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Sequence Detail
ID/Version
Q62108 Q5NCV5 Q91WJ1 Q5NCV7 Q5NCV6 (UniProt | EBI) Last sequence update: 1997-11-01
Last annotation update: 2024-03-27
Sequence
description
from provider
RecName: Full=Disks large homolog 4;AltName: Full=Postsynaptic density protein 95 {ECO:0000305}; Short=PSD-95;AltName: Full=Synapse-associated protein 90; Short=SAP-90; Short=SAP90;
Provider SWISS-PROT
Sequence
Polypeptide 724 aa
For this sequence
Source
Organism mouse
See UniProt | EBI for source
Annotated genes and markers Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.
Type Symbol Name GO Terms Expression
Assays
Orthologs Phenotypic
Alleles
Gene Dlg4 discs large MAGUK scaffold protein 4 216 145 3 22
Sequence references in MGI J:70687 Schultze W, et al., Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95. J Neurochem. 2001 Aug;78(3):482-9
J:77016 Inanobe A, et al., Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses. Am J Physiol Cell Physiol. 2002 Jun;282(6):C1396-403
J:77693 Migaud M, et al., Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein. Nature. 1998 Dec 3;396(6710):433-9
J:112964 Morimura N, et al., Comparative analysis of structure, expression and PSD95-binding capacity of Lrfn, a novel family of neuronal transmembrane proteins. Gene. 2006 Oct 1;380(2):72-83
J:113153 Kim S, et al., NGL family PSD-95-interacting adhesion molecules regulate excitatory synapse formation. Nat Neurosci. 2006 Oct;9(10):1294-301
J:145953 Ng D, et al., Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning. PLoS Biol. 2009 Feb 24;7(2):e41
J:149521 Stohr H, et al., TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals. J Neurosci. 2009 May 27;29(21):6809-18
J:154018 Inagaki S, et al., Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95. J Biol Chem. 2001 Mar 23;276(12):9174-81
J:157696 Ogawa Y, et al., ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated guanylate kinases to juxtaparanodes of myelinated axons. J Neurosci. 2010 Jan 20;30(3):1038-48
J:201867 Han K, et al., SHANK3 overexpression causes manic-like behaviour with unique pharmacogenetic properties. Nature. 2013 Nov 7;503(7474):72-7
J:236346 Klaassen RV, et al., Shisa6 traps AMPA receptors at postsynaptic sites and prevents their desensitization during synaptic activity. Nat Commun. 2016 Mar 02;7:10682
J:255015 Schmitz LJM, et al., The AMPA receptor-associated protein Shisa7 regulates hippocampal synaptic function and contextual memory. Elife. 2017 Dec 4;6:e24192
J:257161 Neuille M, et al., LRIT3 Differentially Affects Connectivity and Synaptic Transmission of Cones to ON- and OFF-Bipolar Cells. Invest Ophthalmol Vis Sci. 2017 Mar 1;58(3):1768-1778
J:263376 Trinidad JC, et al., Comprehensive identification of phosphorylation sites in postsynaptic density preparations. Mol Cell Proteomics. 2006 May;5(5):914-22
J:270005 Li Y, et al., DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95) protein and plays a role in learning and memory. J Biol Chem. 2010 Apr 23;285(17):13022-31
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:292854 Xiao S, et al., Synaptic localization of C9orf72 regulates post-synaptic glutamate receptor 1 levels. Acta Neuropathol Commun. 2019 Oct 24;7(1):161
J:333121 Becamel C, et al., The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins. J Biol Chem. 2004 May 7;279(19):20257-66

Contributing Projects:
Mouse Genome Database (MGD), Gene Expression Database (GXD), Mouse Models of Human Cancer database (MMHCdb) (formerly Mouse Tumor Biology (MTB)), Gene Ontology (GO)
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last database update
04/30/2024
MGI 6.23
The Jackson Laboratory