COX4I2

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Cytochrome c oxidase subunit IV isoform 2 (lung)
Identifiers
Symbols COX4I2 ; COX4; COX4-2; COX4B; COX4L2; COXIV-2; dJ857M17.2
External IDs Template:OMIM5 Template:MGI HomoloGene13082
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Cytochrome c oxidase subunit IV isoform 2 (lung), also known as COX4I2, is a human gene.[1]

Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.[1]

References

  1. 1.0 1.1 "Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)".

Further reading

  • Lynch SR, Sherman D, Copeland RA (1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase". J. Biol. Chem. 267 (1): 298–302. PMID 1309738.
  • Garber EA, Margoliash E (1990). "Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition". Biochim. Biophys. Acta. 1015 (2): 279–87. PMID 2153405.
  • Bolli R, Nałecz KA, Azzi A (1985). "The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase". Biochimie. 67 (1): 119–28. PMID 2986725.
  • Michel B, Bosshard HR (1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase". J. Biol. Chem. 259 (16): 10085–91. PMID 6088481.
  • Hare JF, Ching E, Attardi G (1980). "Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase". Biochemistry. 19 (10): 2023–30. PMID 6246917.
  • Papadopoulou LC, Tsiftsoglou AS (1996). "Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin)". Biochem. Pharmacol. 52 (5): 713–22. PMID 8765469.
  • Wiedemann FR, Vielhaber S, Schröder R; et al. (2000). "Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples". Anal. Biochem. 279 (1): 55–60. doi:10.1006/abio.1999.4434. PMID 10683230.
  • Hüttemann M, Kadenbach B, Grossman LI (2001). "Mammalian subunit IV isoforms of cytochrome c oxidase". Gene. 267 (1): 111–23. PMID 11311561.
  • Sampson V, Alleyne T (2002). "Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover". Eur. J. Biochem. 268 (24): 6534–44. PMID 11737208.
  • Deloukas P, Matthews LH, Ashurst J; et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
  • Vizirianakis IS, Pappas IS, Tsiftsoglou AS (2002). "Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells". Biochem. Pharmacol. 63 (5): 1009–17. PMID 11911854.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Fukuda R, Zhang H, Kim JW; et al. (2007). "HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells". Cell. 129 (1): 111–22. doi:10.1016/j.cell.2007.01.047. PMID 17418790.

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