[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=DBA/2;
TISSUE=Brain;
Kohmura N.,
Yagi T.;
"Mouse homologue of rat PSD-95/SAP90A.";
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6;
TISSUE=Retina;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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FUNCTION, AND NULL MUTANT.
DOI=10.1038/24790; PubMed=9853749 [NCBI, ExPASy, EBI, Israel, Japan]
Migaud M.,
Charlesworth P.,
Dempster M.,
Webster L.C.,
Watabe A.M.,
Makhinson M.,
He Y.,
Ramsay M.F.,
Morris R.G.M.,
Morrison J.H.,
O'Dell T.J.,
Grant S.G.N.;
"Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein.";
Nature 396:433-439(1998).
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[5]
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INTERACTION WITH HTR2A.
DOI=10.1074/jbc.M312106200; PubMed=14988405 [NCBI, ExPASy, EBI, Israel, Japan]
Becamel C.,
Gavarini S.,
Chanrion B.,
Alonso G.,
Galeotti N.,
Dumuis A.,
Bockaert J.,
Marin P.;
"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins.";
J. Biol. Chem. 279:20257-20266(2004).
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[6]
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INTERACTION WITH ADR1B, DOMAIN, AND FUNCTION.
DOI=10.1074/jbc.M404876200; PubMed=15358775 [NCBI, ExPASy, EBI, Israel, Japan]
He J.,
Bellini M.,
Xu J.,
Castleberry A.M.,
Hall R.A.;
"Interaction with cystic fibrosis transmembrane conductance regulator-associated ligand (CAL) inhibits beta1-adrenergic receptor surface expression.";
J. Biol. Chem. 279:50190-50196(2004).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-418 AND TYR-432, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/jbc.M411220200; PubMed=15572359 [NCBI, ExPASy, EBI, Israel, Japan]
Collins M.O.,
Yu L.,
Coba M.P.,
Husi H.,
Campuzano I.,
Blackstock W.P.,
Choudhary J.S.,
Grant S.G.;
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
J. Biol. Chem. 280:5972-5982(2005).
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[8]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; TYR-240 AND SER-295, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.T500041-MCP200; PubMed=16452087 [NCBI, ExPASy, EBI, Israel, Japan]
Trinidad J.C.,
Specht C.G.,
Thalhammer A.,
Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
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[9]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; TYR-397; TYR-580; TYR-604 AND TYR-715, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A.,
Carey G.R.,
Sunyaev S.R.,
Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
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[10]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; SER-415 AND SER-418, AND MASS SPECTROMETRY.
TISSUE=Brain cortex;
DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan]
Munton R.P.,
Tweedie-Cullen R.,
Livingstone-Zatchej M.,
Weinandy F.,
Waidelich M.,
Longo D.,
Gehrig P.,
Potthast F.,
Rutishauser D.,
Gerrits B.,
Panse C.,
Schlapbach R.,
Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
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- FUNCTION: Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ACCN3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.
- SUBUNIT: Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D, ACCN3, certain splice forms of GRIN1, KCND2, CXADR, SYNGAP1, KCNA1, KCNA2, KCNA3, KCNA4 and ERBB4. Interacts through its first PDZ domain with GRIK2, KCNA4 and CRIPT. Interacts through its second PDZ domain with the PDZ domain of NOS1 or the C-terminus of CAPON. Interacts through its third PDZ domain with NLGN1 and CRIPT, and probably with NLGN2 and NLGN3. Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A, BEGAIN and KIF13B. Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK. Interacts with ANKS1B, LRFN1 and PRR7 (By similarity). Interacts with ADR1B. May interact with HTR2A.
- INTERACTION:
P35436:Grin2a; NbExp=1; IntAct=EBI-300895, EBI-400115;
Q01097:Grin2b; NbExp=1; IntAct=EBI-300895, EBI-400125;
Q80TG9:Lrfn2; NbExp=2; IntAct=EBI-300895, EBI-877092;
Q91ZX7:Lrp1; NbExp=1; IntAct=EBI-300895, EBI-300955;
Q9JLB3:Lrp2; NbExp=1; IntAct=EBI-300895, EBI-300875;
Q924X6:Lrp8; NbExp=1; IntAct=EBI-300895, EBI-432319;
Q8IUH5:ZDHHC17 (xeno); NbExp=1; IntAct=EBI-300895, EBI-524753;
- SUBCELLULAR LOCATION: Membrane (By similarity). Cell junction, synapse, postsynaptic cell membrane, postsynaptic density (By similarity). Cell junction, synapse (By similarity). Note=Membrane-associated. High levels in postsynaptic density of neurons in the forebrain. Also in presynaptic region of inhibitory synapses formed by cerebellar basket cells on axon hillocks of Purkinje cells (By similarity).
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Synonyms | PSD95-beta |
| Isoform ID | Q62108-2 |
| Features which should be applied to build the isoform sequence: VSP_014930. |
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| Name | 3 |
| Isoform ID | Q62108-3 |
| Note: No experimental confirmation available. |
| Features which should be applied to build the isoform sequence: VSP_014931. |
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- DOMAIN: The PDZ domain 3 mediates interaction with ADR1B.
- DOMAIN: The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to post-synaptic density (By similarity).
- PTM: Palmitoylation of isoform 1 is required for targeting to postsynaptic density (By similarity).
- MISCELLANEOUS: Mice with a stop codon in the third PDZ domain have impaired spatial learning. NMDA-mediated synaptic plasticity is lost even though receptor levels and localization are unchanged. Long-term potentiation of synaptic transmission is enhanced due to minimal long-term depression.
- SIMILARITY: Belongs to the MAGUK family.
- SIMILARITY: Contains 1 guanylate kinase-like domain.
- SIMILARITY: Contains 3 PDZ (DHR) domains.
- SIMILARITY: Contains 1 SH3 domain.
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