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] |
|
FXN Викиҗыентыкта |
FXN (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[26][27]
- ↑ 1,0 1,1 UniProt
- ↑ Shan Y., Cortopassi G. Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly // Mitochondrion — Elsevier BV, 2015. — ISSN 1567-7249; 1872-8278 — doi:10.1016/J.MITO.2015.12.005 — PMID:26702583
- ↑ Vázquez-Manrique R. P., Sanz P., Palau F. Frataxin interacts functionally with mitochondrial electron transport chain proteins // Human Molecular Genetics — OUP, 2005. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDI214 — PMID:15961414
- ↑ 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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.C400107200 — PMID:15123683
- ↑ 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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.C400107200 — PMID:15123683
- ↑ 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. Stang — ACS, 2003. — ISSN 0002-7863; 1520-5126; 1943-2984 — doi:10.1021/JA027967I — PMID:12785837
- ↑ 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
- ↑ 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 Chemistry — Springer Science+Business Media, 2007. — ISSN 0949-8257; 1432-1327 — doi:10.1007/S00775-007-0205-2 — PMID:17285345
- ↑ 9,0 9,1 9,2 9,3 9,4 9,5 9,6 GOA
- ↑ 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; 1432-1033 — doi:10.1111/J.1742-4658.2008.06512.X — PMID:18537827
- ↑ Heather A O'Neill, Gakh O., Park S. et al. Assembly of human frataxin is a mechanism for detoxifying redox-active iron // Biochemistry / A. Schepartz — ACS, 2005. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI048459J — PMID:15641778
- ↑ 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. Schepartz — ACS, 2005. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI048459J — PMID:15641778
- ↑ 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. Stang — ACS, 2003. — ISSN 0002-7863; 1520-5126; 1943-2984 — doi:10.1021/JA027967I — PMID:12785837
- ↑ 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 Chemistry — Springer Science+Business Media, 2007. — ISSN 0949-8257; 1432-1327 — doi:10.1007/S00775-007-0205-2 — PMID:17285345
- ↑ 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; 1432-1033 — doi:10.1111/J.1742-4658.2008.06512.X — PMID:18537827
- ↑ 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; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
- ↑ Condò I., Ventura N., Malisan F. et al. In vivo maturation of human frataxin // Human Molecular Genetics — OUP, 2007. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDM102 — PMID:17468497
- ↑ Condò I., Ventura N., Malisan F. et al. In vivo maturation of human frataxin // Human Molecular Genetics — OUP, 2007. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDM102 — PMID:17468497
- ↑ 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 Physiology — Frontiers Media, 2018. — ISSN 1664-042X — doi:10.3389/FPHYS.2018.00050 — PMID:29491838
- ↑ 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. Acta — Elsevier BV, 2008. — ISSN 0006-3002; 1878-2434 — doi:10.1016/J.BBADIS.2007.11.006 — PMID:18160053
- ↑ Li K., Besse E. K., Ha D. et al. Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia // Human Molecular Genetics — OUP, 2008. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDN127 — PMID:18424449
- ↑ 22,0 22,1 Mühlenhoff U., Lill R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin // Human Molecular Genetics — OUP, 2004. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDH324 — PMID:15509595
- ↑ 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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2006. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M511960200 — PMID:16608849
- ↑ 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. Acta — Elsevier BV, 2008. — ISSN 0006-3002; 1878-2434 — doi:10.1016/J.BBADIS.2007.11.006 — PMID:18160053
- ↑ Guccini I., Condò I., Malisan F. Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin // Human Molecular Genetics — OUP, 2010. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDP592 — PMID:20053667
- ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
- ↑ 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.)