DLG3

已知的結構

直系同源搜索: PDBe RCSB

PDBID列表
1UM7、2FE5、2I1N

識別號

别名

DLG3；, MRX, MRX90, NEDLG, PPP1R82, SAP102, XLMR, discs large homolog 3, discs large MAGUK scaffold protein 3, XLID90

外部ID

OMIM：300189 MGI：1888986 HomoloGene：41157 GeneCards：DLG3

相關疾病

non-syndromic X-linked intellectual disability^[1]

基因位置（人类）

染色体	X染色體^[2]

基因座	Xq13.1	起始	70,444,835 bp^[2]
基因座	Xq13.1	终止	70,505,490 bp^[2]

基因位置（小鼠）

染色体	小鼠X染色体^[3]

基因座	X\|X C3	起始	99,811,328 bp^[3]
基因座	X\|X C3	终止	99,862,016 bp^[3]

RNA表达模式

查阅更多表达数据

基因本體
分子功能	• phosphatase binding • PDZ domain binding • protein domain specific binding • guanylate kinase activity • 激酶结合 • protein C-terminus binding • 血浆蛋白结合 • ionotropic glutamate receptor binding • protein phosphatase binding • 泛素蛋白连接酶结合 • ligand-gated ion channel activity • structural constituent of postsynaptic density
細胞組分	• 細胞質 • postsynaptic membrane • 突触后致密物质 • cell-cell junction • 双细胞紧密连接 • 生长锥 • 细胞膜 • 突触 • dendritic shaft • neuronal cell body • basolateral plasma membrane • AMPA glutamate receptor complex • ionotropic glutamate receptor complex • 細胞外空間 • 细胞质基质 • 细胞连接 • 神经肌肉接点 • 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 • 化学性突触传递 • 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
Sources:Amigo / QuickGO

直系同源

物種

人類

小鼠

Entrez


1741


53310

Ensembl


ENSG00000082458


ENSMUSG00000000881

UniProt


Q92796


P70175

mRNA序列


NM_001166278 NM_020730 NM_021120


NM_001177778 NM_001177779 NM_001177780 NM_001290402 NM_016747

蛋白序列


NP_001159750 NP_065781 NP_066943


NP_001171249 NP_001171250 NP_001171251 NP_001277331 NP_058027

基因位置（UCSC）

Chr X: 70.44 – 70.51 Mb

Chr X: 99.81 – 99.86 Mb

PubMed查找

^[4]

^[5]

維基數據

檢視/編輯人類

檢視/編輯小鼠

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。^[6]^[7] 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。

与其它蛋白的相互作用

DLG3已经被发现可以与以下蛋白相互作用:

APC,^[8]
CRIPT,^[9]
DLG4,^[10]
EXOC3,^[11]
EXOC4,^[11]
GRIN2A,^[9]^[12]
GRIN2B,^[9]^[11]^[12]^[13]
GRIN2C,^[9]
KCNJ12^[14]
PTK2B,^[15] and
SYNGAP1.^[16]

模式生物

*Dlg3* 基因剔除小鼠表现型
特征	表现型
所有可用数据来自^[17]^[18]
外周血白细胞（6周）	正常
胰岛素	正常
血液（6周）	正常
P14上纯合子存活能力	正常
纯合子生育能力	正常
一般性意见	异常
体重	正常
神经系统评估	正常
抓握能力	正常
畸形学	正常
间接热量	正常
葡萄糖耐性测试	正常
听觉脑干反应	正常
DEXA	正常
X光成像	正常
眼睛形态	正常
临床用化学	正常
血液（16周）	正常
外周血白细胞（16周）	正常
心脏重量	正常
沙门氏菌感染	正常
细胞毒性T细胞的功能	正常
脾免疫	正常
肠系膜淋巴结免疫	正常
骨髓免疫	正常
表皮免疫的组成	正常
流感威胁	正常

被用来研究DLG3的模式生物之一是称作Dlg3^{tm1a(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。^[19] 其雄性与雌性个体都经历了标准化的表现型筛查^[17]，以确保基因剔除的结果。^[20]^[21]^[22]^[23] 此外，其深度的免疫学表现型也被额外筛选。^[18]

参考资料

^ 與DLG3相關的疾病；在維基數據上查看/編輯參考.
^ ^2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000082458 - Ensembl, May 2017
^ ^3.0 ^3.1 ^3.2 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.
^ ^9.0 ^9.1 ^9.2 ^9.3 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.
^ ^11.0 ^11.1 ^11.2 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.
^ ^12.0 ^12.1 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.
^ ^17.0 ^17.1 International Mouse Phenotyping Consortium. [2018-01-23]. （原始内容存档于2016-01-26）.
^ ^18.0 ^18.1 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.

进一步阅读

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.