Wikipedia

CD74

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

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]

Искәрмәләр

үзгәртү
  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; 1540-9538 — doi:10.1084/JEM.20030286 — PMID: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. Skipper — NPG, Springer Science+Business Media, 1995. — ISSN 1476-4687; 0028-0836 — doi:10.1038/378457A0 — PMID: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 // Immunity — Cell Press, Elsevier BV, 2006. — ISSN 1074-7613; 1097-4180 — doi:10.1016/J.IMMUNI.2006.08.020 — PMID: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. Skipper — NPG, Springer Science+Business Media, 1992. — ISSN 1476-4687; 0028-0836 — doi:10.1038/360474A0 — PMID: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 1750-1326 — doi:10.1186/1750-1326-4-41 — PMID: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 // Immunology — Wiley-Blackwell, 2014. — ISSN 0019-2805; 1365-2567 — doi:10.1111/IMM.12249 — PMID: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; 1521-4141 — doi:10.1002/EJI.200636811 — PMID: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 // Onco_target / M. Blagosklonny — Impact Journals LLC, 2017. — ISSN 1949-2553 — doi:10.18632/ONCO_target.20922 — PMID: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 Morphology — Lippincott Williams & Wilkins, 2000. — ISSN 1062-3345; 1533-4058; 1541-2016 — doi:10.1097/00022744-200009000-00007 — PMID: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. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M702950200 — PMID: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; 1070-6321 — doi:10.1128/JVI.00616-14 — PMID: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 Biology — Wiley, 2010. — ISSN 0818-9641; 1440-1711 — doi:10.1038/ICB.2010.64 — PMID: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; 1096-9888 — doi:10.1002/JMS.1696 — PMID: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; 1540-9538 — doi:10.1084/JEM.20030286 — PMID:12782713
  18. ↑ Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom. — Wiley, 2010. — ISSN 1076-5174; 1096-9888 — doi:10.1002/JMS.1696 — PMID: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 Biology — Wiley, 2010. — ISSN 0818-9641; 1440-1711 — doi:10.1038/ICB.2010.64 — PMID: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.

Чыганаклар

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.)


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