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Q12959 (DLG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disks large homolog 1
Alternative name(s):
Synapse-associated protein 97
Short name=SAP-97
Short name=SAP97
hDlg
Gene names
Name:DLG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length904 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.16 Ref.19 Ref.20 Ref.30 Ref.32

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.21 Ref.24 Ref.25 Ref.26 Ref.27 Ref.30 Ref.32

Subcellular location

Membrane; 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. Ref.1 Ref.8 Ref.12 Ref.16 Ref.17 Ref.18

Tissue specificity

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. Ref.1 Ref.16 Ref.30

Domain

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.

Post-translational modification

Phosphorylated by MAPK12. Phosphorylation of Ser-232 regulates association with GRIN2A. Isoform 2 is phosphorylated on Ser-698. Isoform 3 is phosphorylated on Ser-665 By similarity. Ref.32

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 1 L27 domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell junction
Cell membrane
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation

Inferred from electronic annotation. Source: Ensembl

T cell cytokine production

Inferred from electronic annotation. Source: Ensembl

actin filament organization

Inferred from direct assay Ref.19. Source: UniProtKB

activation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

amyloid precursor protein metabolic process

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion

Inferred from direct assay Ref.19. Source: UniProtKB

cortical actin cytoskeleton organization

Inferred from direct assay Ref.19. Source: UniProtKB

dephosphorylation

Traceable author statement PubMed 15302935. Source: GOC

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

endothelial cell proliferation

Inferred from direct assay Ref.19. Source: UniProtKB

establishment or maintenance of cell polarity

Traceable author statement Ref.22. Source: UniProtKB

hard palate development

Inferred from electronic annotation. Source: Ensembl

immunological synapse formation

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

membrane raft organization

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle checkpoint

Non-traceable author statement Ref.13. Source: UniProtKB

negative regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.13. Source: UniProtKB

nucleotide phosphorylation

Traceable author statement Ref.1. Source: GOC

peristalsis

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of establishment of protein localization to plasma membrane

Inferred from direct assay PubMed 12970345. Source: BHF-UCL

positive regulation of potassium ion transport

Inferred from direct assay PubMed 12970345. Source: BHF-UCL

protein localization to plasma membrane

Inferred from mutant phenotype Ref.26. Source: BHF-UCL

regulation of membrane potential

Inferred from direct assay PubMed 12970345. Source: BHF-UCL

regulation of sodium ion transmembrane transport

Traceable author statement PubMed 21164104. Source: BHF-UCL

reproductive structure development

Inferred from electronic annotation. Source: Ensembl

smooth muscle tissue development

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

tight junction assembly

Inferred from direct assay Ref.26. Source: BHF-UCL

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 21615688. Source: UniProtKB

MPP7-DLG1-LIN7 complex

Inferred from direct assay Ref.25. Source: BHF-UCL

basolateral plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

cell junction

Inferred from direct assay PubMed 12857860. Source: UniProtKB

cell projection membrane

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay PubMed 21615688. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 21615688. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 21615688. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from direct assay PubMed 21615688. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

immunological synapse

Traceable author statement PubMed 19841189. Source: BHF-UCL

intercalated disc

Traceable author statement PubMed 21164104. Source: BHF-UCL

lateral loop

Inferred from electronic annotation. Source: Ensembl

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from direct assay PubMed 21615688. Source: UniProtKB

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

node of Ranvier

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.25. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay PubMed 21615688. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

tight junction

Inferred from direct assay Ref.26. Source: BHF-UCL

   Molecular_functionL27 domain binding

Inferred from physical interaction Ref.26. Source: BHF-UCL

cytoskeletal protein binding

Traceable author statement PubMed 8825652. Source: ProtInc

guanylate kinase activity

Traceable author statement Ref.1. Source: ProtInc

ion channel binding

Inferred from physical interaction PubMed 12970345. Source: BHF-UCL

mitogen-activated protein kinase kinase binding

Inferred from physical interaction PubMed 21615688. Source: UniProtKB

phosphatase binding

Inferred from physical interaction PubMed 10646847. Source: UniProtKB

phosphoprotein phosphatase activity

Traceable author statement PubMed 15302935. Source: UniProtKB

potassium channel regulator activity

Non-traceable author statement Ref.14. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 11274188. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.14Ref.19PubMed 9341123. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12959-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q12959-2)

The sequence of this isoform differs from the canonical sequence as follows:
     669-680: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ
Note: Contains a phosphoserine at position 698 (By similarity).
Isoform 3 (identifier: Q12959-3)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
Isoform 4 (identifier: Q12959-4)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
     669-680: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ
Note: Contains a phosphoserine at position 665 (By similarity).
Isoform 5 (identifier: Q12959-5)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
     195-212: Missing.
Isoform 6 (identifier: Q12959-6)

The sequence of this isoform differs from the canonical sequence as follows:
     681-693: Missing.
Isoform 7 (identifier: Q12959-7)

The sequence of this isoform differs from the canonical sequence as follows:
     693-693: Y → YLILITDEYGCSKG
Isoform 8 (identifier: Q12959-8)

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.
Isoform 9 (identifier: Q12959-9)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 904904Disks large homolog 1
PRO_0000094548

Regions

Domain4 – 6461L27
Domain224 – 31087PDZ 1
Domain319 – 40587PDZ 2
Domain466 – 54681PDZ 3
Domain581 – 65171SH3
Domain714 – 889176Guanylate kinase-like
Region162 – 21251Interaction with SH3 domains

Amino acid modifications

Modified residue1151Phosphothreonine Ref.29
Modified residue1221Phosphoserine Ref.29
Modified residue1581Phosphoserine Ref.33
Modified residue2321Phosphoserine By similarity
Modified residue3991Phosphotyrosine By similarity
Modified residue5681Phosphoserine Ref.33
Modified residue5751Phosphoserine Ref.29 Ref.31 Ref.33
Modified residue6191Phosphoserine Ref.28
Modified residue6841Phosphoserine Ref.29
Modified residue6871Phosphoserine Ref.29 Ref.33

Natural variations

Alternative sequence1 – 7777MPVRK…SEPIQ → MNYIFGNNTLLYSRGSRGGN TSSSHGSAGPKQKHWAKKGS SDELQAEPEPSRWQQIVAFF TRRHSFIDCISVATSST in isoform 8 and isoform 9.
VSP_045896
Alternative sequence78 – 193116Missing in isoform 8 and isoform 9.
VSP_045897
Alternative sequence162 – 19433Missing in isoform 3, isoform 4 and isoform 5.
VSP_012862
Alternative sequence195 – 21218Missing in isoform 5.
VSP_012863
Alternative sequence669 – 68012EIPDD…SKGLK → QSFNDKRKKNLFSRKFPFYK NKDQSEQETSDADQ in isoform 2 and isoform 4.
VSP_003150
Alternative sequence681 – 69313Missing in isoform 6.
VSP_012864
Alternative sequence6931Y → YLILITDEYGCSKG in isoform 7 and isoform 9.
VSP_012865
Alternative sequence6941Missing in isoform 9.
VSP_045898
Natural variant1401K → R.
Corresponds to variant rs1802668 [ dbSNP | Ensembl ].
VAR_054334
Natural variant2781R → Q. Ref.1 Ref.2
Corresponds to variant rs1134986 [ dbSNP | Ensembl ].
VAR_054335
Natural variant8991P → L.
Corresponds to variant rs34492126 [ dbSNP | Ensembl ].
VAR_054336

Experimental info

Mutagenesis38 – 403INI → ANA: Loss of membrane association and DLG2-binding. Ref.18
Sequence conflict2371S → N in BAG57902. Ref.2
Sequence conflict8011E → G in AAA50598. Ref.1
Sequence conflict8011E → G in AAA50599. Ref.1
Isoform 4:
Sequence conflict6361Missing in AAI44652. Ref.6

Secondary structure

............................................................................................ 904
Helix Strand Turn

Details...

Sequences

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

Last modified February 10, 2009. Version 2.
Checksum: 6722993A84D0F761

FASTA904100,455
        10         20         30         40         50         60 
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 

        70         80         90        100        110        120 
LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 

       130        140        150        160        170        180 
ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP 

       190        200        210        220        230        240 
VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 

       250        260        270        280        290        300 
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 

       310        320        330        340        350        360 
SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 

       370        380        390        400        410        420 
KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT 

       430        440        450        460        470        480 
NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 

       490        500        510        520        530        540 
VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 

       550        560        570        580        590        600 
IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 

       610        620        630        640        650        660 
PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 

       670        680        690        700        710        720 
NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYRGQEEYV LSYEPVNQQE VNYTRPVIIL 

       730        740        750        760        770        780 
GPMKDRINDD LISEFPDKFG SCVPHTTRPK RDYEVDGRDY HFVTSREQME KDIQEHKFIE 

       790        800        810        820        830        840 
AGQYNNHLYG TSVQSVREVA EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME 

       850        860        870        880        890        900 
MNKRLTEEQA RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGSYIWVPA 


KEKL 

« Hide

Isoform 2 [UniParc].

Checksum: 85BD4E93A17D74C4
Show »

FASTA926103,321
Isoform 3 [UniParc].

Checksum: 78CB64FC6DE66BB1
Show »

FASTA87197,076
Isoform 4 [UniParc].

Checksum: 3A026E9BAA62FFB7
Show »

FASTA89399,942
Isoform 5 [UniParc].

Checksum: 2E7EE3F5954BA3E0
Show »

FASTA85395,166
Isoform 6 [UniParc].

Checksum: 5DB5256100623D0B
Show »

FASTA89199,090
Isoform 7 [UniParc].

Checksum: FE8911BB05B03211
Show »

FASTA917101,849
Isoform 8 [UniParc].

Checksum: 8EB77B3368768FBD
Show »

FASTA78887,248
Isoform 9 [UniParc].

Checksum: C67306E88A5A473D
Show »

FASTA80088,485

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9), VARIANT GLN-278.
Tissue: Brain.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Discs large (Dlg1) complexes in lymphocyte activation."
Xavier R., Rabizadeh S., Ishiguro K., Andre N., Ortiz J.B., Wachtel H., Morris D.G., Lopez-Ilasaca M., Shaw A.C., Swat W., Seed B.
J. Cell Biol. 166:173-178(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Crystal structure of a PDZ domain."
Cabral J.H., Petosa C., Sutcliffe M.J., Raza S., Byron O., Poy F., Marfatia S.M., Chishti A.H., Liddington R.C.
Nature 382:649-652(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 460-555.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI38756.
I38757.
RefSeqNP_001091894.1. NM_001098424.1.
NP_001191315.1. NM_001204386.1.
NP_001191316.1. NM_001204387.1.
NP_001191317.1. NM_001204388.1.
NP_004078.2. NM_004087.2.
XP_005269346.1. XM_005269289.1.
XP_005269347.1. XM_005269290.2.
XP_005269348.1. XM_005269291.1.
XP_005269349.1. XM_005269292.1.
XP_005269355.1. XM_005269298.1.
XP_005269356.1. XM_005269299.1.
UniGeneHs.292549.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDRX-ray2.80A457-552[»]
2M3MNMR-A318-406[»]
2OQSNMR-A318-405[»]
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[»]
ProteinModelPortalQ12959.
SMRQ12959. Positions 2-65, 220-904.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108083. 45 interactions.
IntActQ12959. 29 interactions.
MINTMINT-107690.
STRING9606.ENSP00000345731.

PTM databases

PhosphoSiteQ12959.

Polymorphism databases

DMDM223590196.

Proteomic databases

PaxDbQ12959.
PRIDEQ12959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314062; ENSP00000321087; ENSG00000075711. [Q12959-5]
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]
GeneID1739.
KEGGhsa:1739.
UCSCuc003fxn.4. human. [Q12959-2]
uc003fxo.4. human. [Q12959-1]
uc010iam.1. human. [Q12959-3]
uc011bue.2. human. [Q12959-4]

Organism-specific databases

CTD1739.
GeneCardsGC03M196769.
HGNCHGNC:2900. DLG1.
HPACAB016307.
MIM601014. gene.
neXtProtNX_Q12959.
PharmGKBPA27356.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOVERGENHBG107814.
KOK12076.
OMAQHITSNA.
OrthoDBEOG79GT6P.
PhylomeDBQ12959.
TreeFamTF323171.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ12959.
BgeeQ12959.
CleanExHS_DLG1.
GenevestigatorQ12959.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProIPR016313. DLG1.
IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR004172. L27.
IPR015143. L27_1.
IPR019590. MAGUK_PEST_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR23119. PTHR23119. 1 hit.
PfamPF00625. Guanylate_kin. 1 hit.
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]
PIRSFPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTSM00072. GuKc. 1 hit.
SM00569. L27. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ12959.
GeneWikiDLG1.
GenomeRNAi1739.
NextBio7051.
PMAP-CutDBA5YKK7.
PROQ12959.
SOURCESearch...

Entry information

Entry nameDLG1_HUMAN
AccessionPrimary (citable) accession number: Q12959
Secondary accession number(s): A5YKK7 expand/collapse secondary AC list , B4DGU1, B4DGZ8, B7ZMM0, B9EIQ5, D3DXB8, D3DXB9, E7EWL7, E9PG21, Q12958
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM