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Q12959

- DLG1_HUMAN

UniProt

Q12959 - DLG1_HUMAN

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Protein

Disks large homolog 1

Gene

DLG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 C-terminus binding Source: UniProtKB
  10. 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 protein kinase B signaling Source: Ensembl
  19. negative regulation of T cell proliferation Source: Ensembl
  20. nucleotide phosphorylation Source: GOC
  21. peristalsis Source: Ensembl
  22. positive regulation of actin filament polymerization Source: Ensembl
  23. positive regulation of cell proliferation Source: Ensembl
  24. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  25. positive regulation of potassium ion transport Source: BHF-UCL
  26. protein localization to plasma membrane Source: BHF-UCL
  27. regulation of membrane potential Source: BHF-UCL
  28. regulation of myelination Source: Ensembl
  29. regulation of sodium ion transmembrane transport Source: BHF-UCL
  30. reproductive structure development Source: Ensembl
  31. single organismal cell-cell adhesion Source: UniProtKB
  32. smooth muscle tissue development Source: Ensembl
  33. synaptic transmission Source: Reactome
  34. T cell activation Source: Ensembl
  35. T cell cytokine production Source: Ensembl
  36. tight junction assembly Source: BHF-UCL
  37. viral process Source: UniProtKB-KW
Complete GO annotation...

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. basal lamina Source: Ensembl
  2. basolateral plasma membrane Source: UniProtKB
  3. cell-cell junction Source: UniProtKB
  4. cell junction Source: UniProtKB
  5. cell projection membrane Source: Ensembl
  6. cytoplasm Source: UniProtKB
  7. cytoplasmic side of plasma membrane Source: UniProtKB
  8. cytosol Source: Reactome
  9. endoplasmic reticulum Source: UniProtKB
  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: Ensembl
  26. postsynaptic membrane Source: UniProtKB-KW
  27. tight junction Source: BHF-UCL
Complete GO annotation...

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 – 1151Phosphothreonine1 Publication
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei399 – 3991PhosphotyrosineBy similarity
Modified residuei568 – 5681Phosphoserine1 Publication
Modified residuei575 – 5751Phosphoserine3 Publications
Modified residuei619 – 6191Phosphoserine1 Publication
Modified residuei684 – 6841Phosphoserine1 Publication
Modified residuei687 – 6871Phosphoserine2 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

BgeeiQ12959.
CleanExiHS_DLG1.
ExpressionAtlasiQ12959. baseline and differential.
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.
GeneTreeiENSGT00760000118866.
HOVERGENiHBG107814.
InParanoidiQ12959.
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) [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

        10         20         30         40         50
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI
60 70 80 90 100
DIQEFYEVTL LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS
110 120 130 140 150
LSPSVEKYRY QDEDTPPQEH ISPQITNEVI GPELVHVSEK NLSEIENVHG
160 170 180 190 200
FVSHSHISPI KPTEAVLPSP PTVPVIPVLP VPAENTVILP TIPQANPPPV
210 220 230 240 250
LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG GTDNPHIGDD
260 270 280 290 300
SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG
310 320 330 340 350
SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV
360 370 380 390 400
TKIIEGGAAH KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL
410 420 430 440 450
KVAKPTSMYM NDGYAPPDIT NSSSQPVDNH VSPSSFLGQT PASPARYSPV
460 470 480 490 500
SKAVLGDDEI TREPRKVVLH RGSTGLGFNI VGGEDGEGIF ISFILAGGPA
510 520 530 540 550
DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT IVAQYRPEEY
560 570 580 590 600
SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL
610 620 630 640 650
PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK
660 670 680 690 700
ERARLKTVKF NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYRGQEEYV
710 720 730 740 750
LSYEPVNQQE VNYTRPVIIL GPMKDRINDD LISEFPDKFG SCVPHTTRPK
760 770 780 790 800
RDYEVDGRDY HFVTSREQME KDIQEHKFIE AGQYNNHLYG TSVQSVREVA
810 820 830 840 850
EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME MNKRLTEEQA
860 870 880 890 900
RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGSYIWVPA

KEKL
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.
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 .
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.
GeneTreei ENSGT00760000118866.
HOVERGENi HBG107814.
InParanoidi Q12959.
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

Bgeei Q12959.
CleanExi HS_DLG1.
ExpressionAtlasi Q12959. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 169 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

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