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P31016 (DLG4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.17 Ref.19 Ref.27

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-terminus 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-terminus domain). Interacts with SHANK3. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29

Subcellular location

Cell membrane; Peripheral membrane protein. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapse. 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. Ref.6 Ref.7 Ref.14

Tissue specificity

Detected in brain (at protein level). Brain. Highest levels of isoform 2 in cerebellum, cortex, hippocampus, and corpus striatum. Ref.14 Ref.16

Domain

The PDZ domain 3 mediates interaction with ADR1B By similarity.

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

Post-translational modification

Palmitoylation of isoform 1 is required for targeting to postsynaptic density. Ref.12

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 term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering

Inferred from mutant phenotype PubMed 21525273. Source: BHF-UCL

dendritic spine morphogenesis

Inferred from mutant phenotype PubMed 21525273. Source: BHF-UCL

establishment of protein localization

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

locomotory exploration behavior

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

negative regulation of receptor internalization

Inferred from direct assay PubMed 11526121. Source: UniProtKB

neuromuscular process controlling balance

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

neuronal ion channel clustering

Traceable author statement PubMed 11152698. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 20531396. Source: RGD

positive regulation of excitatory postsynaptic membrane potential

Inferred from direct assay PubMed 12930820. Source: BHF-UCL

positive regulation of synaptic transmission

Inferred from direct assay PubMed 12930820. Source: BHF-UCL

protein complex assembly

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

protein localization to synapse

Inferred from mutant phenotype PubMed 15620359. Source: BHF-UCL

receptor localization to synapse

Inferred from mutant phenotype PubMed 21525273. Source: BHF-UCL

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

Inferred from direct assay PubMed 12930820. Source: BHF-UCL

regulation of grooming behavior

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

regulation of long-term neuronal synaptic plasticity

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

social behavior

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

synaptic vesicle maturation

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

vocalization behavior

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

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

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

cell junction

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

cytoplasm

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

dendrite cytoplasm

Inferred from direct assay Ref.1. Source: BHF-UCL

endoplasmic reticulum

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

excitatory synapse

Inferred from direct assay PubMed 19730411. Source: BHF-UCL

extrinsic component of cytoplasmic side of plasma membrane

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

juxtaparanode region of axon

Inferred from direct assay PubMed 19109503. Source: MGI

neuron projection terminus

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

neuron spine

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

neuronal postsynaptic density

Inferred from direct assay PubMed 21525273. Source: BHF-UCL

postsynaptic density

Inferred from direct assay Ref.14. Source: UniProtKB

postsynaptic membrane

Inferred from direct assay PubMed 11483650. Source: MGI

synapse

Inferred from direct assay PubMed 11483650PubMed 15657400PubMed 15681343. Source: MGI

synaptic vesicle

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

   Molecular_functionD1 dopamine receptor binding

Inferred from physical interaction PubMed 23041629. Source: RGD

P2Y1 nucleotide receptor binding

Inferred from physical interaction PubMed 20847060. Source: BHF-UCL

PDZ domain binding

Inferred from physical interaction PubMed 15024025. Source: RGD

acetylcholine receptor binding

Inferred from direct assay PubMed 22593058. Source: RGD

beta-1 adrenergic receptor binding

Inferred from physical interaction PubMed 11526121. Source: UniProtKB

glutamate receptor binding

Inferred from physical interaction PubMed 20847060. Source: BHF-UCL

ionotropic glutamate receptor binding

Inferred from physical interaction PubMed 16540568PubMed 16606616. Source: RGD

protein C-terminus binding

Inferred from physical interaction PubMed 11274188PubMed 9808460. Source: UniProtKB

protein complex binding

Inferred from physical interaction PubMed 11178875PubMed 12618293PubMed 20197063PubMed 22843680. Source: RGD

protein phosphatase binding

Inferred from physical interaction PubMed 20410104. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 9808460. Source: UniProtKB

scaffold protein binding

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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]
Isoform 1 (identifier: P31016-1)

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: P31016-2)

Also known as: PSD95-beta;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Disks large homolog 4
PRO_0000094562

Regions

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

Amino acid modifications

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

Experimental info

Mutagenesis31C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.12
Mutagenesis51C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.12
Sequence conflict611M → L in CAA47103. Ref.2
Sequence conflict781S → T in CAA47103. Ref.2
Sequence conflict177 – 1826GVGNQH → ALGTSI in CAA47103. Ref.2
Sequence conflict2001A → G in CAA47103. Ref.2
Sequence conflict2541S → T in CAA47103. Ref.2
Sequence conflict540 – 55516LGPTK…LLSEF → SLDPPKTVPTMIFSPSS in CAA47103. Ref.2
Sequence conflict623 – 6253GKH → RDQ in AAB38270. Ref.4

Secondary structure

................................................................................................................ 724
Helix Strand Turn

Details...

Sequences

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

Last modified July 1, 1993. Version 1.
Checksum: 7922D4E8E0F9AD85

FASTA72480,465
        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 RKPPAEKVME 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 ALSFRFGDVL HVIDAGDEEW 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) (Sequence not available).

References

[1]"The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein."
Cho K.-O., Hunt C.A., Kennedy M.B.
Neuron 9:929-942(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A."
Kistner U., Wenzel B.M., Veh R.W., Cases-Langhoff C., Garner A.M., Appeltauer U., Voss B., Gundelfinger E.D., Garner C.C.
J. Biol. Chem. 268:4580-4583(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]Lubec G., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 113-126; 212-233; 300-312; 381-399 AND 598-617, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]Adams L.D., Werny I., Schwartz S.M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 566-625.
Strain: Wistar Kyoto.
Tissue: Vascular smooth muscle.
[5]"Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95."
Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.
Science 269:1737-1740(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIN2A; GRIN2B; GRIN2C AND GRIN2D.
[6]"Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein."
Brenman J.E., Christopherson K.S., Craven S.E., McGee A.W., Bredt D.S.
J. Neurosci. 16:7407-7415(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density."
Takeuchi M., Hata Y., Hirao K., Toyoda A., Irie M., Takai Y.
J. Biol. Chem. 272:11943-11951(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4, SUBCELLULAR LOCATION.
Tissue: Brain.
[8]"BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein."
Deguchi M., Hata Y., Takeuchi M., Ide N., Hirao K., Yao I., Irie M., Toyoda A., Takai Y.
J. Biol. Chem. 273:26269-26272(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BEGAIN AND DLGAP1.
[9]"Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A."
Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T., Ralston H.J., Bredt D.S.
J. Neurosci. 18:8805-8813(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1A.
[10]"SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family."
Kim J.H., Liao D., Lau L.-F., Huganir R.L.
Neuron 20:683-691(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNGAP1.
[11]"CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90."
Niethammer M., Valtschanoff J.G., Kapoor T.M., Allison D.W., Weinberg R.J., Craig A.M., Sheng M.
Neuron 20:693-707(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRIPT.
[12]"Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering."
El-Husseini A.E., Craven S.E., Chetkovich D.M., Firestein B.L., Schnell E., Aoki C., Bredt D.S.
J. Cell Biol. 148:159-172(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-3 AND CYS-5, PALMITOYLATION AT CYS-3 AND CYS-5.
[13]"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.
[14]"Regulation of dendritic spine morphology by SPAR, a PSD-95-associated RapGAP."
Pak D.T., Yang S., Rudolph-Correia S., Kim E., Sheng M.
Neuron 31:289-303(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIPA1L1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]"Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2."
Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C.
J. Biol. Chem. 277:20423-20430(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCND2.
[16]"Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms."
Chetkovich D.M., Bunn R.C., Kuo S.-H., Kawasaki Y., Kohwi M., Bredt D.S.
J. Neurosci. 22:6415-6425(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[17]"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."
Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.
J. Biol. Chem. 279:46962-46968(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASIC3, FUNCTION.
[18]"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth."
Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J.
J. Cell Sci. 117:4401-4409(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CXADR.
[19]"A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin."
Prange O., Wong T.P., Gerrow K., Wang Y.T., El-Husseini A.
Proc. Natl. Acad. Sci. U.S.A. 101:13915-13920(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor."
Murata Y., Doi T., Taniguchi H., Fujiyoshi Y.
Biochem. Biophys. Res. Commun. 327:183-191(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRR7.
[21]"Interactions between CAP70 and actinfilin are important for integrity of actin cytoskeleton structures in neurons."
Chen Y., Li M.
Neuropharmacology 49:1026-1041(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHL17.
[22]"A novel family of adhesion-like molecules that interacts with the NMDA receptor."
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.
J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN2.
[23]"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN1.
[24]"Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission."
Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M.
Science 313:1792-1795(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM22 AND LGI1.
[25]"Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons."
Jordan B.A., Fernholz B.D., Khatri L., Ziff E.B.
Nat. Neurosci. 10:427-435(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKS1B.
[26]"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
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.
J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRMPD4.
[27]"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."
Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.
J. Biol. Chem. 288:6438-6450(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GPER1 AND NOS1.
[28]"Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ."
Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., Mackinnon R.
Cell 85:1067-1076(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 302-402.
[29]"Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95."
Tochio H., Hung F., Li M., Bredt D.S., Zhang M.
J. Mol. Biol. 295:225-237(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 155-246, INTERACTION WITH NOS1 AND CAPON.
[30]"Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins."
McGee A.W., Dakoji S.R., Olsen O., Bredt D.S., Lim W.A., Prehoda K.E.
Mol. Cell 8:1291-1301(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 430-724.
[31]"Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95."
Tavares G.A., Panepucci E.H., Brunger A.T.
Mol. Cell 8:1313-1325(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 430-724.
[32]"Targeting specific PDZ domains of PSD-95; structural basis for enhanced affinity and enzymatic stability of a cyclic peptide."
Piserchio A., Salinas G.D., Li T., Marshall J., Spaller M.R., Mierke D.F.
Chem. Biol. 11:469-473(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 62-154 IN COMPLEX WITH CYCLIC PEPTIDE.
[33]"Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: a revisit to N-terminal tandem PDZ domains of PSD-95."
Wang W., Weng J., Zhang X., Liu M., Zhang M.
J. Am. Chem. Soc. 131:787-796(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 61-249 IN COMPLEX WITH PEPTIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96853 mRNA. Translation: AAA41971.1.
X66474 mRNA. Translation: CAA47103.1.
U77090 mRNA. Translation: AAB38270.1.
PIRA45436.
JH0800.
RefSeqNP_062567.1. NM_019621.1.
UniGeneRn.9765.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE9X-ray1.82A302-402[»]
1BFEX-ray2.30A302-402[»]
1IU0NMR-A61-151[»]
1IU2NMR-A61-151[»]
1JXMX-ray2.00A430-724[»]
1JXOX-ray2.30A/B430-724[»]
1KJWX-ray1.80A430-724[»]
1QLCNMR-A155-249[»]
1RGRNMR-A62-154[»]
1TP3X-ray1.99A302-402[»]
1TP5X-ray1.54A302-402[»]
1TQ3X-ray1.89A302-402[»]
2KA9NMR-A61-249[»]
2XKXOther22.90A/B1-724[»]
3GSLX-ray2.05A/B61-249[»]
ProteinModelPortalP31016.
SMRP31016. Positions 62-249, 306-402, 430-724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248135. 17 interactions.
DIPDIP-29264N.
IntActP31016. 352 interactions.
MINTMINT-93329.

Chemistry

DrugBankDB00536. Guanidine.

PTM databases

PhosphoSiteP31016.

Proteomic databases

PaxDbP31016.
PRIDEP31016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000068493; ENSRNOP00000059045; ENSRNOG00000018526. [P31016-1]
GeneID29495.
KEGGrno:29495.
UCSCRGD:68424. rat. [P31016-1]

Organism-specific databases

CTD1742.
RGD68424. Dlg4.

Phylogenomic databases

eggNOGCOG0194.
GeneTreeENSGT00660000095130.
HOGENOMHOG000232102.
HOVERGENHBG107814.
InParanoidP31016.
KOK11828.
OMAWIPTRER.
OrthoDBEOG79GT6P.
PhylomeDBP31016.

Gene expression databases

GenevestigatorP31016.

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

EvolutionaryTraceP31016.
NextBio609380.
PROP31016.

Entry information

Entry nameDLG4_RAT
AccessionPrimary (citable) accession number: P31016
Secondary accession number(s): P97631
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 160 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references