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Q12959

- DLG1_HUMAN

UniProt

Q12959 - DLG1_HUMAN

Protein

Disks large homolog 1

Gene

DLG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Essential multidomain scaffolding protein required for normal development By similarity. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel.By similarity6 Publications

    GO - Molecular functioni

    1. cytoskeletal protein binding Source: ProtInc
    2. guanylate kinase activity Source: ProtInc
    3. ion channel binding Source: BHF-UCL
    4. L27 domain binding Source: BHF-UCL
    5. mitogen-activated protein kinase kinase binding Source: UniProtKB
    6. phosphatase binding Source: UniProtKB
    7. phosphoprotein phosphatase activity Source: UniProtKB
    8. potassium channel regulator activity Source: UniProtKB
    9. protein binding Source: IntAct
    10. protein C-terminus binding Source: UniProtKB
    11. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: UniProtKB
    2. activation of protein kinase activity Source: Ensembl
    3. amyloid precursor protein metabolic process Source: Ensembl
    4. axon guidance Source: Reactome
    5. branching involved in ureteric bud morphogenesis Source: Ensembl
    6. cortical actin cytoskeleton organization Source: UniProtKB
    7. dephosphorylation Source: GOC
    8. embryonic skeletal system morphogenesis Source: Ensembl
    9. endothelial cell proliferation Source: UniProtKB
    10. establishment or maintenance of cell polarity Source: UniProtKB
    11. hard palate development Source: Ensembl
    12. immunological synapse formation Source: Ensembl
    13. lens development in camera-type eye Source: Ensembl
    14. membrane raft organization Source: Ensembl
    15. mitotic cell cycle checkpoint Source: UniProtKB
    16. negative regulation of epithelial cell proliferation Source: Ensembl
    17. negative regulation of mitotic cell cycle Source: UniProtKB
    18. negative regulation of T cell proliferation Source: Ensembl
    19. nucleotide phosphorylation Source: GOC
    20. peristalsis Source: Ensembl
    21. positive regulation of actin filament polymerization Source: Ensembl
    22. positive regulation of cell proliferation Source: Ensembl
    23. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    24. positive regulation of potassium ion transport Source: BHF-UCL
    25. protein localization to plasma membrane Source: BHF-UCL
    26. regulation of membrane potential Source: BHF-UCL
    27. regulation of sodium ion transmembrane transport Source: BHF-UCL
    28. reproductive structure development Source: Ensembl
    29. single organismal cell-cell adhesion Source: UniProtKB
    30. smooth muscle tissue development Source: Ensembl
    31. synaptic transmission Source: Reactome
    32. T cell activation Source: Ensembl
    33. T cell cytokine production Source: Ensembl
    34. tight junction assembly Source: BHF-UCL
    35. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_18307. Trafficking of AMPA receptors.
    REACT_21346. Activation of Ca-permeable Kainate Receptor.
    REACT_22329. NrCAM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disks large homolog 1
    Alternative name(s):
    Synapse-associated protein 97
    Short name:
    SAP-97
    Short name:
    SAP97
    hDlg
    Gene namesi
    Name:DLG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2900. DLG1.

    Subcellular locationi

    Membrane By similarity; Peripheral membrane protein By similarity. Basolateral cell membrane By similarity. Endoplasmic reticulum membrane By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapse. Cell membranesarcolemma
    Note: Colocalizes with EPB41 at regions of intercellular contacts. Basolateral in epithelial cells. May also associate with endoplasmic reticulum membranes. Mainly found in neurons soma, moderately found at postsynaptic densities By similarity.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB
    2. cell-cell junction Source: UniProtKB
    3. cell junction Source: UniProtKB
    4. cell projection membrane Source: Ensembl
    5. cytoplasm Source: UniProtKB
    6. cytoplasmic side of plasma membrane Source: UniProtKB
    7. cytosol Source: Reactome
    8. endoplasmic reticulum Source: UniProtKB
    9. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    10. extracellular vesicular exosome Source: UniProt
    11. Golgi apparatus Source: UniProtKB
    12. immunological synapse Source: BHF-UCL
    13. intercalated disc Source: BHF-UCL
    14. lateral loop Source: Ensembl
    15. lateral plasma membrane Source: Ensembl
    16. membrane raft Source: Ensembl
    17. microtubule Source: UniProtKB
    18. MPP7-DLG1-LIN7 complex Source: BHF-UCL
    19. myelin sheath abaxonal region Source: Ensembl
    20. neuromuscular junction Source: Ensembl
    21. node of Ranvier Source: Ensembl
    22. nucleus Source: BHF-UCL
    23. perinuclear region of cytoplasm Source: UniProtKB
    24. plasma membrane Source: Reactome
    25. postsynaptic density Source: UniProtKB-SubCell
    26. postsynaptic membrane Source: UniProtKB-KW
    27. sarcolemma Source: UniProtKB-SubCell
    28. tight junction Source: BHF-UCL

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 403INI → ANA: Loss of membrane association and DLG2-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA27356.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 904904Disks large homolog 1PRO_0000094548Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151Phosphothreonine2 Publications
    Modified residuei122 – 1221Phosphoserine2 Publications
    Modified residuei158 – 1581Phosphoserine2 Publications
    Modified residuei232 – 2321PhosphoserineBy similarity
    Modified residuei399 – 3991PhosphotyrosineBy similarity
    Modified residuei568 – 5681Phosphoserine2 Publications
    Modified residuei575 – 5751Phosphoserine4 Publications
    Modified residuei619 – 6191Phosphoserine2 Publications
    Modified residuei684 – 6841Phosphoserine2 Publications
    Modified residuei687 – 6871Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by MAPK12. Phosphorylation of Ser-232 regulates association with GRIN2A By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12959.
    PaxDbiQ12959.
    PRIDEiQ12959.

    PTM databases

    PhosphoSiteiQ12959.

    Miscellaneous databases

    PMAP-CutDBA5YKK7.

    Expressioni

    Tissue specificityi

    Abundantly expressed in atrial myocardium (at protein level). Expressed in lung fibroblasts, cervical epithelial and B-cells (at protein level). Widely expressed, with isoforms displaying different expression profiles.3 Publications

    Gene expression databases

    ArrayExpressiQ12959.
    BgeeiQ12959.
    CleanExiHS_DLG1.
    GenevestigatoriQ12959.

    Organism-specific databases

    HPAiCAB016307.

    Interactioni

    Subunit structurei

    Homotetramer Probable. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A. May interact with HTR2A By similarity. Interacts with LRFN1 By similarity. Interacts through its PDZ domains with GRIN2A, KCNA1, KCNA2, KCNA3, KCNA4, KCNA5, KCND2, KCND3, GRIA1, GPR124 and GPR125. Interacts with KCNF1. Interacts with CAMK2 By similarity. Interacts with cytoskeleton-associated proteins EPB41 and EZR. Found in a complex with KCNA5 and CAV3. Found in a complex with APC and CTNNB1. Interacts with CDH1 through binding to PIK3R1. Forms multiprotein complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12. Interacts through its guanylate kinase-like domain with KIF13B. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with TJAP1. Interacts with TOPK and the HTLV-1 viral Tax and HPV-18 E6 papillomavirus (HPV) oncoproteins. Interacts with PTEN By similarity. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2, LRFN4 and SFPQ.By similarity19 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAM17P785367EBI-357481,EBI-78188
    BTRCQ9Y2972EBI-357481,EBI-307461
    Dlg4P310169EBI-357500,EBI-375655From a different organism.
    E6O571252EBI-357481,EBI-7461590From a different organism.
    E6P031262EBI-357481,EBI-1177242From a different organism.
    E6P064633EBI-357481,EBI-1186926From a different organism.
    E6P367992EBI-357481,EBI-7363822From a different organism.
    KIF13BQ9NQT83EBI-357500,EBI-766408
    KIF1BO60333-34EBI-357481,EBI-465669
    MAP2K2P3650710EBI-357481,EBI-1056930
    se6Q9ICL13EBI-357481,EBI-7461477From a different organism.

    Protein-protein interaction databases

    BioGridi108083. 45 interactions.
    IntActiQ12959. 32 interactions.
    MINTiMINT-107690.
    STRINGi9606.ENSP00000345731.

    Structurei

    Secondary structure

    1
    904
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 2016
    Beta strandi24 – 263
    Helixi30 – 4213
    Helixi44 – 5512
    Turni60 – 623
    Beta strandi221 – 2288
    Beta strandi233 – 2397
    Beta strandi254 – 2585
    Helixi263 – 2675
    Beta strandi275 – 2795
    Helixi289 – 29810
    Beta strandi301 – 3099
    Beta strandi317 – 3237
    Beta strandi331 – 3377
    Beta strandi348 – 3536
    Helixi358 – 3625
    Beta strandi370 – 3745
    Beta strandi377 – 3826
    Helixi384 – 3929
    Beta strandi396 – 4038
    Beta strandi465 – 4706
    Beta strandi472 – 4743
    Beta strandi477 – 4826
    Beta strandi484 – 4874
    Beta strandi489 – 4946
    Helixi499 – 5035
    Beta strandi510 – 5156
    Helixi525 – 5339
    Beta strandi537 – 5459
    Helixi547 – 5548
    Beta strandi717 – 7215
    Helixi724 – 73411
    Turni736 – 7383
    Turni756 – 7583
    Helixi766 – 7749
    Beta strandi778 – 7847
    Beta strandi787 – 7926
    Helixi793 – 8008
    Turni801 – 8033
    Beta strandi805 – 8084
    Helixi813 – 8208
    Beta strandi826 – 8305
    Helixi855 – 86410
    Helixi865 – 8673
    Beta strandi869 – 8724
    Helixi877 – 89216
    Helixi900 – 9023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PDRX-ray2.80A457-555[»]
    2M3MNMR-A318-406[»]
    2OQSNMR-A318-406[»]
    2X7ZX-ray2.00A311-407[»]
    3LRAX-ray2.95A2-65[»]
    3RL7X-ray2.30A/B/C/D/E/F220-317[»]
    3RL8X-ray2.20A/B/C/D/E315-410[»]
    3W9YX-ray2.20A712-904[»]
    4AMHX-ray2.30A/B315-405[»]
    4G69X-ray2.00A310-407[»]
    ProteinModelPortaliQ12959.
    SMRiQ12959. Positions 2-65, 220-904.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12959.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 6461L27PROSITE-ProRule annotationAdd
    BLAST
    Domaini224 – 31087PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini319 – 40587PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini466 – 54681PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini581 – 65171SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini714 – 889176Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni162 – 21251Interaction with SH3 domainsAdd
    BLAST

    Domaini

    The alternatively spliced domain I3 corresponding to amino acids (636-669) of isoform 4 is an EPB41 binding site mediating association to membranes in polarized and non-polarized cells.
    The PDZ domains may also mediate association to membranes by binding to EPB41 and GPR124 together with the L27 domain that binds CASK and DLG2.
    The L27 domain may regulate DLG1 self-association. The N-terminal alternatively spliced region is capable of binding several SH3 domains and also moderates the level of protein oligomerization.

    Sequence similaritiesi

    Belongs to the MAGUK family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
    Contains 1 L27 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.
    HOVERGENiHBG107814.
    KOiK12076.
    OMAiDNENITT.
    OrthoDBiEOG79GT6P.
    PhylomeDBiQ12959.
    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.
    IPR004172. L27.
    IPR015143. L27_1.
    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.
    PF09058. L27_1. 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.
    SM00569. L27. 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.
    PS51022. L27. 1 hit.
    PS50106. PDZ. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12959-1) [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

    MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI    50
    DIQEFYEVTL LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS 100
    LSPSVEKYRY QDEDTPPQEH ISPQITNEVI GPELVHVSEK NLSEIENVHG 150
    FVSHSHISPI KPTEAVLPSP PTVPVIPVLP VPAENTVILP TIPQANPPPV 200
    LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG GTDNPHIGDD 250
    SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 300
    SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV 350
    TKIIEGGAAH KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL 400
    KVAKPTSMYM NDGYAPPDIT NSSSQPVDNH VSPSSFLGQT PASPARYSPV 450
    SKAVLGDDEI TREPRKVVLH RGSTGLGFNI VGGEDGEGIF ISFILAGGPA 500
    DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT IVAQYRPEEY 550
    SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 600
    PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK 650
    ERARLKTVKF NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYRGQEEYV 700
    LSYEPVNQQE VNYTRPVIIL GPMKDRINDD LISEFPDKFG SCVPHTTRPK 750
    RDYEVDGRDY HFVTSREQME KDIQEHKFIE AGQYNNHLYG TSVQSVREVA 800
    EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME MNKRLTEEQA 850
    RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGSYIWVPA 900
    KEKL 904
    Length:904
    Mass (Da):100,455
    Last modified:February 10, 2009 - v2
    Checksum:i6722993A84D0F761
    GO
    Isoform 2 (identifier: Q12959-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         669-680: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ

    Show »
    Length:926
    Mass (Da):103,321
    Checksum:i85BD4E93A17D74C4
    GO
    Isoform 3 (identifier: Q12959-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-194: Missing.

    Show »
    Length:871
    Mass (Da):97,076
    Checksum:i78CB64FC6DE66BB1
    GO
    Isoform 4 (identifier: Q12959-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-194: Missing.
         669-680: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ

    Show »
    Length:893
    Mass (Da):99,942
    Checksum:i3A026E9BAA62FFB7
    GO
    Isoform 5 (identifier: Q12959-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-194: Missing.
         195-212: Missing.

    Show »
    Length:853
    Mass (Da):95,166
    Checksum:i2E7EE3F5954BA3E0
    GO
    Isoform 6 (identifier: Q12959-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         681-693: Missing.

    Show »
    Length:891
    Mass (Da):99,090
    Checksum:i5DB5256100623D0B
    GO
    Isoform 7 (identifier: Q12959-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         693-693: Y → YLILITDEYGCSKG

    Show »
    Length:917
    Mass (Da):101,849
    Checksum:iFE8911BB05B03211
    GO
    Isoform 8 (identifier: Q12959-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: MPVRKQDTQR...DRSKPSEPIQ → MNYIFGNNTL...DCISVATSST
         78-193: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:788
    Mass (Da):87,248
    Checksum:i8EB77B3368768FBD
    GO
    Isoform 9 (identifier: Q12959-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: MPVRKQDTQR...DRSKPSEPIQ → MNYIFGNNTL...DCISVATSST
         78-193: Missing.
         693-693: Y → YLILITDEYGCSKG
         694-694: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:800
    Mass (Da):88,485
    Checksum:iC67306E88A5A473D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371S → N in BAG57902. (PubMed:14702039)Curated
    Sequence conflicti801 – 8011E → G in AAA50598. (PubMed:7937897)Curated
    Sequence conflicti801 – 8011E → G in AAA50599. (PubMed:7937897)Curated
    Isoform 4 (identifier: Q12959-4)
    Sequence conflicti636 – 6361Missing in AAI44652. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401K → R.
    Corresponds to variant rs1802668 [ dbSNP | Ensembl ].
    VAR_054334
    Natural varianti278 – 2781R → Q.2 Publications
    Corresponds to variant rs1134986 [ dbSNP | Ensembl ].
    VAR_054335
    Natural varianti899 – 8991P → L.
    Corresponds to variant rs34492126 [ dbSNP | Ensembl ].
    VAR_054336

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7777MPVRK…SEPIQ → MNYIFGNNTLLYSRGSRGGN TSSSHGSAGPKQKHWAKKGS SDELQAEPEPSRWQQIVAFF TRRHSFIDCISVATSST in isoform 8 and isoform 9. 1 PublicationVSP_045896Add
    BLAST
    Alternative sequencei78 – 193116Missing in isoform 8 and isoform 9. 1 PublicationVSP_045897Add
    BLAST
    Alternative sequencei162 – 19433Missing in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_012862Add
    BLAST
    Alternative sequencei195 – 21218Missing in isoform 5. CuratedVSP_012863Add
    BLAST
    Alternative sequencei669 – 68012EIPDD…SKGLK → QSFNDKRKKNLFSRKFPFYK NKDQSEQETSDADQ in isoform 2 and isoform 4. 2 PublicationsVSP_003150Add
    BLAST
    Alternative sequencei681 – 69313Missing in isoform 6. CuratedVSP_012864Add
    BLAST
    Alternative sequencei693 – 6931Y → YLILITDEYGCSKG in isoform 7 and isoform 9. 1 PublicationVSP_012865
    Alternative sequencei694 – 6941Missing in isoform 9. 1 PublicationVSP_045898

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13896 mRNA. Translation: AAA50598.1.
    U13897 mRNA. Translation: AAA50599.1.
    AK294772 mRNA. Translation: BAG57902.1.
    AK294855 mRNA. Translation: BAG57959.1.
    EF553524 mRNA. Translation: ABQ66269.1.
    AC068302 Genomic DNA. No translation available.
    AC092937 Genomic DNA. No translation available.
    CH471191 Genomic DNA. Translation: EAW53610.1.
    CH471191 Genomic DNA. Translation: EAW53611.1.
    CH471191 Genomic DNA. Translation: EAW53612.1.
    CH471191 Genomic DNA. Translation: EAW53614.1.
    BC140841 mRNA. Translation: AAI40842.1.
    BC144651 mRNA. Translation: AAI44652.1.
    CCDSiCCDS3327.1. [Q12959-2]
    CCDS43194.1. [Q12959-1]
    CCDS56300.1. [Q12959-8]
    CCDS56301.1. [Q12959-9]
    PIRiI38756.
    I38757.
    RefSeqiNP_001091894.1. NM_001098424.1. [Q12959-1]
    NP_001191315.1. NM_001204386.1.
    NP_001191316.1. NM_001204387.1. [Q12959-9]
    NP_001191317.1. NM_001204388.1. [Q12959-8]
    NP_001277912.1. NM_001290983.1. [Q12959-1]
    NP_004078.2. NM_004087.2. [Q12959-2]
    XP_005269346.1. XM_005269289.1. [Q12959-2]
    XP_005269347.1. XM_005269290.2. [Q12959-2]
    XP_005269348.1. XM_005269291.1. [Q12959-2]
    XP_005269349.1. XM_005269292.1. [Q12959-2]
    XP_005269355.1. XM_005269298.1. [Q12959-3]
    XP_005269356.1. XM_005269299.1. [Q12959-5]
    UniGeneiHs.292549.

    Genome annotation databases

    EnsembliENST00000346964; ENSP00000345731; ENSG00000075711. [Q12959-2]
    ENST00000357674; ENSP00000350303; ENSG00000075711. [Q12959-4]
    ENST00000392382; ENSP00000376187; ENSG00000075711. [Q12959-3]
    ENST00000419354; ENSP00000407531; ENSG00000075711. [Q12959-1]
    ENST00000422288; ENSP00000413238; ENSG00000075711. [Q12959-5]
    ENST00000443183; ENSP00000396658; ENSG00000075711. [Q12959-9]
    ENST00000448528; ENSP00000391732; ENSG00000075711. [Q12959-1]
    ENST00000450955; ENSP00000411278; ENSG00000075711. [Q12959-4]
    ENST00000452595; ENSP00000398939; ENSG00000075711. [Q12959-8]
    GeneIDi1739.
    KEGGihsa:1739.
    UCSCiuc003fxn.4. human. [Q12959-2]
    uc003fxo.4. human. [Q12959-1]
    uc010iam.1. human. [Q12959-3]
    uc011bue.2. human. [Q12959-4]

    Polymorphism databases

    DMDMi223590196.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13896 mRNA. Translation: AAA50598.1 .
    U13897 mRNA. Translation: AAA50599.1 .
    AK294772 mRNA. Translation: BAG57902.1 .
    AK294855 mRNA. Translation: BAG57959.1 .
    EF553524 mRNA. Translation: ABQ66269.1 .
    AC068302 Genomic DNA. No translation available.
    AC092937 Genomic DNA. No translation available.
    CH471191 Genomic DNA. Translation: EAW53610.1 .
    CH471191 Genomic DNA. Translation: EAW53611.1 .
    CH471191 Genomic DNA. Translation: EAW53612.1 .
    CH471191 Genomic DNA. Translation: EAW53614.1 .
    BC140841 mRNA. Translation: AAI40842.1 .
    BC144651 mRNA. Translation: AAI44652.1 .
    CCDSi CCDS3327.1. [Q12959-2 ]
    CCDS43194.1. [Q12959-1 ]
    CCDS56300.1. [Q12959-8 ]
    CCDS56301.1. [Q12959-9 ]
    PIRi I38756.
    I38757.
    RefSeqi NP_001091894.1. NM_001098424.1. [Q12959-1 ]
    NP_001191315.1. NM_001204386.1.
    NP_001191316.1. NM_001204387.1. [Q12959-9 ]
    NP_001191317.1. NM_001204388.1. [Q12959-8 ]
    NP_001277912.1. NM_001290983.1. [Q12959-1 ]
    NP_004078.2. NM_004087.2. [Q12959-2 ]
    XP_005269346.1. XM_005269289.1. [Q12959-2 ]
    XP_005269347.1. XM_005269290.2. [Q12959-2 ]
    XP_005269348.1. XM_005269291.1. [Q12959-2 ]
    XP_005269349.1. XM_005269292.1. [Q12959-2 ]
    XP_005269355.1. XM_005269298.1. [Q12959-3 ]
    XP_005269356.1. XM_005269299.1. [Q12959-5 ]
    UniGenei Hs.292549.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PDR X-ray 2.80 A 457-555 [» ]
    2M3M NMR - A 318-406 [» ]
    2OQS NMR - A 318-406 [» ]
    2X7Z X-ray 2.00 A 311-407 [» ]
    3LRA X-ray 2.95 A 2-65 [» ]
    3RL7 X-ray 2.30 A/B/C/D/E/F 220-317 [» ]
    3RL8 X-ray 2.20 A/B/C/D/E 315-410 [» ]
    3W9Y X-ray 2.20 A 712-904 [» ]
    4AMH X-ray 2.30 A/B 315-405 [» ]
    4G69 X-ray 2.00 A 310-407 [» ]
    ProteinModelPortali Q12959.
    SMRi Q12959. Positions 2-65, 220-904.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108083. 45 interactions.
    IntActi Q12959. 32 interactions.
    MINTi MINT-107690.
    STRINGi 9606.ENSP00000345731.

    PTM databases

    PhosphoSitei Q12959.

    Polymorphism databases

    DMDMi 223590196.

    Proteomic databases

    MaxQBi Q12959.
    PaxDbi Q12959.
    PRIDEi Q12959.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346964 ; ENSP00000345731 ; ENSG00000075711 . [Q12959-2 ]
    ENST00000357674 ; ENSP00000350303 ; ENSG00000075711 . [Q12959-4 ]
    ENST00000392382 ; ENSP00000376187 ; ENSG00000075711 . [Q12959-3 ]
    ENST00000419354 ; ENSP00000407531 ; ENSG00000075711 . [Q12959-1 ]
    ENST00000422288 ; ENSP00000413238 ; ENSG00000075711 . [Q12959-5 ]
    ENST00000443183 ; ENSP00000396658 ; ENSG00000075711 . [Q12959-9 ]
    ENST00000448528 ; ENSP00000391732 ; ENSG00000075711 . [Q12959-1 ]
    ENST00000450955 ; ENSP00000411278 ; ENSG00000075711 . [Q12959-4 ]
    ENST00000452595 ; ENSP00000398939 ; ENSG00000075711 . [Q12959-8 ]
    GeneIDi 1739.
    KEGGi hsa:1739.
    UCSCi uc003fxn.4. human. [Q12959-2 ]
    uc003fxo.4. human. [Q12959-1 ]
    uc010iam.1. human. [Q12959-3 ]
    uc011bue.2. human. [Q12959-4 ]

    Organism-specific databases

    CTDi 1739.
    GeneCardsi GC03M196769.
    HGNCi HGNC:2900. DLG1.
    HPAi CAB016307.
    MIMi 601014. gene.
    neXtProti NX_Q12959.
    PharmGKBi PA27356.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0194.
    HOVERGENi HBG107814.
    KOi K12076.
    OMAi DNENITT.
    OrthoDBi EOG79GT6P.
    PhylomeDBi Q12959.
    TreeFami TF323171.

    Enzyme and pathway databases

    Reactomei REACT_18307. Trafficking of AMPA receptors.
    REACT_21346. Activation of Ca-permeable Kainate Receptor.
    REACT_22329. NrCAM interactions.

    Miscellaneous databases

    EvolutionaryTracei Q12959.
    GeneWikii DLG1.
    GenomeRNAii 1739.
    NextBioi 7051.
    PMAP-CutDB A5YKK7.
    PROi Q12959.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12959.
    Bgeei Q12959.
    CleanExi HS_DLG1.
    Genevestigatori Q12959.

    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.
    IPR004172. L27.
    IPR015143. L27_1.
    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.
    PF09058. L27_1. 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.
    SM00569. L27. 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.
    PS51022. L27. 1 hit.
    PS50106. PDZ. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1."
      Lue R.A., Marfatia S.M., Branton D., Chishti A.H.
      Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EPB41, VARIANT GLN-278.
    2. "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 8 AND 9), VARIANT GLN-278.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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] (ISOFORMS 2 AND 4).
      Tissue: Brain.
    7. "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.
    8. "Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain."
      Lue R.A., Brandin E., Chan E.P., Branton D.
      J. Cell Biol. 135:1125-1137(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPB41, SUBCELLULAR LOCATION.
    9. "Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein."
      Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H., Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.
      Science 272:1020-1023(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APC.
    10. "Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein."
      Lee S.S., Weiss R.S., Javier R.T.
      Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VIRAL ONCOPROTEIN TAX AND HPV-18 E6.
    11. "Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila discs large tumor suppressor protein, hDLG, and perturbs its function in cell growth control."
      Suzuki T., Ohsugi Y., Uchida-Toita M., Akiyama T., Yoshida M.
      Oncogene 18:5967-5972(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX-1.
    12. "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, SUBCELLULAR LOCATION.
    13. "The APC-hDLG complex negatively regulates cell cycle progression from the G0/G1 to S phase."
      Ishidate T., Matsumine A., Toyoshima K., Akiyama T.
      Oncogene 19:365-372(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APC, FUNCTION IN CELL PROLIFERATION.
    14. "Characterization of PDZ-binding kinase, a mitotic kinase."
      Gaudet S., Branton D., Lue R.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOPK.
    15. "Pilt, a novel peripheral membrane protein at tight junctions in epithelial cells."
      Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K., Takeuchi M., Takai Y.
      J. Biol. Chem. 276:48350-48355(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INTERACTION WITH TJAP1.
    16. "Expression, regulation and role of the MAGUK protein SAP-97 in human atrial myocardium."
      Godreau D., Vranckx R., Maguy A., Rucker-Martin C., Goyenvalle C., Abdelshafy S., Tessier S., Couetil J.P., Hatem S.N.
      Cardiovasc. Res. 56:433-442(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH KCNF1.
    17. "The distribution and function of alternatively spliced insertions in hDlg."
      McLaughlin M., Hale R., Ellston D., Gaudet S., Lue R.A., Viel A.
      J. Biol. Chem. 277:6406-6412(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 5; 6 AND 7), SUBCELLULAR LOCATION.
    18. "Protein 4.1-mediated membrane targeting of human discs large in epithelial cells."
      Hanada T., Takeuchi A., Sondarva G., Chishti A.H.
      J. Biol. Chem. 278:34445-34450(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 38-ILE--ILE-40.
    19. "Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells."
      Laprise P., Viel A., Rivard N.
      J. Biol. Chem. 279:10157-10166(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1 AND CDH1, FUNCTION IN ADHERENS JUNCTION ASSEMBLY.
    20. Cited for: FUNCTION IN T-CELL ACTIVATION.
    21. "Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein."
      Yamamoto Y., Irie K., Asada M., Mino A., Mandai K., Takai Y.
      Oncogene 23:3889-3897(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPR124 AND GPR125.
    22. "Dlg, Scribble and Lgl in cell polarity, cell proliferation and cancer."
      Humbert P., Russell S., Richardson H.
      Bioessays 25:542-553(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    23. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "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.
    25. "The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions."
      Bohl J., Brimer N., Lyons C., Vande Pol S.B.
      J. Biol. Chem. 282:9392-9400(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIN7A; LIN7C AND MPP7.
    26. "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation."
      Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.
      Mol. Biol. Cell 18:1744-1755(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPP7.
    27. "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.
    28. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575; SER-684 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. "Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes."
      El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N.
      Circ. Res. 104:758-769(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH KCND2 AND KCND3.
    31. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    32. "p38gamma regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock."
      Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A., Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A.
      J. Cell Sci. 123:2596-2604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPK12, INTERACTION WITH SFPQ, FUNCTION.
    33. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-568; SER-575 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 460-555.
    36. "Structural basis for tandem L27 domain-mediated polymerization."
      Yang X., Xie X., Chen L., Zhou H., Wang Z., Zhao W., Tian R., Zhang R., Tian C., Long J., Shen Y.
      FASEB J. 24:4806-4815(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-65 IN COMPLEX WITH MPP7 AND LIN7C, SUBUNIT.

    Entry informationi

    Entry nameiDLG1_HUMAN
    AccessioniPrimary (citable) accession number: Q12959
    Secondary accession number(s): A5YKK7
    , B4DGU1, B4DGZ8, B7ZMM0, B9EIQ5, D3DXB8, D3DXB9, E7EWL7, E9PG21, Q12958
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 168 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 3
      Human chromosome 3: 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