Details for: Dlg4

Gene ID: 29495

Symbol: Dlg4

Ensembl ID: ENSRNOG00000018526

Description: discs large MAGUK scaffold protein 4

Associated with

Other Information

Genular Protein ID: 3042381683

Symbol: DLG4_RAT

Name: Disks large homolog 4

UniProtKB Accession Codes:

P31016 P97631

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 BMRB 1 Bgee 1 BioGRID 1 CDD 3 CORUM 1 CTD 1 ChEMBL 1 DIP 1 DisProt 1 ELM 1 EMBL 3 EMDB 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 83 Gene3D 4 Genevisible 1 HOGENOM 1 InParanoid 1 IntAct 1 InterPro 11 KEGG 1 MINT 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PDB 54 PDBsum 40 PIR 2 PIRSF 1 PRO 1 PROSITE 4 PROSITE-ProRule 3 PaxDb 1 Pfam 5 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 RGD 2 Reactome 8 RefSeq 1 SAM 1 SMART 4 SMR 1 STRING 1 SUPFAM 3 SwissPalm 1 UCSC 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1

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

DOI: 10.1016/0896-6273(92)90245-9

PubMed ID: 7680343

Title: SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A.

PubMed ID: 7680343

DOI: 10.1016/s0021-9258(18)53433-5

PubMed ID: 7569905

Title: Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.

PubMed ID: 7569905

DOI: 10.1126/science.7569905

PubMed ID: 8922396

Title: Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein.

PubMed ID: 8922396

DOI: 10.1523/jneurosci.16-23-07407.1996

PubMed ID: 9115257

Title: SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.

PubMed ID: 9115257

DOI: 10.1074/jbc.272.18.11943

PubMed ID: 9756850

Title: BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein.

PubMed ID: 9756850

DOI: 10.1074/jbc.273.41.26269

PubMed ID: 9786987

Title: Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.

PubMed ID: 9786987

DOI: 10.1523/jneurosci.18-21-08805.1998

PubMed ID: 9581761

Title: SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family.

PubMed ID: 9581761

DOI: 10.1016/s0896-6273(00)81008-9

PubMed ID: 9581762

Title: CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90.

PubMed ID: 9581762

DOI: 10.1016/s0896-6273(00)81009-0

PubMed ID: 10629226

Title: Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering.

PubMed ID: 10629226

DOI: 10.1083/jcb.148.1.159

PubMed ID: 11134026

Title: Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95.

PubMed ID: 11134026

DOI: 10.1074/jbc.m009051200

PubMed ID: 11483650

Title: Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95.

PubMed ID: 11483650

DOI: 10.1046/j.1471-4159.2001.00447.x

PubMed ID: 11502259

Title: Regulation of dendritic spine morphology by SPAR, a PSD-95-associated RapGAP.

PubMed ID: 11502259

DOI: 10.1016/s0896-6273(01)00355-5

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

DOI: 10.1074/jbc.m109412200

PubMed ID: 12151521

Title: Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms.

PubMed ID: 12151521

DOI: 10.1523/jneurosci.22-15-06415.2002

PubMed ID: 11997254

Title: Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses.

PubMed ID: 11997254

DOI: 10.1152/ajpcell.00615.2001

PubMed ID: 14642282

Title: Ubiquitination regulates PSD-95 degradation and AMPA receptor surface expression.

PubMed ID: 14642282

DOI: 10.1016/s0896-6273(03)00687-1

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

DOI: 10.1074/jbc.m405874200

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

DOI: 10.1016/j.neuron.2004.12.005

PubMed ID: 15358863

Title: A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin.

PubMed ID: 15358863

DOI: 10.1073/pnas.0405939101

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

DOI: 10.1016/j.bbrc.2004.11.154

PubMed ID: 16054660

Title: Interactions between CAP70 and actinfilin are important for integrity of actin cytoskeleton structures in neurons.

PubMed ID: 16054660

DOI: 10.1016/j.neuropharm.2005.05.022

PubMed ID: 16495444

Title: A novel family of adhesion-like molecules that interacts with the NMDA receptor.

PubMed ID: 16495444

DOI: 10.1523/jneurosci.3799-05.2006

PubMed ID: 16630835

Title: SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses.

PubMed ID: 16630835

DOI: 10.1016/j.neuron.2006.04.005

PubMed ID: 16990550

Title: Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission.

PubMed ID: 16990550

DOI: 10.1126/science.1129947

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

DOI: 10.1523/jneurosci.3112-08.2008

PubMed ID: 19596852

Title: Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95.

PubMed ID: 19596852

DOI: 10.1083/jcb.200903101

PubMed ID: 20628354

Title: PTEN is recruited to the postsynaptic terminal for NMDA receptor-dependent long-term depression.

PubMed ID: 20628354

DOI: 10.1038/emboj.2010.160

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

DOI: 10.1523/jneurosci.1711-10.2010

PubMed ID: 20089912

Title: ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated guanylate kinases to juxtaparanodes of myelinated axons.

PubMed ID: 20089912

DOI: 10.1523/jneurosci.4661-09.2010

PubMed ID: 21119615

Title: DGKiota regulates presynaptic release during mGluR-dependent LTD.

PubMed ID: 21119615

DOI: 10.1038/emboj.2010.286

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

DOI: 10.1074/jbc.m112.412478

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

DOI: 10.15252/embj.201593070

PubMed ID: 27307232

Title: Identification of PSD-95 Depalmitoylating Enzymes.

PubMed ID: 27307232

DOI: 10.1523/jneurosci.0419-16.2016

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

DOI: 10.1016/j.celrep.2018.06.071

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

DOI: 10.1016/s0092-8674(00)81307-0

PubMed ID: 10623522

Title: Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95.

PubMed ID: 10623522

DOI: 10.1006/jmbi.1999.3350

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

DOI: 10.1016/s1097-2765(01)00411-7

PubMed ID: 11779506

Title: Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.

PubMed ID: 11779506

DOI: 10.1016/s1097-2765(01)00416-6

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

DOI: 10.1016/j.chembiol.2004.03.013

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.