Эчтәлеккә күчү

CD74

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/CD74 latin yazuında])
CD74
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген CD74[d][1]
Молекуляр функция nitric-oxide synthase binding[d][2], связывание похожих белков[d][3], MHC class II protein binding, via antigen binding groove[d][4], cytokine receptor activity[d][2][5], macrophage migration inhibitory factor binding[d][5], protein folding chaperone activity[d][4], MHC class II protein complex binding[d][6], amyloid-beta binding[d][7], связывание с белками плазмы[d][8][9][10][…], MHC class II protein binding[d][11][2][2][…], cytokine binding[d][3][12][2] һәм CD4 receptor binding[d][13]
Күзәнәк компоненты lysosomal lumen[d][2], экзосома[d][14], MHC class II protein complex[d][2][2], lysosomal membrane[d][2], late endosome[d][2], endocytic vesicle membrane[d][2], transport vesicle membrane[d][2], мембрана өлеше[d][2][2][3], ER to Golgi transport vesicle membrane[d][2], multivesicular body[d][2], Гольджи аппараты[2][2], Golgi membrane[d][2], trans-Golgi network membrane[d][2], macrophage migration inhibitory factor receptor complex[d][2][5], мембрана[d][15][15][16], күзәнәк өслеге[d][5], внутренний компонент клетки[d][17], integral component of lumenal side of endoplasmic reticulum membrane[d][2], эндоплазматик челтәр[2][2], endoplasmic reticulum membrane[d][2], күзәнәк мембранасы[d][2][2][2], лизосома[2][2], вакуоль[d][7], эндосома[d][2], clathrin-coated endocytic vesicle membrane[d][2], NOS2-CD74 complex[d][2], наружная сторона клеточной мембраны[d][2], мембрана[d][2][2][18] һәм экзосома[d][19]
Биологик процесс иммун җавап[d][2], positive regulation of T cell differentiation[d][2], негативная регуляция апоптоза[d][3], передача сигнала[d][3], positive thymic T cell selection[d][2], chaperone cofactor-dependent protein refolding[d][2], T cell selection[d][11], positive regulation of type 2 immune response[d][2], positive regulation of dendritic cell antigen processing and presentation[d][2], antigen processing and presentation of exogenous peptide antigen via MHC class II[d][2][2], adaptive immune response[d][2], antigen processing and presentation[d][2][2], positive regulation of peptidyl-tyrosine phosphorylation[d][2][5], negative regulation of mature B cell apoptotic process[d][2], regulation of macrophage activation[d][3], negative regulation of DNA damage response, signal transduction by p53 class mediator[d][2][5], immunoglobulin mediated immune response[d][2][2], leukocyte migration[d][2], positive regulation of neutrophil chemotaxis[d][2][2], positive regulation of chemokine (C-X-C motif) ligand 2 production[d][2][2], macrophage migration inhibitory factor signaling pathway[d][2], prostaglandin biosynthetic process[d][3], пролиферация[d][2][3], antigen processing and presentation of endogenous antigen[d][11], immune system process[d][2], defense response[d][2], negative regulation of peptide secretion[d][7], negative regulation of T cell differentiation[d][2], positive regulation of macrophage cytokine production[d][2][2], positive regulation of B cell proliferation[d][3], negative thymic T cell selection[d][2], positive regulation of fibroblast proliferation[d][3], intracellular protein transport[d][2][2][2], positive regulation of ERK1 and ERK2 cascade[d][3][2][13][…], negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator[d][5][2], positive regulation of cytokine-mediated signaling pathway[d][3][2], positive regulation of protein phosphorylation[d][13], positive regulation of kinase activity[d][13], positive regulation of I-kappaB kinase/NF-kappaB signaling[d][13], positive regulation of MAPK cascade[d][13], positive regulation of monocyte differentiation[d][13], ДНК-зависимая позитивная регуляция транскрипции[d][13], positive regulation of viral entry into host cell[d][13], protein heterotetramerization[d][13], protein trimerization[d][2] һәм protein-containing complex assembly[d][2][2]

CD74 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[20][21]

  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 GOA
  3. 3,00 3,01 3,02 3,03 3,04 3,05 3,06 3,07 3,08 3,09 3,10 3,11 Bucala R., Metz C. N. MIF signal transduction initiated by binding to CD74 // J. Exp. Med.Rockefeller University Press, 2003. — ISSN 0022-1007; 1540-9538doi:10.1084/JEM.20030286PMID:12782713
  4. 4,0 4,1 P Ghosh, M Amaya, E Mellins et al. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3 // Nature / M. SkipperNPG, Springer Science+Business Media, 1995. — ISSN 1476-4687; 0028-0836doi:10.1038/378457A0PMID:7477400
  5. 5,0 5,1 5,2 5,3 5,4 5,5 5,6 Bucala R., Wang T. CD44 is the signaling component of the macrophage migration inhibitory factor-CD74 receptor complex // ImmunityCell Press, Elsevier BV, 2006. — ISSN 1074-7613; 1097-4180doi:10.1016/J.IMMUNI.2006.08.020PMID:17045821
  6. Riberdy J. M., Newcomb J. R., Surman M. J. et al. HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides // Nature / M. SkipperNPG, Springer Science+Business Media, 1992. — ISSN 1476-4687; 0028-0836doi:10.1038/360474A0PMID:1448172
  7. 7,0 7,1 7,2 D'Adamio L. CD74 interacts with APP and suppresses the production of Abeta // Mol. Neurodegener.BMC, Springer Science+Business Media, 2009. — ISSN 1750-1326doi:10.1186/1750-1326-4-41PMID:19849849
  8. Kalbacher H., Holzer U., Haug M. Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove // ImmunologyWiley-Blackwell, 2014. — ISSN 0019-2805; 1365-2567doi:10.1111/IMM.12249PMID:24428437
  9. Kalbacher H., Holzer U., Haug M. 70-kDa heat shock proteins: specific interactions with HLA-DR molecules and their peptide fragments // Eur. J. Immunol.Wiley-Blackwell, 2007. — ISSN 0014-2980; 1521-4141doi:10.1002/EJI.200636811PMID:17357109
  10. Ssadh H. A., Spencer P. S., Alabdulmenaim W. et al. Measurements of heterotypic associations between cluster of differentiation CD74 and CD44 in human breast cancer-derived cells // Oncotarget / M. BlagosklonnyImpact Journals LLC, 2017. — ISSN 1949-2553doi:10.18632/ONCOTARGET.20922PMID:29190904
  11. 11,0 11,1 11,2 Freeman G. J., Nadler L. M. Expression of MHC class II-associated invariant chain (Ii;CD74) in thymic epithelial neoplasms // Applied Immunohistochemistry & Molecular MorphologyLippincott Williams & Wilkins, 2000. — ISSN 1062-3345; 1533-4058; 1541-2016doi:10.1097/00022744-200009000-00007PMID:10981873
  12. Bucala R. Structural and functional characterization of a secreted hookworm Macrophage Migration Inhibitory Factor (MIF) that interacts with the human MIF receptor CD74 // 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.M702950200PMID:17567581
  13. 13,00 13,01 13,02 13,03 13,04 13,05 13,06 13,07 13,08 13,09 Zack J. A. CD4 ligation on human blood monocytes triggers macrophage differentiation and enhances HIV infection // J. Virol.ASM, 2014. — ISSN 0022-538X; 1098-5514; 1070-6321doi:10.1128/JVI.00616-14PMID:24942581
  14. Buschow S. I., Stoorvogel W., Wauben M. MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis // Immunology & Cell BiologyWiley, 2010. — ISSN 0818-9641; 1440-1711doi:10.1038/ICB.2010.64PMID:20458337
  15. 15,0 15,1 GOA
  16. Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom.Wiley, 2010. — ISSN 1076-5174; 1096-9888doi:10.1002/JMS.1696PMID:19946888
  17. Bucala R., Metz C. N. MIF signal transduction initiated by binding to CD74 // J. Exp. Med.Rockefeller University Press, 2003. — ISSN 0022-1007; 1540-9538doi:10.1084/JEM.20030286PMID:12782713
  18. Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom.Wiley, 2010. — ISSN 1076-5174; 1096-9888doi:10.1002/JMS.1696PMID:19946888
  19. Buschow S. I., Stoorvogel W., Wauben M. MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis // Immunology & Cell BiologyWiley, 2010. — ISSN 0818-9641; 1440-1711doi:10.1038/ICB.2010.64PMID:20458337
  20. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  21. 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.)