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P78352

- DLG4_HUMAN

UniProt

P78352 - DLG4_HUMAN

Protein

Disks large homolog 4

Gene

DLG4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (02 Aug 2005)
      Previous versions | rss
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    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.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

    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 1 Publication; Peripheral membrane protein 1 Publication. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density 1 Publication. Cell junctionsynapse 1 Publication
    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.

    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

    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 cysteineBy similarity
    Lipidationi5 – 51S-palmitoyl cysteineBy similarity
    Modified residuei142 – 1421PhosphoserineBy similarity
    Modified residuei240 – 2401PhosphotyrosineBy similarity
    Modified residuei580 – 5801PhosphotyrosineBy similarity
    Modified residuei715 – 7151PhosphotyrosineBy 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.By similarity

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78352.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 15187PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 24687PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini313 – 39381PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini428 – 49871SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini534 – 709176Guanylate kinase-likePROSITE-ProRule annotationAdd
    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.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
    Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: P78352-2)
    Sequence conflicti46 – 461E → V in AAD56173. (PubMed:10582582)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1010MDCLCIVTTK → MSQRPRAPRSALWLLAPPLL RWAPPLLTVLHSDLFQALLD ILDYYEASLSESQ in isoform 2. 1 PublicationVSP_014929
    Alternative sequencei51 – 533Missing in isoform 3. CuratedVSP_047247

    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

    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: October 1, 2014
    This is version 167 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