Эчтәлеккә күчү

CCR2

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CCR2
Рәсем
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген CCR2[d][1]
Молекуляр функция CCR2 chemokine receptor binding[d][2], G protein-coupled receptor activity[d][3][3], гомодимеризация белка[d][3], signal transducer activity[d][4], chemokine receptor activity[d][5][3], C-C chemokine receptor activity[d][4][4], связывание с белками плазмы[d][6], cytokine binding[d][3], chemokine (C-C motif) ligand 2 binding[d][3], chemokine (C-C motif) ligand 12 binding[d][3], chemokine (C-C motif) ligand 7 binding[d][3], C-C chemokine receptor activity[d][3][3][7], chemokine binding[d][7] һәм C-C chemokine binding[d][7]
Күзәнәк компоненты мембрана өлеше[d][8][3][3], перикарион[d][3], мембрана[d][3], күзәнәк мембранасы[d][3][9][3][…], күзәнәк мембранасы өлеше[d][10], soma[d][3], дендрит[d][3], perinuclear region of cytoplasm[d][3], цитоплазма[11], цитозоль[d][3], наружная сторона клеточной мембраны[d][4], цитоплазма[2][7] һәм наружная сторона клеточной мембраны[d][3][7]
Биологик процесс negative regulation of adenylate cyclase activity[d][12], receptor signaling pathway via JAK-STAT[d][13], chemokine-mediated signaling pathway[d][3], cellular calcium ion homeostasis[d][3], positive regulation of monocyte chemotaxis[d][3][3][3][…], dendritic cell chemotaxis[d][14], хемотаксис[d][15][4], blood vessel remodeling[d][3][3], response to wounding[d][10], иммун җавап[d][16][4][4], воспалительная реакция[d][15][4][4], вирусный процесс[d][3], positive regulation of astrocyte chemotaxis[d][17], передача сигнала[d][3], positive regulation of cytosolic calcium ion concentration[d][18], G protein-coupled receptor signaling pathway[d][3][3][3], monocyte chemotaxis[d][3], positive regulation of T-helper 1 type immune response[d][3][3], negative regulation of type 2 immune response[d][3][3], humoral immune response[d][3], cellular defense response[d][19][3], regulation of vascular endothelial growth factor production[d][3][3], positive regulation of T cell chemotaxis[d][3][3], negative regulation of angiogenesis[d][3][3], ноцицепция[d][4], cellular homeostasis[d][3][3], regulation of cell migration[d][3], positive regulation of interferon-gamma production[d][3][3], positive regulation of interleukin-2 production[d][3][3], T-helper 17 cell chemotaxis[d][3][3], negative regulation of eosinophil degranulation[d][3][3], positive regulation of alpha-beta T cell proliferation[d][3][3], homeostasis of number of cells within a tissue[d][3], positive regulation of inflammatory response[d][3][3], positive regulation of T cell activation[d][3][3], leukocyte adhesion to vascular endothelial cell[d][3], positive regulation of immune complex clearance by monocytes and macrophages[d][3][3], neutrophil clearance[d][3], positive regulation of leukocyte tethering or rolling[d][3], positive regulation of monocyte extravasation[d][3][3], positive regulation of CD8-positive, alpha-beta T cell extravasation[d][3][3], positive regulation of hematopoietic stem cell migration[d][3][3], cytokine-mediated signaling pathway[d][3][2], гемопоэз[d][3], хемотаксис[d][5][3][7], воспалительная реакция[d][5][3][3][…], иммун җавап[d][20][3][3][…], positive regulation of cytosolic calcium ion concentration[d][21][7], calcium-mediated signaling[d][7], cell chemotaxis[d][7], positive regulation of cold-induced thermogenesis[d][22][3], regulation of T cell cytokine production[d][3][3], ноцицепция[d][3][3], monocyte extravasation[d][3][3], regulation of T cell differentiation[d][3][3], regulation of inflammatory response[d][3][3], positive regulation of synaptic transmission, glutamatergic[d][3][3], inflammatory response to wounding[d][3][3], macrophage migration[d][3][3], positive regulation of thymocyte migration[d][3][3] һәм positive regulation of NMDA glutamate receptor activity[d][3]

CCR2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[23][24]

  1. 1 2 UniProt
  2. 1 2 3 Terashima Y., Kanegasaki S. Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis // Nat. Immunol.USA: NPG, 2005. — ISSN 1529-2908; 1529-2916doi:10.1038/NI1222PMID:15995708
  3. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 66 67 68 69 70 71 72 73 74 75 76 77 78 79 80 81 82 83 84 85 86 87 88 89 90 91 92 93 94 95 96 97 98 99 100 101 102 GOA
  4. 1 2 3 4 5 6 7 8 9 10 GOA
  5. 1 2 3 B Bottazzi, F Balkwill, A Mantovani Defective expression of the monocyte chemotactic protein-1 receptor CCR2 in macrophages associated with human ovarian carcinoma // J. Immunol.Baltimore: 2000. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.164.2.733PMID:10623817
  6. Paula V. d., Almeida F. C. L., Valente A. P. Structural basis for the interaction of human β-defensin 6 and its putative chemokine receptor CCR2 and breast cancer microvesicles // Journal of Molecular Biology / P. WrightElsevier, 2013. — ISSN 0022-2836; 1089-8638doi:10.1016/J.JMB.2013.08.001PMID:23938203
  7. 1 2 3 4 5 6 7 8 9 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; 1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  8. C Combadiere, Ahuja S. K., Damme J. V. et al. Monocyte chemoattractant protein-3 is a functional ligand for CC chemokine receptors 1 and 2B, Monocyte Chemoattractant Protein-3 Is a Functional Ligand for CC Chemokine Receptors 1 and 2B // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1995. — 5 p. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.270.50.29671PMID:8530354
  9. Agace W. W., Roberts A. I., L Wu et al. Human intestinal lamina propria and intraepithelial lymphocytes express receptors specific for chemokines induced by inflammation // Eur. J. Immunol.Wiley-Blackwell, 2000. — ISSN 0014-2980; 1521-4141<819::AID-IMMU819>3.0.CO;2-Y doi:10.1002/1521-4141(200003)30:3<819::AID-IMMU819>3.0.CO;2-YPMID:10741397
  10. 1 2 Charo I. F., Myers S. J., A Herman et al. Molecular cloning and functional expression of two monocyte chemoattractant protein 1 receptors reveals alternative splicing of the carboxyl-terminal tails // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum[Washington, etc.], USA: National Academy of Sciences [etc.], 1994. — ISSN 0027-8424; 1091-6490doi:10.1073/PNAS.91.7.2752PMID:8146186
  11. Terashima Y., Kanegasaki S. Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis // Nat. Immunol.USA: NPG, 2005. — ISSN 1529-2908; 1529-2916doi:10.1038/NI1222PMID:15995708
  12. Wong L. M., Myers S. J., Tsou C. L. et al. Organization and differential expression of the human monocyte chemoattractant protein 1 receptor gene. Evidence for the role of the carboxyl-terminal tail in receptor trafficking // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1997. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.272.2.1038PMID:8995400
  13. A. Aragay, A. Serrano The chemokine monocyte chemotactic protein 1 triggers Janus kinase 2 activation and tyrosine phosphorylation of the CCR2B receptor // J. Immunol.Baltimore: 1998. — ISSN 0022-1767; 1550-6606PMID:9670957
  14. Rodríguez-Fernández J. L. The multiple personalities of the chemokine receptor CCR7 in dendritic cells // J. Immunol.Baltimore: 2006. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.176.9.5153PMID:16621978
  15. 1 2 B Bottazzi, F Balkwill, A Mantovani Defective expression of the monocyte chemotactic protein-1 receptor CCR2 in macrophages associated with human ovarian carcinoma // J. Immunol.Baltimore: 2000. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.164.2.733PMID:10623817
  16. McManus C. M., K Weidenheim, Woodman S. E. et al. Chemokine and chemokine-receptor expression in human glial elements: induction by the HIV protein, Tat, and chemokine autoregulation // Am. J. Pathol.Elsevier, 2000. — ISSN 0002-9440; 1525-2191doi:10.1016/S0002-9440(10)65013-4PMID:10751368
  17. Andjelkovic A. V., Song L., Dzenko K. A. et al. Functional expression of CCR2 by human fetal astrocytes // J. Neurosci. Res.Wiley, 2002. — ISSN 0360-4012; 1097-4547doi:10.1002/JNR.10372PMID:12271471
  18. Frade J. M., M. Mellado, G. del Real et al. Characterization of the CCR2 chemokine receptor: functional CCR2 receptor expression in B cells // J. Immunol.Baltimore: 1997. — ISSN 0022-1767; 1550-6606PMID:9548499
  19. Rabin R. L., Park M. K., F Liao et al. Chemokine receptor responses on T cells are achieved through regulation of both receptor expression and signaling // J. Immunol.Baltimore: 1999. — ISSN 0022-1767; 1550-6606PMID:10201901
  20. McManus C. M., K Weidenheim, Woodman S. E. et al. Chemokine and chemokine-receptor expression in human glial elements: induction by the HIV protein, Tat, and chemokine autoregulation // Am. J. Pathol.Elsevier, 2000. — ISSN 0002-9440; 1525-2191doi:10.1016/S0002-9440(10)65013-4PMID:10751368
  21. Frade J. M., M. Mellado, G. del Real et al. Characterization of the CCR2 chemokine receptor: functional CCR2 receptor expression in B cells // J. Immunol.Baltimore: 1997. — ISSN 0022-1767; 1550-6606PMID:9548499
  22. Qiu Y., Tian X. Y., Locksley R. M. Eosinophils and type 2 cytokine signaling in macrophages orchestrate development of functional beige fat // CellCell Press, Elsevier, 2014. — ISSN 0092-8674; 1097-4172doi:10.1016/J.CELL.2014.03.066PMID:24906148
  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.
  • 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.)