CEACAM1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/CEACAM1 latin yazuında])
CEACAM1
Нинди таксонда бар H. sapiens[d][1][1]
Кодирующий ген CEACAM1[d][1][1]
Молекулярная функция связывание с белками плазмы[d][2][3][4][…], kinase binding[d][5], гомодимеризация белка[d][6][7], protein phosphatase binding[d][8], protein tyrosine kinase binding[d][8], filamin binding[d][9], bile acid transmembrane transporter activity[d][6], protein dimerization activity[d][6], actin binding[d][10], calmodulin binding[d][6], молекулярная функция[d][6] һәм связывание похожих белков[d][11]
Күзәнәк компоненты мембрана[d][12], часть мембраны[d][12], внеклеточная область[d][6], часть клеточной мембраны[d][13], экзосома[d][14][15], T cell receptor complex[d][8], cell-cell junction[d][9], мембрана[d][16][6], поверхность клетки[d][6][3], часть мембраны[d][6][17], күзәнәк мембраны[d][6][6][10], Адгезионные контакты[d][6][6], basal plasma membrane[d][6][6], apical plasma membrane[d][18][18], lateral plasma membrane[d][6][6], Межклеточные контакты[d][6][6][19], transport vesicle membrane[d][6], цитоплазматическая везикула[d][6], microvillus membrane[d][6], specific granule membrane[d][6], cell projection[d][6], tertiary granule membrane[d][6], apical plasma membrane[d][6][6][20] һәм экзосома[d][21][22]
Биологический процесс integrin-mediated signaling pathway[d][13], миграция клеток[d][13], Ангиогенез[d][13], leukocyte migration[d][6], insulin catabolic process[d][6], positive regulation of vasculogenesis[d][6], cellular response to insulin stimulus[d][6], negative regulation of cytotoxic T cell degranulation[d][8], regulation of ERK1 and ERK2 cascade[d][6], regulation of homophilic cell adhesion[d][6], negative regulation of vascular permeability[d][6], regulation of endothelial cell migration[d][6], negative regulation of interleukin-1 production[d][6], homophilic cell adhesion via plasma membrane adhesion molecules[d][13][6], granulocyte colony-stimulating factor signaling pathway[d][6], wound healing, spreading of cells[d][9], negative regulation of hepatocyte proliferation[d][6], negative regulation of granulocyte differentiation[d][6], negative regulation of platelet aggregation[d][6], развитие кровеносных сосудов[d][6], negative regulation of lipid biosynthetic process[d][6], bile acid and bile salt transport[d][6], regulation of blood vessel remodeling[d][6], negative regulation of T cell receptor signaling pathway[d][8], negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target[d][2], regulation of cell growth[d][6], insulin receptor internalization[d][6], negative regulation of T cell mediated cytotoxicity[d][8], regulation of sprouting angiogenesis[d][6], negative regulation of protein kinase activity[d][6], negative regulation of fatty acid biosynthetic process[d][6], regulation of cell migration[d][9], regulation of phosphatidylinositol 3-kinase signaling[d][6], common myeloid progenitor cell proliferation[d][6], regulation of epidermal growth factor receptor signaling pathway[d][6], regulation of endothelial cell differentiation[d][6], Агрегация клеток[d][6], neutrophil degranulation[d][6] һәм cell-cell adhesion via plasma-membrane adhesion molecules[d][6]

CEACAM1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[23][24]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. 1,0 1,1 1,2 1,3 UniProt
  2. 2,0 2,1 Zeissig S., Mandelboim O. CEACAM1 on activated NK cells inhibits NKG2D-mediated cytolytic function and signaling // Eur. J. Immunol.Wiley-Blackwell, 2013. — ISSN 0014-2980; 1521-4141doi:10.1002/EJI.201242676PMID:23696226
  3. 3,0 3,1 Pertel T., Petersen B., Chen Q. et al. CEACAM1 regulates TIM-3-mediated tolerance and exhaustion // Nature / M. SkipperNPG, Springer Science+Business Media, 2014. — ISSN 1476-4687; 0028-0836doi:10.1038/NATURE13848PMID:25363763
  4. Geijtenbeek T. B. H. Interactions of DC-SIGN with Mac-1 and CEACAM1 regulate contact between dendritic cells and neutrophils // FEBS LettersElsevier BV, 2005. — ISSN 0014-5793; 1873-3468doi:10.1016/J.FEBSLET.2005.09.089PMID:16246332
  5. Brümmer J, Neumaier M, Göpfert C et al. Association of pp60c-src with biliary glycoprotein (CD66a), an adhesion molecule of the carcinoembryonic antigen family downregulated in colorectal carcinomas // OncogeneNPG, 1995. — ISSN 0950-9232; 1476-5594PMID:7478590
  6. 6,00 6,01 6,02 6,03 6,04 6,05 6,06 6,07 6,08 6,09 6,10 6,11 6,12 6,13 6,14 6,15 6,16 6,17 6,18 6,19 6,20 6,21 6,22 6,23 6,24 6,25 6,26 6,27 6,28 6,29 6,30 6,31 6,32 6,33 6,34 6,35 6,36 6,37 6,38 6,39 6,40 6,41 6,42 6,43 6,44 6,45 6,46 6,47 6,48 6,49 6,50 6,51 6,52 6,53 6,54 6,55 6,56 GOA
  7. Klaile E. The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters // J. Cell Biol. / J. NunnariRockefeller University Press, 2009. — ISSN 0021-9525; 1540-8140doi:10.1083/JCB.200904149PMID:19948502
  8. 8,0 8,1 8,2 8,3 8,4 8,5 Qiao S. Carcinoembryonic antigen-related cell adhesion molecule 1 inhibits proximal TCR signaling by targeting ZAP-70 // J. Immunol.Baltimore: 2008. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.180.9.6085PMID:18424730
  9. 9,0 9,1 9,2 9,3 Klaile E., Müller M. M. CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration // J. Cell Sci.The Company of Biologists, 2005. — ISSN 0021-9533; 1477-9137doi:10.1242/JCS.02660PMID:16291724
  10. 10,0 10,1 Chen C., Kirshner J., Sherman M. A. et al. Mutation analysis of the short cytoplasmic domain of the cell-cell adhesion molecule CEACAM1 identifies residues that orchestrate actin binding and lumen formation // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M610903200PMID:17192268
  11. Günther S., Sundberg E. J. Diverse oligomeric states of CEACAM IgV domains // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 2015. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.1509511112PMID:26483485
  12. 12,0 12,1 GOA
  13. 13,0 13,1 13,2 13,3 13,4 Müller M. M., Klaile E. Transmembrane CEACAM1 affects integrin-dependent signaling and regulates extracellular matrix protein-specific morphology and migration of endothelial cells // BloodAmerican Society of Hematology, Elsevier BV, 2005. — ISSN 0006-4971; 1528-0020doi:10.1182/BLOOD-2004-09-3618PMID:15687237
  14. 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. YatesACS, 2009. — ISSN 1535-3893; 1535-3907doi:10.1021/PR800658CPMID:19199708
  15. Sinha A., Kislinger T. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine // Proteomics / L. StimsonWiley, 2013. — ISSN 1615-9853; 1615-9861doi:10.1002/PMIC.201200561PMID:23533145
  16. Y Hinoda, M Neumaier, Hefta S. A. et al. Molecular cloning of a cDNA coding biliary glycoprotein I: primary structure of a glycoprotein immunologically crossreactive with carcinoembryonic antigen // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1988. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.85.18.6959PMID:2457922
  17. Singer B. B., Scheffrahn I., Heymann R. et al. Carcinoembryonic antigen-related cell adhesion molecule 1 expression and signaling in human, mouse, and rat leukocytes: evidence for replacement of the short cytoplasmic domain isoform by glycosylphosphatidylinositol-linked proteins in human leukocytes // J. Immunol.Baltimore: 2002. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.168.10.5139PMID:11994468
  18. 18,0 18,1 GOA
  19. Watt S. M., J. Fawcett, Murdoch S. J. et al. CD66 identifies the biliary glycoprotein (BGP) adhesion molecule: cloning, expression, and adhesion functions of the BGPc splice variant // BloodAmerican Society of Hematology, Elsevier BV, 1994. — ISSN 0006-4971; 1528-0020PMID:8018919
  20. L Frängsmyr, V Baranov, S Hammarström Four carcinoembryonic antigen subfamily members, CEA, NCA, BGP and CGM2, selectively expressed in the normal human colonic epithelium, are integral components of the fuzzy coat // Tumor Biology: from basic science to clinical applicationSAGE Publishing, 1999. — ISSN 1010-4283; 1423-0380doi:10.1159/000030075PMID:10436421
  21. 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. YatesACS, 2009. — ISSN 1535-3893; 1535-3907doi:10.1021/PR800658CPMID:19199708
  22. Sinha A., Kislinger T. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine // Proteomics / L. StimsonWiley, 2013. — ISSN 1615-9853; 1615-9861doi:10.1002/PMIC.201200561PMID:23533145
  23. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  24. 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.)