DAG1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/DAG1 latin yazuında])
DAG1
Нинди таксонда бар H. sapiens[d][1]
Кодирующий ген DAG1[d][1]
Молекулярная функция calcium ion binding[d][2], связывание с белками плазмы[d][3][4][5][…], virus receptor activity[d][2], alpha-actinin binding[d][6], vinculin binding[d][6], actin binding[d][6], tubulin binding[d][6], structural constituent of muscle[d][7], SH2 domain binding[d][8], laminin binding[d][2], laminin-1 binding[d][2][2] һәм dystroglycan binding[d][2]
Күзәнәк компоненты cell-cell junction[d][2], Төш[2][2], Синапс[2][2], contractile ring[d][6], filopodium[d][6], Перехваты Ранвье[d][2], costamere[d][2], lamellipodium[d][6], dystroglycan complex[d][2], Липидный рафт[d][2], Межклеточные контакты[d][2], Цитоскелет[d][2], мембрана[d][2][2][2], экзосома[d][9][10][11], basolateral plasma membrane[d][2], postsynaptic membrane[d][2], Сарколемма[d][2][2], Цитоплазма[2][2][12], часть мембраны[d][2][13], Фокальные контакты[d][14][15][16], күзәнәк мембраны[d][2][2][2][…], dystrophin-associated glycoprotein complex[d][2][2][17], нуклеоплазма[d][2][12], Базальная мембрана[d][2][18], цитозоль[d][2], внеклеточное пространство[d][14][14][19][…], endoplasmic reticulum lumen[d][2], Люмен аппарата Гольджи[d][2], plasma membrane raft[d][2], наружная сторона клеточной мембраны[d][2], nuclear periphery[d][2], внеклеточный матрикс[d][20], внеклеточная область[d][14][14][21], внеклеточная область[d][2][2][22], внеклеточное пространство[d][2][2][23][…], Фокальные контакты[d][2][6][24], collagen-containing extracellular matrix[d][25], экзосома[d][26][27], glutamatergic synapse[d][2], GABA-ergic synapse[d][2] һәм postsynaptic cytosol[d][2]
Биологический процесс NLS-bearing protein import into nucleus[d][28], extracellular matrix organization[d][2], вирусный процесс[d][2], regulation of embryonic cell shape[d][2], response to peptide hormone[d][2], regulation of epithelial to mesenchymal transition[d][29], positive regulation of basement membrane assembly involved in embryonic body morphogenesis[d][29], viral entry into host cell[d][2], regulation of gastrulation[d][29], negative regulation of cell migration[d][30], Schwann cell development[d][2], membrane protein ectodomain proteolysis[d][31], calcium-dependent cell-matrix adhesion[d][2], negative regulation of MAPK cascade[d][30], nerve maturation[d][2], microtubule anchoring[d][6], commissural neuron axon guidance[d][2], branching involved in salivary gland morphogenesis[d][2], negative regulation of protein kinase B signaling[d][30], morphogenesis of an epithelial sheet[d][2], myelination in peripheral nervous system[d][2], basement membrane organization[d][2], epithelial tube branching involved in lung morphogenesis[d][2], modulation by virus of host process[d][32], protein O-linked glycosylation[d][14], positive regulation of cell-matrix adhesion[d][2], старение человека[d][2], Schwann cell differentiation[d][2], response to denervation involved in regulation of muscle adaptation[d][2], nerve development[d][2], axon regeneration[d][2], positive regulation of myelination[d][2], skeletal muscle tissue regeneration[d][2], positive regulation of protein kinase activity[d][2], positive regulation of oligodendrocyte differentiation[d][2], cellular response to mechanical stimulus[d][2], cellular response to cholesterol[d][2], angiogenesis involved in wound healing[d][2], regulation of synapse organization[d][2], regulation of neurotransmitter receptor localization to postsynaptic specialization membrane[d][2] һәм retrograde trans-synaptic signaling by trans-synaptic protein complex[d][2]
Изображение Gene Atlas

DAG1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[33][34]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 2,35 2,36 2,37 2,38 2,39 2,40 2,41 2,42 2,43 2,44 2,45 2,46 2,47 2,48 2,49 2,50 2,51 2,52 2,53 2,54 2,55 2,56 2,57 2,58 2,59 2,60 2,61 2,62 2,63 2,64 2,65 2,66 2,67 2,68 2,69 2,70 2,71 2,72 2,73 2,74 2,75 2,76 2,77 GOA
  3. ↑ Macioce P. Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M005321200 — PMID:10988290
  4. ↑ Fletcher G. C., S Patel, K Tyson et al. hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan // Br. J. Cancer, BJC — NPG, 2003. — ISSN 0007-0920; 1532-1827 — doi:10.1038/SJ.BJC.6600740 — PMID:12592373
  5. ↑ Brancaccio A. Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1998. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.273.1.600 — PMID:9417121
  6. ↑ 6,0 6,1 6,2 6,3 6,4 6,5 6,6 6,7 6,8 Cerecedo D., Cisneros B., Suárez-Sánchez R. et al. beta-Dystroglycan modulates the interplay between actin and microtubules in human-adhered platelets // Br. J. Haematol. — Wiley-Blackwell, 2008. — ISSN 0007-1048; 1365-2141 — doi:10.1111/J.1365-2141.2008.07048.X — PMID:18341635
  7. ↑ Muntoni F., Jimenez-Mallebrera C., Topaloglu H. et al. A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity // Brain Pathol. — Wiley, 2009. — ISSN 1015-6305; 1750-3639 — doi:10.1111/J.1750-3639.2008.00198.X — PMID:18691338
  8. ↑ F Sotgia, H Lee, Bedford M. T. et al. Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins // Biochemistry / A. Schepartz — ACS, 2001. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI011247R — PMID:11724572
  9. ↑ Gonzalez-Begne M., Lu B., Han X. et al. Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT) // J. Proteome Res. / J. Yates — ACS, 2009. — ISSN 1535-3893; 1535-3907 — doi:10.1021/PR800658C — PMID:19199708
  10. ↑ Sinha A., Kislinger T. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine // Proteomics / L. Stimson — Wiley, 2013. — ISSN 1615-9853; 1615-9861 — doi:10.1002/PMIC.201200561 — PMID:23533145
  11. ↑ Farina A., Lane L., Lescuyer P. et al. Proteomic analysis of podocyte exosome-enriched fraction from normal human urine // Journal of Proteomics — Elsevier BV, 2013. — ISSN 1874-3919; 0165-022X — doi:10.1016/J.JPROT.2013.01.012 — PMID:23376485
  12. ↑ 12,0 12,1 Oppizzi M. L., Akhavan A., Singh M. et al. Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins // Traffic — Wiley-Blackwell, 2008. — ISSN 1398-9219; 1600-0854 — doi:10.1111/J.1600-0854.2008.00822.X — PMID:18764929
  13. ↑ Muntoni F., Bove K. E., Horssen J. v. et al. MLC1 is associated with the dystrophin-glycoprotein complex at astrocytic endfeet // Acta Neuropathol. (Berl) — Springer Science+Business Media, 2007. — ISSN 0001-6322; 1432-0533 — doi:10.1007/S00401-007-0247-0 — PMID:17628813
  14. ↑ 14,0 14,1 14,2 14,3 14,4 14,5 GOA
  15. ↑ Waterman C. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  16. ↑ Cerecedo D., Cisneros B., Suárez-Sánchez R. et al. beta-Dystroglycan modulates the interplay between actin and microtubules in human-adhered platelets // Br. J. Haematol. — Wiley-Blackwell, 2008. — ISSN 0007-1048; 1365-2141 — doi:10.1111/J.1365-2141.2008.07048.X — PMID:18341635
  17. ↑ Sharma P., Gerthoffer W. T., Halayko A. J. Expression of the dystrophin-glycoprotein complex is a marker for human airway smooth muscle phenotype maturation // American Journal of Physiology: Lung Cellular and Molecular Physiology — 2008. — ISSN 1040-0605; 1522-1504 — doi:10.1152/AJPLUNG.00378.2007 — PMID:17993586
  18. ↑ Ishiyama A., Mowry S. E., Lopez I. A. et al. Immunohistochemical distribution of basement membrane proteins in the human inner ear from older subjects // Hearing Research — Springer Science+Business Media, Elsevier BV, 2009. — ISSN 0378-5955; 1878-5891 — doi:10.1016/J.HEARES.2009.03.014 — PMID:19348877
  19. ↑ Palmer D. J., Kelly V. C., Smit A. et al. Human colostrum: identification of minor proteins in the aqueous phase by proteomics // Proteomics / L. Stimson — Wiley, 2006. — ISSN 1615-9853; 1615-9861 — doi:10.1002/PMIC.200500558 — PMID:16502470
  20. ↑ Mayr M., Iozzo R. V., Barallobre-Barreiro J. et al. Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation // Circulation — Lippincott Williams & Wilkins, 2016. — ISSN 0009-7322; 1524-4539 — doi:10.1161/CIRCULATIONAHA.115.016423 — PMID:27559042
  21. ↑ Yin X., Mayr M., Porter K. E. Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins // Cardiovascular Research — OUP, 2016. — ISSN 0008-6363; 1755-3245 — doi:10.1093/CVR/CVW075 — PMID:27068509
  22. ↑ Yin X., Mayr M., Porter K. E. Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins // Cardiovascular Research — OUP, 2016. — ISSN 0008-6363; 1755-3245 — doi:10.1093/CVR/CVW075 — PMID:27068509
  23. ↑ Saito F., Saito-Arai Y., Nakamura A. et al. Processing and secretion of the N-terminal domain of alpha-dystroglycan in cell culture media // FEBS Letters — Elsevier BV, 2008. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2008.01.006 — PMID:18201566
  24. ↑ Waterman C. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  25. ↑ Mayr M., Iozzo R. V., Barallobre-Barreiro J. et al. Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation // Circulation — Lippincott Williams & Wilkins, 2016. — ISSN 0009-7322; 1524-4539 — doi:10.1161/CIRCULATIONAHA.115.016423 — PMID:27559042
  26. ↑ Gonzalez-Begne M., Lu B., Han X. et al. Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT) // J. Proteome Res. / J. Yates — ACS, 2009. — ISSN 1535-3893; 1535-3907 — doi:10.1021/PR800658C — PMID:19199708
  27. ↑ Sinha A., Kislinger T. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine // Proteomics / L. Stimson — Wiley, 2013. — ISSN 1615-9853; 1615-9861 — doi:10.1002/PMIC.201200561 — PMID:23533145
  28. ↑ Lara-Chacón B., León M. B., Leocadio D. et al. Characterization of an Importin alpha/beta-recognized nuclear localization signal in beta-dystroglycan // J. Cell. Biochem. — Wiley, 2010. — ISSN 0730-2312; 1097-4644; 0733-1959 — doi:10.1002/JCB.22581 — PMID:20512930
  29. ↑ 29,0 29,1 29,2 Nakaya Y., Sukowati E. W., Sheng G. Epiblast integrity requires CLASP and Dystroglycan-mediated microtubule anchoring to the basal cortex // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2013. — 15 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.201302075 — PMID:23940118
  30. ↑ 30,0 30,1 30,2 Bao X., Kobayashi M., Hatakeyama S. et al. Tumor suppressor function of laminin-binding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2009. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0904515106 — PMID:19587235
  31. ↑ Sbardella D., Sciandra F., Brancaccio A. et al. Enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9: identification of the main cleavage site // IUBMB Life — Wiley-Blackwell, IUBMB, 2009. — ISSN 1521-6543; 1521-6551 — doi:10.1002/IUB.273 — PMID:19946898
  32. ↑ Callewaert N., Brancaccio A., Oxenius A. O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function // J. Virol. — ASM, 2005. — ISSN 0022-538X; 1098-5514; 1070-6321 — doi:10.1128/JVI.79.22.14297-14308.2005 — PMID:16254364
  33. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  34. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар[үзгәртү | вики-текстны үзгәртү]

  • 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.)


Миоглобин молекуласы
 Бу — аксым турында мәкалә төпчеге.
Сез мәкаләне үзгәртеп һәм мәгълүмат өстәп, Википедия проектына ярдәм итә аласыз.
Чыганак — https://tt.wikipedia.org/w/index.php?title=DAG1&oldid=4126961