ATP13A3

ATP13A3

ATPase type 13A3, also known as ATP13A3, is a human gene.cite web | title = Entrez Gene: ATP13A3 ATPase type 13A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79572| accessdate = ]

PBB_Summary
section_title =
summary_text =

References

Further reading

PBB_Further_reading
citations =
*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=Wick M, Bürger C, Brüsselbach S, "et al." |title=Identification of serum-inducible genes: different patterns of gene regulation during G0-->S and G1-->S progression. |journal=J. Cell. Sci. |volume=107 ( Pt 1) |issue= |pages= 227–39 |year= 1994 |pmid= 8175911 |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=Habtemichael N, Kovacs G |title=Cloning the AFURS1 gene which is up-regulated in senescent human parenchymal kidney cells. |journal=Gene |volume=283 |issue= 1-2 |pages= 271–5 |year= 2002 |pmid= 11867234 |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=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=Suzuki Y, Yamashita R, Shirota M, "et al." |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711–8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604
*cite journal | author=Otsuki T, Ota T, Nishikawa T, "et al." |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117
*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=Muzny DM, Scherer SE, Kaul R, "et al." |title=The DNA sequence, annotation and analysis of human chromosome 3. |journal=Nature |volume=440 |issue= 7088 |pages= 1194–8 |year= 2006 |pmid= 16641997 |doi= 10.1038/nature04728
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026

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


Wikimedia Foundation. 2010.

Игры ⚽ Поможем решить контрольную работу

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”