Details for: Dlg4
Associated with
Other Information
Genular Protein ID: 3042381683
Symbol: DLG4_RAT
Name: Disks large homolog 4
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 1419001
Title: The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein.
PubMed ID: 1419001
PubMed ID: 7680343
Title: SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A.
PubMed ID: 7680343
PubMed ID: 7569905
Title: Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
PubMed ID: 7569905
PubMed ID: 8922396
Title: Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein.
PubMed ID: 8922396
PubMed ID: 9115257
Title: SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.
PubMed ID: 9115257
PubMed ID: 9756850
Title: BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein.
PubMed ID: 9756850
PubMed ID: 9786987
Title: Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.
PubMed ID: 9786987
PubMed ID: 9581761
Title: SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family.
PubMed ID: 9581761
PubMed ID: 9581762
Title: CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90.
PubMed ID: 9581762
PubMed ID: 10629226
Title: Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering.
PubMed ID: 10629226
PubMed ID: 11134026
Title: Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95.
PubMed ID: 11134026
PubMed ID: 11483650
Title: Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95.
PubMed ID: 11483650
PubMed ID: 11502259
Title: Regulation of dendritic spine morphology by SPAR, a PSD-95-associated RapGAP.
PubMed ID: 11502259
PubMed ID: 11923279
Title: Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2.
PubMed ID: 11923279
PubMed ID: 12151521
Title: Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms.
PubMed ID: 12151521
PubMed ID: 11997254
Title: Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses.
PubMed ID: 11997254
PubMed ID: 14642282
Title: Ubiquitination regulates PSD-95 degradation and AMPA receptor surface expression.
PubMed ID: 14642282
PubMed ID: 15317815
Title: PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current.
PubMed ID: 15317815
PubMed ID: 15304526
Title: A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth.
PubMed ID: 15304526
DOI: 10.1242/jcs.01300
PubMed ID: 15603741
Title: Identification of PSD-95 palmitoylating enzymes.
PubMed ID: 15603741
PubMed ID: 15358863
Title: A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin.
PubMed ID: 15358863
PubMed ID: 15629447
Title: Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor.
PubMed ID: 15629447
PubMed ID: 16054660
Title: Interactions between CAP70 and actinfilin are important for integrity of actin cytoskeleton structures in neurons.
PubMed ID: 16054660
PubMed ID: 16495444
Title: A novel family of adhesion-like molecules that interacts with the NMDA receptor.
PubMed ID: 16495444
PubMed ID: 16630835
Title: SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses.
PubMed ID: 16630835
PubMed ID: 16990550
Title: Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission.
PubMed ID: 16990550
PubMed ID: 17334360
Title: Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons.
PubMed ID: 17334360
DOI: 10.1038/nn1867
PubMed ID: 19118189
Title: Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis.
PubMed ID: 19118189
PubMed ID: 19596852
Title: Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95.
PubMed ID: 19596852
PubMed ID: 20628354
Title: PTEN is recruited to the postsynaptic terminal for NMDA receptor-dependent long-term depression.
PubMed ID: 20628354
PubMed ID: 20962234
Title: Regulation of synaptic Rac1 activity, long-term potentiation maintenance, and learning and memory by BCR and ABR Rac GTPase-activating proteins.
PubMed ID: 20962234
PubMed ID: 20089912
Title: ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated guanylate kinases to juxtaparanodes of myelinated axons.
PubMed ID: 20089912
PubMed ID: 21119615
Title: DGKiota regulates presynaptic release during mGluR-dependent LTD.
PubMed ID: 21119615
PubMed ID: 22673903
Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
PubMed ID: 22673903
DOI: 10.1038/ncomms1871
PubMed ID: 23300088
Title: Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled receptor 30 (GPR30), an estrogen receptor that can be identified in hippocampal dendritic spines.
PubMed ID: 23300088
PubMed ID: 26679993
Title: Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex.
PubMed ID: 26679993
DOI: 10.1038/ncomms10181
PubMed ID: 27458189
Title: Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates NMDA-mediated excitotoxicity.
PubMed ID: 27458189
PubMed ID: 27307232
Title: Identification of PSD-95 Depalmitoylating Enzymes.
PubMed ID: 27307232
PubMed ID: 27756895
Title: MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density.
PubMed ID: 27756895
DOI: 10.1038/srep35283
PubMed ID: 30021165
Title: Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.
PubMed ID: 30021165
PubMed ID: 31189538
Title: Regulation of dendrite morphology and excitatory synapse formation by zDHHC15.
PubMed ID: 31189538
DOI: 10.1242/jcs.230052
PubMed ID: 8674113
Title: Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ.
PubMed ID: 8674113
PubMed ID: 10623522
Title: Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95.
PubMed ID: 10623522
PubMed ID: 11779504
Title: Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins.
PubMed ID: 11779504
PubMed ID: 11779506
Title: Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.
PubMed ID: 11779506
PubMed ID: 15123241
Title: Targeting specific PDZ domains of PSD-95; structural basis for enhanced affinity and enzymatic stability of a cyclic peptide.
PubMed ID: 15123241
PubMed ID: 19072119
Title: Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: a revisit to N-terminal tandem PDZ domains of PSD-95.
PubMed ID: 19072119
DOI: 10.1021/ja8076022
Sequence Information:
- Length: 724
- Mass: 80465
- Checksum: 7922D4E8E0F9AD85
- Sequence:
MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKVME IKLIKGPKGL GFSIAGGVGN QHIPGDNSIY VTKIIEGGAA HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY LKVAKPSNAY LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDQIL SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF EAKIHDLREQ LMNSSLGSGT ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ ALSFRFGDVL HVIDAGDEEW WQARRVHSDS ETDDIGFIPS KRRVERREWS RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL GPTKDRANDD LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI RPRSLENVLE INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI YHKVKRVIED LSGPYIWVPA RERL
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.