bone marrow stromal cells: high-throughput expressed sequence tag sequencing analysis. |journal=Genomics |volume=79 |issue= 1 |pages= 7–17 |year= 2002 |pmid= 11827452 |doi= 10.1006/geno.2001.6683
*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=Cross RL |title=Molecular motors: turning the ATP motor. |journal=Nature |volume=427 |issue= 6973 |pages= 407–8 |year= 2004 |pmid= 14749816 |doi= 10.1038/427407b
*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=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=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

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


Wikimedia Foundation. 2010.

Игры ⚽ Нужно сделать НИР?

Look at other dictionaries:

  • 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

  • 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

  • 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

  • Cotransporter — A cotransporter is an integral membrane protein that is involved in secondary active transport. It works by binding to two molecules or ions at a time and using the gradient of one solute s concentration to force the other molecule or ion against …   Wikipedia

  • Band 3 — Solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group) Atomic microscope image of Band 3 …   Wikipedia

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

  • Sodium-glucose transport proteins — solute carrier family 5 (sodium/glucose cotransporter), member 1 Identifiers Symbol SLC5A1 Alt. symbols SGLT1 Entrez …   Wikipedia

  • Sodium-chloride symporter — Solute carrier family 12 (sodium/chloride transporters), member 3 Identifiers Symbols SLC12A3; FLJ96318; NCCT; TSC External IDs …   Wikipedia

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

  • Chloride potassium symporter 5 — Solute carrier family 12 (potassium/chloride transporter), member 5 Identifiers Symbols SLC12A5; KCC2; KIAA1176 External IDs …   Wikipedia

Share the article and excerpts

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