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Disks large homolog 4 (Postsynaptic density protein 95) (PSD-95) (Synapse-associated protein 90) (SAP-90) (SAP90)

 DLG4_RAT                Reviewed;         724 AA.
P31016; P97631;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
22-NOV-2017, entry version 198.
RecName: Full=Disks large homolog 4;
AltName: Full=Postsynaptic density protein 95;
Short=PSD-95;
AltName: Full=Synapse-associated protein 90;
Short=SAP-90;
Short=SAP90;
Name=Dlg4; Synonyms=Dlgh4, Psd95 {ECO:0000303|PubMed:27756895};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1419001; DOI=10.1016/0896-6273(92)90245-9;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7680343;
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).
[3]
PROTEIN SEQUENCE OF 113-126; 212-233; 300-312; 381-399 AND 598-617,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Diao W.;
Submitted (APR-2007) to UniProtKB.
[4]
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.
[5]
INTERACTION WITH GRIN2A; GRIN2B; GRIN2C AND GRIN2D.
PubMed=7569905; DOI=10.1126/science.7569905;
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).
[6]
SUBCELLULAR LOCATION.
PubMed=8922396;
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).
[7]
INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=9115257; DOI=10.1074/jbc.272.18.11943;
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).
[8]
INTERACTION WITH BEGAIN AND DLGAP1.
PubMed=9756850; DOI=10.1074/jbc.273.41.26269;
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).
[9]
INTERACTION WITH MAP1A.
PubMed=9786987;
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).
[10]
INTERACTION WITH SYNGAP1.
PubMed=9581761; DOI=10.1016/S0896-6273(00)81008-9;
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).
[11]
INTERACTION WITH CRIPT.
PubMed=9581762; DOI=10.1016/S0896-6273(00)81009-0;
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).
[12]
MUTAGENESIS OF CYS-3 AND CYS-5, AND PALMITOYLATION AT CYS-3 AND CYS-5.
PubMed=10629226; DOI=10.1083/jcb.148.1.159;
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).
[13]
INTERACTION WITH SEMA4C.
PubMed=11134026; DOI=10.1074/jbc.M009051200;
Inagaki S., Ohoka Y., Sugimoto H., Fujioka S., Amazaki M.,
Kurinami H., Miyazaki N., Tohyama M., Furuyama T.;
"Sema4c, a transmembrane semaphorin, interacts with a post-synaptic
density protein, PSD-95.";
J. Biol. Chem. 276:9174-9181(2001).
[14]
INTERACTION WITH SIPA1L1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=11502259; DOI=10.1016/S0896-6273(01)00355-5;
Pak D.T., Yang S., Rudolph-Correia S., Kim E., Sheng M.;
"Regulation of dendritic spine morphology by SPAR, a PSD-95-associated
RapGAP.";
Neuron 31:289-303(2001).
[15]
INTERACTION WITH KCND2.
PubMed=11923279; DOI=10.1074/jbc.M109412200;
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).
[16]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=12151521;
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).
[17]
INTERACTION WITH KCNJ4, AND SUBCELLULAR LOCATION.
PubMed=11997254; DOI=10.1152/ajpcell.00615.2001;
Inanobe A., Fujita A., Ito M., Tomoike H., Inageda K., Kurachi Y.;
"Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic
membrane of excitatory synapses.";
Am. J. Physiol. 282:C1396-C1403(2002).
[18]
SUBCELLULAR LOCATION, UBIQUITINATION, AND MUTAGENESIS OF
13-ARG--HIS-24.
PubMed=14642282;
Colledge M., Snyder E.M., Crozier R.A., Soderling J.A., Jin Y.,
Langeberg L.K., Lu H., Bear M.F., Scott J.D.;
"Ubiquitination regulates PSD-95 degradation and AMPA receptor surface
expression.";
Neuron 40:595-607(2003).
[19]
INTERACTION WITH ASIC3, AND FUNCTION.
PubMed=15317815; DOI=10.1074/jbc.M405874200;
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).
[20]
INTERACTION WITH CXADR.
PubMed=15304526; DOI=10.1242/jcs.01300;
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).
[21]
FUNCTION.
PubMed=15358863; DOI=10.1073/pnas.0405939101;
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).
[22]
INTERACTION WITH PRR7.
PubMed=15629447; DOI=10.1016/j.bbrc.2004.11.154;
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).
[23]
INTERACTION WITH KLHL17.
PubMed=16054660; DOI=10.1016/j.neuropharm.2005.05.022;
Chen Y., Li M.;
"Interactions between CAP70 and actinfilin are important for integrity
of actin cytoskeleton structures in neurons.";
Neuropharmacology 49:1026-1041(2005).
[24]
INTERACTION WITH LRFN2.
PubMed=16495444; DOI=10.1523/JNEUROSCI.3799-05.2006;
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K.,
Wenthold R.J.;
"A novel family of adhesion-like molecules that interacts with the
NMDA receptor.";
J. Neurosci. 26:2174-2183(2006).
[25]
INTERACTION WITH LRFN1.
PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
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).
[26]
INTERACTION WITH ADAM22 AND LGI1.
PubMed=16990550; DOI=10.1126/science.1129947;
Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M.;
"Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate
synaptic transmission.";
Science 313:1792-1795(2006).
[27]
INTERACTION WITH ANKS1B.
PubMed=17334360; DOI=10.1038/nn1867;
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).
[28]
INTERACTION WITH FRMPD4.
PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
Kang G.B., Eom S.H., Kim H., Kim E.;
"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
regulates dendritic spine morphogenesis.";
J. Neurosci. 28:14546-14556(2008).
[29]
INTERACTION WITH ADAM22, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=20089912; DOI=10.1523/JNEUROSCI.4661-09.2010;
Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E.,
Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.;
"ADAM22, a Kv1 channel-interacting protein, recruits membrane-
associated guanylate kinases to juxtaparanodes of myelinated axons.";
J. Neurosci. 30:1038-1048(2010).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; SER-295; SER-418;
THR-420; SER-422; SER-449 AND SER-654, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[31]
FUNCTION, AND INTERACTION WITH GPER1 AND NOS1.
PubMed=23300088; DOI=10.1074/jbc.M112.412478;
Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.;
"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.";
J. Biol. Chem. 288:6438-6450(2013).
[32]
IDENTIFICATION IN A COMPLEX WITH PRR7 AND GRIN1, AND INTERACTION WITH
PRR7.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
[33]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH CACNG2
AND MPP2.
PubMed=27756895; DOI=10.1038/srep35283;
Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
"MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
adhesion molecules to core components of the postsynaptic density.";
Sci. Rep. 6:35283-35283(2016).
[34]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 302-402.
PubMed=8674113; DOI=10.1016/S0092-8674(00)81307-0;
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).
[35]
STRUCTURE BY NMR OF 155-246, AND INTERACTION WITH NOS1 AND CAPON.
PubMed=10623522; DOI=10.1006/jmbi.1999.3350;
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).
[36]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 430-724.
PubMed=11779504; DOI=10.1016/S1097-2765(01)00411-7;
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).
[37]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 430-724.
PubMed=11779506; DOI=10.1016/S1097-2765(01)00416-6;
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).
[38]
STRUCTURE BY NMR OF 62-154 IN COMPLEX WITH CYCLIC PEPTIDE.
PubMed=15123241; DOI=10.1016/j.chembiol.2004.03.013;
Piserchio A., Salinas G.D., Li T., Marshall J., Spaller M.R.,
Mierke D.F.;
"Targeting specific PDZ domains of PSD-95; structural basis for
enhanced affinity and enzymatic stability of a cyclic peptide.";
Chem. Biol. 11:469-473(2004).
[39]
STRUCTURE BY NMR OF 61-249 IN COMPLEX WITH PEPTIDE.
PubMed=19072119; DOI=10.1021/ja8076022;
Wang W., Weng J., Zhang X., Liu M., Zhang M.;
"Creating conformational entropy by increasing interdomain mobility in
ligand binding regulation: a revisit to N-terminal tandem PDZ domains
of PSD-95.";
J. Am. Chem. Soc. 131:787-796(2009).
-!- 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 ASIC3
acid-evoked currents by retaining the channel intracellularly. May
regulate the intracellular trafficking of ADR1B.
{ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:15358863,
ECO:0000269|PubMed:23300088}.
-!- SUBUNIT: Interacts through its PDZ domains with ANO2 and NETO1 (By
similarity). Interacts with KCNJ4 (PubMed:11997254). Interacts
through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C and
GRIN2D (PubMed:7569905). Interacts with ERBB4 (By similarity).
Interacts with KCNA1, KCNA2, KCNA3 and KCNA4 (By similarity).
Interacts with LRRC4 and LRRC4B (By similarity). Interacts with
SYNGAP1 (PubMed:9581761). Interacts with ASIC3 (PubMed:15317815).
Interacts with SEMA4C (PubMed:11134026). Interacts with CXADR
(PubMed:15304526). Interacts with KCND2 (PubMed:11923279).
Interacts (via first PDZ domain) with CRIPT (PubMed:9581762).
Interacts through its first PDZ domain with GRIK2 and KCNA4 (By
similarity). Interacts through its second PDZ domain with the PDZ
domain of NOS1 or the C-terminus of CAPON (PubMed:23300088).
Interacts through its third PDZ domain with NLGN1 and CRIPT, and
probably with NLGN2 and NLGN3 (By similarity). Interacts through
its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3,
DLGAP4, MAP1A, BEGAIN and SIPA1L1 (PubMed:9115257, PubMed:9756850,
PubMed:11502259, PubMed:9786987). Interacts through its guanylate
kinase-like domain with KIF13B (By similarity). Isoform 2
interacts through an L27 domain with HGS/HRS and the first L27
domain of CASK (By similarity). Interacts with ANKS1B
(PubMed:17334360). Interacts with ADR1B (By similarity). May
interact with HTR2A (By similarity). Interacts with ADAM22, KLHL17
and LGI1 (PubMed:16054660, PubMed:16990550, PubMed:20089912).
Interacts with FRMPD4 (via C-terminus) (PubMed:19118189).
Interacts with LRFN1 and LRFN2 (PubMed:16495444, PubMed:16630835).
Interacts with LRFN4 (By similarity). Interacts (via N-terminal
tandem pair of PDZ domains) with GPER1 (via C-terminus tail
motif); the interaction is direct and induces the increase of
GPER1 protein levels residing at the plasma membrane surface in a
estradiol-independent manner (PubMed:23300088). Interacts (via N-
terminus tandem pair of PDZ domains) with NOS1 (via N-terminal
domain) (PubMed:23300088). Interacts with SHANK3 (By similarity).
Interacts with GPR85 (By similarity). Interacts with CACNG2 and
MPP2 (via the SH3-Guanylate kinase-like sub-module)
(PubMed:27756895). Interacts with ADGRB1 (By similarity). Found in
a complex with PRR7 and GRIN1 (PubMed:27458189). Interacts (via
PDZ3 domain and to lesser degree via PDZ2 domain) with PRR7
(PubMed:27458189, PubMed:15629447). {ECO:0000250|UniProtKB:P78352,
ECO:0000269|PubMed:11134026, ECO:0000269|PubMed:11502259,
ECO:0000269|PubMed:11923279, ECO:0000269|PubMed:11997254,
ECO:0000269|PubMed:14642282, ECO:0000269|PubMed:15304526,
ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:15629447,
ECO:0000269|PubMed:16054660, ECO:0000269|PubMed:16495444,
ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:16990550,
ECO:0000269|PubMed:17334360, ECO:0000269|PubMed:19118189,
ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:23300088,
ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:27756895,
ECO:0000269|PubMed:7569905, ECO:0000269|PubMed:9115257,
ECO:0000269|PubMed:9581761, ECO:0000269|PubMed:9581762,
ECO:0000269|PubMed:9756850, ECO:0000269|PubMed:9786987}.
-!- INTERACTION:
P10608:Adrb2; NbExp=2; IntAct=EBI-375655, EBI-7090342;
P70478:Apc; NbExp=2; IntAct=EBI-375655, EBI-631663;
Q71RJ2:Cacng2; NbExp=2; IntAct=EBI-375655, EBI-8538384;
Q9Z1T4:Cnksr2; NbExp=4; IntAct=EBI-375655, EBI-8548356;
Q9P021:CRIPT (xeno); NbExp=2; IntAct=EBI-375655, EBI-946968;
Q810C5:Dgki; NbExp=5; IntAct=EBI-375655, EBI-8523614;
O08560:Dgkz; NbExp=6; IntAct=EBI-375655, EBI-8570505;
Q12959-2:DLG1 (xeno); NbExp=9; IntAct=EBI-375655, EBI-357500;
Q62696:Dlg1; NbExp=2; IntAct=EBI-375655, EBI-389325;
P97836:Dlgap1; NbExp=9; IntAct=EBI-375655, EBI-80901;
P97837:Dlgap2; NbExp=2; IntAct=EBI-375655, EBI-81025;
Q8R4T5:Grasp; NbExp=3; IntAct=EBI-375655, EBI-7361884;
P35439:Grin1; NbExp=4; IntAct=EBI-375655, EBI-877897;
Q12879:GRIN2A (xeno); NbExp=2; IntAct=EBI-375655, EBI-7249937;
Q00959:Grin2a; NbExp=5; IntAct=EBI-375655, EBI-630970;
Q13224:GRIN2B (xeno); NbExp=2; IntAct=EBI-375655, EBI-2256942;
Q00960:Grin2b; NbExp=8; IntAct=EBI-375655, EBI-396905;
Q14957:GRIN2C (xeno); NbExp=2; IntAct=EBI-375655, EBI-8285963;
Q9WVI4:Gucy1a2; NbExp=7; IntAct=EBI-375655, EBI-7665590;
P20595:Gucy1b3; NbExp=2; IntAct=EBI-375655, EBI-7980539;
P22459:KCNA4 (xeno); NbExp=3; IntAct=EBI-375655, EBI-631235;
Q8K430:Klhl17; NbExp=2; IntAct=EBI-375655, EBI-7713653;
Q460M5:Lrfn2; NbExp=3; IntAct=EBI-375655, EBI-877185;
P70587:Lrrc7; NbExp=5; IntAct=EBI-375655, EBI-7798464;
P34926:Map1a; NbExp=16; IntAct=EBI-375655, EBI-631571;
O54857:Pten; NbExp=5; IntAct=EBI-375655, EBI-8074312;
Q9WV48:Shank1; NbExp=3; IntAct=EBI-375655, EBI-80909;
P28572:Slc6a9; NbExp=2; IntAct=EBI-375655, EBI-848783;
P28572-2:Slc6a9; NbExp=4; IntAct=EBI-375655, EBI-848796;
P05480:Src (xeno); NbExp=9; IntAct=EBI-375655, EBI-298680;
P30937:Sstr4; NbExp=3; IntAct=EBI-375655, EBI-7665959;
Q9QUH6:Syngap1; NbExp=3; IntAct=EBI-375655, EBI-2310349;
Q80Z96:Vangl1 (xeno); NbExp=4; IntAct=EBI-375655, EBI-1750708;
Q91ZD4:Vangl2 (xeno); NbExp=6; IntAct=EBI-375655, EBI-1750744;
Q6IN36:Wipf1; NbExp=5; IntAct=EBI-375655, EBI-6986245;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Cell junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000269|PubMed:27756895}. Cell junction, synapse
{ECO:0000269|PubMed:14642282}. Membrane
{ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:20089912}. Cell
projection, axon {ECO:0000269|PubMed:20089912}. 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:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PSD95-alpha;
IsoId=P31016-1; Sequence=Displayed;
Name=2; Synonyms=PSD95-beta;
IsoId=P31016-2; Sequence=Not described;
-!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
Detected in juxtaparanodal zones in the central nervous system and
at nerve terminal plexuses of basket cells in the cerebellum
(PubMed:20089912). Expressed in hippocampal neurons
(PubMed:27756895). Highest levels of isoform 2 in cerebellum,
cortex, hippocampus, and corpus striatum.
{ECO:0000269|PubMed:11502259, ECO:0000269|PubMed:12151521,
ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:27756895}.
-!- DOMAIN: The PDZ domain 3 mediates interaction with ADR1B.
{ECO:0000250}.
-!- DOMAIN: The L27 domain near the N-terminus of isoform 2 is
required for HGS/HRS-dependent targeting to postsynaptic density.
{ECO:0000250}.
-!- PTM: Palmitoylation of isoform 1 is required for targeting to
postsynaptic density. {ECO:0000269|PubMed:10629226}.
-!- PTM: Ubiquitinated by MDM2 in response to NMDA receptor
activation, leading to proteasome-mediated degradation of DLG4
which is required for AMPA receptor endocytosis.
{ECO:0000269|PubMed:14642282}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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EMBL; M96853; AAA41971.1; -; mRNA.
EMBL; X66474; CAA47103.1; -; mRNA.
EMBL; U77090; AAB38270.1; -; mRNA.
PIR; A45436; A45436.
PIR; JH0800; JH0800.
RefSeq; NP_062567.1; NM_019621.1. [P31016-1]
UniGene; Rn.9765; -.
PDB; 1BE9; X-ray; 1.82 A; A=302-430.
PDB; 1BFE; X-ray; 2.30 A; A=302-402.
PDB; 1IU0; NMR; -; A=61-151.
PDB; 1IU2; NMR; -; A=61-151.
PDB; 1JXM; X-ray; 2.00 A; A=430-724.
PDB; 1JXO; X-ray; 2.30 A; A/B=430-724.
PDB; 1KJW; X-ray; 1.80 A; A=430-724.
PDB; 1QLC; NMR; -; A=155-249.
PDB; 1RGR; NMR; -; A=62-154.
PDB; 1TP3; X-ray; 1.99 A; A=302-402.
PDB; 1TP5; X-ray; 1.54 A; A=302-402.
PDB; 1TQ3; X-ray; 1.89 A; A=302-402.
PDB; 2KA9; NMR; -; A=61-249.
PDB; 2MHO; NMR; -; A=60-155.
PDB; 2XKX; Other; 22.90 A; A/B=1-724.
PDB; 3GSL; X-ray; 2.05 A; A/B=61-249.
PDB; 3WP0; X-ray; 2.04 A; A=531-713.
PDB; 3WP1; X-ray; 2.80 A; B=531-713.
PDB; 5B64; X-ray; 2.70 A; A=531-713.
PDB; 5D13; X-ray; 2.15 A; A/B/C/D=302-402.
PDB; 5GNV; X-ray; 2.60 A; A=531-713.
PDB; 5HDY; X-ray; 1.80 A; A=302-402.
PDB; 5HEB; X-ray; 1.65 A; A=302-402.
PDB; 5HED; X-ray; 1.70 A; A=302-402.
PDB; 5HET; X-ray; 2.00 A; A=302-402.
PDB; 5HEY; X-ray; 1.50 A; A=302-402.
PDB; 5HF1; X-ray; 1.75 A; A=302-402.
PDB; 5HF4; X-ray; 1.75 A; A=302-402.
PDB; 5HFB; X-ray; 1.62 A; A=302-402.
PDB; 5HFC; X-ray; 1.85 A; A=302-402.
PDB; 5HFD; X-ray; 1.60 A; A=302-402.
PDB; 5HFE; X-ray; 1.80 A; A=302-402.
PDB; 5HFF; X-ray; 1.75 A; A=302-402.
PDB; 5MZ7; X-ray; 1.53 A; A/B/C/D=303-402.
PDBsum; 1BE9; -.
PDBsum; 1BFE; -.
PDBsum; 1IU0; -.
PDBsum; 1IU2; -.
PDBsum; 1JXM; -.
PDBsum; 1JXO; -.
PDBsum; 1KJW; -.
PDBsum; 1QLC; -.
PDBsum; 1RGR; -.
PDBsum; 1TP3; -.
PDBsum; 1TP5; -.
PDBsum; 1TQ3; -.
PDBsum; 2KA9; -.
PDBsum; 2MHO; -.
PDBsum; 2XKX; -.
PDBsum; 3GSL; -.
PDBsum; 3WP0; -.
PDBsum; 3WP1; -.
PDBsum; 5B64; -.
PDBsum; 5D13; -.
PDBsum; 5GNV; -.
PDBsum; 5HDY; -.
PDBsum; 5HEB; -.
PDBsum; 5HED; -.
PDBsum; 5HET; -.
PDBsum; 5HEY; -.
PDBsum; 5HF1; -.
PDBsum; 5HF4; -.
PDBsum; 5HFB; -.
PDBsum; 5HFC; -.
PDBsum; 5HFD; -.
PDBsum; 5HFE; -.
PDBsum; 5HFF; -.
PDBsum; 5MZ7; -.
ProteinModelPortal; P31016; -.
SMR; P31016; -.
BioGrid; 248135; 23.
CORUM; P31016; -.
DIP; DIP-29264N; -.
ELM; P31016; -.
IntAct; P31016; 352.
MINT; MINT-93329; -.
STRING; 10116.ENSRNOP00000059045; -.
ChEMBL; CHEMBL3797015; -.
iPTMnet; P31016; -.
PhosphoSitePlus; P31016; -.
SwissPalm; P31016; -.
PaxDb; P31016; -.
PRIDE; P31016; -.
Ensembl; ENSRNOT00000068493; ENSRNOP00000059045; ENSRNOG00000018526. [P31016-1]
GeneID; 29495; -.
KEGG; rno:29495; -.
UCSC; RGD:68424; rat. [P31016-1]
CTD; 1742; -.
RGD; 68424; Dlg4.
eggNOG; KOG0708; Eukaryota.
eggNOG; COG0194; LUCA.
GeneTree; ENSGT00760000118866; -.
HOGENOM; HOG000232102; -.
HOVERGEN; HBG107814; -.
InParanoid; P31016; -.
KO; K11828; -.
PhylomeDB; P31016; -.
Reactome; R-RNO-399719; Trafficking of AMPA receptors.
Reactome; R-RNO-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-RNO-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-RNO-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-RNO-5625900; RHO GTPases activate CIT.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-5682910; LGI-ADAM interactions.
Reactome; R-RNO-6794361; Neurexins and neuroligins.
Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
EvolutionaryTrace; P31016; -.
PRO; PR:P31016; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000018526; -.
ExpressionAtlas; P31016; baseline and differential.
Genevisible; P31016; RN.
GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
GO; GO:0030054; C:cell junction; ISS:BHF-UCL.
GO; GO:0071944; C:cell periphery; ISO:RGD.
GO; GO:0044300; C:cerebellar mossy fiber; ISO:RGD.
GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0032839; C:dendrite cytoplasm; IDA:BHF-UCL.
GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0044306; C:neuron projection terminus; ISS:BHF-UCL.
GO; GO:0044309; C:neuron spine; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0097060; C:synaptic membrane; ISO:RGD.
GO; GO:0008021; C:synaptic vesicle; ISS:BHF-UCL.
GO; GO:0033130; F:acetylcholine receptor binding; IDA:RGD.
GO; GO:0031697; F:beta-1 adrenergic receptor binding; IPI:UniProtKB.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:ARUK-UCL.
GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
GO; GO:0035254; F:glutamate receptor binding; IPI:BHF-UCL.
GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0019900; F:kinase binding; ISO:RGD.
GO; GO:0019894; F:kinesin binding; IPI:RGD.
GO; GO:0097109; F:neuroligin family protein binding; IPI:BHF-UCL.
GO; GO:0031812; F:P2Y1 nucleotide receptor binding; IPI:BHF-UCL.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL.
GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:BHF-UCL.
GO; GO:0060997; P:dendritic spine morphogenesis; IMP:BHF-UCL.
GO; GO:0045184; P:establishment of protein localization; ISS:BHF-UCL.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
GO; GO:0035641; P:locomotory exploration behavior; ISS:BHF-UCL.
GO; GO:0002091; P:negative regulation of receptor internalization; IDA:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
GO; GO:0045161; P:neuronal ion channel clustering; TAS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
GO; GO:0050806; P:positive regulation of synaptic transmission; IDA:BHF-UCL.
GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; IMP:SynGO.
GO; GO:0006461; P:protein complex assembly; ISS:BHF-UCL.
GO; GO:0035418; P:protein localization to synapse; IMP:BHF-UCL.
GO; GO:0097120; P:receptor localization to synapse; IMP:BHF-UCL.
GO; GO:2000821; P:regulation of grooming behavior; ISS:BHF-UCL.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISS:BHF-UCL.
GO; GO:2000310; P:regulation of NMDA receptor activity; IDA:BHF-UCL.
GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
GO; GO:0016188; P:synaptic vesicle maturation; ISS:BHF-UCL.
GO; GO:0071625; P:vocalization behavior; ISS:BHF-UCL.
InterPro; IPR016313; DLG1-like.
InterPro; IPR019590; DLG1_PEST_dom.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR020590; Guanylate_kinase_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR019583; PDZ_assoc.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF10608; MAGUK_N_PEST; 1.
Pfam; PF00595; PDZ; 3.
Pfam; PF10600; PDZ_assoc; 1.
Pfam; PF00018; SH3_1; 1.
PIRSF; PIRSF001741; MAGUK_DLGH; 1.
SMART; SM00072; GuKc; 1.
SMART; SM01277; MAGUK_N_PEST; 1.
SMART; SM00228; PDZ; 3.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS50106; PDZ; 3.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Direct protein sequencing;
Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain;
Synapse; Ubl conjugation.
CHAIN 1 724 Disks large homolog 4.
/FTId=PRO_0000094562.
DOMAIN 65 151 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 160 246 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 313 393 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 428 498 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 534 709 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 240 240 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 420 420 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 580 580 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 606 606 Phosphoserine.
{ECO:0000250|UniProtKB:Q62108}.
MOD_RES 654 654 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 715 715 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62108}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10629226}.
LIPID 5 5 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10629226}.
MUTAGEN 3 3 C->S: Loss of palmitoylation and
targeting to postsynaptic density.
{ECO:0000269|PubMed:10629226}.
MUTAGEN 5 5 C->S: Loss of palmitoylation and
targeting to postsynaptic density.
{ECO:0000269|PubMed:10629226}.
MUTAGEN 13 24 Missing: Greatly reduced ubiquitination.
{ECO:0000269|PubMed:14642282}.
CONFLICT 61 61 M -> L (in Ref. 2; CAA47103).
{ECO:0000305}.
CONFLICT 78 78 S -> T (in Ref. 2; CAA47103).
{ECO:0000305}.
CONFLICT 177 182 GVGNQH -> ALGTSI (in Ref. 2; CAA47103).
{ECO:0000305}.
CONFLICT 200 200 A -> G (in Ref. 2; CAA47103).
{ECO:0000305}.
CONFLICT 254 254 S -> T (in Ref. 2; CAA47103).
{ECO:0000305}.
CONFLICT 540 555 LGPTKDRANDDLLSEF -> SLDPPKTVPTMIFSPSS (in
Ref. 2; CAA47103). {ECO:0000305}.
CONFLICT 623 625 GKH -> RDQ (in Ref. 4; AAB38270).
{ECO:0000305}.
STRAND 61 69 {ECO:0000244|PDB:3GSL}.
STRAND 71 73 {ECO:0000244|PDB:2KA9}.
STRAND 74 80 {ECO:0000244|PDB:3GSL}.
STRAND 82 85 {ECO:0000244|PDB:1IU0}.
STRAND 88 91 {ECO:0000244|PDB:1IU0}.
STRAND 94 99 {ECO:0000244|PDB:3GSL}.
STRAND 101 103 {ECO:0000244|PDB:2KA9}.
HELIX 104 108 {ECO:0000244|PDB:3GSL}.
STRAND 116 120 {ECO:0000244|PDB:3GSL}.
HELIX 125 127 {ECO:0000244|PDB:1IU2}.
HELIX 130 138 {ECO:0000244|PDB:3GSL}.
STRAND 142 151 {ECO:0000244|PDB:3GSL}.
STRAND 156 166 {ECO:0000244|PDB:3GSL}.
STRAND 172 178 {ECO:0000244|PDB:3GSL}.
STRAND 189 194 {ECO:0000244|PDB:3GSL}.
HELIX 199 203 {ECO:0000244|PDB:3GSL}.
STRAND 211 215 {ECO:0000244|PDB:3GSL}.
STRAND 221 224 {ECO:0000244|PDB:1QLC}.
HELIX 225 233 {ECO:0000244|PDB:3GSL}.
STRAND 237 247 {ECO:0000244|PDB:3GSL}.
HELIX 302 304 {ECO:0000244|PDB:1TP5}.
STRAND 312 317 {ECO:0000244|PDB:5HEY}.
STRAND 325 328 {ECO:0000244|PDB:5HEY}.
STRAND 331 334 {ECO:0000244|PDB:5HEY}.
STRAND 337 341 {ECO:0000244|PDB:5HEY}.
HELIX 348 350 {ECO:0000244|PDB:5HEY}.
STRAND 357 362 {ECO:0000244|PDB:5HEY}.
HELIX 372 380 {ECO:0000244|PDB:5HEY}.
STRAND 384 392 {ECO:0000244|PDB:5HEY}.
HELIX 394 398 {ECO:0000244|PDB:5HEY}.
STRAND 414 416 {ECO:0000244|PDB:1BE9}.
STRAND 431 437 {ECO:0000244|PDB:1KJW}.
HELIX 441 445 {ECO:0000244|PDB:1KJW}.
STRAND 449 451 {ECO:0000244|PDB:1KJW}.
STRAND 459 464 {ECO:0000244|PDB:1KJW}.
STRAND 467 475 {ECO:0000244|PDB:1KJW}.
STRAND 486 489 {ECO:0000244|PDB:1KJW}.
HELIX 491 499 {ECO:0000244|PDB:1KJW}.
TURN 504 507 {ECO:0000244|PDB:1JXO}.
STRAND 523 530 {ECO:0000244|PDB:1KJW}.
STRAND 537 541 {ECO:0000244|PDB:1KJW}.
HELIX 544 554 {ECO:0000244|PDB:1KJW}.
TURN 556 558 {ECO:0000244|PDB:1KJW}.
TURN 576 578 {ECO:0000244|PDB:1KJW}.
HELIX 586 594 {ECO:0000244|PDB:1KJW}.
STRAND 598 604 {ECO:0000244|PDB:1KJW}.
STRAND 607 612 {ECO:0000244|PDB:1KJW}.
HELIX 613 621 {ECO:0000244|PDB:1KJW}.
STRAND 625 628 {ECO:0000244|PDB:1KJW}.
HELIX 634 640 {ECO:0000244|PDB:1KJW}.
STRAND 646 650 {ECO:0000244|PDB:1KJW}.
HELIX 655 661 {ECO:0000244|PDB:1KJW}.
STRAND 663 665 {ECO:0000244|PDB:1JXM}.
HELIX 667 684 {ECO:0000244|PDB:1KJW}.
HELIX 685 687 {ECO:0000244|PDB:1KJW}.
STRAND 689 692 {ECO:0000244|PDB:1KJW}.
HELIX 697 711 {ECO:0000244|PDB:1KJW}.
STRAND 714 719 {ECO:0000244|PDB:1KJW}.
SEQUENCE 724 AA; 80465 MW; 7922D4E8E0F9AD85 CRC64;
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


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EIAAB11381 Disks large homolog 1,DLG1,hDlg,Homo sapiens,Human,SAP97,SAP-97,Synapse-associated protein 97
EIAAB11404 DAP-5,Discs large homolog 7,Disks large-associated protein 5,Disks large-associated protein DLG7,DLG7,DLGAP5,Hepatoma up-regulated protein,Homo sapiens,Human,HURP,KIAA0008
EIAAB11387 Disks large homolog 3,DLG3,Homo sapiens,Human,KIAA1232,Neuroendocrine-DLG,SAP102,SAP-102,Synapse-associated protein 102,XLMR
EIAAB11391 Discs large protein P-dlg,Disks large homolog 5,DLG5,Homo sapiens,Human,KIAA0583,PDLG,Placenta and prostate DLG
EIAAB33773 43 kDa postsynaptic protein,43 kDa receptor-associated protein of the synapse,Acetylcholine receptor-associated 43 kDa protein,Homo sapiens,Human,RAPSN,RAPsyn,RING finger protein 205,RNF205
EIAAB33771 43 kDa postsynaptic protein,43 kDa receptor-associated protein of the synapse,Acetylcholine receptor-associated 43 kDa protein,Mouse,Mus musculus,Rapsn,RAPsyn
EIAAB33772 43 kDa postsynaptic protein,43 kDa receptor-associated protein of the synapse,Acetylcholine receptor-associated 43 kDa protein,Chicken,Gallus gallus,RAPSN,RAPsyn
EIAAB11392 DAP-1,Disks large-associated protein 1,Dlgap1,Guanylate kinase-associated protein,Kiaa4162,Mouse,Mus musculus,PSD-95_SAP90-binding protein 1,SAP90_PSD-95-associated protein 1,SAPAP1
EIAAB11394 DAP-1,Disks large-associated protein 1,Dlgap1,Gkap,Guanylate kinase-associated protein,PSD-95_SAP90-binding protein 1,Rat,Rattus norvegicus,rGKAP,SAP90_PSD-95-associated protein 1,SAPAP1
EIAAB11393 DAP1,DAP-1,Disks large-associated protein 1,DLGAP1,GKAP,Guanylate kinase-associated protein,hGKAP,Homo sapiens,Human,PSD-95_SAP90-binding protein 1,SAP90_PSD-95-associated protein 1,SAPAP1
EIAAB11397 Dap2,DAP-2,Disks large-associated protein 2,Dlgap2,PSD-95_SAP90-binding protein 2,Rat,Rattus norvegicus,SAP90_PSD-95-associated protein 2,SAPAP2
EIAAB11399 Dap3,DAP-3,Disks large-associated protein 3,Dlgap3,Mouse,Mus musculus,PSD-95_SAP90-binding protein 3,SAP90_PSD-95-associated protein 3,SAPAP3
EIAAB11398 Dap3,DAP-3,Disks large-associated protein 3,Dlgap3,PSD-95_SAP90-binding protein 3,Rat,Rattus norvegicus,SAP90_PSD-95-associated protein 3,SAPAP3


 

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