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Q811D0 (DLG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disks large homolog 1
Alternative name(s):
Embryo-dlg/synapse-associated protein 97
Short name=E-dlg/SAP97
Synapse-associated protein 97
Short name=SAP-97
Short name=SAP97
Gene names
Name:Dlg1
Synonyms:Dlgh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length905 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential multidomain scaffolding protein required for normal development. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels By similarity. Functional regulator of Kv1.5 channel By similarity. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Ref.6

Subunit structure

Homotetramer Probable. Interacts with KCNF1 and CAMK2 By similarity. Interacts through its PDZ domains with KCND2 and KCND3 By similarity. Interacts with CAMK2 By similarity. Interacts through its PDZ domains with GRIN2A, KCNA1, KCNA2, KCNA3, KCNA4, KCNA5, GRIA1, GPR124 and GPR125. 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 DLGAP1, DLGAP2, DLGAP3, DLGAP4, MAP1A and KIF13B. Interacts with TOPK. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with TJAP1 By similarity. May interact with HTR2A. Interacts with LRFN1, LRFN2, LRFN4 and SFPQ By similarity. Interacts with PTEN By similarity. Interacts with FRMPD4 (via C-terminus) By similarity. Ref.4 Ref.5 Ref.7 Ref.8

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. 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.

Tissue specificity

Expressed in epithelial, mesenchymal, neuronal, endothelial and hematopoietic cells during embryogenesis. Expressed in fibroblasts and T-cells. Widely expressed in adult mice. Ref.6

Domain

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 By similarity.

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 By similarity.

Post-translational modification

Phosphorylated by MAPK12 By similarity. Phosphorylation of Ser-232 regulates association with GRIN2A By similarity. Isoform 2 is phosphorylated on Ser-665. Isoform 3 is phosphorylated on Ser-699.

Disruption phenotype

Mice have craniofacial abnormalities as well as a cleft palate. They are smaller than heterozygous littermates, unable to feed and die within 24 hours of birth. Ref.6

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

Inferred from mutant phenotype PubMed 15699074PubMed 17187070. Source: MGI

T cell cytokine production

Inferred from mutant phenotype PubMed 15699074. Source: MGI

actin filament organization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of protein kinase activity

Inferred from mutant phenotype PubMed 17187070. Source: MGI

amyloid precursor protein metabolic process

Inferred from genetic interaction PubMed 17301176. Source: MGI

branching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 16105026PubMed 17172448PubMed 17435047. Source: MGI

cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cortical actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic skeletal system morphogenesis

Inferred from mutant phenotype Ref.6. Source: MGI

endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

hard palate development

Inferred from mutant phenotype Ref.6PubMed 17435047. Source: MGI

immunological synapse formation

Inferred from mutant phenotype PubMed 15699074. Source: MGI

lens development in camera-type eye

Inferred from mutant phenotype PubMed 14645510. Source: MGI

membrane raft organization

Inferred from mutant phenotype PubMed 15699074. Source: MGI

negative regulation of T cell proliferation

Inferred from mutant phenotype PubMed 17724087. Source: MGI

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 14645510. Source: MGI

negative regulation of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

peristalsis

Inferred from mutant phenotype PubMed 17172448. Source: MGI

positive regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 15699074. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 17435047. Source: MGI

positive regulation of developmental growth

Traceable author statement PubMed 12766944. Source: UniProtKB

positive regulation of establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Traceable author statement PubMed 12766944. Source: UniProtKB

positive regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from mutant phenotype PubMed 17301176. Source: MGI

protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from genetic interaction Ref.7. Source: MGI

reproductive structure development

Inferred from mutant phenotype PubMed 17435047. Source: MGI

smooth muscle tissue development

Inferred from mutant phenotype PubMed 17172448. Source: MGI

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

tissue morphogenesis

Inferred from mutant phenotype PubMed 17172448. Source: MGI

ureteric bud development

Inferred from mutant phenotype PubMed 17435047. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

MPP7-DLG1-LIN7 complex

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from direct assay PubMed 21920314. Source: MGI

cell projection membrane

Inferred from direct assay PubMed 16621792. Source: MGI

cell-cell adherens junction

Traceable author statement PubMed 12766944. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

immunological synapse

Inferred from direct assay PubMed 15699074. Source: MGI

lateral loop

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

lateral plasma membrane

Inferred from direct assay PubMed 16105026. Source: MGI

membrane raft

Inferred from direct assay PubMed 15699074. Source: MGI

microtubule

Inferred from electronic annotation. Source: Ensembl

myelin sheath abaxonal region

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

neuromuscular junction

Inferred from direct assay PubMed 9674605. Source: MGI

node of Ranvier

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.7PubMed 16882004. Source: MGI

postsynaptic density

Inferred from direct assay PubMed 17301176. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from direct assay PubMed 16882004. Source: MGI

tight junction

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex scaffold

Inferred from mutant phenotype PubMed 15699074. Source: MGI

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q811D0-1)

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: Q811D0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
     670-681: EIPDDMGSKGLK → SFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ
Note: Contains a phosphoserine at position 676.
Isoform 3 (identifier: Q811D0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     670-681: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ
Note: Contains a phosphoserine at position 699. Contains a phosphoserine at position 710.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 905905Disks large homolog 1
PRO_0000094549

Regions

Domain4 – 6461L27
Domain224 – 31188PDZ 1
Domain319 – 40688PDZ 2
Domain466 – 54782PDZ 3
Domain581 – 65171SH3
Domain715 – 890176Guanylate kinase-like
Region162 – 21251Interaction with SH3 domains By similarity

Amino acid modifications

Modified residue1221Phosphoserine By similarity
Modified residue1581Phosphoserine By similarity
Modified residue2321Phosphoserine By similarity
Modified residue3991Phosphotyrosine Ref.10
Modified residue5681Phosphoserine By similarity
Modified residue5751Phosphoserine By similarity
Modified residue6191Phosphoserine By similarity
Modified residue6851Phosphoserine By similarity
Modified residue6881Phosphoserine By similarity

Natural variations

Alternative sequence162 – 19433Missing in isoform 2.
VSP_012866
Alternative sequence670 – 68112EIPDD…SKGLK → SFNDKRKKNLFSRKFPFYKN KDQSEQETSDADQ in isoform 2.
VSP_012867
Alternative sequence670 – 68112EIPDD…SKGLK → QSFNDKRKKNLFSRKFPFYK NKDQSEQETSDADQ in isoform 3.
VSP_012868

Experimental info

Sequence conflict2631A → R in AAC31653. Ref.1
Sequence conflict2761I → V in AAC31653. Ref.1
Sequence conflict3121P → L in AAC31653. Ref.1
Sequence conflict3371V → I in AAC31653. Ref.1
Sequence conflict4701H → R in AAN87264. Ref.2
Sequence conflict4821G → A in AAC31653. Ref.1
Sequence conflict550 – 5512YS → SR in AAC31653. Ref.1
Sequence conflict5681S → R in AAC31653. Ref.1
Sequence conflict5761L → P in AAC31653. Ref.1
Sequence conflict6471V → A in AAC31653. Ref.1
Sequence conflict7001Y → C in AAC31653. Ref.1
Sequence conflict7541Y → I in AAC31653. Ref.1
Sequence conflict769 – 7702QM → RV in AAC31653. Ref.1
Sequence conflict9001P → L in AAC31653. Ref.1

Secondary structure

............... 905
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2003. Version 1.
Checksum: 950A465824AE3210

FASTA905100,120
        10         20         30         40         50         60 
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 

        70         80         90        100        110        120 
LDNPKCVDHS KQCEPVQPVT TWEIASLPST AVTSETLPGS LSPPVEKYRY QDEEVLPPEH 

       130        140        150        160        170        180 
ISPQVTNEVL GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP 

       190        200        210        220        230        240 
VPAESTVVLP SAPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 

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

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

       370        380        390        400        410        420 
KDGKLQIGDK LLAVNSVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYI NDGYAPPDIT 

       430        440        450        460        470        480 
NSSSQSVDNH VSPSSCLGQT PTSPARYSPI SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 

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

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

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

       670        680        690        700        710        720 
NSKTRGDKGE IPDDMGSKGL KHVTSNASDS ESSYRGQEEY VLSYEPVNQQ EVNYTRPVII 

       730        740        750        760        770        780 
LGPMKDRVND DLISEFPDKF GSCVPHTTRP KRDYEVDGRD YHFVTSREQM EKDIQEHKFI 

       790        800        810        820        830        840 
EAGQYNNHLY GTSVQSVRAV AEKGKHCILD VSGNAIKRLQ IAQLYPISIF IKPKSMENIM 

       850        860        870        880        890        900 
EMNKRLTEEQ ARKTFERAMK LEQEFTEHFT AIVQGDTLED IYNQVKQIIE EQSGPYIWVP 


AKEKL 

« Hide

Isoform 2 [UniParc].

Checksum: 085DFCCCC2067FEB
Show »

FASTA89399,630
Isoform 3 [UniParc].

Checksum: 885671B7DACA7CD3
Show »

FASTA927102,986

References

« Hide 'large scale' references
[1]"Identification of the mouse homologue of human discs large and rat SAP97 genes."
Lin L., Sahr K.E., Chishti A.H.
Biochim. Biophys. Acta 1362:1-5(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Bone marrow.
[2]"Cloning and characterization of a novel mouse homolog E-dlg/SAP97 of the Drosophila discs large tumor suppressor binds to SAP102."
Mao P., Tao Y.-X., Levine C., Tao F., Li D., Johns R.A.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57BL/6J.
[3]"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 1 AND 3).
Strain: C57BL/6.
Tissue: Brain and Colon.
[4]"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 EZR.
[5]"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 AND CTNNB1.
[6]"Craniofacial dysmorphogenesis including cleft palate in mice with an insertional mutation in the discs large gene."
Caruana G., Bernstein A.
Mol. Cell. Biol. 21:1475-1483(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[7]"Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5."
Folco E.J., Liu G.-X., Koren G.
Am. J. Physiol. 287:H681-H690(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNA5 AND CAV3.
[8]"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins."
Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P.
J. Biol. Chem. 279:20257-20266(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTR2A.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U93309 mRNA. Translation: AAC31653.1.
AY159380 mRNA. Translation: AAN87264.1.
BC047142 mRNA. Translation: AAH47142.1.
BC057118 mRNA. Translation: AAH57118.1.
RefSeqNP_001239362.1. NM_001252433.1.
NP_001239363.1. NM_001252434.1.
NP_001239364.1. NM_001252435.1.
NP_031888.2. NM_007862.3.
XP_006521831.1. XM_006521768.1.
UniGeneMm.382.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4OAJX-ray2.30A317-406[»]
ProteinModelPortalQ811D0.
SMRQ811D0. Positions 2-65, 221-905.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199228. 15 interactions.
IntActQ811D0. 13 interactions.
MINTMINT-136497.

PTM databases

PhosphoSiteQ811D0.

Proteomic databases

PaxDbQ811D0.
PRIDEQ811D0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064477; ENSMUSP00000064280; ENSMUSG00000022770. [Q811D0-3]
ENSMUST00000100001; ENSMUSP00000097581; ENSMUSG00000022770. [Q811D0-1]
ENSMUST00000115205; ENSMUSP00000110859; ENSMUSG00000022770. [Q811D0-1]
GeneID13383.
KEGGmmu:13383.
UCSCuc007yxo.2. mouse. [Q811D0-1]
uc007yxp.2. mouse. [Q811D0-3]
uc007yxs.2. mouse. [Q811D0-2]

Organism-specific databases

CTD1739.
MGIMGI:107231. Dlg1.

Phylogenomic databases

eggNOGCOG0194.
GeneTreeENSGT00660000095130.
HOGENOMHOG000232102.
HOVERGENHBG107814.
KOK12076.
OrthoDBEOG79GT6P.
PhylomeDBQ811D0.
TreeFamTF323171.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressQ811D0.
BgeeQ811D0.
CleanExMM_DLG1.
GenevestigatorQ811D0.

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

ChiTaRSdlg1. mouse.
NextBio283732.
PROQ811D0.
SOURCESearch...

Entry information

Entry nameDLG1_MOUSE
AccessionPrimary (citable) accession number: Q811D0
Secondary accession number(s): Q62402, Q6PGB5, Q8CGN7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot