Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 DLG4_MOUSE              Reviewed;         724 AA.
Q62108; Q5NCV5; Q5NCV6; Q5NCV7; Q91WJ1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 185.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=DBA/2J; TISSUE=Brain;
Kohmura N., Yagi T.;
"Mouse homologue of rat PSD-95/SAP90A.";
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9853749; DOI=10.1038/24790;
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).
[5]
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).
[6]
INTERACTION WITH KCNJ4.
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).
[7]
INTERACTION WITH HTR2A.
PubMed=14988405; DOI=10.1074/jbc.M312106200;
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).
[8]
INTERACTION WITH ADR1B, DOMAIN, AND FUNCTION.
PubMed=15358775; DOI=10.1074/jbc.M404876200;
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).
[9]
INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
STRAIN=Swiss Webster;
PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
Morimura N., Inoue T., Katayama K., Aruga J.;
"Comparative analysis of structure, expression and PSD95-binding
capacity of Lrfn, a novel family of neuronal transmembrane proteins.";
Gene 380:72-83(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
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).
[11]
INTERACTION WITH LRRC4B AND LRRC4.
PubMed=16980967; DOI=10.1038/nn1763;
Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K.,
Kim H., Weinberg R.J., Kim E.;
"NGL family PSD-95-interacting adhesion molecules regulate excitatory
synapse formation.";
Nat. Neurosci. 9:1294-1301(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; TYR-580 AND
TYR-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
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).
[13]
INTERACTION WITH ANO2.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=19474308; DOI=10.1523/JNEUROSCI.5546-08.2009;
Stoehr H., Heisig J.B., Benz P.M., Schoeberl S., Milenkovic V.M.,
Strauss O., Aartsen W.M., Wijnholds J., Weber B.H.F., Schulz H.L.;
"TMEM16B, a novel protein with calcium-dependent chloride channel
activity, associates with a presynaptic protein complex in
photoreceptor terminals.";
J. Neurosci. 29:6809-6818(2009).
[14]
INTERACTION WITH NETO1.
PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
Roder J.C., Salter M.W., McInnes R.R.;
"Neto1 is a novel CUB-domain NMDA receptor-interacting protein
required for synaptic plasticity and learning.";
PLoS Biol. 7:E41-E41(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; TYR-240; SER-415;
SER-418; THR-420; SER-422; SER-425; SER-480 AND SER-606, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
INTERACTION WITH ADAM22.
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).
[17]
INTERACTION WITH SHANK3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24153177; DOI=10.1038/nature12630;
Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H.,
Tang J., Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M.,
Patel A., Lu H.C., Zoghbi H.Y.;
"SHANK3 overexpression causes manic-like behaviour with unique
pharmacogenetic properties.";
Nature 503:72-77(2013).
-!- 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:15358775, ECO:0000269|PubMed:9853749}.
-!- SUBUNIT: Interacts through its PDZ domains with ANO2 and NETO1
(PubMed:19474308, PubMed:19243221). Interacts with KCNJ4 (By
similarity). Interacts through its first two PDZ domains with
GRIN2A, GRIN2B, GRIN2C, GRIN2D (By similarity). Interacts with
ERBB4 (By similarity). Interacts with KCNA1, KCNA2, KCNA3 and
KCNA4 (By similarity). Interacts with SYNGAP1 (By similarity).
Interacts with ASIC3 (By similarity). Interacts with CXADR (By
similarity). Interacts with KCND2 (By similarity). Interacts with
SEMA4C (PubMed:11134026). Interacts with LRRC4 and LRRC4B
(PubMed:16980967). Interacts through its first PDZ domain with
GRIK2 and CRIPT (By similarity). Interacts through its second PDZ
domain with the PDZ domain of NOS1 or the C-terminus of CAPON (By
similarity). 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, SIPA1L1 and
KIF13B (By similarity). Isoform 2 interacts through an L27 domain
with HGS/HRS and the first L27 domain of CASK (By similarity).
Interacts with ADR1B (PubMed:15358775). Interacts with ANKS1B and
PRR7 (By similarity). May interact with HTR2A (PubMed:14988405).
Interacts with ADAM22, KLHL17 and LGI1 (PubMed:20089912) (By
similarity). Interacts with FRMPD4 (via C-terminus) (By
similarity). Interacts with LRFN1, LRFN2 and LRFN4
(PubMed:16828986). 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 (By similarity). Interacts (via N-terminus tandem pair of
PDZ domains) with NOS1 (via N-terminal domain) (By similarity).
Interacts with SHANK3 (PubMed:24153177). Interacts with KCNJ4
(PubMed:11997254). Interacts with GPR85 (By similarity). Interacts
with CACNG2 and MPP2 (via the SH3-Guanylate kinase-like sub-
module) (By similarity). Interacts with ADGRB1 (By similarity).
Found in a complex with PRR7 and GRIN1 (By similarity). Interacts
(via PDZ3 domain and to lesser degree via PDZ2 domain) with PRR7
(By similarity). {ECO:0000250|UniProtKB:P31016,
ECO:0000250|UniProtKB:P78352, ECO:0000269|PubMed:11134026,
ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:14988405,
ECO:0000269|PubMed:15358775, ECO:0000269|PubMed:16828986,
ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:19243221,
ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:20089912,
ECO:0000269|PubMed:24153177}.
-!- INTERACTION:
Q8K4G5:Ablim1; NbExp=4; IntAct=EBI-300895, EBI-2307994;
P12023:App; NbExp=4; IntAct=EBI-300895, EBI-78814;
Q9WV31:Arc; NbExp=6; IntAct=EBI-300895, EBI-397779;
Q8BKX1:Baiap2; NbExp=3; IntAct=EBI-300895, EBI-771498;
P11798:Camk2a; NbExp=3; IntAct=EBI-300895, EBI-400384;
Q811D0:Dlg1; NbExp=3; IntAct=EBI-300895, EBI-514290;
Q91XM9:Dlg2; NbExp=5; IntAct=EBI-300895, EBI-400138;
P70175:Dlg3; NbExp=3; IntAct=EBI-300895, EBI-396969;
Q61090:Fzd7; NbExp=4; IntAct=EBI-300895, EBI-8473104;
Q9R111:Gda; NbExp=5; IntAct=EBI-300895, EBI-2308876;
P35438:Grin1; NbExp=15; IntAct=EBI-300895, EBI-400084;
P35436:Grin2a; NbExp=10; IntAct=EBI-300895, EBI-400115;
Q01097:Grin2b; NbExp=19; IntAct=EBI-300895, EBI-400125;
Q9WVI4:Gucy1a2 (xeno); NbExp=3; IntAct=EBI-300895, EBI-7665590;
Q80TG9:Lrfn2; NbExp=2; IntAct=EBI-300895, EBI-877092;
Q91ZX7:Lrp1; NbExp=3; IntAct=EBI-300895, EBI-300955;
A2ARV4:Lrp2; NbExp=2; IntAct=EBI-300895, EBI-300875;
Q924X6:Lrp8; NbExp=3; IntAct=EBI-300895, EBI-432319;
P63085:Mapk1; NbExp=3; IntAct=EBI-300895, EBI-397697;
P23804:Mdm2; NbExp=3; IntAct=EBI-300895, EBI-641788;
Q8R4I7:Neto1; NbExp=6; IntAct=EBI-300895, EBI-2314926;
Q810U4:Nrcam; NbExp=2; IntAct=EBI-300895, EBI-8321816;
P46460:Nsf; NbExp=4; IntAct=EBI-300895, EBI-398006;
P15209:Ntrk2; NbExp=4; IntAct=EBI-300895, EBI-309647;
Q80TE2:Pcdh10; NbExp=4; IntAct=EBI-300895, EBI-6661550;
P63001:Rac1; NbExp=2; IntAct=EBI-300895, EBI-413646;
Q8R550:Sh3kbp1; NbExp=3; IntAct=EBI-300895, EBI-642709;
P30873:Sstr1; NbExp=3; IntAct=EBI-300895, EBI-7665262;
P49660:Sstr4; NbExp=3; IntAct=EBI-300895, EBI-7665342;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Cell junction, synapse {ECO:0000269|PubMed:24153177}. Cell
projection, axon {ECO:0000250|UniProtKB:P31016}. 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). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=PSD95-alpha;
IsoId=Q62108-1; Sequence=Displayed;
Name=2; Synonyms=PSD95-beta;
IsoId=Q62108-2; Sequence=VSP_014930;
Name=3;
IsoId=Q62108-3; Sequence=VSP_014931;
Note=No experimental confirmation available.;
-!- DOMAIN: The PDZ domain 3 mediates interaction with ADR1B.
{ECO:0000269|PubMed:15358775}.
-!- 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:0000250|UniProtKB:P31016}.
-!- 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:0000250|UniProtKB:P31016}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:9853749}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D50621; BAA09297.1; -; mRNA.
EMBL; AL596185; CAI35168.1; -; Genomic_DNA.
EMBL; AL596185; CAI35169.1; -; Genomic_DNA.
EMBL; AL596185; CAI35170.1; -; Genomic_DNA.
EMBL; BC014807; AAH14807.1; -; mRNA.
CCDS; CCDS36202.1; -. [Q62108-1]
CCDS; CCDS48829.1; -. [Q62108-3]
RefSeq; NP_001103222.1; NM_001109752.1. [Q62108-3]
RefSeq; NP_031890.1; NM_007864.3. [Q62108-1]
UniGene; Mm.27256; -.
ProteinModelPortal; Q62108; -.
SMR; Q62108; -.
BioGrid; 199230; 146.
CORUM; Q62108; -.
DIP; DIP-29888N; -.
IntAct; Q62108; 343.
MINT; MINT-136080; -.
STRING; 10090.ENSMUSP00000018700; -.
ChEMBL; CHEMBL1795134; -.
iPTMnet; Q62108; -.
PhosphoSitePlus; Q62108; -.
SwissPalm; Q62108; -.
PaxDb; Q62108; -.
PeptideAtlas; Q62108; -.
PRIDE; Q62108; -.
Ensembl; ENSMUST00000018700; ENSMUSP00000018700; ENSMUSG00000020886. [Q62108-1]
Ensembl; ENSMUST00000108588; ENSMUSP00000104229; ENSMUSG00000020886. [Q62108-3]
Ensembl; ENSMUST00000108589; ENSMUSP00000104230; ENSMUSG00000020886. [Q62108-2]
GeneID; 13385; -.
KEGG; mmu:13385; -.
UCSC; uc007jtp.2; mouse. [Q62108-1]
UCSC; uc007jtq.2; mouse. [Q62108-3]
CTD; 1742; -.
MGI; MGI:1277959; Dlg4.
eggNOG; KOG0708; Eukaryota.
eggNOG; COG0194; LUCA.
GeneTree; ENSGT00760000118866; -.
HOGENOM; HOG000232102; -.
HOVERGEN; HBG107814; -.
InParanoid; Q62108; -.
KO; K11828; -.
OMA; QVEVHYA; -.
OrthoDB; EOG091G0BB1; -.
PhylomeDB; Q62108; -.
TreeFam; TF323171; -.
Reactome; R-MMU-399719; Trafficking of AMPA receptors.
Reactome; R-MMU-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-MMU-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-MMU-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-MMU-5625900; RHO GTPases activate CIT.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-5682910; LGI-ADAM interactions.
Reactome; R-MMU-6794361; Neurexins and neuroligins.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
ChiTaRS; Dlg4; mouse.
PRO; PR:Q62108; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020886; -.
CleanEx; MM_DLG4; -.
ExpressionAtlas; Q62108; baseline and differential.
Genevisible; Q62108; MM.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
GO; GO:0030054; C:cell junction; IDA:MGI.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0044300; C:cerebellar mossy fiber; IDA:MGI.
GO; GO:0030863; C:cortical cytoskeleton; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0032839; C:dendrite cytoplasm; ISS:BHF-UCL.
GO; GO:0043197; C:dendritic spine; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:MGI.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
GO; GO:0044309; C:neuron spine; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0098794; C:postsynapse; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:ParkinsonsUK-UCL.
GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0097060; C:synaptic membrane; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0033130; F:acetylcholine receptor binding; ISS:BHF-UCL.
GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:BHF-UCL.
GO; GO:0031748; F:D1 dopamine receptor binding; ISS:BHF-UCL.
GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:BHF-UCL.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0042043; F:neurexin family protein binding; NAS:UniProtKB.
GO; GO:0097109; F:neuroligin family protein binding; ISS:BHF-UCL.
GO; GO:0031812; F:P2Y1 nucleotide receptor binding; ISS:BHF-UCL.
GO; GO:0030165; F:PDZ domain binding; ISS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; ISS:BHF-UCL.
GO; GO:0032403; F:protein complex binding; ISS:BHF-UCL.
GO; GO:0019903; F:protein phosphatase binding; ISS:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0098919; F:structural constituent of postsynaptic density; IC:SynGO.
GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
GO; GO:0097113; P:AMPA glutamate receptor clustering; ISS:BHF-UCL.
GO; GO:0060997; P:dendritic spine morphogenesis; IDA: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:0007626; P:locomotory behavior; NAS:UniProtKB.
GO; GO:0035641; P:locomotory exploration behavior; IMP:BHF-UCL.
GO; GO:0002091; P:negative regulation of receptor internalization; ISS:BHF-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:0050806; P:positive regulation of synaptic transmission; ISS:BHF-UCL.
GO; GO:0006461; P:protein complex assembly; ISS:BHF-UCL.
GO; GO:0035418; P:protein localization to synapse; IDA:MGI.
GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
GO; GO:0097120; P:receptor localization to synapse; ISS:BHF-UCL.
GO; GO:2000821; P:regulation of grooming behavior; IMP:BHF-UCL.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IGI:MGI.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; NAS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:BHF-UCL.
GO; GO:0042220; P:response to cocaine; NAS:UniProtKB.
GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
GO; GO:0016188; P:synaptic vesicle maturation; IDA:MGI.
GO; GO:0071625; P:vocalization behavior; IMP: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;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain;
Synapse; Ubl conjugation.
CHAIN 1 724 Disks large homolog 4.
/FTId=PRO_0000094561.
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:0000244|PubMed:21183079}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 240 240 Phosphotyrosine.
{ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:P31016}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 420 420 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000250|UniProtKB:P31016}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 580 580 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 606 606 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 654 654 Phosphoserine.
{ECO:0000250|UniProtKB:P31016}.
MOD_RES 715 715 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 5 5 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 1 10 MDCLCIVTTK -> MSQRPRAPRSALWLLAPPLLRWAPPLL
TVLHSDLFQALLDILDYYEACISESQ (in isoform
2). {ECO:0000305}.
/FTId=VSP_014930.
VAR_SEQ 51 53 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014931.
CONFLICT 203 203 D -> E (in Ref. 3; AAH14807).
{ECO:0000305}.
SEQUENCE 724 AA; 80472 MW; 7EFFC99E1FFF90BA CRC64;
MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE
MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV
NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKIIE 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 ALSFHFGDVL HVIDASDEEW 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


Related products :

Catalog number Product name Quantity
EIAAB11388 Disks large homolog 4,DLG4,Homo sapiens,Human,Postsynaptic density protein 95,PSD95,PSD-95,SAP90,SAP-90,Synapse-associated protein 90
EIAAB11389 Disks large homolog 4,Dlg4,Dlgh4,Postsynaptic density protein 95,Psd95,PSD-95,Rat,Rattus norvegicus,SAP90,SAP-90,Synapse-associated protein 90
EIAAB11390 Disks large homolog 4,Dlg4,Dlgh4,Mouse,Mus musculus,Postsynaptic density protein 95,Psd95,PSD-95,SAP90,SAP-90,Synapse-associated protein 90
18-662-20010 Discs large homolog 4 - Postsynaptic density protein 95; PSD-95; Synapse-associated protein 90; SAP90 Polyclonal 0.1 ml
EIAAB11383 Channel-associated protein of synapse-110,Chapsyn-110,Disks large homolog 2,Dlg2,Dlgh2,Postsynaptic density protein PSD-93,Rat,Rattus norvegicus
EIAAB11382 Channel-associated protein of synapse-110,Chapsyn-110,Disks large homolog 2,DLG2,Homo sapiens,Human,Postsynaptic density protein PSD-93
EIAAB11384 Channel-associated protein of synapse-110,Chapsyn-110,Disks large homolog 2,Dlg2,Dlgh2,Mouse,Mus musculus,Postsynaptic density protein PSD-93
EIAAB11385 Disks large homolog 3,Dlg3,Dlgh3,PSD-95_SAP90-related protein 1,Rat,Rattus norvegicus,SAP102,SAP-102,Synapse-associated protein 102
EIAAB11380 Disks large homolog 1,Dlg1,Dlgh1,E-dlg_SAP97,Embryo-dlg_synapse-associated protein 97,Mouse,Mus musculus,SAP97,SAP-97,Synapse-associated protein 97
EIAAB11405 DAP-5,Discs large homolog 7,Disks large-associated protein 5,Disks large-associated protein DLG7,Dlg7,Dlgap5,Hepatoma up-regulated protein homolog,HURP,Kiaa0008,Mouse,Mus musculus
EIAAB11379 Disks large homolog 1,Dlg1,Dlgh1,Rat,Rattus norvegicus,SAP97,SAP-97,Synapse-associated protein 97
EIAAB11386 Disks large homolog 3,Dlg3,Dlgh3,Mouse,Mus musculus,SAP102,SAP-102,Synapse-associated protein 102
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur