CEACAM1

CEACAM1
Нинди таксонда бар H. sapiens[1][1]
Кодлаучы ген CEACAM1[d][1][1]
Молекуляр 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], молекуляр функция[d][6] һәм связывание похожих белков[d][11]
Күзәнәк компоненты мембрана[d][12], мембрана өлеше[d][12], күзәнәк тышындагы өлкә[d][6], күзәнәк мембранасы өлеше[d][13], экзосома[d][14][15], T cell receptor complex[d][8], cell-cell junction[d][9], мембрана[d][16][6], күзәнәк өслеге[d][6][3], мембрана өлеше[d][6][17], күзәнәк мембранасы[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]
Биологик 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], кан тамырлары үсеше[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

  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; 1521-4141 — doi:10.1002/EJI.201242676 — PMID:23696226
  3. ↑ 3,0 3,1 Pertel T., Petersen B., Chen Q. et al. CEACAM1 regulates TIM-3-mediated tolerance and exhaustion // Nature / M. Skipper — NPG, Springer Science+Business Media, 2014. — ISSN 1476-4687; 0028-0836 — doi:10.1038/NATURE13848 — PMID:25363763
  4. ↑ Geijtenbeek T. B. H. Interactions of DC-SIGN with Mac-1 and CEACAM1 regulate contact between dendritic cells and neutrophils // FEBS Letters — Elsevier, 2005. — ISSN 0014-5793; 1873-3468 — doi:10.1016/J.FEBSLET.2005.09.089 — PMID: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 // Oncogene — NPG, 1995. — ISSN 0950-9232; 1476-5594 — PMID: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. Nunnari — Rockefeller University Press, 2009. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200904149 — PMID: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; 1550-6606 — doi:10.4049/JIMMUNOL.180.9.6085 — PMID: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; 1477-9137 — doi:10.1242/JCS.02660 — PMID:16291724
  10. ↑ 10,0 10,1 Shively J. E. 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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M610903200 — PMID: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; 1091-6490 — doi:10.1073/PNAS.1509511112 — PMID: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 // Blood — American Society of Hematology, Elsevier, 2005. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2004-09-3618 — PMID:15687237
  14. ↑ Yates J. R. 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
  15. ↑ 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
  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; 1091-6490 — doi:10.1073/PNAS.85.18.6959 — PMID: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; 1550-6606 — doi:10.4049/JIMMUNOL.168.10.5139 — PMID: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 // Blood — American Society of Hematology, Elsevier, 1994. — ISSN 0006-4971; 1528-0020 — PMID: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 application — Sage Publishing, 1999. — ISSN 1010-4283; 1423-0380 — doi:10.1159/000030075 — PMID:10436421
  21. ↑ Yates J. R. 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
  22. ↑ 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
  23. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  24. ↑ 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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