FXN

FXN
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген Фратаксин[d][1]
Молекуляр функция связывание с белками плазмы[d][2][3][4], iron chaperone activity[d][5], 2 iron, 2 sulfur cluster binding[d][6], oxidoreductase activity[d][7], ferrous iron binding[d][8][5][6], связывание с ионом металла[d][7], ferric iron binding[d][9][6][10], ferroxidase activity[d][9][9][11], ferroxidase activity[d][7][7][12][…], ferrous iron binding[d][13][14][4][…], ferric iron binding[d][7][13][15][…], iron chaperone activity[d][4][16] һәм 2 iron, 2 sulfur cluster binding[d][13][16]
Күзәнәк компоненты цитоплазма[7], цитозоль[d][7][17], митохондриальный матрикс[d][7][14][7], митохондрия[9][9][18], L-cysteine desulfurase complex[d][19] һәм митохондрия[7][7][7][…]
Биологик процесс regulation of ferrochelatase activity[d][4], позитивная регуляция пролиферации клеток[d][20], response to iron ion[d][21], iron-sulfur cluster assembly[d][9], ion transport[d][7], positive regulation of aconitate hydratase activity[d][20], positive regulation of cell growth[d][22], cellular response to hydrogen peroxide[d][12], negative regulation of release of cytochrome c from mitochondria[d][23], positive regulation of succinate dehydrogenase activity[d][20], protein autoprocessing[d][13], негативная регуляция апоптоза[d][23], small molecule metabolic process[d][7], iron ion homeostasis[d][7], iron incorporation into metallo-sulfur cluster[d][6], cellular iron ion homeostasis[d][24][9], Биосинтез гема[d][4][7], positive regulation of lyase activity[d][20][25], positive regulation of catalytic activity[d][22], iron-sulfur cluster assembly[d][7][7][19], оксидлашулы фосфориллау[d][7], cellular iron ion homeostasis[d][20][7][7][…], mitochondrion organization[d][7][16], adult walking behavior[d][7], аэробное дыхание[d][7], embryo development ending in birth or egg hatching[d][7], iron incorporation into metallo-sulfur cluster[d][13][16], проприоцепция[d][7], negative regulation of multicellular organism growth[d][7] һәм negative regulation of organ growth[d][7]
Изображение Gene Atlas
 FXN Викиҗыентыкта

FXN (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[26][27]

  1. 1,0 1,1 UniProt
  2. Shan Y., Cortopassi G. Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly // MitochondrionElsevier BV, 2015. — ISSN 1567-7249; 1872-8278doi:10.1016/J.MITO.2015.12.005PMID:26702583
  3. Vázquez-Manrique R. P., Sanz P., Palau F. Frataxin interacts functionally with mitochondrial electron transport chain proteins // Human Molecular GeneticsOUP, 2005. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDI214PMID:15961414
  4. 4,0 4,1 4,2 4,3 4,4 Yoon T., Cowan J. A. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.C400107200PMID:15123683
  5. 5,0 5,1 Yoon T., Cowan J. A. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.C400107200PMID:15123683
  6. 6,0 6,1 6,2 6,3 Yoon T., Cowan J. A. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S clusters in ISU-type proteins] // J. Am. Chem. Soc. / P. J. StangACS, 2003. — ISSN 0002-7863; 1520-5126; 1943-2984doi:10.1021/JA027967IPMID:12785837
  7. 7,00 7,01 7,02 7,03 7,04 7,05 7,06 7,07 7,08 7,09 7,10 7,11 7,12 7,13 7,14 7,15 7,16 7,17 7,18 7,19 7,20 7,21 7,22 7,23 7,24 7,25 7,26 7,27 GOA
  8. Yoon T., Dizin E., Cowan J. A. N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins // Journal of Biological Inorganic ChemistrySpringer Science+Business Media, 2007. — ISSN 0949-8257; 1432-1327doi:10.1007/S00775-007-0205-2PMID:17285345
  9. 9,0 9,1 9,2 9,3 9,4 9,5 9,6 GOA
  10. Pastore A., Adinolfi S., Gomes C. M. Dynamics, stability and iron-binding activity of frataxin clinical mutants // FEBS J.Wiley-Blackwell, 2008. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033doi:10.1111/J.1742-4658.2008.06512.XPMID:18537827
  11. Heather A O'Neill, Gakh O., Park S. et al. Assembly of human frataxin is a mechanism for detoxifying redox-active iron // Biochemistry / A. SchepartzACS, 2005. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI048459JPMID:15641778
  12. 12,0 12,1 Heather A O'Neill, Gakh O., Park S. et al. Assembly of human frataxin is a mechanism for detoxifying redox-active iron // Biochemistry / A. SchepartzACS, 2005. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI048459JPMID:15641778
  13. 13,0 13,1 13,2 13,3 13,4 Yoon T., Cowan J. A. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S clusters in ISU-type proteins] // J. Am. Chem. Soc. / P. J. StangACS, 2003. — ISSN 0002-7863; 1520-5126; 1943-2984doi:10.1021/JA027967IPMID:12785837
  14. 14,0 14,1 Yoon T., Dizin E., Cowan J. A. N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins // Journal of Biological Inorganic ChemistrySpringer Science+Business Media, 2007. — ISSN 0949-8257; 1432-1327doi:10.1007/S00775-007-0205-2PMID:17285345
  15. Pastore A., Adinolfi S., Gomes C. M. Dynamics, stability and iron-binding activity of frataxin clinical mutants // FEBS J.Wiley-Blackwell, 2008. — ISSN 1742-464X; 0014-2956; 1742-4658; 1432-1033doi:10.1111/J.1742-4658.2008.06512.XPMID:18537827
  16. 16,0 16,1 16,2 16,3 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform.OUP, 2011. — ISSN 1467-5463; 1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  17. Condò I., Ventura N., Malisan F. et al. In vivo maturation of human frataxin // Human Molecular GeneticsOUP, 2007. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDM102PMID:17468497
  18. Condò I., Ventura N., Malisan F. et al. In vivo maturation of human frataxin // Human Molecular GeneticsOUP, 2007. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDM102PMID:17468497
  19. 19,0 19,1 Missirlis F., Leimkühler S. Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism // Frontiers in PhysiologyFrontiers Media, 2018. — ISSN 1664-042Xdoi:10.3389/FPHYS.2018.00050PMID:29491838
  20. 20,0 20,1 20,2 20,3 20,4 Verardi R., Cavadini P., Zanella I. et al. The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin // Biochim. Biophys. ActaElsevier BV, 2008. — ISSN 0006-3002; 1878-2434doi:10.1016/J.BBADIS.2007.11.006PMID:18160053
  21. Li K., Besse E. K., Ha D. et al. Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia // Human Molecular GeneticsOUP, 2008. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDN127PMID:18424449
  22. 22,0 22,1 Mühlenhoff U., Lill R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin // Human Molecular GeneticsOUP, 2004. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDH324PMID:15509595
  23. 23,0 23,1 Condò I., Ventura N., Malisan F. et al. A pool of extramitochondrial frataxin that promotes cell survival // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2006. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M511960200PMID:16608849
  24. Verardi R., Cavadini P., Zanella I. et al. The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin // Biochim. Biophys. ActaElsevier BV, 2008. — ISSN 0006-3002; 1878-2434doi:10.1016/J.BBADIS.2007.11.006PMID:18160053
  25. Guccini I., Condò I., Malisan F. Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin // Human Molecular GeneticsOUP, 2010. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDP592PMID:20053667
  26. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  27. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)