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P78352 (DLG4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:PSD95
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity.

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.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

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.12

Tissue specificity

Brain.

Domain

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.

Post-translational modification

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

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
Reference proteome
Gene Ontology (GO)
   Biological_processadenosine receptor signaling pathway

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

alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering

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

axon guidance

Traceable author statement. Source: Reactome

dendritic spine morphogenesis

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

establishment of protein localization

Inferred from direct assay PubMed 15496675. Source: BHF-UCL

learning

Traceable author statement PubMed 9853749. Source: ProtInc

negative regulation of receptor internalization

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

nervous system development

Traceable author statement Ref.1. Source: ProtInc

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

positive regulation of transcription from RNA polymerase II promoter

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

protein complex assembly

Inferred from direct assay PubMed 15496675. Source: BHF-UCL

protein localization to synapse

Inferred from direct assay PubMed 15496675. 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 long-term neuronal synaptic plasticity

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

signal transduction

Traceable author statement PubMed 10364559. Source: ProtInc

synaptic transmission

Traceable author statement. Source: Reactome

synaptic vesicle maturation

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

cortical cytoskeleton

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

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

dendrite cytoplasm

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

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum

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

excitatory synapse

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

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 sequence or structural similarity. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from direct assay Ref.12. Source: UniProtKB

synapse

Inferred from direct assay PubMed 15496675. Source: BHF-UCL

synaptic vesicle

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

   Molecular_functionADP-activated nucleotide receptor activity

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

ATP-activated nucleotide receptor activity

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

D1 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 sequence or structural similarity. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction Ref.8. 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 sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78352-1)

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: P78352-2)

Also known as: PSD95-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MDCLCIVTTK → MSQRPRAPRSALWLLAPPLLRWAPPLLTVLHSDLFQALLDILDYYEASLSESQ
Isoform 3 (identifier: P78352-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Disks large homolog 4
PRO_0000094560

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 By similarity
Lipidation51S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence1 – 1010MDCLCIVTTK → MSQRPRAPRSALWLLAPPLL RWAPPLLTVLHSDLFQALLD ILDYYEASLSESQ in isoform 2.
VSP_014929
Alternative sequence51 – 533Missing in isoform 3.
VSP_047247

Experimental info

Isoform 2:
Sequence conflict461E → V in AAD56173. Ref.3

Secondary structure

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

Details...

Sequences

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

Last modified August 2, 2005. Version 3.
Checksum: 7922D3F220F9A101

FASTA72480,495
        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 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: BE1019159E65B2D8
Show »

FASTA76785,430
Isoform 3 [UniParc].

Checksum: 608104D1BF7AE2C7
Show »

FASTA72180,125

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Binding of neuroligins to PSD-95."
Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K., Takai Y., Rosahl T.W., Suedhof T.C.
Science 277:1511-1515(1997) [PubMed] [Europe PMC] [Abstract]
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]"The PDZ1 domain of SAP90. Characterization of structure and binding."
Piserchio A., Pellegrini M., Mehta S., Blackman S.M., Garcia E.P., Marshall J., Mierke D.F.
J. Biol. Chem. 277:6967-6973(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 105-197, INTERACTION WITH GRIK2; KCNA4 AND CRIPT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT09599.
RefSeqNP_001122299.1. NM_001128827.1.
NP_001356.1. NM_001365.3.
XP_005256549.1. XM_005256492.1.
UniGeneHs.463928.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEFNMR-A62-154[»]
3I4WX-ray1.35A/B/C/D302-403[»]
3K82X-ray1.40A305-402[»]
3ZRTX-ray3.40A/B/C/D61-249[»]
ProteinModelPortalP78352.
SMRP78352. Positions 61-724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108086. 86 interactions.
DIPDIP-30919N.
IntActP78352. 29 interactions.
MINTMINT-199061.
STRING9606.ENSP00000293813.

Chemistry

BindingDBP78352.
ChEMBLCHEMBL5666.

PTM databases

PhosphoSiteP78352.

Polymorphism databases

DMDM71658825.

Proteomic databases

PaxDbP78352.
PRIDEP78352.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302955; ENSP00000307471; ENSG00000132535. [P78352-3]
ENST00000399506; ENSP00000382425; ENSG00000132535. [P78352-1]
ENST00000399510; ENSP00000382428; ENSG00000132535. [P78352-2]
GeneID1742.
KEGGhsa:1742.
UCSCuc002get.4. human. [P78352-2]
uc010vtn.2. human. [P78352-1]

Organism-specific databases

CTD1742.
GeneCardsGC17M007033.
HGNCHGNC:2903. DLG4.
HPACAB001999.
CAB002000.
HPA010122.
MIM602887. gene.
neXtProtNX_P78352.
PharmGKBPA27359.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000232102.
HOVERGENHBG107814.
KOK11828.
PhylomeDBP78352.
TreeFamTF323171.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_13685. Neuronal System.
SignaLinkP78352.

Gene expression databases

ArrayExpressP78352.
BgeeP78352.
CleanExHS_DLG4.
GenevestigatorP78352.

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.
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.
PF00018. SH3_1. 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. human.
EvolutionaryTraceP78352.
GeneWikiDLG4.
GenomeRNAi1742.
NextBio7067.
PROP78352.
SOURCESearch...

Entry information

Entry nameDLG4_HUMAN
AccessionPrimary (citable) accession number: P78352
Secondary accession number(s): B7Z1S1 expand/collapse secondary AC list , G5E939, Q92941, Q9UKK8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 2, 2005
Last modified: April 16, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM