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Q92796

- DLG3_HUMAN

UniProt

Q92796 - DLG3_HUMAN

Protein

Disks large homolog 3

Gene

DLG3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling.

    GO - Molecular functioni

    1. phosphatase binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. establishment of planar polarity Source: Ensembl
    3. establishment or maintenance of epithelial cell apical/basal polarity Source: Ensembl
    4. negative regulation of cell proliferation Source: UniProtKB
    5. negative regulation of phosphatase activity Source: UniProtKB
    6. synaptic transmission Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_21346. Activation of Ca-permeable Kainate Receptor.
    REACT_22329. NrCAM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disks large homolog 3
    Alternative name(s):
    Neuroendocrine-DLG
    Synapse-associated protein 102
    Short name:
    SAP-102
    Short name:
    SAP102
    XLMR
    Gene namesi
    Name:DLG3
    Synonyms:KIAA1232
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2902. DLG3.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. dendritic shaft Source: Ensembl
    4. extracellular space Source: UniProt
    5. growth cone Source: Ensembl
    6. neuronal cell body Source: Ensembl
    7. plasma membrane Source: Reactome
    8. synapse Source: Ensembl
    9. tight junction Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked 90 (MRX90) [MIM:300850]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi300850. phenotype.
    Orphaneti777. X-linked non-syndromic intellectual disability.
    PharmGKBiPA164741439.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 817817Disks large homolog 3PRO_0000094557Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei673 – 6731PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92796.
    PaxDbiQ92796.
    PRIDEiQ92796.

    PTM databases

    PhosphoSiteiQ92796.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92796.
    BgeeiQ92796.
    CleanExiHS_DLG3.
    GenevestigatoriQ92796.

    Organism-specific databases

    HPAiHPA001733.

    Interactioni

    Subunit structurei

    Interacts through its PDZ domains with NETO1, GRIN2B and SYNGAP1. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3 and DLGAP4 By similarity. Interacts through its PDZ domains with APC. Interacts through its first two PDZ domains with ERBB4. Interacts through its third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2 and LRFN4.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP1CAP621362EBI-80440,EBI-357253

    Protein-protein interaction databases

    BioGridi108085. 42 interactions.
    IntActiQ92796. 3 interactions.
    MINTiMINT-109320.
    STRINGi9606.ENSP00000363480.

    Structurei

    Secondary structure

    1
    817
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi127 – 1359
    Beta strandi142 – 1476
    Beta strandi160 – 1656
    Helixi170 – 1745
    Beta strandi182 – 1865
    Helixi196 – 20510
    Beta strandi208 – 21710
    Beta strandi224 – 2307
    Beta strandi238 – 2425
    Beta strandi255 – 2606
    Helixi265 – 2695
    Beta strandi277 – 2815
    Helixi291 – 2999
    Beta strandi303 – 3108
    Beta strandi383 – 3908
    Beta strandi396 – 3983
    Beta strandi416 – 4183
    Helixi419 – 4224
    Beta strandi431 – 4377
    Helixi445 – 4539
    Beta strandi457 – 4648
    Helixi467 – 4759

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UM7NMR-A382-475[»]
    2FE5X-ray1.10A223-314[»]
    2I1NX-ray1.85A/B126-222[»]
    ProteinModelPortaliQ92796.
    SMRiQ92796. Positions 61-314, 332-817.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92796.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini130 – 21788PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini226 – 31186PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini379 – 46587PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini503 – 56866SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini627 – 802176Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    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.
    KOiK12075.
    OMAiRASQRWA.
    PhylomeDBiQ92796.
    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. 1 hit.
    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. 2 hits.
    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: Q92796-1) [UniParc]FASTAAdd to Basket

    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

    MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PGGGNGASAG    50
    YGGYSSQTLP SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG 100
    SGPSWWPECT CTNRDWYEQV NGSDGMFKYE EIVLERGNSG LGFSIAGGID 150
    NPHVPDDPGI FITKIIPGGA AAMDGRLGVN DCVLRVNEVD VSEVVHSRAV 200
    EALKEAGPVV RLVVRRRQPP PETIMEVNLL KGPKGLGFSI AGGIGNQHIP 250
    GDNSIYITKI IEGGAAQKDG RLQIGDRLLA VNNTNLQDVR HEEAVASLKN 300
    TSDMVYLKVA KPGSLHLNDM YAPPDYASTF TALADNHISH NSSLGYLGAV 350
    ESKVSYPAPP QVPPTRYSPI PRHMLAEEDF TREPRKIILH KGSTGLGFNI 400
    VGGEDGEGIF VSFILAGGPA DLSGELRRGD RILSVNGVNL RNATHEQAAA 450
    ALKRAGQSVT IVAQYRPEEY SRFESKIHDL REQMMNSSMS SGSGSLRTSE 500
    KRSLYVRALF DYDRTRDSCL PSQGLSFSYG DILHVINASD DEWWQARLVT 550
    PHGESEQIGV IPSKKRVEKK ERARLKTVKF HARTGMIESN RDFPGLSDDY 600
    YGAKNLKGQE DAILSYEPVT RQEIHYARPV IILGPMKDRV NDDLISEFPH 650
    KFGSCVPHTT RPRRDNEVDG QDYHFVVSRE QMEKDIQDNK FIEAGQFNDN 700
    LYGTSIQSVR AVAERGKHCI LDVSGNAIKR LQQAQLYPIA IFIKPKSIEA 750
    LMEMNRRQTY EQANKIYDKA MKLEQEFGEY FTAIVQGDSL EEIYNKIKQI 800
    IEDQSGHYIW VPSPEKL 817
    Length:817
    Mass (Da):90,314
    Last modified:December 16, 2008 - v2
    Checksum:iCE125E9BEE3EEC66
    GO
    Isoform 2 (identifier: Q92796-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-336: Missing.
         337-381: HISHNSSLGY...RHMLAEEDFT → MERARKFSGS...LRSLRPGGDA
         592-606: DFPGLSDDYYGAKNL → SIKTKRKKSFRLSRKFPFYKSKENMAQESSIQEQGVTSNTSDSESSS

    Note: No experimental confirmation available.

    Show »
    Length:512
    Mass (Da):57,937
    Checksum:i9330A330FF9F8FE5
    GO
    Isoform 3 (identifier: Q92796-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-483: Missing.
         592-606: DFPGLSDDYYGAKNL → SIKTKRKKSFRLSRKFPFYKSKENMAQESSIQEQGVTSNTSDSESSS

    Note: No experimental confirmation available.

    Show »
    Length:366
    Mass (Da):42,112
    Checksum:i91BEFB73D3CA7C8D
    GO

    Sequence cautioni

    The sequence BAA86546.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871P → L in AAB61453. (PubMed:9188857)Curated
    Sequence conflicti190 – 1901D → E in AAB61453. (PubMed:9188857)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401G → R in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036591

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 483483Missing in isoform 3. 1 PublicationVSP_043717Add
    BLAST
    Alternative sequencei1 – 336336Missing in isoform 2. 2 PublicationsVSP_035940Add
    BLAST
    Alternative sequencei337 – 38145HISHN…EEDFT → MERARKFSGSGLAMGLGSAS ASAWRRASQRWAWPLRSLRP GGDA in isoform 2. 2 PublicationsVSP_035941Add
    BLAST
    Alternative sequencei592 – 60615DFPGL…GAKNL → SIKTKRKKSFRLSRKFPFYK SKENMAQESSIQEQGVTSNT SDSESSS in isoform 2 and isoform 3. 2 PublicationsVSP_035942Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49089 mRNA. Translation: AAB61453.1.
    AB033058 mRNA. Translation: BAA86546.1. Different initiation.
    AK303377 mRNA. Translation: BAG64433.1.
    AK304020 mRNA. Translation: BAG64935.1.
    AK316518 mRNA. Translation: BAH14889.1.
    AL139109 Genomic DNA. No translation available.
    AL139398 Genomic DNA. Translation: CAI41022.1.
    AL139398 Genomic DNA. Translation: CAI41023.1.
    CH471132 Genomic DNA. Translation: EAX05333.1.
    CH471132 Genomic DNA. Translation: EAX05335.1.
    CH471132 Genomic DNA. Translation: EAX05337.1.
    CH471132 Genomic DNA. Translation: EAX05338.1.
    BC093864 mRNA. Translation: AAH93864.1.
    BC093866 mRNA. Translation: AAH93866.1.
    CCDSiCCDS14403.1. [Q92796-1]
    CCDS43967.1. [Q92796-2]
    CCDS55439.1. [Q92796-3]
    RefSeqiNP_001159750.1. NM_001166278.1. [Q92796-3]
    NP_065781.1. NM_020730.2. [Q92796-2]
    NP_066943.2. NM_021120.3. [Q92796-1]
    XP_005262305.1. XM_005262248.1. [Q92796-3]
    UniGeneiHs.721586.

    Genome annotation databases

    EnsembliENST00000374355; ENSP00000363475; ENSG00000082458. [Q92796-2]
    ENST00000374360; ENSP00000363480; ENSG00000082458. [Q92796-1]
    ENST00000542398; ENSP00000441393; ENSG00000082458. [Q92796-3]
    GeneIDi1741.
    KEGGihsa:1741.
    UCSCiuc004dyi.2. human. [Q92796-1]
    uc004dyj.2. human. [Q92796-2]
    uc011mpn.2. human. [Q92796-3]

    Polymorphism databases

    DMDMi218512007.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49089 mRNA. Translation: AAB61453.1 .
    AB033058 mRNA. Translation: BAA86546.1 . Different initiation.
    AK303377 mRNA. Translation: BAG64433.1 .
    AK304020 mRNA. Translation: BAG64935.1 .
    AK316518 mRNA. Translation: BAH14889.1 .
    AL139109 Genomic DNA. No translation available.
    AL139398 Genomic DNA. Translation: CAI41022.1 .
    AL139398 Genomic DNA. Translation: CAI41023.1 .
    CH471132 Genomic DNA. Translation: EAX05333.1 .
    CH471132 Genomic DNA. Translation: EAX05335.1 .
    CH471132 Genomic DNA. Translation: EAX05337.1 .
    CH471132 Genomic DNA. Translation: EAX05338.1 .
    BC093864 mRNA. Translation: AAH93864.1 .
    BC093866 mRNA. Translation: AAH93866.1 .
    CCDSi CCDS14403.1. [Q92796-1 ]
    CCDS43967.1. [Q92796-2 ]
    CCDS55439.1. [Q92796-3 ]
    RefSeqi NP_001159750.1. NM_001166278.1. [Q92796-3 ]
    NP_065781.1. NM_020730.2. [Q92796-2 ]
    NP_066943.2. NM_021120.3. [Q92796-1 ]
    XP_005262305.1. XM_005262248.1. [Q92796-3 ]
    UniGenei Hs.721586.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UM7 NMR - A 382-475 [» ]
    2FE5 X-ray 1.10 A 223-314 [» ]
    2I1N X-ray 1.85 A/B 126-222 [» ]
    ProteinModelPortali Q92796.
    SMRi Q92796. Positions 61-314, 332-817.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108085. 42 interactions.
    IntActi Q92796. 3 interactions.
    MINTi MINT-109320.
    STRINGi 9606.ENSP00000363480.

    PTM databases

    PhosphoSitei Q92796.

    Polymorphism databases

    DMDMi 218512007.

    Proteomic databases

    MaxQBi Q92796.
    PaxDbi Q92796.
    PRIDEi Q92796.

    Protocols and materials databases

    DNASUi 1741.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374355 ; ENSP00000363475 ; ENSG00000082458 . [Q92796-2 ]
    ENST00000374360 ; ENSP00000363480 ; ENSG00000082458 . [Q92796-1 ]
    ENST00000542398 ; ENSP00000441393 ; ENSG00000082458 . [Q92796-3 ]
    GeneIDi 1741.
    KEGGi hsa:1741.
    UCSCi uc004dyi.2. human. [Q92796-1 ]
    uc004dyj.2. human. [Q92796-2 ]
    uc011mpn.2. human. [Q92796-3 ]

    Organism-specific databases

    CTDi 1741.
    GeneCardsi GC0XP069664.
    H-InvDB HIX0016853.
    HGNCi HGNC:2902. DLG3.
    HPAi HPA001733.
    MIMi 300189. gene.
    300850. phenotype.
    neXtProti NX_Q92796.
    Orphaneti 777. X-linked non-syndromic intellectual disability.
    PharmGKBi PA164741439.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0194.
    HOGENOMi HOG000232102.
    HOVERGENi HBG107814.
    KOi K12075.
    OMAi RASQRWA.
    PhylomeDBi Q92796.
    TreeFami TF323171.

    Enzyme and pathway databases

    Reactomei REACT_21346. Activation of Ca-permeable Kainate Receptor.
    REACT_22329. NrCAM interactions.

    Miscellaneous databases

    ChiTaRSi DLG3. human.
    EvolutionaryTracei Q92796.
    GenomeRNAii 1741.
    NextBioi 7061.
    PROi Q92796.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92796.
    Bgeei Q92796.
    CleanExi HS_DLG3.
    Genevestigatori Q92796.

    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. 1 hit.
    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. 2 hits.
    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. "Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein."
      Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T., Sasaki J., Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H.
      Oncogene 14:2425-2433(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APC.
      Tissue: Fetal brain.
    2. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "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] (ISOFORMS 2 AND 3).
      Tissue: Thymus and Trachea.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. Cited for: INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
    8. "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.
    9. Cited for: INVOLVEMENT IN MRX90.
    10. "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.
    11. "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.
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of the third PDZ domain of synapse-associated protein 102."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAR-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 382-475.
    15. "The crystal structure of the second PDZ domain of human DLG3."
      Structural genomics consortium (SGC)
      Submitted (DEC-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 223-314.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-40.

    Entry informationi

    Entry nameiDLG3_HUMAN
    AccessioniPrimary (citable) accession number: Q92796
    Secondary accession number(s): B4E0H1
    , D3DVU5, Q5JUW6, Q5JUW7, Q9ULI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 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 X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3