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P31016

- DLG4_RAT

UniProt

P31016 - DLG4_RAT

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Protein
Disks large homolog 4
Gene
Dlg4, Dlgh4, Psd95
Organism
Rattus norvegicus (Rat)
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.3 Publications

GO - Molecular functioni

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

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 exploration behavior Source: BHF-UCL
  5. negative regulation of receptor internalization Source: UniProtKB
  6. neuromuscular process controlling balance Source: BHF-UCL
  7. neuronal ion channel clustering Source: UniProtKB
  8. positive regulation of cytosolic calcium ion concentration Source: RGD
  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 N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  15. regulation of grooming behavior Source: BHF-UCL
  16. regulation of long-term neuronal synaptic plasticity Source: BHF-UCL
  17. social behavior Source: BHF-UCL
  18. synaptic vesicle maturation Source: BHF-UCL
  19. vocalization behavior Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_196392. CREB phosphorylation through the activation of CaMKII.
REACT_196422. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi68424. Dlg4.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31C → S: Loss of palmitoylation and targeting to postsynaptic density. 1 Publication
Mutagenesisi5 – 51C → S: Loss of palmitoylation and targeting to postsynaptic density. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Disks large homolog 4
PRO_0000094562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi3 – 31S-palmitoyl cysteine1 Publication
Lipidationi5 – 51S-palmitoyl cysteine1 Publication
Modified residuei142 – 1421Phosphoserine By similarity
Modified residuei240 – 2401Phosphotyrosine By similarity
Modified residuei580 – 5801Phosphotyrosine By similarity
Modified residuei715 – 7151Phosphotyrosine By similarity

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP31016.
PRIDEiP31016.

PTM databases

PhosphoSiteiP31016.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP31016.

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 By similarity.20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Adrb2P106082EBI-375655,EBI-7090342
ApcP704782EBI-375655,EBI-631663
Cacng2Q71RJ22EBI-375655,EBI-8538384
Cnksr2Q9Z1T44EBI-375655,EBI-8548356
CRIPTQ9P0212EBI-375655,EBI-946968From a different organism.
DgkiQ810C55EBI-375655,EBI-8523614
DgkzO085606EBI-375655,EBI-8570505
DLG1Q12959-29EBI-375655,EBI-357500From a different organism.
Dlg1Q626962EBI-375655,EBI-389325
Dlgap1P978369EBI-375655,EBI-80901
Dlgap2P978372EBI-375655,EBI-81025
GraspQ8R4T53EBI-375655,EBI-7361884
Grin1P354394EBI-375655,EBI-877897
GRIN2AQ128792EBI-375655,EBI-7249937From a different organism.
Grin2aQ009595EBI-375655,EBI-630970
GRIN2BQ132242EBI-375655,EBI-2256942From a different organism.
Grin2bQ009608EBI-375655,EBI-396905
GRIN2CQ149572EBI-375655,EBI-8285963From a different organism.
Gucy1a2Q9WVI47EBI-375655,EBI-7665590
Gucy1b3P205952EBI-375655,EBI-7980539
KCNA4P224593EBI-375655,EBI-631235From a different organism.
Klhl17Q8K4302EBI-375655,EBI-7713653
Lrfn2Q460M53EBI-375655,EBI-877185
Lrrc7P705875EBI-375655,EBI-7798464
Map1aP3492612EBI-375655,EBI-631571
PtenO548575EBI-375655,EBI-8074312
Shank1Q9WV483EBI-375655,EBI-80909
Slc6a9P285722EBI-375655,EBI-848783
Slc6a9P28572-24EBI-375655,EBI-848796
SrcP054809EBI-375655,EBI-298680From a different organism.
Sstr4P309373EBI-375655,EBI-7665959
Syngap1Q9QUH63EBI-375655,EBI-2310349
Vangl1Q80Z964EBI-375655,EBI-1750708From a different organism.
Vangl2Q91ZD46EBI-375655,EBI-1750744From a different organism.
Wipf1Q6IN365EBI-375655,EBI-6986245

Protein-protein interaction databases

BioGridi248135. 17 interactions.
DIPiDIP-29264N.
IntActiP31016. 352 interactions.
MINTiMINT-93329.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 699
Beta strandi71 – 733
Beta strandi74 – 807
Beta strandi82 – 854
Beta strandi88 – 914
Beta strandi94 – 996
Beta strandi101 – 1033
Helixi104 – 1085
Beta strandi116 – 1205
Helixi125 – 1273
Helixi130 – 1389
Beta strandi142 – 15110
Beta strandi156 – 16611
Beta strandi172 – 1787
Beta strandi189 – 1946
Helixi199 – 2035
Beta strandi211 – 2155
Beta strandi221 – 2244
Helixi225 – 2339
Beta strandi237 – 24711
Helixi302 – 3043
Beta strandi312 – 3176
Beta strandi325 – 3295
Helixi331 – 3333
Beta strandi336 – 3416
Helixi346 – 3505
Beta strandi357 – 3626
Helixi372 – 3809
Beta strandi384 – 3929
Helixi394 – 3985
Beta strandi414 – 4163
Beta strandi431 – 4377
Helixi441 – 4455
Beta strandi449 – 4513
Beta strandi459 – 4646
Beta strandi467 – 4759
Beta strandi486 – 4894
Helixi491 – 4999
Turni504 – 5074
Beta strandi523 – 5308
Beta strandi537 – 5415
Helixi544 – 55411
Turni556 – 5583
Turni576 – 5783
Helixi586 – 5949
Beta strandi598 – 6047
Beta strandi607 – 6126
Helixi613 – 6219
Beta strandi625 – 6284
Helixi634 – 6407
Beta strandi646 – 6505
Helixi655 – 6617
Beta strandi663 – 6653
Helixi667 – 68418
Helixi685 – 6873
Beta strandi689 – 6924
Helixi697 – 71115
Beta strandi714 – 7196

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE9X-ray1.82A302-430[»]
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[»]
2MHONMR-A60-155[»]
2XKXOther22.90A/B1-724[»]
3GSLX-ray2.05A/B61-249[»]
3WP0X-ray2.04A531-713[»]
3WP1X-ray2.80B531-713[»]
ProteinModelPortaliP31016.
SMRiP31016. Positions 62-249, 306-402, 430-724.

Miscellaneous databases

EvolutionaryTraceiP31016.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 15187PDZ 1
Add
BLAST
Domaini160 – 24687PDZ 2
Add
BLAST
Domaini313 – 39381PDZ 3
Add
BLAST
Domaini428 – 49871SH3
Add
BLAST
Domaini534 – 709176Guanylate kinase-like
Add
BLAST

Domaini

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.

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.
InParanoidiP31016.
KOiK11828.
OMAiWIPTRER.
OrthoDBiEOG79GT6P.
PhylomeDBiP31016.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P31016-1) [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
RKPPAEKVME 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
ALSFRFGDVL HVIDAGDEEW 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):80,465
Last modified:July 1, 1993 - v1
Checksum:i7922D4E8E0F9AD85
GO
Isoform 2 (identifier: P31016-2)

Also known as: PSD95-beta

Sequence is not available
Length:
Mass (Da):

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611M → L in CAA47103. 1 Publication
Sequence conflicti78 – 781S → T in CAA47103. 1 Publication
Sequence conflicti177 – 1826GVGNQH → ALGTSI in CAA47103. 1 Publication
Sequence conflicti200 – 2001A → G in CAA47103. 1 Publication
Sequence conflicti254 – 2541S → T in CAA47103. 1 Publication
Sequence conflicti540 – 55516LGPTK…LLSEF → SLDPPKTVPTMIFSPSS in CAA47103. 1 Publication
Add
BLAST
Sequence conflicti623 – 6253GKH → RDQ in AAB38270. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96853 mRNA. Translation: AAA41971.1.
X66474 mRNA. Translation: CAA47103.1.
U77090 mRNA. Translation: AAB38270.1.
PIRiA45436.
JH0800.
RefSeqiNP_062567.1. NM_019621.1. [P31016-1]
UniGeneiRn.9765.

Genome annotation databases

EnsembliENSRNOT00000068493; ENSRNOP00000059045; ENSRNOG00000018526. [P31016-1]
GeneIDi29495.
KEGGirno:29495.
UCSCiRGD:68424. rat. [P31016-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96853 mRNA. Translation: AAA41971.1 .
X66474 mRNA. Translation: CAA47103.1 .
U77090 mRNA. Translation: AAB38270.1 .
PIRi A45436.
JH0800.
RefSeqi NP_062567.1. NM_019621.1. [P31016-1 ]
UniGenei Rn.9765.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BE9 X-ray 1.82 A 302-430 [» ]
1BFE X-ray 2.30 A 302-402 [» ]
1IU0 NMR - A 61-151 [» ]
1IU2 NMR - A 61-151 [» ]
1JXM X-ray 2.00 A 430-724 [» ]
1JXO X-ray 2.30 A/B 430-724 [» ]
1KJW X-ray 1.80 A 430-724 [» ]
1QLC NMR - A 155-249 [» ]
1RGR NMR - A 62-154 [» ]
1TP3 X-ray 1.99 A 302-402 [» ]
1TP5 X-ray 1.54 A 302-402 [» ]
1TQ3 X-ray 1.89 A 302-402 [» ]
2KA9 NMR - A 61-249 [» ]
2MHO NMR - A 60-155 [» ]
2XKX Other 22.90 A/B 1-724 [» ]
3GSL X-ray 2.05 A/B 61-249 [» ]
3WP0 X-ray 2.04 A 531-713 [» ]
3WP1 X-ray 2.80 B 531-713 [» ]
ProteinModelPortali P31016.
SMRi P31016. Positions 62-249, 306-402, 430-724.
ModBasei Search...

Protein-protein interaction databases

BioGridi 248135. 17 interactions.
DIPi DIP-29264N.
IntActi P31016. 352 interactions.
MINTi MINT-93329.

Chemistry

DrugBanki DB00536. Guanidine.

PTM databases

PhosphoSitei P31016.

Proteomic databases

PaxDbi P31016.
PRIDEi P31016.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000068493 ; ENSRNOP00000059045 ; ENSRNOG00000018526 . [P31016-1 ]
GeneIDi 29495.
KEGGi rno:29495.
UCSCi RGD:68424. rat. [P31016-1 ]

Organism-specific databases

CTDi 1742.
RGDi 68424. Dlg4.

Phylogenomic databases

eggNOGi COG0194.
GeneTreei ENSGT00660000095130.
HOGENOMi HOG000232102.
HOVERGENi HBG107814.
InParanoidi P31016.
KOi K11828.
OMAi WIPTRER.
OrthoDBi EOG79GT6P.
PhylomeDBi P31016.

Enzyme and pathway databases

Reactomei REACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_196392. CREB phosphorylation through the activation of CaMKII.
REACT_196422. Activation of Ca-permeable Kainate Receptor.

Miscellaneous databases

EvolutionaryTracei P31016.
NextBioi 609380.
PROi P31016.

Gene expression databases

Genevestigatori P31016.

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

  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.

Entry informationi

Entry nameiDLG4_RAT
AccessioniPrimary (citable) accession number: P31016
Secondary accession number(s): P97631
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 164 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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