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Q62108

- DLG4_MOUSE

UniProt

Q62108 - DLG4_MOUSE

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Protein

Disks large homolog 4

Gene
Dlg4, Dlgh4, Psd95
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. acetylcholine receptor binding Source: BHF-UCL
  2. beta-1 adrenergic receptor binding Source: BHF-UCL
  3. D1 dopamine receptor binding Source: BHF-UCL
  4. ionotropic glutamate receptor binding Source: BHF-UCL
  5. neurexin family protein binding Source: UniProtKB
  6. P2Y1 nucleotide receptor binding Source: BHF-UCL
  7. PDZ domain binding Source: BHF-UCL
  8. protein binding Source: UniProtKB
  9. protein complex binding Source: BHF-UCL
  10. protein C-terminus binding Source: BHF-UCL
  11. protein phosphatase binding Source: BHF-UCL
  12. scaffold protein binding Source: BHF-UCL
  13. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering Source: BHF-UCL
  2. dendritic spine morphogenesis Source: BHF-UCL
  3. establishment of protein localization Source: BHF-UCL
  4. locomotory behavior Source: UniProtKB
  5. locomotory exploration behavior Source: BHF-UCL
  6. negative regulation of receptor internalization Source: BHF-UCL
  7. neuromuscular process controlling balance Source: BHF-UCL
  8. positive regulation of cytosolic calcium ion concentration Source: BHF-UCL
  9. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  10. positive regulation of synaptic transmission Source: BHF-UCL
  11. protein complex assembly Source: BHF-UCL
  12. protein localization to synapse Source: BHF-UCL
  13. receptor localization to synapse Source: BHF-UCL
  14. regulation of grooming behavior Source: BHF-UCL
  15. regulation of long-term neuronal synaptic plasticity Source: MGI
  16. regulation of neuronal synaptic plasticity Source: UniProtKB
  17. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  18. response to cocaine Source: UniProtKB
  19. social behavior Source: BHF-UCL
  20. synaptic vesicle maturation Source: MGI
  21. vocalization behavior Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_198248. CREB phosphorylation through the activation of CaMKII.
REACT_198694. Activation of Ca-permeable Kainate Receptor.

Names & Taxonomyi

Protein namesi
Recommended name:
Disks large homolog 4
Alternative name(s):
Postsynaptic density protein 95
Short name:
PSD-95
Synapse-associated protein 90
Short name:
SAP-90
Short name:
SAP90
Gene namesi
Name:Dlg4
Synonyms:Dlgh4, Psd95
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1277959. Dlg4.

Subcellular locationi

Cell membrane; Peripheral membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapse
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.1 Publication

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: MGI
  2. cell junction Source: MGI
  3. cerebellar mossy fiber Source: MGI
  4. cortical cytoskeleton Source: Ensembl
  5. cytoplasm Source: MGI
  6. dendrite Source: MGI
  7. dendrite cytoplasm Source: BHF-UCL
  8. dendritic spine Source: ParkinsonsUK-UCL
  9. endoplasmic reticulum Source: MGI
  10. excitatory synapse Source: BHF-UCL
  11. extrinsic component of cytoplasmic side of plasma membrane Source: MGI
  12. juxtaparanode region of axon Source: MGI
  13. membrane Source: MGI
  14. neuronal postsynaptic density Source: BHF-UCL
  15. neuron projection terminus Source: MGI
  16. neuron spine Source: BHF-UCL
  17. plasma membrane Source: MGI
  18. postsynaptic density Source: UniProtKB
  19. postsynaptic membrane Source: UniProtKB-KW
  20. synapse Source: MGI
  21. synaptic vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Disks large homolog 4PRO_0000094561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi3 – 31S-palmitoyl cysteine By similarity
Lipidationi5 – 51S-palmitoyl cysteine By similarity
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei240 – 2401Phosphotyrosine1 Publication
Modified residuei580 – 5801Phosphotyrosine1 Publication
Modified residuei715 – 7151Phosphotyrosine1 Publication

Post-translational modificationi

Palmitoylation of isoform 1 is required for targeting to postsynaptic density By similarity.

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ62108.
PaxDbiQ62108.
PRIDEiQ62108.

PTM databases

PhosphoSiteiQ62108.

Expressioni

Gene expression databases

ArrayExpressiQ62108.
BgeeiQ62108.
CleanExiMM_DLG4.
GenevestigatoriQ62108.

Interactioni

Subunit structurei

Interacts through its PDZ domains with ANO2 and NETO1. Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D, ASIC3, certain splice forms of GRIN1, KCND2, CXADR, SYNGAP1, KCNA1, KCNA2, KCNA3, KCNA4, ERBB4, LRRC4; LRRC4B and SEMA4C. 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, SIPA1L1 and KIF13B. Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK. Interacts with ADR1B, ANKS1B and PRR7. May interact with HTR2A. Interacts with ADAM22, KLHL17 and LGI1. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2 and LRFN4, but not with LRFN3 nor LRFN5. 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. Interacts (via N-terminus tandem pair of PDZ domains) with NOS1 (via N-terminal domain). Interacts with SHANK3. Interacts with KCNJ4.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ablim1Q8K4G54EBI-300895,EBI-2307994
AppP120234EBI-300895,EBI-78814
ArcQ9WV313EBI-300895,EBI-397779
Baiap2Q8BKX13EBI-300895,EBI-771498
Camk2aP117983EBI-300895,EBI-400384
Dlg1Q811D03EBI-300895,EBI-514290
Dlg2Q91XM95EBI-300895,EBI-400138
Dlg3P701753EBI-300895,EBI-396969
Fzd7Q610904EBI-300895,EBI-8473104
GdaQ9R1115EBI-300895,EBI-2308876
Grin1P3543810EBI-300895,EBI-400084
Grin2aP354367EBI-300895,EBI-400115
Grin2bQ0109716EBI-300895,EBI-400125
Gucy1a2Q9WVI43EBI-300895,EBI-7665590From a different organism.
Lrfn2Q80TG92EBI-300895,EBI-877092
Lrp1Q91ZX73EBI-300895,EBI-300955
Lrp2A2ARV42EBI-300895,EBI-300875
Lrp8Q924X63EBI-300895,EBI-432319
Mapk1P630853EBI-300895,EBI-397697
Mdm2P238043EBI-300895,EBI-641788
NrcamQ810U42EBI-300895,EBI-8321816
NsfP464604EBI-300895,EBI-398006
Pcdh10Q80TE24EBI-300895,EBI-6661550
Rac1P630012EBI-300895,EBI-413646
Sh3kbp1Q8R5503EBI-300895,EBI-642709
Sstr1P308733EBI-300895,EBI-7665262
Sstr4P496603EBI-300895,EBI-7665342

Protein-protein interaction databases

BioGridi199230. 299 interactions.
DIPiDIP-29888N.
IntActiQ62108. 342 interactions.
MINTiMINT-136080.

Structurei

3D structure databases

ProteinModelPortaliQ62108.
SMRiQ62108. Positions 60-724.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 15187PDZ 1Add
BLAST
Domaini160 – 24687PDZ 2Add
BLAST
Domaini313 – 39381PDZ 3Add
BLAST
Domaini428 – 49871SH3Add
BLAST
Domaini534 – 709176Guanylate kinase-likeAdd
BLAST

Domaini

The PDZ domain 3 mediates interaction with ADR1B.1 Publication
The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to postsynaptic density By similarity.1 Publication

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 3 PDZ (DHR) domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00660000095130.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
KOiK11828.
OMAiWIPTRER.
OrthoDBiEOG79GT6P.
PhylomeDBiQ62108.
TreeFamiTF323171.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProiIPR016313. DLG1.
IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR019590. MAGUK_PEST_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23119. PTHR23119. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF10608. MAGUK_N_PEST. 2 hits.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PIRSFiPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q62108-1) [UniParc]FASTAAdd to Basket

Also known as: PSD95-alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY    50
ELQVNGTEGE MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII 100
PGGAAAQDGR LRVNDSILFV NEVDVREVTH SAAVEALKEA GSIVRLYVMR 150
RKPPAEKIIE IKLIKGPKGL GFSIAGGVGN QHIPGDNSIY VTKIIEGGAA 200
HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY LKVAKPSNAY 250
LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD 300
LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS 350
GELRKGDQIL SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF 400
EAKIHDLREQ LMNSSLGSGT ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ 450
ALSFHFGDVL HVIDASDEEW WQARRVHSDS ETDDIGFIPS KRRVERREWS 500
RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL GPTKDRANDD 550
LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE 600
AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI 650
RPRSLENVLE INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI 700
YHKVKRVIED LSGPYIWVPA RERL 724
Length:724
Mass (Da):80,472
Last modified:November 1, 1997 - v1
Checksum:i7EFFC99E1FFF90BA
GO
Isoform 2 (identifier: Q62108-2) [UniParc]FASTAAdd to Basket

Also known as: PSD95-beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MDCLCIVTTK → MSQRPRAPRSALWLLAPPLLRWAPPLLTVLHSDLFQALLDILDYYEACISESQ

Show »
Length:767
Mass (Da):85,423
Checksum:i650F267DF8139740
GO
Isoform 3 (identifier: Q62108-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-53: Missing.

Note: No experimental confirmation available.

Show »
Length:721
Mass (Da):80,102
Checksum:i675C1EBD807CD37C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1010MDCLCIVTTK → MSQRPRAPRSALWLLAPPLL RWAPPLLTVLHSDLFQALLD ILDYYEACISESQ in isoform 2. VSP_014930
Alternative sequencei51 – 533Missing in isoform 3. VSP_014931

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031D → E in AAH14807. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50621 mRNA. Translation: BAA09297.1.
AL596185 Genomic DNA. Translation: CAI35168.1.
AL596185 Genomic DNA. Translation: CAI35169.1.
AL596185 Genomic DNA. Translation: CAI35170.1.
BC014807 mRNA. Translation: AAH14807.1.
CCDSiCCDS36202.1. [Q62108-1]
CCDS48829.1. [Q62108-3]
RefSeqiNP_001103222.1. NM_001109752.1. [Q62108-3]
NP_031890.1. NM_007864.3. [Q62108-1]
UniGeneiMm.27256.

Genome annotation databases

EnsembliENSMUST00000018700; ENSMUSP00000018700; ENSMUSG00000020886. [Q62108-1]
ENSMUST00000108588; ENSMUSP00000104229; ENSMUSG00000020886. [Q62108-3]
ENSMUST00000108589; ENSMUSP00000104230; ENSMUSG00000020886. [Q62108-2]
GeneIDi13385.
KEGGimmu:13385.
UCSCiuc007jtp.2. mouse. [Q62108-1]
uc007jtq.2. mouse. [Q62108-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50621 mRNA. Translation: BAA09297.1 .
AL596185 Genomic DNA. Translation: CAI35168.1 .
AL596185 Genomic DNA. Translation: CAI35169.1 .
AL596185 Genomic DNA. Translation: CAI35170.1 .
BC014807 mRNA. Translation: AAH14807.1 .
CCDSi CCDS36202.1. [Q62108-1 ]
CCDS48829.1. [Q62108-3 ]
RefSeqi NP_001103222.1. NM_001109752.1. [Q62108-3 ]
NP_031890.1. NM_007864.3. [Q62108-1 ]
UniGenei Mm.27256.

3D structure databases

ProteinModelPortali Q62108.
SMRi Q62108. Positions 60-724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199230. 299 interactions.
DIPi DIP-29888N.
IntActi Q62108. 342 interactions.
MINTi MINT-136080.

Chemistry

ChEMBLi CHEMBL1795134.

PTM databases

PhosphoSitei Q62108.

Proteomic databases

MaxQBi Q62108.
PaxDbi Q62108.
PRIDEi Q62108.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018700 ; ENSMUSP00000018700 ; ENSMUSG00000020886 . [Q62108-1 ]
ENSMUST00000108588 ; ENSMUSP00000104229 ; ENSMUSG00000020886 . [Q62108-3 ]
ENSMUST00000108589 ; ENSMUSP00000104230 ; ENSMUSG00000020886 . [Q62108-2 ]
GeneIDi 13385.
KEGGi mmu:13385.
UCSCi uc007jtp.2. mouse. [Q62108-1 ]
uc007jtq.2. mouse. [Q62108-3 ]

Organism-specific databases

CTDi 1742.
MGIi MGI:1277959. Dlg4.

Phylogenomic databases

eggNOGi COG0194.
GeneTreei ENSGT00660000095130.
HOGENOMi HOG000232102.
HOVERGENi HBG107814.
KOi K11828.
OMAi WIPTRER.
OrthoDBi EOG79GT6P.
PhylomeDBi Q62108.
TreeFami TF323171.

Enzyme and pathway databases

Reactomei REACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_198248. CREB phosphorylation through the activation of CaMKII.
REACT_198694. Activation of Ca-permeable Kainate Receptor.

Miscellaneous databases

ChiTaRSi DLG4. mouse.
NextBioi 283740.
PROi Q62108.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q62108.
Bgeei Q62108.
CleanExi MM_DLG4.
Genevestigatori Q62108.

Family and domain databases

Gene3Di 2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProi IPR016313. DLG1.
IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR019590. MAGUK_PEST_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR23119. PTHR23119. 1 hit.
Pfami PF00625. Guanylate_kin. 1 hit.
PF10608. MAGUK_N_PEST. 2 hits.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF001741. MAGUK_DLGH. 1 hit.
SMARTi SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse homologue of rat PSD-95/SAP90A."
    Kohmura N., Yagi T.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: DBA/2.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6.
    Tissue: Retina.
  4. "Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein."
    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.
    Nature 396:433-439(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95."
    Inagaki S., Ohoka Y., Sugimoto H., Fujioka S., Amazaki M., Kurinami H., Miyazaki N., Tohyama M., Furuyama T.
    J. Biol. Chem. 276:9174-9181(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEMA4C.
  6. "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses."
    Inanobe A., Fujita A., Ito M., Tomoike H., Inageda K., Kurachi Y.
    Am. J. Physiol. 282:C1396-C1403(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNJ4.
  7. "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins."
    Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P.
    J. Biol. Chem. 279:20257-20266(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTR2A.
  8. "Interaction with cystic fibrosis transmembrane conductance regulator-associated ligand (CAL) inhibits beta1-adrenergic receptor surface expression."
    He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.
    J. Biol. Chem. 279:50190-50196(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADR1B, DOMAIN, FUNCTION.
  9. "Comparative analysis of structure, expression and PSD95-binding capacity of Lrfn, a novel family of neuronal transmembrane proteins."
    Morimura N., Inoue T., Katayama K., Aruga J.
    Gene 380:72-83(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
    Strain: Swiss Webster.
  10. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  11. "NGL family PSD-95-interacting adhesion molecules regulate excitatory synapse formation."
    Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K., Kim H., Weinberg R.J., Kim E.
    Nat. Neurosci. 9:1294-1301(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRRC4B AND LRRC4.
  12. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; TYR-580 AND TYR-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  13. "TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals."
    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.
    J. Neurosci. 29:6809-6818(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANO2.
    Strain: C57BL/6.
    Tissue: Retina.
  14. "Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning."
    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.
    PLoS Biol. 7:E41-E41(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NETO1.
  15. "SHANK3 overexpression causes manic-like behaviour with unique pharmacogenetic properties."
    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.
    Nature 503:72-77(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHANK3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiDLG4_MOUSE
AccessioniPrimary (citable) accession number: Q62108
Secondary accession number(s): Q5NCV5
, Q5NCV6, Q5NCV7, Q91WJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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