SPARC |
Нинди таксонда бар |
H. sapiens[d][1] |
Кодлаучы ген |
SPARC[d][1] |
Молекуляр функция |
calcium ion binding[d][2][2][3], связывание с ионом металла[d][4], связывание с белками плазмы[d][5][6][7][…], extracellular matrix binding[d][4][8], collagen binding[d][2][3][9], extracellular matrix structural constituent[d][10], calcium ion binding[d][4][4][11][…], collagen binding[d][4][12][11][…], extracellular matrix structural constituent[d][13][13] һәм extracellular matrix structural constituent[d][13] |
Күзәнәк компоненты |
цитоплазма[14][15][16][…], альфа-гранула тромбоцитов[d][16], endocytic vesicle lumen[d][4], Ядерный скелет[d][15], күзәнәк мембранасы[d][16], внутренний компонент клетки[d][2], базаль мембрана[d][4], күзәнәк өслеге[d][15][17], platelet alpha granule membrane[d][16], митохондрия[16], platelet alpha granule lumen[d][4], төш[4], күзәнәк тышындагы мохит[d][4][4][8], везикула[d][4], күзәнәк тышындагы өлкә[d][2][18][2][…], күзәнәк тышындагы өлкә[d][4][19][4][…], внеклеточный матрикс[d][4], синапс[4], collagen-containing extracellular matrix[d][4][13] һәм glutamatergic synapse[d][4] |
Биологик процесс |
response to cytokine[d][4], response to cadmium ion[d][4], оссификация[d][4], үпкәләр үсеше[d][4], cellular response to growth factor stimulus[d][4], response to peptide hormone[d][4], platelet degranulation[d][4], extracellular matrix organization[d][4], response to L-ascorbic acid[d][4], response to glucocorticoid[d][4], Заживление ран[d][4], рецепторно-опосредованный эндоцитоз[d][4], negative regulation of endothelial cell proliferation[d][20], positive regulation of endothelial cell migration[d][20], response to calcium ion[d][4], response to gravity[d][4], йөрәк үсеше[d][4], response to lipopolysaccharide[d][4], response to lead ion[d][4], regulation of cell population proliferation[d][4], negative regulation of angiogenesis[d][20], inner ear development[d][4], regulation of cell morphogenesis[d][15], response to cAMP[d][4], response to ethanol[d][4], развитие костей[d][4], передача сигнала[d][2], пигментация[d][4] һәм regulation of synapse organization[d][4] |
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SPARC (ген) (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[21][22]
- ↑ 1,0 1,1 UniProt
- ↑ 2,0 2,1 2,2 2,3 2,4 2,5 2,6 GOA
- ↑ 3,0 3,1 Termine J. D., Kleinman H. K., Whitson S. W. et al. Osteonectin, a bone-specific protein linking mineral to collagen // Cell — Cell Press, Elsevier BV, 1981. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(81)90037-4 — PMID:7034958
- ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 4,12 4,13 4,14 4,15 4,16 4,17 4,18 4,19 4,20 4,21 4,22 4,23 4,24 4,25 4,26 4,27 4,28 4,29 4,30 4,31 4,32 4,33 4,34 4,35 4,36 4,37 4,38 4,39 4,40 4,41 GOA
- ↑ Bächinger H. P., Farndale R. W., Hohenester E. et al. Structural basis of sequence-specific collagen recognition by SPARC // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2008. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0808452105 — PMID:19011090
- ↑ Mörgelin M. Identification of a novel protein promoting the colonization and survival of Finegoldia magna, a bacterial commensal and opportunistic pathogen // Mol. Microbiol. — Wiley-Blackwell, 2008. — ISSN 0950-382X; 1365-2958 — doi:10.1111/J.1365-2958.2008.06439.X — PMID:18808384
- ↑ José Daniel Aroca Aguilar, Escribano J. Interaction of recombinant myocilin with the matricellular protein SPARC: functional implications // Investigative Ophthalmology & Visual Science — Cadmus Press, 2011. — ISSN 0146-0404; 1552-5783 — doi:10.1167/IOVS.09-4866 — PMID:20926826
- ↑ 8,0 8,1 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
- ↑ T Sasaki, E Hohenester, W Göhring et al. Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin // EMBO J. — NPG, 1998. — ISSN 0261-4189; 1460-2075 — doi:10.1093/EMBOJ/17.6.1625 — PMID:9501084
- ↑ Naba A., Hynes R. O., Langer R. et al. Comprehensive proteomic characterization of stem cell-derived extracellular matrices // Biomaterials — Elsevier BV, 2017. — 13 p. — ISSN 0142-9612; 1878-5905 — doi:10.1016/J.BIOMATERIALS.2017.03.008 — PMID:28327460
- ↑ 11,0 11,1 Termine J. D., Kleinman H. K., Whitson S. W. et al. Osteonectin, a bone-specific protein linking mineral to collagen // Cell — Cell Press, Elsevier BV, 1981. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(81)90037-4 — PMID:7034958
- ↑ T Sasaki, E Hohenester, W Göhring et al. Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin // EMBO J. — NPG, 1998. — ISSN 0261-4189; 1460-2075 — doi:10.1093/EMBOJ/17.6.1625 — PMID:9501084
- ↑ 13,0 13,1 13,2 13,3 Naba A., Hynes R. O., Langer R. et al. Comprehensive proteomic characterization of stem cell-derived extracellular matrices // Biomaterials — Elsevier BV, 2017. — 13 p. — ISSN 0142-9612; 1878-5905 — doi:10.1016/J.BIOMATERIALS.2017.03.008 — PMID:28327460
- ↑ Berdal A., Malaval L. Investigation of osteocalcin, osteonectin, and dentin sialophosphoprotein in developing human teeth // Bone — Elsevier BV, 2002. — ISSN 8756-3282; 1873-2763 — doi:10.1016/S8756-3282(01)00683-4 — PMID:11856645
- ↑ 15,0 15,1 15,2 15,3 Hudson A. E., Feng W. C., Delostrinos C. F. et al. Spreading of embryologically distinct urothelial cells is inhibited by SPARC // J. Cell. Physio. — Wiley, 2005. — ISSN 0021-9541; 1097-4652 — doi:10.1002/JCP.20140 — PMID:15389586
- ↑ 16,0 16,1 16,2 16,3 16,4 W Vainchenker Localization of platelet osteonectin at the internal face of the alpha-granule membranes in platelets and megakaryocytes // Blood — American Society of Hematology, Elsevier BV, 1992. — ISSN 0006-4971; 1528-0020 — PMID:1737102
- ↑ R. Albrechtsen Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues characterized by de novo formation of basement membrane // Am. J. Pathol. — Elsevier BV, 1988. — ISSN 0002-9440; 1525-2191; 0097-3599 — PMID:3400777
- ↑ Pounds J. G. The human plasma proteome: a nonredundant list developed by combination of four separate sources // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2004. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M300127-MCP200 — PMID:14718574
- ↑ Pounds J. G. The human plasma proteome: a nonredundant list developed by combination of four separate sources // Mol. Cell. Proteomics — American Society for Biochemistry and Molecular Biology, 2004. — ISSN 1535-9476; 1535-9484 — doi:10.1074/MCP.M300127-MCP200 — PMID:14718574
- ↑ 20,0 20,1 20,2 Sage E. H., Reed M., Funk S. E. et al. Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M302946200 — PMID:12867428
- ↑ 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.)