HFE

HFE
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген HFE[d][1]
Молекуляр функция peptide antigen binding[d][2][3], beta-2-microglobulin binding[d][3][4][5], co-receptor binding[d][6], связывание с белками плазмы[d][7][8][9], transferrin receptor binding[d][10][11][12][…], signaling receptor binding[d][13][14], natural killer cell lectin-like receptor binding[d][15] һәм transferrin receptor binding[d][4][3][16][…]
Күзәнәк компоненты мембрана өлеше[d][17], recycling endosome[d][7], HFE-transferrin receptor complex[d][17][17][18][…], мембрана[d][17], basal part of cell[d][7], күзәнәк мембранасы[d][19][20][19], apical part of cell[d][17][7], күзәнәк мембранасы өлеше[d][13], terminal web[d][17], early endosome[d][7], MHC class I protein complex[d][2][3], perinuclear region of cytoplasm[d][7][5], цитоплазматическая везикула[d][7][18], наружная сторона клеточной мембраны[d][21], күзәнәк тышындагы мохит[d][22], күзәнәк мембранасы[d][17][13][17][…], күзәнәк тышындагы мохит[d][23][24] һәм наружная сторона клеточной мембраны[d][14][24]
Биологик процесс negative regulation of T cell antigen processing and presentation[d][17], positive regulation of peptide hormone secretion[d][23], positive regulation of receptor-mediated endocytosis[d][16], cellular response to iron ion[d][16], antigen processing and presentation[d][3], negative regulation of receptor binding[d][4], regulation of protein localization to cell surface[d][18], antigen processing and presentation of peptide antigen via MHC class I[d][2], женская беременность[d][17], positive regulation of pathway-restricted SMAD protein phosphorylation[d][14], response to iron ion starvation[d][19], iron ion homeostasis[d][23][17][17][…], negative regulation of antigen processing and presentation of endogenous peptide antigen via MHC class I[d][25], ion transport[d][17], BMP signaling pathway[d][14], cellular response to iron ion starvation[d][17], response to iron ion[d][23], multicellular organismal iron ion homeostasis[d][17], positive regulation of ferrous iron binding[d][16], positive regulation of transferrin receptor binding[d][16], positive regulation of signaling receptor activity[d][16], регенерация печени[d][17], positive regulation of gene expression[d][17][17], negative regulation of T cell cytokine production[d][25], acute-phase response[d][17], negative regulation of proteasomal ubiquitin-dependent protein catabolic process[d][14], negative regulation of ubiquitin-dependent protein catabolic process[d][14], positive regulation of receptor binding[d][16], negative regulation of signaling receptor activity[d][4], positive regulation of protein binding[d][16], hormone biosynthetic process[d][17], negative regulation of CD8-positive, alpha-beta T cell activation[d][25], cellular iron ion homeostasis[d][20][19], iron ion import across plasma membrane[d][19][19][26], transferrin transport[d][17], protein-containing complex assembly[d][13], T cell mediated cytotoxicity[d][15], иммун җавап[d][15], natural killer cell activation[d][15], natural killer cell mediated cytotoxicity[d][15], susceptibility to natural killer cell mediated cytotoxicity[d][15], iron ion import across plasma membrane[d][19][19][26][…], regulation of iron ion transport[d][16], cellular iron ion homeostasis[d][17][27], iron ion import across plasma membrane[d][17][24], response to iron ion starvation[d][17][24] һәм iron ion import across plasma membrane[d][17]
Изображение Gene Atlas

HFE (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[28][29]

Искәрмәләр

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,0 2,1 2,2 Feder J. N., A Gnirke, W Thomas et al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis // Nature Genetics / M. Axton, T. Faial — NPG, 1996. — ISSN 1061-4036; 1546-1718 — doi:10.1038/NG0896-399 — PMID:8696333
  3. ↑ 3,0 3,1 3,2 3,3 3,4 Lebrón J. A., Bennett M. J., Vaughn D. E. et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor, Crystal Structure of the Hemochromatosis Protein HFE and Characterization of Its Interaction with Transferrin Receptor // Cell — Cell Press, Elsevier, 1998. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)81151-4 — PMID:9546397
  4. ↑ 4,0 4,1 4,2 4,3 Feder J. N., Penny D. M., A. Irrinki et al. The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.4.1472 — PMID:9465039
  5. ↑ 5,0 5,1 A Waheed, S Parkkila, J Saarnio et al. Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1999. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.96.4.1579 — PMID:9990067
  6. ↑ Hentze M. W., Muckenthaler M. U. The hemochromatosis proteins HFE, TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation // Journal of Hepatology — Elsevier, 2012. — ISSN 0168-8278; 1600-0641 — doi:10.1016/J.JHEP.2012.06.015 — PMID:22728873
  7. ↑ 7,0 7,1 7,2 7,3 7,4 7,5 7,6 Bacharach E. Transferrin receptor co-localizes and interacts with the hemochromatosis factor (HFE) and the divalent metal transporter-1 (DMT1) in trophoblast cells // J. Cell. Physio. — Wiley, 2005. — ISSN 0021-9541; 1097-4652 — doi:10.1002/JCP.20349 — PMID:15880641
  8. ↑ Ka C., Gac G. L., Dupradeau F. et al. The Q283P amino-acid change in HFE leads to structural and functional consequences similar to those described for the mutated 282Y HFE protein // Hum. Genet. — Springer Science+Business Media, 2005. — ISSN 0340-6717; 1432-1203 — doi:10.1007/S00439-005-1307-Y — PMID:15965644
  9. ↑ Liam S O'Driscoll, Carmo-Fonseca M. N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding // FEBS J. — Wiley-Blackwell, 2010. — ISSN 1742-464X; 1742-4658 — doi:10.1111/J.1742-4658.2010.07727.X — PMID:20618438
  10. ↑ A Waheed, S Parkkila, J Saarnio et al. Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1999. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.96.4.1579 — PMID:9990067
  11. ↑ Hentze M. W., Muckenthaler M. U. The hemochromatosis proteins HFE, TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation // Journal of Hepatology — Elsevier, 2012. — ISSN 0168-8278; 1600-0641 — doi:10.1016/J.JHEP.2012.06.015 — PMID:22728873
  12. ↑ Lebrón J. A., Bennett M. J., Vaughn D. E. et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor, Crystal Structure of the Hemochromatosis Protein HFE and Characterization of Its Interaction with Transferrin Receptor // Cell — Cell Press, Elsevier, 1998. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(00)81151-4 — PMID:9546397
  13. ↑ 13,0 13,1 13,2 13,3 Bennett M. J., Lebrón J. A., Bjorkman P. J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor // Nature / M. Skipper — NPG, Springer Science+Business Media, 2000. — ISSN 1476-4687; 0028-0836 — doi:10.1038/47417 — PMID:10638746
  14. ↑ 14,0 14,1 14,2 14,3 14,4 14,5 Cheng W. H., Zhao Y., Yu P. B. et al. HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression // Blood — American Society of Hematology, Elsevier, 2014. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2014-01-552281 — PMID:24904118
  15. ↑ 15,0 15,1 15,2 15,3 15,4 15,5 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
  16. ↑ 16,0 16,1 16,2 16,3 16,4 16,5 16,6 16,7 16,8 Waheed A., Britton R. S., Grubb J. H. et al. HFE association with transferrin receptor 2 increases cellular uptake of transferrin-bound iron // Arch. Biochem. Biophys. — Academic Press, Elsevier, 2008. — ISSN 0003-9861; 1096-0384 — doi:10.1016/J.ABB.2008.02.041 — PMID:18353247
  17. ↑ 17,00 17,01 17,02 17,03 17,04 17,05 17,06 17,07 17,08 17,09 17,10 17,11 17,12 17,13 17,14 17,15 17,16 17,17 17,18 17,19 17,20 17,21 17,22 17,23 17,24 GOA
  18. ↑ 18,0 18,1 18,2 William J H Griffiths, Cox T. M. Co-localization of the mammalian hemochromatosis gene product (HFE) and a newly identified transferrin receptor (TfR2) in intestinal tissue and cells // J. Histochem. Cytochem. — Sage Publishing, 2003. — ISSN 0022-1554; 1551-5044 — doi:10.1177/002215540305100507 — PMID:12704209
  19. ↑ 19,0 19,1 19,2 19,3 19,4 19,5 19,6 19,7 GOA
  20. ↑ 20,0 20,1 Bennett M. J., Lebrón J. A., Bjorkman P. J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor // Nature / M. Skipper — NPG, Springer Science+Business Media, 2000. — ISSN 1476-4687; 0028-0836 — doi:10.1038/47417 — PMID:10638746
  21. ↑ Cheng W. H., Zhao Y., Yu P. B. et al. HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression // Blood — American Society of Hematology, Elsevier, 2014. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2014-01-552281 — PMID:24904118
  22. ↑ Camaschella C., Girelli D., Ganz T. A time course of hepcidin response to iron challenge in patients with HFE and TFR2 hemochromatosis // Haematologica — Ferrata Storti Foundation, 2011. — ISSN 0390-6078; 1592-8721; 1138-0381 — doi:10.3324/HAEMATOL.2010.033449 — PMID:21173098
  23. ↑ 23,0 23,1 23,2 23,3 Camaschella C., Girelli D., Ganz T. A time course of hepcidin response to iron challenge in patients with HFE and TFR2 hemochromatosis // Haematologica — Ferrata Storti Foundation, 2011. — ISSN 0390-6078; 1592-8721; 1138-0381 — doi:10.3324/HAEMATOL.2010.033449 — PMID:21173098
  24. ↑ 24,0 24,1 24,2 24,3 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
  25. ↑ 25,0 25,1 25,2 Lapointe R. The WT hemochromatosis protein HFE inhibits CD8⁺ T-lymphocyte activation, The WT hemochromatosis protein HFE inhibits CD8+ T‐lymphocyte activation // Eur. J. Immunol. — Wiley-Blackwell, 2014. — ISSN 0014-2980; 1521-4141 — doi:10.1002/EJI.201343955 — PMID:24643698
  26. ↑ 26,0 26,1 Roy C. N., Penny D. M., Feder J. N. et al. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1999. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.274.13.9022 — PMID:10085150
  27. ↑ Roy C. N., Penny D. M., Feder J. N. et al. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1999. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.274.13.9022 — PMID:10085150
  28. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  29. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • 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.)

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