[1]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Brain;
DOI=10.1016/0896-6273(92)90245-9; PubMed=1419001 [NCBI, ExPASy, EBI, Israel, Japan]
Cho K.-O.,
Hunt C.A.,
Kennedy M.B.;
"The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein.";
Neuron 9:929-942(1992).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Brain;
PubMed=7680343 [NCBI, ExPASy, EBI, Israel, Japan]
Kistner U.,
Wenzel B.M.,
Veh R.W.,
Cases-Langhoff C.,
Garner A.M.,
Appeltauer U.,
Voss B.,
Gundelfinger E.D.,
Garner C.C.;
"SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A.";
J. Biol. Chem. 268:4580-4583(1993).
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[3]
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PROTEIN SEQUENCE OF 113-126; 212-233; 300-312; 381-399 AND 598-617, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus;
Lubec G.,
Diao W.;
Submitted (APR-2007) to UniProtKB.
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] OF 566-625.
STRAIN=Wistar Kyoto;
TISSUE=Vascular smooth muscle;
Adams L.D.,
Werny I.,
Schwartz S.M.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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[5]
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INTERACTION WITH GRIN2A; GRIN2B; GRIN2C AND GRIN2D.
PubMed=7569905 [NCBI, ExPASy, EBI, Israel, Japan]
Kornau H.C.,
Schenker L.T.,
Kennedy M.B.,
Seeburg P.H.;
"Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.";
Science 269:1737-1740(1995).
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[6]
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SUBCELLULAR LOCATION.
PubMed=8922396 [NCBI, ExPASy, EBI, Israel, Japan]
Brenman J.E.,
Christopherson K.S.,
Craven S.E.,
McGee A.W.,
Bredt D.S.;
"Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein.";
J. Neurosci. 16:7407-7415(1996).
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[7]
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INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
DOI=10.1074/jbc.272.18.11943; PubMed=9115257 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi M.,
Hata Y.,
Hirao K.,
Toyoda A.,
Irie M.,
Takai Y.;
"SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.";
J. Biol. Chem. 272:11943-11951(1997).
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[8]
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INTERACTION WITH BEGAIN AND DLGAP1.
DOI=10.1074/jbc.273.41.26269; PubMed=9756850 [NCBI, ExPASy, EBI, Israel, Japan]
Deguchi M.,
Hata Y.,
Takeuchi M.,
Ide N.,
Hirao K.,
Yao I.,
Irie M.,
Toyoda A.,
Takai Y.;
"BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein.";
J. Biol. Chem. 273:26269-26272(1998).
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[9]
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INTERACTION WITH MAP1A.
PubMed=9786987 [NCBI, ExPASy, EBI, Israel, Japan]
Brenman J.E.,
Topinka J.R.,
Cooper E.C.,
McGee A.W.,
Rosen J.,
Milroy T.,
Ralston H.J.,
Bredt D.S.;
"Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.";
J. Neurosci. 18:8805-8813(1998).
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[10]
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INTERACTION WITH SYNGAP1.
DOI=10.1016/S0896-6273(00)81008-9; PubMed=9581761 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.H.,
Liao D.,
Lau L.-F.,
Huganir R.L.;
"SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family.";
Neuron 20:683-691(1998).
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[11]
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INTERACTION WITH CRIPT.
DOI=10.1016/S0896-6273(00)81009-0; PubMed=9581762 [NCBI, ExPASy, EBI, Israel, Japan]
Niethammer M.,
Valtschanoff J.G.,
Kapoor T.M.,
Allison D.W.,
Weinberg R.J.,
Craig A.M.,
Sheng M.;
"CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90.";
Neuron 20:693-707(1998).
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[12]
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MUTAGENESIS OF CYS-3 AND CYS-5, AND PALMITOYLATION AT CYS-3 AND CYS-5.
DOI=10.1083/jcb.148.1.159; PubMed=10629226 [NCBI, ExPASy, EBI, Israel, Japan]
El-Husseini A.E.,
Craven S.E.,
Chetkovich D.M.,
Firestein B.L.,
Schnell E.,
Aoki C.,
Bredt D.S.;
"Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering.";
J. Cell Biol. 148:159-172(2000).
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[13]
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INTERACTION WITH KCND2.
DOI=10.1074/jbc.M109412200; PubMed=11923279 [NCBI, ExPASy, EBI, Israel, Japan]
Wong W.,
Newell E.W.,
Jugloff D.G.M.,
Jones O.T.,
Schlichter L.C.;
"Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2.";
J. Biol. Chem. 277:20423-20430(2002).
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[14]
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ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=12151521 [NCBI, ExPASy, EBI, Israel, Japan]
Chetkovich D.M.,
Bunn R.C.,
Kuo S.-H.,
Kawasaki Y.,
Kohwi M.,
Bredt D.S.;
"Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms.";
J. Neurosci. 22:6415-6425(2002).
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[15]
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INTERACTION WITH ACCN3, AND FUNCTION.
DOI=10.1074/jbc.M405874200; PubMed=15317815 [NCBI, ExPASy, EBI, Israel, Japan]
Hruska-Hageman A.M.,
Benson C.J.,
Leonard A.S.,
Price M.P.,
Welsh M.J.;
"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current.";
J. Biol. Chem. 279:46962-46968(2004).
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[16]
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INTERACTION WITH CXADR.
DOI=10.1242/jcs.01300; PubMed=15304526 [NCBI, ExPASy, EBI, Israel, Japan]
Ashbourne-Excoffon K.J.D.,
Hruska-Hageman A.M.,
Klotz M.,
Traver G.L.,
Zabner J.;
"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth.";
J. Cell Sci. 117:4401-4409(2004).
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[17]
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FUNCTION.
DOI=10.1073/pnas.0405939101; PubMed=15358863 [NCBI, ExPASy, EBI, Israel, Japan]
Prange O.,
Wong T.P.,
Gerrow K.,
Wang Y.T.,
El-Husseini A.;
"A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin.";
Proc. Natl. Acad. Sci. U.S.A. 101:13915-13920(2004).
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[18]
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INTERACTION WITH PRR7.
DOI=10.1016/j.bbrc.2004.11.154; PubMed=15629447 [NCBI, ExPASy, EBI, Israel, Japan]
Murata Y.,
Doi T.,
Taniguchi H.,
Fujiyoshi Y.;
"Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor.";
Biochem. Biophys. Res. Commun. 327:183-191(2005).
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[19]
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INTERACTION WITH LRFN1.
DOI=10.1016/j.neuron.2006.04.005; PubMed=16630835 [NCBI, ExPASy, EBI, Israel, Japan]
Ko J.,
Kim S.,
Chung H.S.,
Kim K.,
Han K.,
Kim H.,
Jun H.,
Kaang B.-K.,
Kim E.;
"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses.";
Neuron 50:233-245(2006).
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[20]
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INTERACTION WITH ANKS1B.
DOI=10.1038/nn1867; PubMed=17334360 [NCBI, ExPASy, EBI, Israel, Japan]
Jordan B.A.,
Fernholz B.D.,
Khatri L.,
Ziff E.B.;
"Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons.";
Nat. Neurosci. 10:427-435(2007).
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[21]
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X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 302-402.
DOI=10.1016/S0092-8674(00)81307-0; PubMed=8674113 [NCBI, ExPASy, EBI, Israel, Japan]
Doyle D.A.,
Lee A.,
Lewis J.,
Kim E.,
Sheng M.,
Mackinnon R.;
"Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ.";
Cell 85:1067-1076(1996).
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[22]
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STRUCTURE BY NMR OF 155-246, AND INTERACTION WITH NOS1 AND CAPON.
DOI=10.1006/jmbi.1999.3350; PubMed=10623522 [NCBI, ExPASy, EBI, Israel, Japan]
Tochio H.,
Hung F.,
Li M.,
Bredt D.S.,
Zhang M.;
"Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95.";
J. Mol. Biol. 295:225-237(2000).
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[23]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 430-724.
DOI=10.1016/S1097-2765(01)00411-7; PubMed=11779504 [NCBI, ExPASy, EBI, Israel, Japan]
McGee A.W.,
Dakoji S.R.,
Olsen O.,
Bredt D.S.,
Lim W.A.,
Prehoda K.E.;
"Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins.";
Mol. Cell 8:1291-1301(2001).
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[24]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 430-724.
DOI=10.1016/S1097-2765(01)00416-6; PubMed=11779506 [NCBI, ExPASy, EBI, Israel, Japan]
Tavares G.A.,
Panepucci E.H.,
Brunger A.T.;
"Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.";
Mol. Cell 8:1313-1325(2001).
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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 KCNA1, KCNA2, KCNA3, KCNA4 and ERBB4. Interacts through its first PDZ domain with GRIK2, KCNA4 and CRIPT. Interacts through its third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3. May interact with HTR2A. Interacts through its guanylate kinase-like domain with KIF13B. Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK (By similarity). Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D, ACCN3, certain splice forms of GRIN1, KCND2, CXADR and SYNGAP1. Interacts through its second PDZ domain with the PDZ domain of NOS1 or the C-terminus of CAPON. Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A and BEGAIN. Interacts through its third PDZ domain with CRIPT. Interacts with ANKS1B, LRFN1 and PRR7.
- INTERACTION:
P08588:ADRB1 (xeno); NbExp=1; IntAct=EBI-375655, EBI-991009;
P70478:Apc; NbExp=2; IntAct=EBI-375655, EBI-631663;
Q01814-1:ATP2B2 (xeno); NbExp=1; IntAct=EBI-375655, EBI-1174262;
P23634-6:ATP2B4 (xeno); NbExp=1; IntAct=EBI-375655, EBI-1174437;
Q792Q4:Cript; NbExp=1; IntAct=EBI-375655, EBI-632062;
P97836:Dlgap1; NbExp=3; IntAct=EBI-375655, EBI-80901;
P97837:Dlgap2; NbExp=1; IntAct=EBI-375655, EBI-81025;
Q00959:Grin2a; NbExp=2; IntAct=EBI-375655, EBI-630970;
Q00960:Grin2b; NbExp=3; IntAct=EBI-375655, EBI-396905;
Q00961:Grin2c; NbExp=2; IntAct=EBI-375655, EBI-631045;
P97879:Grip1; NbExp=1; IntAct=EBI-375655, EBI-936113;
P22459:KCNA4 (xeno); NbExp=1; IntAct=EBI-375655, EBI-631235;
P15385:Kcna4; NbExp=1; IntAct=EBI-375655, EBI-631417;
Q460M5:Lrfn2; NbExp=1; IntAct=EBI-375655, EBI-877185;
P34926:Map1a; NbExp=6; IntAct=EBI-375655, EBI-631571;
P29476:Nos1; NbExp=1; IntAct=EBI-375655, EBI-349460;
Q9WV48:Shank1; NbExp=1; IntAct=EBI-375655, EBI-80909;
Q9EQL9:Sharpin; NbExp=1; IntAct=EBI-375655, EBI-1394695;
P28572:Slc6a9; NbExp=2; IntAct=EBI-375655, EBI-848783;
P28572-2:Slc6a9; NbExp=2; IntAct=EBI-375655, EBI-848796;
- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse. Note=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.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Synonyms | PSD95-beta |
| Isoform ID | P31016-2 |
| The sequence of this isoform is not described. |
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- TISSUE SPECIFICITY: Brain. Highest levels of isoform 2 in cerebellum, cortex, hippocampus, and corpus striatum.
- DOMAIN: The PDZ domain 3 mediates interaction with ADR1B (By similarity).
- 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.
- 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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