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P31007 (DLG1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. 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 1 tumor suppressor protein
Gene names
Name:dlg1
Synonyms:l(1)dlg1
ORF Names:CG1725
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length970 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

During embryonic development, some isoforms are essential for proper neuronal differentiation and organization. Required for cell polarity; maintenance of apicobasal polarity. Plays a critical role at septate junctions in cellular growth control during larval development. The presence of a guanylate kinase domain suggests involvement in cellular adhesion as well as signal transduction to control cellular proliferation. Ref.1 Ref.2 Ref.7

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell junctionseptate junction. Note: Cytoskeleton- and membrane-associated. Located at the cytoplasmic face of the membrane in the cellular blastoderm and becomes associated with septate junctions which begin to form between epithelial cells at the time of dorsal closure. In adult flies, located at the apical-lateral membrane boundary of epithelial cells. Ref.1 Ref.2 Ref.7

Tissue specificity

During the cellular blastoderm stage, isoform B, isoform F, isoform H, isoform I and isoform L expression is localized to the cell borders. From stage 11 onwards, expression is found predominantly in the developing nervous system: axon bundles in the ventral cord and the brain. Stage 14 and 15 embryos exhibit expression in the developing body wall muscle. Expression in neuropil regions of the CNS and at NMJs persists through to larval development. Other isoforms show expression in embryonic epithelial cells. In larvae, expression is seen as a belt around salivary glands, imaginal disks and proventriculus. Expressed in adult reproductive tissues. In epithelia, coexpressed with scrib throughout development. Ref.1 Ref.2 Ref.7

Developmental stage

Expressed both maternally and zygotically throughout development. Ref.1

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.

Sequence caution

The sequence AAL39553.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
Neurogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   Molecular functionDevelopmental protein
Transducer
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior axis specification, follicular epithelium

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

asymmetric protein localization

Inferred from mutant phenotype PubMed 11117747PubMed 12545176. Source: FlyBase

asymmetric protein localization involved in cell fate determination

Traceable author statement PubMed 15018932. Source: FlyBase

basal protein localization

Inferred from mutant phenotype PubMed 11117748. Source: FlyBase

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell fate commitment involved in pattern specification

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

cell fate specification

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

cell proliferation

Traceable author statement Ref.7. Source: FlyBase

cytoskeleton organization

Non-traceable author statement PubMed 12141438. Source: FlyBase

dorsal closure

Non-traceable author statement PubMed 12147138. Source: FlyBase

establishment of mitotic spindle orientation

Inferred from genetic interaction PubMed 22024168. Source: FlyBase

establishment of spindle orientation

Inferred from mutant phenotype PubMed 16377571. Source: FlyBase

establishment or maintenance of epithelial cell apical/basal polarity

Non-traceable author statement PubMed 11782950. Source: FlyBase

establishment or maintenance of neuroblast polarity

Traceable author statement PubMed 11700298. Source: FlyBase

establishment or maintenance of polarity of embryonic epithelium

Traceable author statement PubMed 11117747PubMed 11117748. Source: FlyBase

establishment or maintenance of polarity of follicular epithelium

Inferred from genetic interaction Ref.7. Source: FlyBase

establishment or maintenance of polarity of larval imaginal disc epithelium

Non-traceable author statement PubMed 11700298. Source: FlyBase

gravitaxis

Inferred from mutant phenotype PubMed 16594976. Source: FlyBase

locomotor rhythm

Inferred from mutant phenotype PubMed 18171947. Source: FlyBase

male courtship behavior

Inferred from mutant phenotype PubMed 18171947. Source: FlyBase

mating behavior

Inferred from mutant phenotype PubMed 18171947. Source: FlyBase

morphogenesis of a polarized epithelium

Traceable author statement PubMed 14644201. Source: FlyBase

morphogenesis of an epithelium

Traceable author statement PubMed 11700298. Source: FlyBase

morphogenesis of follicular epithelium

Inferred from mutant phenotype Ref.7. Source: FlyBase

morphogenesis of larval imaginal disc epithelium

Traceable author statement Ref.7. Source: FlyBase

negative regulation of cell proliferation

Traceable author statement PubMed 12766944. Source: FlyBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

nervous system development

Inferred from mutant phenotype PubMed 11117747. Source: FlyBase

nucleotide phosphorylation

Traceable author statement PubMed 10458610PubMed 11117747. Source: GOC

ovarian follicle cell development

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

pole plasm protein localization

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

positive phototaxis

Inferred from mutant phenotype PubMed 18171947. Source: FlyBase

positive regulation of synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 19244343. Source: FlyBase

protein localization

Inferred from mutant phenotype PubMed 11937021. Source: FlyBase

regulation of JAK-STAT cascade

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

regulation of Notch signaling pathway

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

regulation of border follicle cell delamination

Traceable author statement PubMed 10822261. Source: FlyBase

regulation of cell cycle

Non-traceable author statement PubMed 12766944. Source: FlyBase

regulation of cell proliferation

Traceable author statement PubMed 12141438. Source: FlyBase

regulation of epidermal growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 19948068. Source: BHF-UCL

septate junction assembly

Traceable author statement PubMed 12141438PubMed 12147138. Source: FlyBase

synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 17224403. Source: FlyBase

synaptic transmission

Inferred from mutant phenotype PubMed 10458610PubMed 12451127. Source: FlyBase

   Cellular_componentapical cortex

Inferred from direct assay PubMed 11117748PubMed 16377571. Source: FlyBase

apicolateral plasma membrane

Inferred from direct assay Ref.7. Source: FlyBase

basolateral plasma membrane

Traceable author statement PubMed 14644201. Source: FlyBase

cell cortex

Inferred from direct assay PubMed 11117747. Source: FlyBase

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

lateral plasma membrane

Inferred from direct assay PubMed 18501681. Source: FlyBase

membrane

Traceable author statement PubMed 10458610. Source: FlyBase

neuromuscular junction

Inferred from direct assay PubMed 18070911. Source: FlyBase

perinuclear region of cytoplasm

Inferred from direct assay PubMed 18501681. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 20462449. Source: FlyBase

postsynaptic membrane

Inferred from direct assay PubMed 16413491. Source: FlyBase

septate junction

Non-traceable author statement PubMed 11700298PubMed 12147138. Source: FlyBase

smooth septate junction

Inferred from direct assay PubMed 22854041. Source: FlyBase

synapse

Inferred from direct assay PubMed 17224403. Source: FlyBase

terminal bouton

Inferred from direct assay PubMed 11937021. Source: FlyBase

type Ib terminal bouton

Inferred from direct assay PubMed 15541314. Source: FlyBase

   Molecular_functionepidermal growth factor receptor binding

Traceable author statement PubMed 12766944. Source: FlyBase

guanylate kinase activity

Traceable author statement PubMed 10458610PubMed 11117747. Source: FlyBase

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Traceable author statement PubMed 11494317. Source: FlyBase

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P31007-2)

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.
Note: Contains the N-terminal domain essential for correct neuronal development.
Isoform A (identifier: P31007-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERV → MTTRKKKRDGGGSGGGFIKKVSSLFNLDSLHKASSTK
     38-205: Missing.
     473-473: E → GALNSMGQTV...NRSQSPQPRQ
     747-761: FMLCYTQDDANAEGA → NGVVSSTSEIDINNVNNNQSNEPQP
Note: No experimental confirmation available.
Isoform E (identifier: P31007-1)

Also known as: Dlg-A; D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MPVKKQEAHRALELLEDYHARLSEPQDRA → MTTRKKKRDGGGSGGGFIKKVSSLFNLDS
     30-205: Missing.
     473-473: E → GALNSMGQTV...NRSQSPQPRQ
     747-761: FMLCYTQDDANAEGA → NGVVSSTSEIDINNVNNNQSNEPQP
Isoform F (identifier: P31007-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MPVKKQE → MDSDTDSERE...EEERIADIQK
     473-519: EPGSRYASTN...QKGPQGLGFN → AFMLCYTQDD...NDADYRKSSI
     520-970: Missing.
Note: Contains the N-terminal domain essential for correct neuronal development.
Isoform G (identifier: P31007-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MPVKKQEAHRALELLEDYHARLSEPQDRA → MTTRKKKRDGGGSGGGFIKKVSSLFNLDS
     30-205: Missing.
     473-473: E → GALNSMGQTV...NRSQSPQPRQ
     746-746: P → PNGVVSSTSEIDINNVNNNQSNEPQP
Note: No experimental confirmation available.
Isoform H (identifier: P31007-6)

The sequence of this isoform differs from the canonical sequence as follows:
     93-151: Missing.
Note: Contains the N-terminal domain essential for correct neuronal development.
Isoform I (identifier: P31007-7)

Also known as: C; J;

The sequence of this isoform differs from the canonical sequence as follows:
     93-151: Missing.
     206-267: VNGDDSWLYE...ADGRLSINDI → SQIQIQSLTQ...KMLKRAFEST
     268-970: Missing.
Note: Contains the N-terminal domain essential for correct neuronal development.
Isoform K (identifier: P31007-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: MPVKKQEAHR...KDGQAVKIAD → MIDWVSIVRH...GSRYACCCAN
     93-151: Missing.
Note: No experimental confirmation available.
Isoform L (identifier: P31007-8)

Also known as: S97;

The sequence of this isoform differs from the canonical sequence as follows:
     93-151: Missing.
     205-205: T → TLHKASSTK
     761-761: A → GEIIYRVELPDMEQITLIYLENNDADYP
Note: Contains the N-terminal domain essential for correct neuronal development.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 970970Disks large 1 tumor suppressor protein
PRO_0000094538

Regions

Domain4 – 6461L27
Domain216 – 30388PDZ 1
Domain330 – 42192PDZ 2
Domain506 – 58782PDZ 3
Domain620 – 69071SH3
Domain780 – 955176Guanylate kinase-like

Amino acid modifications

Modified residue4961Phosphoserine Ref.8
Modified residue7141Phosphothreonine Ref.8

Natural variations

Alternative sequence1 – 9292MPVKK…VKIAD → MIDWVSIVRHSRRRFSNYVG SRSPVRMRRRRRQLTAPPPQ QQQQQHYHQQQQQDQHQSRE RQKKDKEKEKETEKDNESGG GIGSRYACCCAN in isoform K.
VSP_039402
Alternative sequence1 – 3737MPVKK…AIERV → MTTRKKKRDGGGSGGGFIKK VSSLFNLDSLHKASSTK in isoform A.
VSP_011403
Alternative sequence1 – 2929MPVKK…PQDRA → MTTRKKKRDGGGSGGGFIKK VSSLFNLDS in isoform E and isoform G.
VSP_011402
Alternative sequence1 – 77MPVKKQE → MDSDTDSEREKSSDPNEGLL SSDDKTFHDDDEPAEDSSPA DDEEEPEEEECLLPQKKAQI RCDQDQPPLVVLVQPSAEAI EVRQEIDDTNPVAVAAKASD MDGDSQLEVMEHQMETVTEP DPEPPKCPTSLRDSVRESVE CFYSAQDLLEYGHMLSSTSM VRTPDVESGYFEKSESDASR DEWEGPSSSSSGAARCRLLS GISGLSVSSSSRHSAEGLRM ELSRFRTMIETLERESLEKS QSELQLKAKSKAKPKPKQRS HVQDAAGESGSEQGSERGFW STIFGQAGLAISQDEEERIA DIQK in isoform F.
VSP_011401
Alternative sequence30 – 205176Missing in isoform E and isoform G.
VSP_011404
Alternative sequence38 – 205168Missing in isoform A.
VSP_011405
Alternative sequence93 – 15159Missing in isoform I, isoform H, isoform K and isoform L.
VSP_011406
Alternative sequence2051T → TLHKASSTK in isoform L.
VSP_011407
Alternative sequence206 – 26762VNGDD…SINDI → SQIQIQSLTQTYPNAHQRKR VLVSLHPHQHQHQSQIQHQH HYQLRHNNGIQAKMLKRAFE ST in isoform I.
VSP_011408
Alternative sequence268 – 970703Missing in isoform I.
VSP_011409
Alternative sequence473 – 51947EPGSR…GLGFN → AFMLCYTQDDANAEGGEIIY RVELPDMEQITLIYLENNDA DYRKSSI in isoform F.
VSP_011411
Alternative sequence4731E → GALNSMGQTVVDSPSIPQAA AAVAAAANASASASVIASNN TISNTTVTTVTATATASNSS SKLPPSLGANSSISISNSNS NSNSNNINNINSINNNNSSS SSTTATVAAATPTAASAAAA AASSPPANSFYNNASMPALP VESNQTNNRSQSPQPRQ in isoform A, isoform E and isoform G.
VSP_011410
Alternative sequence520 – 970451Missing in isoform F.
VSP_011412
Alternative sequence7461P → PNGVVSSTSEIDINNVNNNQ SNEPQP in isoform G.
VSP_011413
Alternative sequence747 – 76115FMLCY…NAEGA → NGVVSSTSEIDINNVNNNQS NEPQP in isoform A and isoform E.
VSP_011414
Alternative sequence7611A → GEIIYRVELPDMEQITLIYL ENNDADYP in isoform L.
VSP_011415

Experimental info

Sequence conflict3651M → T in AAA28468. Ref.1
Sequence conflict3651M → T in AAQ01226. Ref.2
Sequence conflict3691A → R in AAA28468. Ref.1
Sequence conflict3691A → R in AAQ01226. Ref.2
Sequence conflict3951E → G in ACV53090. Ref.6
Isoform E:
Sequence conflict3551S → D in AAA28468. Ref.1

Secondary structure

............................................. 970
Helix Strand Turn

Details...

Sequences

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

Last modified August 31, 2004. Version 2.
Checksum: 544D1E1AD03B0674

FASTA970106,673
        10         20         30         40         50         60 
MPVKKQEAHR ALELLEDYHA RLSEPQDRAL RIAIERVIRI FKSRLFQALL DIQEFYELTL 

        70         80         90        100        110        120 
LDDSKSIQQK TAETLQIATK WEKDGQAVKI ADFIKSSNLN RNCAYEFNND ASSNQTNQSA 

       130        140        150        160        170        180 
LNQNPIANNV SAQAQAEALS RTFKSELEEI LNQRMRIESD TENAKEPTVE QQQKQQQAQQ 

       190        200        210        220        230        240 
RSSRSPQQQN PQQQQGSKSR SGSQTVNGDD SWLYEDIQLE RGNSGLGFSI AGGTDNPHIG 

       250        260        270        280        290        300 
TDTSIYITKL ISGGAAAADG RLSINDIIVS VNDVSVVDVP HASAVDALKK AGNVVKLHVK 

       310        320        330        340        350        360 
RKRGTATTPA AGSAAGDARD SAASGPKVIE IDLVKGGKGL GFSIAGGIGN QHIPGDNGIY 

       370        380        390        400        410        420 
VTKLMDGGAA QVDGRLSIGD KLIAVRTNGS EKNLENVTHE LAVATLKSIT DKVTLIIGKT 

       430        440        450        460        470        480 
QHLTTSASGG GGGGLSSGQQ LSQSQSQLAT SQSQSQVHQQ QHATPMVNSQ STEPGSRYAS 

       490        500        510        520        530        540 
TNVLAAVPPG TPRAVSTEDI TREPRTITIQ KGPQGLGFNI VGGEDGQGIY VSFILAGGPA 

       550        560        570        580        590        600 
DLGSELKRGD QLLSVNNVNL THATHEEAAQ ALKTSGGVVT LLAQYRPEEY NRFEARIQEL 

       610        620        630        640        650        660 
KQQAALGAGG SGTLLRTTQK RSLYVRALFD YDPNRDDGLP SRGLPFKHGD ILHVTNASDD 

       670        680        690        700        710        720 
EWWQARRVLG DNEDEQIGIV PSKRRWERKM RARDRSVKFQ GHAAANNNLD KQSTLDRKKK 

       730        740        750        760        770        780 
NFTFSRKFPF MKSRDEKNED GSDQEPFMLC YTQDDANAEG ASEENVLSYE AVQRLSINYT 

       790        800        810        820        830        840 
RPVIILGPLK DRINDDLISE YPDKFGSCVP HTTRPKREYE VDGRDYHFVS SREQMERDIQ 

       850        860        870        880        890        900 
NHLFIEAGQY NDNLYGTSVA SVREVAEKGK HCILDVSGNA IKRLQVAQLY PVAVFIKPKS 

       910        920        930        940        950        960 
VDSVMEMNRR MTEEQAKKTY ERAIKMEQEF GEYFTGVVQG DTIEEIYSKV KSMIWSQSGP 

       970 
TIWVPSKESL 

« Hide

Isoform A [UniParc].

Checksum: E641D9BE7669331C
Show »

FASTA968103,239
Isoform E (Dlg-A) (D) [UniParc].

Checksum: 26E9B6026226BDA3
Show »

FASTA960102,386
Isoform F [UniParc].

Checksum: 35894E1555DE5AAE
Show »

FASTA81688,662
Isoform G [UniParc].

Checksum: 15D466336AA4194C
Show »

FASTA975104,016
Isoform H [UniParc].

Checksum: 47ACCA6E52AD1168
Show »

FASTA911100,171
Isoform I (C) (J) [UniParc].

Checksum: BB8F4B44E9DE2562
Show »

FASTA20824,378
Isoform K [UniParc].

Checksum: 6FE13A27211F2122
Show »

FASTA911100,458
Isoform L (S97) [UniParc].

Checksum: 6BAFDD6BE66191B7
Show »

FASTA946104,263

References

« Hide 'large scale' references
[1]"The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions."
Woods D.F., Bryant P.J.
Cell 66:451-464(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
Tissue: Embryo.
[2]"Novel isoforms of Dlg are fundamental for neuronal development in Drosophila."
Mendoza C., Olguin P., Lafferte G., Thomas U., Ebitsch S., Gundelfinger E.D., Kukuljan M., Sierralta J.
J. Neurosci. 23:2093-2101(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; F; H; I AND L), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS F AND I), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-970 (ISOFORM G).
Strain: Berkeley.
Tissue: Embryo and Head.
[6]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G).
Strain: Berkeley.
Tissue: Embryo.
[7]"Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors."
Bilder D., Li M., Perrimon N.
Science 289:113-116(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND THR-714, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73529 mRNA. Translation: AAA28468.1.
AY332243 mRNA. Translation: AAQ01226.1.
AE014298 Genomic DNA. Translation: AAF48037.2.
AE014298 Genomic DNA. Translation: AAF48038.2.
AE014298 Genomic DNA. Translation: AAF48039.2.
AE014298 Genomic DNA. Translation: AAN09630.1.
AE014298 Genomic DNA. Translation: AAS65308.1.
AE014298 Genomic DNA. Translation: AAS65309.1.
AE014298 Genomic DNA. Translation: AAS65310.1.
AE014298 Genomic DNA. Translation: AAS65311.1.
AE014298 Genomic DNA. Translation: AAS65312.1.
AE014298 Genomic DNA. Translation: AAS65313.1.
AE014298 Genomic DNA. Translation: ABW09394.1.
AE014298 Genomic DNA. Translation: ABW09395.1.
AY059433 mRNA. Translation: AAL13339.1.
AY069408 mRNA. Translation: AAL39553.1. Different initiation.
AY075410 mRNA. Translation: AAL68235.1.
BT099726 mRNA. Translation: ACV53090.1.
PIRA39651.
RefSeqNP_001096955.1. NM_001103485.3.
NP_001096956.1. NM_001103486.3.
NP_001162719.1. NM_001169248.2.
NP_001245623.1. NM_001258694.2.
NP_001259447.1. NM_001272518.1.
NP_511120.2. NM_078565.5.
NP_727518.1. NM_167280.2.
NP_727519.1. NM_167281.2.
NP_727520.1. NM_167282.4.
NP_996402.1. NM_206679.2.
NP_996403.1. NM_206680.2.
NP_996404.1. NM_206681.4.
NP_996405.1. NM_206682.4.
NP_996406.1. NM_206683.4.
NP_996407.1. NM_206684.4.
UniGeneDm.4352.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TVTX-ray1.60A618-970[»]
ProteinModelPortalP31007.
SMRP31007. Positions 2-65, 214-966.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58494. 21 interactions.
IntActP31007. 19 interactions.
MINTMINT-287852.
STRING7227.FBpp0089352.

Proteomic databases

PaxDbP31007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073488; FBpp0089351; FBgn0001624. [P31007-2]
GeneID32083.
KEGGdme:Dmel_CG1725.
UCSCCG1725-RI. d. melanogaster.

Organism-specific databases

CTD1739.
FlyBaseFBgn0001624. dlg1.

Phylogenomic databases

eggNOGCOG0194.
GeneTreeENSGT00660000095130.
InParanoidP31007.
KOK12076.
OMARTFKNEL.
OrthoDBEOG79GT6P.
PhylomeDBP31007.

Enzyme and pathway databases

SignaLinkP31007.

Gene expression databases

BgeeP31007.

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.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR23119. PTHR23119. 1 hit.
PfamPF00625. Guanylate_kin. 1 hit.
PF09058. L27_1. 1 hit.
PF00595. PDZ. 3 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
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. drosophila.
GenomeRNAi32083.
NextBio776723.

Entry information

Entry nameDLG1_DROME
AccessionPrimary (citable) accession number: P31007
Secondary accession number(s): A4V4A8 expand/collapse secondary AC list , A4V4B0, A8JUR9, A8JUS0, C7LAH6, Q7KV38, Q7KV39, Q7KV40, Q7YXH8, Q8SY37, Q8T0C6, Q95TF5, Q9VYZ4, Q9VYZ5, Q9VYZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase