DLG3

DLG3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UM7, 2FE5, 2I1N
Identifiers
Aliases	DLG3, MRX, MRX90, NEDLG, PPP1R82, SAP102, XLMR, discs large homolog 3, discs large MAGUK scaffold protein 3, XLID90
External IDs	OMIM: 300189 MGI: 1888986 HomoloGene: 41157 GeneCards: DLG3
Gene location (Human) Chr. X chromosome (human) Band Xq13.1 Start 70,444,835 bp End 70,505,490 bp
Gene location (Mouse) Chr. X chromosome (mouse) Band X|X C3 Start 99,811,328 bp End 99,862,016 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas ganglionic eminence rectum islet of Langerhans middle temporal gyrus pancreatic ductal cell prefrontal cortex minor salivary glands right uterine tube gallbladder Top expressed in retinal pigment epithelium superior frontal gyrus hippocampus proper cingulate gyrus piriform cortex olfactory tubercle Region I of hippocampus proper amygdala prefrontal cortex entorhinal cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphatase binding PDZ domain binding protein domain specific binding guanylate kinase activity kinase binding protein C-terminus binding protein binding ionotropic glutamate receptor binding protein phosphatase binding ubiquitin protein ligase binding ligand-gated ion channel activity structural constituent of postsynaptic density Cellular component cytoplasm postsynaptic membrane postsynaptic density cell-cell junction bicellular tight junction growth cone plasma membrane synapse dendritic shaft neuronal cell body basolateral plasma membrane AMPA glutamate receptor complex ionotropic glutamate receptor complex extracellular space cytosol cell junction neuromuscular junction neuron projection postsynaptic density membrane glutamatergic synapse postsynaptic density, intracellular component Biological process receptor localization to synapse negative regulation of phosphatase activity establishment of planar polarity receptor clustering nervous system development establishment or maintenance of epithelial cell apical/basal polarity negative regulation of cell population proliferation ion transmembrane transport GMP metabolic process GDP metabolic process chemical synaptic transmission 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
Orthologs Species Human Mouse Entrez 1741 53310 Ensembl ENSG00000082458 ENSMUSG00000000881 UniProt Q92796 P70175 RefSeq (mRNA) NM_001166278 NM_020730 NM_021120 NM_001177778 NM_001177779 NM_001177780 NM_001290402 NM_016747 RefSeq (protein) NP_001159750 NP_065781 NP_066943 NP_001171249 NP_001171250 NP_001171251 NP_001277331 NP_058027 Location (UCSC) Chr X: 70.44 – 70.51 Mb Chr X: 99.81 – 99.86 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Disks large homolog 3 (DLG3) also known as neuroendocrine-DLG or synapse-associated protein 102 (SAP-102) is a protein that in humans is encoded by the DLG3 gene. DLG3 is a member of the membrane-associated guanylate kinase (MAGUK) superfamily of proteins.

Interactions

DLG3 has been shown to interact with:

• APC,
• CRIPT,
• DLG4,
• EXOC3,
• EXOC4,
• GRIN2A,
• GRIN2B,
• GRIN2C,
• KCNJ12
• PTK2B, and
• SYNGAP1.

Further reading

• Lau LF, Mammen A, Ehlers MD, et al. (1996). "Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102". J. Biol. Chem. 271 (35): 21622–8. doi:10.1074/jbc.271.35.21622. PMID 8702950.
• Müller BM, Kistner U, Kindler S, et al. (1996). "SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo". Neuron. 17 (2): 255–65. doi:10.1016/S0896-6273(00)80157-9. PMID 8780649.
• Takeuchi M, Hata Y, Hirao K, et al. (1997). "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density". J. Biol. Chem. 272 (18): 11943–51. doi:10.1074/jbc.272.18.11943. PMID 9115257.
• Makino K, Kuwahara H, Masuko N, et al. (1997). "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. 14 (20): 2425–33. doi:10.1038/sj.onc.1201087. PMID 9188857. S2CID 6554126.
• Irie M, Hata Y, Takeuchi M, et al. (1997). "Binding of neuroligins to PSD-95". Science. 277 (5331): 1511–5. doi:10.1126/science.277.5331.1511. PMID 9278515.
• Kim JH, Liao D, Lau LF, Huganir RL (1998). "SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family". Neuron. 20 (4): 683–91. doi:10.1016/S0896-6273(00)81008-9. PMID 9581761.
• Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain". Cell. 94 (6): 773–82. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324.
• Garcia EP, Mehta S, Blair LA, et al. (1998). "SAP90 binds and clusters kainate receptors causing incomplete desensitization". Neuron. 21 (4): 727–39. doi:10.1016/S0896-6273(00)80590-5. PMID 9808460.
• Masuko N, Makino K, Kuwahara H, et al. (1999). "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. 274 (9): 5782–90. doi:10.1074/jbc.274.9.5782. PMID 10026200.
• Kuwahara H, Araki N, Makino K, et al. (1999). "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. 274 (45): 32204–14. doi:10.1074/jbc.274.45.32204. PMID 10542258.
• Nagase T, Ishikawa K, Kikuno R, et al. (2000). "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. 6 (5): 337–45. doi:10.1093/dnares/6.5.337. PMID 10574462.
• Firestein BL, Firestein BL, Brenman JE, et al. (2000). "Cypin: a cytosolic regulator of PSD-95 postsynaptic targeting". Neuron. 24 (3): 659–72. doi:10.1016/S0896-6273(00)81120-4. PMID 10595517.
• Garcia RA, Vasudevan K, Buonanno A (2000). "The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3596–601. doi:10.1073/pnas.070042497. PMC 16285. PMID 10725395.
• Husi H, Ward MA, Choudhary JS, et al. (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nat. Neurosci. 3 (7): 661–9. doi:10.1038/76615. hdl:1842/742. PMID 10862698. S2CID 14392630.
• Inagaki S, Ohoka Y, Sugimoto H, et al. (2001). "Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95". J. Biol. Chem. 276 (12): 9174–81. doi:10.1074/jbc.M009051200. PMID 11134026.
• DeMarco SJ, Strehler EE (2001). "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. 276 (24): 21594–600. doi:10.1074/jbc.M101448200. PMID 11274188.
• Russwurm M, Wittau N, Koesling D (2002). "Guanylyl cyclase/PSD-95 interaction: targeting of the nitric oxide-sensitive alpha2beta1 guanylyl cyclase to synaptic membranes". J. Biol. Chem. 276 (48): 44647–52. doi:10.1074/jbc.M105587200. PMID 11572861.
• Lim IA, Hall DD, Hell JW (2002). "Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102". J. Biol. Chem. 277 (24): 21697–711. doi:10.1074/jbc.M112339200. PMID 11937501.
• Cai C, Coleman SK, Niemi K, Keinänen K (2002). "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. 277 (35): 31484–90. doi:10.1074/jbc.M204354200. PMID 12070168.