DLG3

DLG3
已知的結構
PDB	直系同源搜尋：PDBe RCSB
PDBID列表
	1UM7、2FE5、2I1N
標識符
代號	DLG3、盤狀大同系物3
擴展標識	OMIM：300189；MGI：1888986；HomoloGene：41157；GeneCards：DLG3；OMA：DLG3 - orthologs
基因位置（人類）
染色體	X染色體
終止	70,505,490 bp
基因位置（小鼠）
染色體	小鼠X染色體
終止	99,862,016 bp
RNA表現模式
	Top expressed in
	body of pancreas; ; buccal mucosa cell; ; ganglionic eminence; ; olfactory zone of nasal mucosa; ; pancreatic ductal cell; ; mucosa of transverse colon;
	Top expressed in
	dentate gyrus of hippocampal formation granule cell; ; hippocampus proper; ; Region I of hippocampus proper;
	查閱更多表現資料
	; ; ; ;
	查閱更多表現資料
基因本體
分子功能	phosphatase binding; PDZ domain binding; protein domain specific binding; guanylate kinase activity; 激酶結合; protein C-terminus binding; 血漿蛋白結合; ionotropic glutamate receptor binding; protein phosphatase binding; 泛素蛋白連接酶結合; ligand-gated ion channel activity; structural constituent of postsynaptic density;
細胞組分	細胞質; postsynaptic membrane; 突觸後緻密物質; cell-cell junction; 雙細胞緊密連接; 生長錐; 細胞膜; 突觸; dendritic shaft; soma; basolateral plasma membrane; AMPA glutamate receptor complex; ionotropic glutamate receptor complex; 細胞外空間; 細胞質基質; 細胞連接; 神經肌肉接點; neuron projection; postsynaptic density membrane; glutamatergic synapse; postsynaptic density, intracellular component;
生物學過程	receptor localization to synapse; negative regulation of phosphatase activity; establishment of planar polarity; receptor clustering; 神經系統的發育; establishment or maintenance of epithelial cell apical/basal polarity; negative regulation of cell population proliferation; ion transmembrane transport; GMP metabolic process; GDP metabolic process; 化學性突觸傳遞; MAPK cascade; positive regulation of protein tyrosine kinase activity; cell-cell adhesion; regulation of postsynaptic membrane neurotransmitter receptor levels; maintenance of postsynaptic density structure; regulation of NMDA receptor activity;
	來源：Amigo / QuickGO
直系同源
	1741
	53310
	ENSG00000082458
	ENSMUSG00000000881
	Q92796
	P70175
	NM_001166278; NM_020730; NM_021120
	NM_001177778; NM_001177779; NM_001177780; NM_001290402; NM_016747
	NP_001159750; NP_065781; NP_066943
	NP_001171249; NP_001171250; NP_001171251; NP_001277331; NP_058027
	維基數據
檢視/編輯人類	檢視/編輯小鼠

盤狀大同系物3（英語：discs large homolog 3，簡稱DLG3），也被稱為神經內分泌-DLG（英語：neuroendocrine-DLG）或突觸相關蛋白102（英語：synapse-associated protein 102，簡稱SAP-102），是一種由人體DLG3基因編碼的蛋白質。^[5]^[6]DLG3是膜相關鳥苷酸激酶（英語：membrane-associated guanylate kinase，簡稱MAGUK）蛋白總科的一種。

與其它蛋白的相互作用

DLG3已經被發現可以與以下蛋白相互作用:

模式生物

*Dlg3* 基因剔除小鼠表現型
特徵	表現型
所有可用資料來自^[16]^[17]
外周血白血球（6周）	正常
胰島素	正常
血液（6周）	正常
P14上純合子存活能力	正常
純合子生育能力	正常
一般性意見	異常
體重	正常
神經系統評估	正常
抓握能力	正常
畸形學	正常
間接熱量	正常
葡萄糖耐性測試	正常
聽覺腦幹反應	正常
DEXA	正常
X光成像	正常
眼睛形態	正常
臨床用化學	正常
血液（16周）	正常
外周血白血球（16周）	正常
心臟重量	正常
沙門氏菌感染	正常
細胞毒性T細胞的功能	正常
脾免疫	正常
腸繫膜淋巴結免疫	正常
骨髓免疫	正常
表皮免疫的組成	正常
流感威脅	正常

被用來研究DLG3的模式生物之一是稱作Dlg3^{tm1a(EUCOMM)Wtsi}的條件性基因剔除後的小鼠族系，由位於英國的桑格中心（Wellcome Trust Sanger Institute）提供。^[18]其雄性與雌性個體都經歷了標準化的表現型篩查^[16]，以確保基因剔除的結果。^[19]^[20]^[21]^[22]此外，其深度的免疫學表現型也被額外篩選。^[17]

參考資料

^ ^1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000082458 – Ensembl, May 2017
^ ^2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000000881 – Ensembl, 2017年5月
^ 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). （原始內容存檔於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.
^ ^8.0 ^8.1 ^8.2 ^8.3 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.
^ ^10.0 ^10.1 ^10.2 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.
^ ^11.0 ^11.1 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.
^ ^16.0 ^16.1 International Mouse Phenotyping Consortium. [2018-01-23]. （原始內容存檔於2016-01-26）.
^ ^17.0 ^17.1 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.

進一步閱讀

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.

[refGRCh38Ensembl-1] 1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000082458 – Ensembl, May 2017

[refGRCm38Ensembl-2] 2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000000881 – Ensembl, 2017年5月

[3] Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9598320-5] 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.

[6] Entrez Gene: DLG3 Discs, large homolog 3 (neuroendocrine-dlg, Drosophila). （原始內容存檔於2010-03-08）.

[pmid9188857-7] 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.

[pmid11937501-8] 8.0 ^8.1 ^8.2 ^8.3 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.

[pmid10026200-9] 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.

[pmid12738960-10] 10.0 ^10.1 ^10.2 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.

[pmid9278515-11] 11.0 ^11.1 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.

[pmid11997254-12] 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.

[pmid15024025-13] 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.

[pmid12576483-14] 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.

[pmid9581761-15] 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.

[IMPCsearch_ref-16] 16.0 ^16.1 International Mouse Phenotyping Consortium. [2018-01-23]. （原始內容存檔於2016-01-26）.

[iii_ref-17] 17.0 ^17.1 Infection and Immunity Immunophenotyping (3i) Consortium. ^{[永久失效連結]}

[mgp_reference-18] 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.

[pmid21677750-19] 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.

[mouse_library-20] Dolgin E. Mouse library set to be knockout. Nature. Jun 2011, 474 (7351): 262–3. PMID 21677718. doi:10.1038/474262a.

[mouse_for_all_reasons-21] 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.

[pmid23870131-22] 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.

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[6]

[7]

[8]

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[16]

[17]

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[22]