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P78352

- DLG4_HUMAN

UniProt

P78352 - DLG4_HUMAN

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Protein

Disks large homolog 4

Gene
DLG4, PSD95
Organism
Homo sapiens (Human)
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 By similarity.

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. P2Y1 nucleotide receptor binding Source: BHF-UCL
  6. PDZ domain binding Source: BHF-UCL
  7. protein binding Source: UniProtKB
  8. protein complex binding Source: BHF-UCL
  9. protein C-terminus binding Source: UniProtKB
  10. protein phosphatase binding Source: BHF-UCL
  11. scaffold protein binding Source: BHF-UCL

GO - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_18307. Trafficking of AMPA receptors.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_22329. NrCAM interactions.
SignaLinkiP78352.

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:PSD95
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:2903. 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.1 Publication

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: UniProtKB
  4. cytoplasm Source: BHF-UCL
  5. dendrite cytoplasm Source: BHF-UCL
  6. endocytic vesicle membrane Source: Reactome
  7. endoplasmic reticulum Source: BHF-UCL
  8. excitatory synapse Source: BHF-UCL
  9. extrinsic component of cytoplasmic side of plasma membrane Source: BHF-UCL
  10. juxtaparanode region of axon Source: BHF-UCL
  11. neuronal postsynaptic density Source: BHF-UCL
  12. neuron projection terminus Source: BHF-UCL
  13. neuron spine Source: BHF-UCL
  14. plasma membrane Source: Reactome
  15. postsynaptic density Source: UniProtKB
  16. postsynaptic membrane Source: UniProtKB
  17. synapse Source: BHF-UCL
  18. synaptic vesicle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27359.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724Disks large homolog 4PRO_0000094560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi3 – 31S-palmitoyl cysteine By similarity
Lipidationi5 – 51S-palmitoyl cysteine By similarity
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 By similarity.

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP78352.
PaxDbiP78352.
PRIDEiP78352.

PTM databases

PhosphoSiteiP78352.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

ArrayExpressiP78352.
BgeeiP78352.
CleanExiHS_DLG4.
GenevestigatoriP78352.

Organism-specific databases

HPAiCAB001999.
CAB002000.
HPA010122.

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRIPTQ9P0214EBI-80389,EBI-946968
DLGAP1O144905EBI-80389,EBI-1753207
Dlgap1P97836-53EBI-80389,EBI-6269434From a different organism.
ERBB4Q153036EBI-80389,EBI-80371
Gpsm2Q8VDU07EBI-80389,EBI-7575403From a different organism.
GRIN2AQ128793EBI-80389,EBI-7249937
GRIN2BQ132242EBI-80389,EBI-2256942
GRIN2CQ149574EBI-80389,EBI-8285963
KCNA1Q094702EBI-80389,EBI-8286599
Kcna1P104992EBI-80389,EBI-631463From a different organism.
Kcna2P631422EBI-80389,EBI-631446From a different organism.
Kcna3P153842EBI-80389,EBI-631478From a different organism.
KCNA4P224592EBI-80389,EBI-631235
Kcna4P153859EBI-80389,EBI-631417From a different organism.
KIF1BO60333-34EBI-80389,EBI-465669
MDM2Q009873EBI-80389,EBI-389668

Protein-protein interaction databases

BioGridi108086. 86 interactions.
DIPiDIP-30919N.
IntActiP78352. 29 interactions.
MINTiMINT-199061.
STRINGi9606.ENSP00000293813.

Structurei

Secondary structure

1
724
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 699
Beta strandi72 – 743
Beta strandi77 – 815
Beta strandi83 – 853
Beta strandi87 – 904
Beta strandi94 – 996
Helixi104 – 1085
Beta strandi116 – 1205
Beta strandi126 – 1283
Helixi130 – 1389
Beta strandi142 – 15110
Beta strandi156 – 1649
Beta strandi169 – 1768
Beta strandi178 – 1803
Beta strandi189 – 1946
Helixi199 – 2035
Beta strandi211 – 2155
Helixi225 – 2339
Beta strandi237 – 2459
Beta strandi312 – 3176
Beta strandi324 – 3296
Beta strandi336 – 3416
Helixi346 – 3505
Beta strandi357 – 3626
Helixi372 – 3809
Beta strandi384 – 3929
Helixi394 – 4018

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEFNMR-A62-154[»]
3I4WX-ray1.35A/B/C/D302-403[»]
3K82X-ray1.40A305-402[»]
3ZRTX-ray3.40A/B/C/D61-249[»]
ProteinModelPortaliP78352.
SMRiP78352. Positions 61-724.

Miscellaneous databases

EvolutionaryTraceiP78352.

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0194.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
KOiK11828.
OMAiWIPTRER.
PhylomeDBiP78352.
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.
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.
PF00018. SH3_1. 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: P78352-1) [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 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):80,495
Last modified:August 2, 2005 - v3
Checksum:i7922D3F220F9A101
GO
Isoform 2 (identifier: P78352-2) [UniParc]FASTAAdd to Basket

Also known as: PSD95-beta

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

Show »
Length:767
Mass (Da):85,430
Checksum:iBE1019159E65B2D8
GO
Isoform 3 (identifier: P78352-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:721
Mass (Da):80,125
Checksum:i608104D1BF7AE2C7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1010MDCLCIVTTK → MSQRPRAPRSALWLLAPPLL RWAPPLLTVLHSDLFQALLD ILDYYEASLSESQ in isoform 2. VSP_014929
Alternative sequencei51 – 533Missing in isoform 3. VSP_047247

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P78352-2)
Sequence conflicti46 – 461E → V in AAD56173. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83192 mRNA. Translation: AAC52113.1.
AF156495 Genomic DNA. Translation: AAD56173.1.
AK293835 mRNA. Translation: BAH11607.1.
AC120057 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90255.1.
U68138 mRNA. Translation: AAB07736.1. Sequence problems.
CCDSiCCDS45599.1. [P78352-2]
CCDS45600.1. [P78352-3]
PIRiT09599.
RefSeqiNP_001122299.1. NM_001128827.1. [P78352-3]
NP_001356.1. NM_001365.3. [P78352-2]
XP_005256549.1. XM_005256492.1. [P78352-1]
UniGeneiHs.463928.

Genome annotation databases

EnsembliENST00000302955; ENSP00000307471; ENSG00000132535. [P78352-3]
ENST00000399506; ENSP00000382425; ENSG00000132535. [P78352-1]
ENST00000399510; ENSP00000382428; ENSG00000132535. [P78352-2]
GeneIDi1742.
KEGGihsa:1742.
UCSCiuc002get.4. human. [P78352-2]
uc010cly.3. human.
uc010vtn.2. human. [P78352-1]

Polymorphism databases

DMDMi71658825.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83192 mRNA. Translation: AAC52113.1 .
AF156495 Genomic DNA. Translation: AAD56173.1 .
AK293835 mRNA. Translation: BAH11607.1 .
AC120057 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90255.1 .
U68138 mRNA. Translation: AAB07736.1 . Sequence problems.
CCDSi CCDS45599.1. [P78352-2 ]
CCDS45600.1. [P78352-3 ]
PIRi T09599.
RefSeqi NP_001122299.1. NM_001128827.1. [P78352-3 ]
NP_001356.1. NM_001365.3. [P78352-2 ]
XP_005256549.1. XM_005256492.1. [P78352-1 ]
UniGenei Hs.463928.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KEF NMR - A 62-154 [» ]
3I4W X-ray 1.35 A/B/C/D 302-403 [» ]
3K82 X-ray 1.40 A 305-402 [» ]
3ZRT X-ray 3.40 A/B/C/D 61-249 [» ]
ProteinModelPortali P78352.
SMRi P78352. Positions 61-724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108086. 86 interactions.
DIPi DIP-30919N.
IntActi P78352. 29 interactions.
MINTi MINT-199061.
STRINGi 9606.ENSP00000293813.

Chemistry

BindingDBi P78352.
ChEMBLi CHEMBL5666.

PTM databases

PhosphoSitei P78352.

Polymorphism databases

DMDMi 71658825.

Proteomic databases

MaxQBi P78352.
PaxDbi P78352.
PRIDEi P78352.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302955 ; ENSP00000307471 ; ENSG00000132535 . [P78352-3 ]
ENST00000399506 ; ENSP00000382425 ; ENSG00000132535 . [P78352-1 ]
ENST00000399510 ; ENSP00000382428 ; ENSG00000132535 . [P78352-2 ]
GeneIDi 1742.
KEGGi hsa:1742.
UCSCi uc002get.4. human. [P78352-2 ]
uc010cly.3. human.
uc010vtn.2. human. [P78352-1 ]

Organism-specific databases

CTDi 1742.
GeneCardsi GC17M007033.
HGNCi HGNC:2903. DLG4.
HPAi CAB001999.
CAB002000.
HPA010122.
MIMi 602887. gene.
neXtProti NX_P78352.
PharmGKBi PA27359.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0194.
HOGENOMi HOG000232102.
HOVERGENi HBG107814.
KOi K11828.
OMAi WIPTRER.
PhylomeDBi P78352.
TreeFami TF323171.

Enzyme and pathway databases

Reactomei REACT_18307. Trafficking of AMPA receptors.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_22329. NrCAM interactions.
SignaLinki P78352.

Miscellaneous databases

ChiTaRSi DLG4. human.
EvolutionaryTracei P78352.
GeneWikii DLG4.
GenomeRNAii 1742.
NextBioi 7067.
PROi P78352.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78352.
Bgeei P78352.
CleanExi HS_DLG4.
Genevestigatori P78352.

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.
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.
PF00018. SH3_1. 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. "Human postsynaptic density-95 (PSD95): location of the gene (DLG4) and possible function in nonneural as well as in neural tissues."
    Stathakis D.G., Hoover K.B., You Z., Bryant P.J.
    Genomics 44:71-82(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Mammary gland.
  2. Stathakis D.G., Hoover K.H., You Z., Bryant P.J.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Genomic organization of human DLG4, the gene encoding postsynaptic density 95."
    Stathakis D.G., Udar N., Sandgren O., Andreasson S., Bryant P.J., Small K., Forsman-Semb K.
    J. Neurochem. 73:2250-2265(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cerebellum.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Brenman J.E., Bredt D.S., Parkinson J.F., Manzana W.P., McClary J.A.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-398.
    Tissue: Brain.
  8. "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases."
    Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.
    Nature 378:85-88(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA1; KCNA2; KCNA3 AND KCNA4.
  9. Cited for: INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
  10. "GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes."
    Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H.
    J. Biol. Chem. 275:28774-28784(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIF13B.
  11. "The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses."
    Garcia R.A., Vasudevan K., Buonanno A.
    Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB4.
  12. "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, SUBCELLULAR LOCATION, INTERACTION WITH CASK AND HGS.
  13. "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; LRFN2 AND LRFN4.
  14. "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.
  15. Cited for: STRUCTURE BY NMR OF 105-197, INTERACTION WITH GRIK2; KCNA4 AND CRIPT.

Entry informationi

Entry nameiDLG4_HUMAN
AccessioniPrimary (citable) accession number: P78352
Secondary accession number(s): B7Z1S1
, G5E939, Q92941, Q9UKK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 2, 2005
Last modified: September 3, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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