ATP5PO

{{Short description|Protein-coding gene in the species Homo sapiens}}

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ATP synthase subunit O, mitochondrial is an enzyme that in humans is encoded by the ATP5PO gene.{{cite web | title = ATP5PO ATP synthase peripheral stalk subunit OSCP [ Homo sapiens (human) ]| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=539| accessdate = }}

The protein encoded by this gene is a component of the F-type ATPase found in the mitochondrial matrix. F-type ATPases are composed of a catalytic core and a membrane proton channel. The encoded protein appears to be part of the connector linking these two components and may be involved in transmission of conformational changes or proton conductance.

References

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Further reading

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  • {{cite journal | vauthors=Chen H, Morris MA, Rossier C |title=Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by exon trapping and mapping to chromosome 21q22.1-q22.2. |journal=Genomics |volume=28 |issue= 3 |pages= 470–6 |year= 1996 |pmid= 7490082 |doi=10.1006/geno.1995.1176 |display-authors=etal}}
  • {{cite journal | vauthors=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=10.1016/0378-1119(94)90802-8 }}
  • {{cite journal | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |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=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
  • {{cite journal | vauthors=Hattori M, Fujiyama A, Taylor TD |title=The DNA sequence of human chromosome 21 |journal=Nature |volume=405 |issue= 6784 |pages= 311–9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 |bibcode=2000Natur.405..311H |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Aggeler R, Coons J, Taylor SW |title=A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 33906–12 |year= 2002 |pmid= 12110673 |doi= 10.1074/jbc.M204538200 |display-authors=etal|doi-access= free}}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Gevaert K, Goethals M, Martens L |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 |s2cid=23783563 |display-authors=etal}}
  • {{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |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 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}}
  • {{cite journal | vauthors=Johnson KM, Chen X, Boitano A |title=Identification and validation of the mitochondrial F1F0-ATPase as the molecular target of the immunomodulatory benzodiazepine Bz-423 |journal=Chem. Biol. |volume=12 |issue= 4 |pages= 485–96 |year= 2005 |pmid= 15850986 |doi= 10.1016/j.chembiol.2005.02.012 |display-authors=etal|doi-access=free }}

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