MOUSE:DLG4

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Species (Taxon ID)	Mus musculus (Mouse). ([1])
Gene Name(s)	Dlg4 (synonyms: Dlgh4, Psd95)
Protein Name(s)	Disks large homolog 4 Postsynaptic density protein 95 PSD-95 Synapse-associated protein 90 SAP-90 SAP90
External Links
EMBL	D50621 AL596185 AL596185 AL596185 BC014807
IPI	IPI00122094 IPI00622720 IPI00626797
RefSeq	NP_001103222.1 NP_031890.1
UniGene	Mm.27256
ProteinModelPortal	Q62108
SMR	Q62108
DIP	DIP-29888N
IntAct	Q62108
MINT	MINT-136080
STRING	Q62108
PhosphoSite	Q62108
PRIDE	Q62108
Ensembl	ENSMUST00000018700 ENSMUST00000108588 ENSMUST00000108589
GeneID	13385
KEGG	mmu:13385
UCSC	uc007jtp.2 uc007jtq.2
CTD	1742
MGI	MGI:1277959
eggNOG	roNOG08565
HOVERGEN	HBG107814
OMA	WIPTRER
Reactome	REACT_92778
NextBio	283740
ArrayExpress	Q62108
Bgee	Q62108
CleanEx	MM_DLG4
Genevestigator	Q62108
GermOnline	ENSMUSG00000020886
GO	GO:0032281 GO:0030054 GO:0032839 GO:0060076 GO:0031234 GO:0044224 GO:0044306 GO:0014069 GO:0045211 GO:0019717 GO:0042043 GO:0008022 GO:0097110 GO:0005198 GO:0097113 GO:0060997 GO:0045184 GO:0035641 GO:0050885 GO:0006461 GO:0097120 GO:2000821 GO:0048169 GO:0042220 GO:0035176 GO:0016188 GO:0071625
InterPro	IPR008144 IPR008145 IPR020590 IPR016313 IPR019590 IPR001478 IPR019583 IPR011511 IPR001452
Pfam	PF00625 PF10608 PF00595 PF10600 PF07653
PIRSF	PIRSF001741
SMART	SM00072 SM00228 SM00326
SUPFAM	SSF50156 SSF50044
PROSITE	PS00856 PS50052 PS50106 PS50002

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005102	receptor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	F	Seeded From UniProt
	GO:0005102	receptor binding	GO_REF:0000029	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0005198	structural molecule activity	PMID:14980210^[1]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10827173^[2]	IPI: Inferred from Physical Interaction	UniProtKB:A2ARV4	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10827173^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q91ZX7	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10862698^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P35438	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11483650^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Z123	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11925566^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QYR6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15082773^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q9JI18	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15663482^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QVP4	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15883194^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P23818	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15883194^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P23819	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15883194^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Z2W8	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16332682^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P35436	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16332682^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q01097	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16332682^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q924X6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16495444^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q80TG9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16882004^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q810U4	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19022416^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9R111	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19243221^[13]	IPI: Inferred from Physical Interaction	UniProtKB:Q8R4I7	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P11798	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P46460	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P63001	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P63085	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P70175	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q811D0	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q8BKX1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q8K4G5	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q91XM9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19455133^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WV31	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19474308^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q8CFW1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19571134^[16]	IPI: Inferred from Physical Interaction	UniProtKB:Q925H0	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9647694^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P35436	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9647694^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P35439	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9647694^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q00960	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9647694^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q00961	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9647694^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q62645	F	Seeded From UniProt
	GO:0005624	membrane fraction	PMID:15082773^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000029	NAS: Non-traceable Author Statement		C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:11483650^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_22207	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0006461	protein complex assembly	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P78352	P	Seeded From UniProt
	GO:0007416	synapse assembly	GO_REF:0000029	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0007626	locomotory behavior	PMID:14980210^[1]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0008022	protein C-terminus binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	F	Seeded From UniProt
	GO:0008022	protein C-terminus binding	GO_REF:0000029	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0014069	postsynaptic density	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	C	Seeded From UniProt
	GO:0014069	postsynaptic density	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0297	C	Seeded From UniProt
	GO:0014069	postsynaptic density	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P31016	C	Seeded From UniProt
	GO:0014069	postsynaptic density	PMID:15317856^[18]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0014069	postsynaptic density	PMID:17018287^[19]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0014069	postsynaptic density	PMID:17093100^[20]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016188	synaptic vesicle maturation	PMID:15603741^[21]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0016188	synaptic vesicle maturation	PMID:15603741^[21]	IGI: Inferred from Genetic Interaction	MGI:MGI:1915336	P	Seeded From UniProt
	GO:0019717	synaptosome	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0771	C	Seeded From UniProt
	GO:0019717	synaptosome	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	C	Seeded From UniProt
	GO:0019717	synaptosome	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0261	C	Seeded From UniProt
	GO:0019717	synaptosome	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P31016	C	Seeded From UniProt
	GO:0019717	synaptosome	PMID:14645471^[22]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0019903	protein phosphatase binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	F	Seeded From UniProt
	GO:0030054	cell junction	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0965	C	Seeded From UniProt
	GO:0030165	PDZ domain binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	F	Seeded From UniProt
	GO:0031234	extrinsic to internal side of plasma membrane	PMID:11483650^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0032281	alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex	PMID:15883194^[8]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0032839	dendrite cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P31016	C	Seeded From UniProt
	GO:0035176	social behavior	PMID:20952458^[23]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0035255	ionotropic glutamate receptor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	F	Seeded From UniProt
	GO:0035418	protein localization to synapse	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P78352	P	Seeded From UniProt
	GO:0035641	locomotory exploration behavior	PMID:20952458^[23]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0042043	neurexin family protein binding	PMID:9278515^[24]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0042220	response to cocaine	PMID:14980210^[1]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0044224	juxtaparanode region of axon	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	C	Seeded From UniProt
	GO:0044224	juxtaparanode region of axon	PMID:19109503^[25]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0044306	neuron projection terminus	PMID:12115694^[26]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0044309	neuron spine	PMID:16606358^[27]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045184	establishment of protein localization	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P78352	P	Seeded From UniProt
	GO:0045202	synapse	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0770	C	Seeded From UniProt
	GO:0045202	synapse	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	C	Seeded From UniProt
	GO:0045202	synapse	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0258	C	Seeded From UniProt
	GO:0045202	synapse	PMID:12972605^[28]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045202	synapse	PMID:14622577^[29]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045202	synapse	PMID:15071120^[30]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045202	synapse	PMID:16818724^[31]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045211	postsynaptic membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0628	C	Seeded From UniProt
	GO:0045211	postsynaptic membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000025211	C	Seeded From UniProt
	GO:0048168	regulation of neuronal synaptic plasticity	PMID:14980210^[1]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0048169	regulation of long-term neuronal synaptic plasticity	PMID:12427827^[32]	IGI: Inferred from Genetic Interaction	MGI:MGI:3039785	P	Seeded From UniProt
	GO:0050885	neuromuscular process controlling balance	PMID:20952458^[23]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0060076	excitatory synapse	PMID:18272690^[33]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0060997	dendritic spine morphogenesis	PMID:20952458^[23]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0071625	vocalization behavior	PMID:20952458^[23]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0097110	scaffold protein binding	PMID:16606358^[27]	IPI: Inferred from Physical Interaction	UniProtKB:Q4ACU6	F	Seeded From UniProt
	GO:0097113	alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor clustering	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P31016	P	Seeded From UniProt
	GO:0097120	receptor localization to synapse	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P31016	P	Seeded From UniProt
	GO:2000821	regulation of grooming behavior	PMID:20952458^[23]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0014069	postsynaptic density	PMID:21664258^[34]	IMP: Inferred from Mutant Phenotype		C	Figure 2A- from Synaptosomal fraction found in postsynaptic density fraction of wild type and adult heterozygous reeler mice.	complete
	GO:0019717	synaptosome	PMID:21664258^[34]	IMP: Inferred from Mutant Phenotype		C	Figure 2A- from Synaptosomal fraction found in postsynaptic density fraction of wild type and adult heterozygous reeler mice. Synaptosomal fraction from brain of wild type mice, figure 5A.	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Yao WD et al. (2004) Identification of PSD-95 as a regulator of dopamine-mediated synaptic and behavioral plasticity. Neuron 41: 625-38 PubMed GONUTS page
↑ ^2.0 ^2.1 Gotthardt M et al. (2000) Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J Biol Chem 275: 25616-24 PubMed GONUTS page
↑ Husi H et al. (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat Neurosci 3: 661-9 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Schultze W et al. (2001) Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95. J Neurochem 78: 482-9 PubMed GONUTS page
↑ Ikeda A et al. (2002) Microtubule-associated protein 1A is a modifier of tubby hearing (moth1). Nat Genet 30: 401-5 PubMed GONUTS page
↑ ^6.0 ^6.1 Marschang P et al. (2004) Normal development and fertility of knockout mice lacking the tumor suppressor gene LRP1b suggest functional compensation by LRP1. Mol Cell Biol 24: 3782-93 PubMed GONUTS page
↑ Amparan D et al. (2005) Direct interaction of myosin regulatory light chain with the NMDA receptor. J Neurochem 92: 349-61 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Fukata Y et al. (2005) Molecular constituents of neuronal AMPA receptors. J Cell Biol 169: 399-404 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Hoe HS et al. (2006) Apolipoprotein E receptor 2 interactions with the N-methyl-D-aspartate receptor. J Biol Chem 281: 3425-31 PubMed GONUTS page
↑ Wang CY et al. (2006) A novel family of adhesion-like molecules that interacts with the NMDA receptor. J Neurosci 26: 2174-83 PubMed GONUTS page
↑ Dirks P et al. (2006) The cytoplasmic domain of NrCAM binds to PDZ domains of synapse-associated proteins SAP90/PSD95 and SAP97. Eur J Neurosci 24: 25-31 PubMed GONUTS page
↑ Klemmer P et al. (2009) Proteomics analysis of immuno-precipitated synaptic protein complexes. J Proteomics 72: 82-90 PubMed GONUTS page
↑ Ng D et al. (2009) Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning. PLoS Biol 7: e41 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 ^14.7 ^14.8 ^14.9 Fernández E et al. (2009) Targeted tandem affinity purification of PSD-95 recovers core postsynaptic complexes and schizophrenia susceptibility proteins. Mol Syst Biol 5: 269 PubMed GONUTS page
↑ Stöhr H et al. (2009) TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals. J Neurosci 29: 6809-18 PubMed GONUTS page
↑ Zha XM et al. (2009) ASIC2 subunits target acid-sensing ion channels to the synapse via an association with PSD-95. J Neurosci 29: 8438-46 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 Kurschner C et al. (1998) CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins. Mol Cell Neurosci 11: 161-72 PubMed GONUTS page
↑ Abe M et al. (2004) NMDA receptor GluRepsilon/NR2 subunits are essential for postsynaptic localization and protein stability of GluRzeta1/NR1 subunit. J Neurosci 24: 7292-304 PubMed GONUTS page
↑ Offenhäuser N et al. (2006) Increased ethanol resistance and consumption in Eps8 knockout mice correlates with altered actin dynamics. Cell 127: 213-26 PubMed GONUTS page
↑ Lai C et al. (2006) Amyotrophic lateral sclerosis 2-deficiency leads to neuronal degeneration in amyotrophic lateral sclerosis through altered AMPA receptor trafficking. J Neurosci 26: 11798-806 PubMed GONUTS page
↑ ^21.0 ^21.1 Fukata M et al. (2004) Identification of PSD-95 palmitoylating enzymes. Neuron 44: 987-96 PubMed GONUTS page
↑ Köhr G et al. (2003) Intracellular domains of NMDA receptor subtypes are determinants for long-term potentiation induction. J Neurosci 23: 10791-9 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Feyder M et al. (2010) Association of mouse Dlg4 (PSD-95) gene deletion and human DLG4 gene variation with phenotypes relevant to autism spectrum disorders and Williams' syndrome. Am J Psychiatry 167: 1508-17 PubMed GONUTS page
↑ Irie M et al. (1997) Binding of neuroligins to PSD-95. Science 277: 1511-5 PubMed GONUTS page
↑ Horresh I et al. (2008) Multiple molecular interactions determine the clustering of Caspr2 and Kv1 channels in myelinated axons. J Neurosci 28: 14213-22 PubMed GONUTS page
↑ Jellali A et al. (2002) Cellular localization of the vesicular inhibitory amino acid transporter in the mouse and human retina. J Comp Neurol 449: 76-87 PubMed GONUTS page
↑ ^27.0 ^27.1 Uchino S et al. (2006) Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-containing synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor. J Neurochem 97: 1203-14 PubMed GONUTS page
↑ Khalili K et al. (2003) Puralpha is essential for postnatal brain development and developmentally coupled cellular proliferation as revealed by genetic inactivation in the mouse. Mol Cell Biol 23: 6857-75 PubMed GONUTS page
↑ Bamji SX et al. (2003) Role of beta-catenin in synaptic vesicle localization and presynaptic assembly. Neuron 40: 719-31 PubMed GONUTS page
↑ Gitler D et al. (2004) Molecular determinants of synapsin targeting to presynaptic terminals. J Neurosci 24: 3711-20 PubMed GONUTS page
↑ Ahmad-Annuar A et al. (2006) Signaling across the synapse: a role for Wnt and Dishevelled in presynaptic assembly and neurotransmitter release. J Cell Biol 174: 127-39 PubMed GONUTS page
↑ Komiyama NH et al. (2002) SynGAP regulates ERK/MAPK signaling, synaptic plasticity, and learning in the complex with postsynaptic density 95 and NMDA receptor. J Neurosci 22: 9721-32 PubMed GONUTS page
↑ Hung AY et al. (2008) Smaller dendritic spines, weaker synaptic transmission, but enhanced spatial learning in mice lacking Shank1. J Neurosci 28: 1697-708 PubMed GONUTS page
↑ ^34.0 ^34.1 Ventruti A et al. (2011) Reelin deficiency causes specific defects in the molecular composition of the synapses in the adult brain. Neuroscience 189: 32-42 PubMed GONUTS page

[PMID:14980210-0] 1.0 ^1.1 ^1.2 ^1.3 Yao WD et al. (2004) Identification of PSD-95 as a regulator of dopamine-mediated synaptic and behavioral plasticity. Neuron 41: 625-38 PubMed GONUTS page

[PMID:10827173-1] 2.0 ^2.1 Gotthardt M et al. (2000) Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J Biol Chem 275: 25616-24 PubMed GONUTS page

[PMID:10862698-2] Husi H et al. (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat Neurosci 3: 661-9 PubMed GONUTS page

[PMID:11483650-3] 4.0 ^4.1 ^4.2 Schultze W et al. (2001) Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95. J Neurochem 78: 482-9 PubMed GONUTS page

[PMID:11925566-4] Ikeda A et al. (2002) Microtubule-associated protein 1A is a modifier of tubby hearing (moth1). Nat Genet 30: 401-5 PubMed GONUTS page

[PMID:15082773-5] 6.0 ^6.1 Marschang P et al. (2004) Normal development and fertility of knockout mice lacking the tumor suppressor gene LRP1b suggest functional compensation by LRP1. Mol Cell Biol 24: 3782-93 PubMed GONUTS page

[PMID:15663482-6] Amparan D et al. (2005) Direct interaction of myosin regulatory light chain with the NMDA receptor. J Neurochem 92: 349-61 PubMed GONUTS page

[PMID:15883194-7] 8.0 ^8.1 ^8.2 ^8.3 Fukata Y et al. (2005) Molecular constituents of neuronal AMPA receptors. J Cell Biol 169: 399-404 PubMed GONUTS page

[PMID:16332682-8] 9.0 ^9.1 ^9.2 Hoe HS et al. (2006) Apolipoprotein E receptor 2 interactions with the N-methyl-D-aspartate receptor. J Biol Chem 281: 3425-31 PubMed GONUTS page

[PMID:16495444-9] Wang CY et al. (2006) A novel family of adhesion-like molecules that interacts with the NMDA receptor. J Neurosci 26: 2174-83 PubMed GONUTS page

[PMID:16882004-10] Dirks P et al. (2006) The cytoplasmic domain of NrCAM binds to PDZ domains of synapse-associated proteins SAP90/PSD95 and SAP97. Eur J Neurosci 24: 25-31 PubMed GONUTS page

[PMID:19022416-11] Klemmer P et al. (2009) Proteomics analysis of immuno-precipitated synaptic protein complexes. J Proteomics 72: 82-90 PubMed GONUTS page

[PMID:19243221-12] Ng D et al. (2009) Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning. PLoS Biol 7: e41 PubMed GONUTS page

[PMID:19455133-13] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 ^14.7 ^14.8 ^14.9 Fernández E et al. (2009) Targeted tandem affinity purification of PSD-95 recovers core postsynaptic complexes and schizophrenia susceptibility proteins. Mol Syst Biol 5: 269 PubMed GONUTS page

[PMID:19474308-14] Stöhr H et al. (2009) TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals. J Neurosci 29: 6809-18 PubMed GONUTS page

[PMID:19571134-15] Zha XM et al. (2009) ASIC2 subunits target acid-sensing ion channels to the synapse via an association with PSD-95. J Neurosci 29: 8438-46 PubMed GONUTS page

[PMID:9647694-16] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 Kurschner C et al. (1998) CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins. Mol Cell Neurosci 11: 161-72 PubMed GONUTS page

[PMID:15317856-17] Abe M et al. (2004) NMDA receptor GluRepsilon/NR2 subunits are essential for postsynaptic localization and protein stability of GluRzeta1/NR1 subunit. J Neurosci 24: 7292-304 PubMed GONUTS page

[PMID:17018287-18] Offenhäuser N et al. (2006) Increased ethanol resistance and consumption in Eps8 knockout mice correlates with altered actin dynamics. Cell 127: 213-26 PubMed GONUTS page

[PMID:17093100-19] Lai C et al. (2006) Amyotrophic lateral sclerosis 2-deficiency leads to neuronal degeneration in amyotrophic lateral sclerosis through altered AMPA receptor trafficking. J Neurosci 26: 11798-806 PubMed GONUTS page

[PMID:15603741-20] 21.0 ^21.1 Fukata M et al. (2004) Identification of PSD-95 palmitoylating enzymes. Neuron 44: 987-96 PubMed GONUTS page

[PMID:14645471-21] Köhr G et al. (2003) Intracellular domains of NMDA receptor subtypes are determinants for long-term potentiation induction. J Neurosci 23: 10791-9 PubMed GONUTS page

[PMID:20952458-22] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Feyder M et al. (2010) Association of mouse Dlg4 (PSD-95) gene deletion and human DLG4 gene variation with phenotypes relevant to autism spectrum disorders and Williams' syndrome. Am J Psychiatry 167: 1508-17 PubMed GONUTS page

[PMID:9278515-23] Irie M et al. (1997) Binding of neuroligins to PSD-95. Science 277: 1511-5 PubMed GONUTS page

[PMID:19109503-24] Horresh I et al. (2008) Multiple molecular interactions determine the clustering of Caspr2 and Kv1 channels in myelinated axons. J Neurosci 28: 14213-22 PubMed GONUTS page

[PMID:12115694-25] Jellali A et al. (2002) Cellular localization of the vesicular inhibitory amino acid transporter in the mouse and human retina. J Comp Neurol 449: 76-87 PubMed GONUTS page

[PMID:16606358-26] 27.0 ^27.1 Uchino S et al. (2006) Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-containing synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor. J Neurochem 97: 1203-14 PubMed GONUTS page

[PMID:12972605-27] Khalili K et al. (2003) Puralpha is essential for postnatal brain development and developmentally coupled cellular proliferation as revealed by genetic inactivation in the mouse. Mol Cell Biol 23: 6857-75 PubMed GONUTS page

[PMID:14622577-28] Bamji SX et al. (2003) Role of beta-catenin in synaptic vesicle localization and presynaptic assembly. Neuron 40: 719-31 PubMed GONUTS page

[PMID:15071120-29] Gitler D et al. (2004) Molecular determinants of synapsin targeting to presynaptic terminals. J Neurosci 24: 3711-20 PubMed GONUTS page

[PMID:16818724-30] Ahmad-Annuar A et al. (2006) Signaling across the synapse: a role for Wnt and Dishevelled in presynaptic assembly and neurotransmitter release. J Cell Biol 174: 127-39 PubMed GONUTS page

[PMID:12427827-31] Komiyama NH et al. (2002) SynGAP regulates ERK/MAPK signaling, synaptic plasticity, and learning in the complex with postsynaptic density 95 and NMDA receptor. J Neurosci 22: 9721-32 PubMed GONUTS page

[PMID:18272690-32] Hung AY et al. (2008) Smaller dendritic spines, weaker synaptic transmission, but enhanced spatial learning in mice lacking Shank1. J Neurosci 28: 1697-708 PubMed GONUTS page

[PMID:21664258-33] 34.0 ^34.1 Ventruti A et al. (2011) Reelin deficiency causes specific defects in the molecular composition of the synapses in the adult brain. Neuroscience 189: 32-42 PubMed GONUTS page

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