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Q62108 (DLG4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dlg4
Synonyms:Dlgh4, Psd95
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.8

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15

Subcellular location

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. Ref.15

Domain

The PDZ domain 3 mediates interaction with ADR1B. Ref.8

The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to postsynaptic density By similarity. Ref.8

Post-translational modification

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

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. Ref.4

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering

Inferred from sequence or structural similarity. Source: BHF-UCL

dendritic spine morphogenesis

Inferred from direct assay PubMed 20952458. Source: BHF-UCL

establishment of protein localization

Inferred from sequence or structural similarity. Source: BHF-UCL

locomotory behavior

Non-traceable author statement PubMed 14980210. Source: UniProtKB

locomotory exploration behavior

Inferred from mutant phenotype PubMed 20952458. Source: BHF-UCL

negative regulation of receptor internalization

Inferred from sequence or structural similarity. Source: BHF-UCL

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 20952458. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

protein complex assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to synapse

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor localization to synapse

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of grooming behavior

Inferred from mutant phenotype PubMed 20952458. Source: BHF-UCL

regulation of long-term neuronal synaptic plasticity

Inferred from genetic interaction PubMed 12427827. Source: MGI

regulation of neuronal synaptic plasticity

Non-traceable author statement PubMed 14980210. Source: UniProtKB

response to cocaine

Non-traceable author statement PubMed 14980210. Source: UniProtKB

social behavior

Inferred from mutant phenotype PubMed 20952458. Source: BHF-UCL

synaptic vesicle maturation

Inferred from direct assay PubMed 15603741. Source: MGI

vocalization behavior

Inferred from mutant phenotype PubMed 20952458. Source: BHF-UCL

   Cellular_componentalpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from direct assay PubMed 15883194PubMed 22632720. Source: MGI

cell junction

Inferred from direct assay PubMed 21920314. Source: MGI

cerebellar mossy fiber

Inferred from direct assay PubMed 23791195. Source: MGI

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 11483650. Source: MGI

dendrite

Inferred from direct assay PubMed 23395379. Source: MGI

dendrite cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

dendritic spine

Inferred from direct assay PubMed 24464040. Source: ParkinsonsUK-UCL

endoplasmic reticulum

Inferred from direct assay PubMed 16814779. Source: MGI

excitatory synapse

Inferred from direct assay PubMed 18272690. Source: BHF-UCL

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 11483650. Source: MGI

juxtaparanode region of axon

Inferred from direct assay PubMed 19109503. Source: MGI

membrane

Inferred from direct assay PubMed 15082773PubMed 15978582. Source: MGI

neuron projection terminus

Inferred from direct assay PubMed 12115694. Source: MGI

neuron spine

Inferred from direct assay PubMed 16606358. Source: BHF-UCL

neuronal postsynaptic density

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 16520334. Source: MGI

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from direct assay PubMed 12972605PubMed 14622577PubMed 14645471PubMed 15071120PubMed 16818724PubMed 23791195PubMed 23986251. Source: MGI

synaptic vesicle

Inferred from direct assay PubMed 16520334. Source: MGI

   Molecular_functionD1 dopamine receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

P2Y1 nucleotide receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

PDZ domain binding

Inferred from sequence or structural similarity. Source: BHF-UCL

acetylcholine receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

beta-1 adrenergic receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

ionotropic glutamate receptor binding

Inferred from physical interaction PubMed 15207857. Source: BHF-UCL

neurexin family protein binding

Non-traceable author statement PubMed 9278515. Source: UniProtKB

protein C-terminus binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.14Ref.13. Source: UniProtKB

protein complex binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein phosphatase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

scaffold protein binding

Inferred from physical interaction PubMed 16606358. Source: BHF-UCL

structural molecule activity

Non-traceable author statement PubMed 14980210. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62108-1)

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.
Isoform 2 (identifier: Q62108-2)

Also known as: PSD95-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MDCLCIVTTK → MSQRPRAPRSALWLLAPPLLRWAPPLLTVLHSDLFQALLDILDYYEACISESQ
Isoform 3 (identifier: Q62108-3)

The sequence of this isoform differs from the canonical sequence as follows:
     51-53: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Disks large homolog 4
PRO_0000094561

Regions

Domain65 – 15187PDZ 1
Domain160 – 24687PDZ 2
Domain313 – 39381PDZ 3
Domain428 – 49871SH3
Domain534 – 709176Guanylate kinase-like

Amino acid modifications

Modified residue1421Phosphoserine Ref.10
Modified residue2401Phosphotyrosine Ref.12
Modified residue5801Phosphotyrosine Ref.12
Modified residue7151Phosphotyrosine Ref.12
Lipidation31S-palmitoyl cysteine By similarity
Lipidation51S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence1 – 1010MDCLCIVTTK → MSQRPRAPRSALWLLAPPLL RWAPPLLTVLHSDLFQALLD ILDYYEACISESQ in isoform 2.
VSP_014930
Alternative sequence51 – 533Missing in isoform 3.
VSP_014931

Experimental info

Sequence conflict2031D → E in AAH14807. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PSD95-alpha) [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 7EFFC99E1FFF90BA

FASTA72480,472
        10         20         30         40         50         60 
MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE 

        70         80         90        100        110        120 
MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV 

       130        140        150        160        170        180 
NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKIIE IKLIKGPKGL GFSIAGGVGN 

       190        200        210        220        230        240 
QHIPGDNSIY VTKIIEGGAA HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY 

       250        260        270        280        290        300 
LKVAKPSNAY LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD 

       310        320        330        340        350        360 
LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDQIL 

       370        380        390        400        410        420 
SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF EAKIHDLREQ LMNSSLGSGT 

       430        440        450        460        470        480 
ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ ALSFHFGDVL HVIDASDEEW WQARRVHSDS 

       490        500        510        520        530        540 
ETDDIGFIPS KRRVERREWS RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL 

       550        560        570        580        590        600 
GPTKDRANDD LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE 

       610        620        630        640        650        660 
AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI RPRSLENVLE 

       670        680        690        700        710        720 
INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI YHKVKRVIED LSGPYIWVPA 


RERL 

« Hide

Isoform 2 (PSD95-beta) [UniParc].

Checksum: 650F267DF8139740
Show »

FASTA76785,423
Isoform 3 [UniParc].

Checksum: 675C1EBD807CD37C
Show »

FASTA72180,102

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36202.1. [Q62108-1]
CCDS48829.1. [Q62108-3]
RefSeqNP_001103222.1. NM_001109752.1. [Q62108-3]
NP_031890.1. NM_007864.3. [Q62108-1]
UniGeneMm.27256.

3D structure databases

ProteinModelPortalQ62108.
SMRQ62108. Positions 60-724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199230. 299 interactions.
DIPDIP-29888N.
IntActQ62108. 342 interactions.
MINTMINT-136080.

Chemistry

ChEMBLCHEMBL1795134.

PTM databases

PhosphoSiteQ62108.

Proteomic databases

MaxQBQ62108.
PaxDbQ62108.
PRIDEQ62108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018700; ENSMUSP00000018700; ENSMUSG00000020886. [Q62108-1]
ENSMUST00000108588; ENSMUSP00000104229; ENSMUSG00000020886. [Q62108-3]
ENSMUST00000108589; ENSMUSP00000104230; ENSMUSG00000020886. [Q62108-2]
GeneID13385.
KEGGmmu:13385.
UCSCuc007jtp.2. mouse. [Q62108-1]
uc007jtq.2. mouse. [Q62108-3]

Organism-specific databases

CTD1742.
MGIMGI:1277959. Dlg4.

Phylogenomic databases

eggNOGCOG0194.
GeneTreeENSGT00660000095130.
HOGENOMHOG000232102.
HOVERGENHBG107814.
KOK11828.
OMAWIPTRER.
OrthoDBEOG79GT6P.
PhylomeDBQ62108.
TreeFamTF323171.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressQ62108.
BgeeQ62108.
CleanExMM_DLG4.
GenevestigatorQ62108.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProIPR016313. 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]
PANTHERPTHR23119. PTHR23119. 1 hit.
PfamPF00625. 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]
PIRSFPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDLG4. mouse.
NextBio283740.
PROQ62108.
SOURCESearch...

Entry information

Entry nameDLG4_MOUSE
AccessionPrimary (citable) accession number: Q62108
Secondary accession number(s): Q5NCV5 expand/collapse secondary AC list , Q5NCV6, Q5NCV7, Q91WJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot