DLG3

盘状大同系物3（英語：discs large homolog 3，简称DLG3），也被称为神经内分泌-DLG（英語：neuroendocrine-DLG）或突触相关蛋白102（英語：synapse-associated protein 102，简称SAP-102），是一种由人体DLG3基因编码的蛋白质 。 DLG3是膜相关鸟苷酸激酶（英語：membrane-associated guanylate kinase，简称MAGUK）蛋白总科的一种。 DLG3已经被发现可以与以下蛋白相互作用: APC, CRIPT, DLG4, EXOC3, EXOC4, GRIN2A, GRIN2B, GRIN2C, KCNJ12 PTK2B, and SYNGAP1. 被用来研究DLG3的模式生物之一是称作Dlg3tm1a(EUCOMM)Wtsi的条件性基因剔除后的小鼠族系，由位于英国的桑格中心（Wellcome Trust Sanger Institute）提供。 其雄性与雌性个体都经历了标准化的表现型筛查，以确保基因剔除的结果。 此外，其深度的免疫学表现型也被额外筛选。 與DLG3相關的疾病；在維基數據上查看/編輯參考.  GRCh38: Ensembl release 89: ENSG00000082458 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000000881 - Ensembl, May 2017 Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.  Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.  Stathakis DG, Lee D, Bryant PJ. DLG3, the gene encoding human neuroendocrine Dlg (NE-Dlg), is located within the 1.8-Mb dystonia-parkinsonism region at Xq13.1. Genomics. Aug 1998, 49 (2): 310–3. PMID 9598320. doi:10.1006/geno.1998.5243.  Entrez Gene: DLG3 Discs, large homolog 3 (neuroendocrine-dlg, Drosophila). （原始内容存档于2010-03-08）.  Makino K, Kuwahara H, Masuko N, Nishiyama Y, Morisaki T, Sasaki J, Nakao M, Kuwano A, Nakata M, Ushio Y, Saya H. Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein. Oncogene. May 1997, 14 (20): 2425–33. PMID 9188857. doi:10.1038/sj.onc.1201087.  Lim IA, Hall DD, Hell JW. Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102. J. Biol. Chem. Jun 2002, 277 (24): 21697–711. PMID 11937501. doi:10.1074/jbc.M112339200.  Masuko N, Makino K, Kuwahara H, Fukunaga K, Sudo T, Araki N, Yamamoto H, Yamada Y, Miyamoto E, Saya H. Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites. J. Biol. Chem. Feb 1999, 274 (9): 5782–90. PMID 10026200. doi:10.1074/jbc.274.9.5782.  Sans N, Prybylowski K, Petralia RS, Chang K, Wang YX, Racca C, Vicini S, Wenthold RJ. NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex. Nat. Cell Biol. Jun 2003, 5 (6): 520–30. PMID 12738960. doi:10.1038/ncb990.  Irie M, Hata Y, Takeuchi M, Ichtchenko K, Toyoda A, Hirao K, Takai Y, Rosahl TW, Südhof TC. Binding of neuroligins to PSD-95. Science. Sep 1997, 277 (5331): 1511–5. PMID 9278515. doi:10.1126/science.277.5331.1511.  Inanobe A, Fujita A, Ito M, Tomoike H, Inageda K, Kurachi Y. Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses. Am. J. Physiol., Cell Physiol. Jun 2002, 282 (6): C1396–403. PMID 11997254. doi:10.1152/ajpcell.00615.2001.  Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA. Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins. J. Biol. Chem. May 2004, 279 (21): 22331–46. PMID 15024025. doi:10.1074/jbc.M400285200.  Seabold GK, Burette A, Lim IA, Weinberg RJ, Hell JW. Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102. J. Biol. Chem. Apr 2003, 278 (17): 15040–8. PMID 12576483. doi:10.1074/jbc.M212825200.  Kim JH, Liao D, Lau LF, Huganir RL. SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron. Apr 1998, 20 (4): 683–91. PMID 9581761. doi:10.1016/S0896-6273(00)81008-9.  International Mouse Phenotyping Consortium. [2018-01-23]. （原始内容存档于2016-01-26）.  Infection and Immunity Immunophenotyping (3i) Consortium. [永久失效連結] Gerdin AK. The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice. Acta Ophthalmologica. 2010, 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.  Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A. A conditional knockout resource for the genome-wide study of mouse gene function. Nature. Jun 2011, 474 (7351): 337–42. PMC 3572410 . PMID 21677750. doi:10.1038/nature10163.  Dolgin E. Mouse library set to be knockout. Nature. Jun 2011, 474 (7351): 262–3. PMID 21677718. doi:10.1038/474262a.  Collins FS, Rossant J, Wurst W. A mouse for all reasons. Cell. Jan 2007, 128 (1): 9–13. PMID 17218247. doi:10.1016/j.cell.2006.12.018.  White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Sanger Institute Mouse Genetics Project, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP. Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes. Cell. 2013, 154 (2): 452–64. PMC 3717207 . PMID 23870131. doi:10.1016/j.cell.2013.06.022.  Lau LF, Mammen A, Ehlers MD, et al. Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102.. J. Biol. Chem. 1996, 271 (35): 21622–8. PMID 8702950. doi:10.1074/jbc.271.35.21622.  Müller BM, Kistner U, Kindler S, et al. SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo.. Neuron. 1996, 17 (2): 255–65. PMID 8780649. doi:10.1016/S0896-6273(00)80157-9.  Takeuchi M, Hata Y, Hirao K, et al. SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.. J. Biol. Chem. 1997, 272 (18): 11943–51. PMID 9115257. doi:10.1074/jbc.272.18.11943.  Makino K, Kuwahara H, Masuko N, et al. Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein.. Oncogene. 1997, 14 (20): 2425–33. PMID 9188857. doi:10.1038/sj.onc.1201087.  Irie M, Hata Y, Takeuchi M, et al. Binding of neuroligins to PSD-95.. Science. 1997, 277 (5331): 1511–5. PMID 9278515. doi:10.1126/science.277.5331.1511.  Kim JH, Liao D, Lau LF, Huganir RL. SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family.. Neuron. 1998, 20 (4): 683–91. PMID 9581761. doi:10.1016/S0896-6273(00)81008-9.  Butz S, Okamoto M, Südhof TC. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain.. Cell. 1998, 94 (6): 773–82. PMID 9753324. doi:10.1016/S0092-8674(00)81736-5.  Garcia EP, Mehta S, Blair LA, et al. SAP90 binds and clusters kainate receptors causing incomplete desensitization.. Neuron. 1998, 21 (4): 727–39. PMID 9808460. doi:10.1016/S0896-6273(00)80590-5.  Masuko N, Makino K, Kuwahara H, et al. Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites.. J. Biol. Chem. 1999, 274 (9): 5782–90. PMID 10026200. doi:10.1074/jbc.274.9.5782.  Kuwahara H, Araki N, Makino K, et al. A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor.. J. Biol. Chem. 1999, 274 (45): 32204–14. PMID 10542258. doi:10.1074/jbc.274.45.32204.  Nagase T, Ishikawa K, Kikuno R, et al. Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.. DNA Res. 2000, 6 (5): 337–45. PMID 10574462. doi:10.1093/dnares/6.5.337.  Firestein BL, Firestein BL, Brenman JE, et al. Cypin: a cytosolic regulator of PSD-95 postsynaptic targeting.. Neuron. 2000, 24 (3): 659–72. PMID 10595517. doi:10.1016/S0896-6273(00)81120-4.  Garcia RA, Vasudevan K, Buonanno A. The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses.. Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (7): 3596–601. PMC 16285 . PMID 10725395. doi:10.1073/pnas.070042497.  Husi H, Ward MA, Choudhary JS, et al. Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.. Nat. Neurosci. 2000, 3 (7): 661–9. PMID 10862698. doi:10.1038/76615.  Inagaki S, Ohoka Y, Sugimoto H, et al. Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95.. J. Biol. Chem. 2001, 276 (12): 9174–81. PMID 11134026. doi:10.1074/jbc.M009051200.  DeMarco SJ, Strehler EE. Plasma membrane Ca2+-atpase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins.. J. Biol. Chem. 2001, 276 (24): 21594–600. PMID 11274188. doi:10.1074/jbc.M101448200.  Russwurm M, Wittau N, Koesling D. Guanylyl cyclase/PSD-95 interaction: targeting of the nitric oxide-sensitive alpha2beta1 guanylyl cyclase to synaptic membranes.. J. Biol. Chem. 2002, 276 (48): 44647–52. PMID 11572861. doi:10.1074/jbc.M105587200.  Lim IA, Hall DD, Hell JW. Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102.. J. Biol. Chem. 2002, 277 (24): 21697–711. PMID 11937501. doi:10.1074/jbc.M112339200.  Cai C, Coleman SK, Niemi K, Keinänen K. Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif.. J. Biol. Chem. 2002, 277 (35): 31484–90. PMID 12070168. doi:10.1074/jbc.M204354200.