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Disks large 1 tumor suppressor protein

 DLG1_DROME              Reviewed;         970 AA.
P31007; A4V4A8; A4V4B0; A8JUR9; A8JUS0; C7LAH6; Q7KV38; Q7KV39;
Q7KV40; Q7YXH8; Q8SY37; Q8T0C6; Q95TF5; Q9VYZ4; Q9VYZ5; Q9VYZ6;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 2.
22-NOV-2017, entry version 196.
RecName: Full=Disks large 1 tumor suppressor protein;
Name=dlg1; Synonyms=l(1)dlg1; ORFNames=CG1725;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Oregon-R; TISSUE=Embryo;
PubMed=1651169; DOI=10.1016/0092-8674(81)90009-X;
Woods D.F., Bryant P.J.;
"The discs-large tumor suppressor gene of Drosophila encodes a
guanylate kinase homolog localized at septate junctions.";
Cell 66:451-464(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; F; H; I AND L), FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=12657668;
Mendoza C., Olguin P., Lafferte G., Thomas U., Ebitsch S.,
Gundelfinger E.D., Kukuljan M., Sierralta J.;
"Novel isoforms of Dlg are fundamental for neuronal development in
Drosophila.";
J. Neurosci. 23:2093-2101(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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., 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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS F AND I), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-970 (ISOFORM G).
STRAIN=Berkeley; TISSUE=Embryo, and Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G).
STRAIN=Berkeley; TISSUE=Embryo;
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.
[7]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10884224; DOI=10.1126/science.289.5476.113;
Bilder D., Li M., Perrimon N.;
"Cooperative regulation of cell polarity and growth by Drosophila
tumor suppressors.";
Science 289:113-116(2000).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND THR-714, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- 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.
{ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:12657668,
ECO:0000269|PubMed:1651169}.
-!- INTERACTION:
Q4AB30:gukh; NbExp=4; IntAct=EBI-389374, EBI-8282973;
Q9VE13:gukh; NbExp=11; IntAct=EBI-389394, EBI-3414026;
P08510:Sh; NbExp=3; IntAct=EBI-389374, EBI-85074;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell
junction, septate 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=B;
IsoId=P31007-2; Sequence=Displayed;
Note=Contains the N-terminal domain essential for correct
neuronal development.;
Name=A;
IsoId=P31007-3; Sequence=VSP_011403, VSP_011405, VSP_011410,
VSP_011414;
Note=No experimental confirmation available.;
Name=E; Synonyms=Dlg-A, D;
IsoId=P31007-1; Sequence=VSP_011402, VSP_011404, VSP_011410,
VSP_011414;
Note=Ref.1 (AAA28468) sequence is in conflict in position:
355:S->D. {ECO:0000305};
Name=F;
IsoId=P31007-4; Sequence=VSP_011401, VSP_011411, VSP_011412;
Note=Contains the N-terminal domain essential for correct
neuronal development.;
Name=G;
IsoId=P31007-5; Sequence=VSP_011402, VSP_011404, VSP_011410,
VSP_011413;
Note=No experimental confirmation available.;
Name=H;
IsoId=P31007-6; Sequence=VSP_011406;
Note=Contains the N-terminal domain essential for correct
neuronal development.;
Name=I; Synonyms=C, J;
IsoId=P31007-7; Sequence=VSP_011406, VSP_011408, VSP_011409;
Note=Contains the N-terminal domain essential for correct
neuronal development.;
Name=K;
IsoId=P31007-9; Sequence=VSP_039402, VSP_011406;
Note=No experimental confirmation available.;
Name=L; Synonyms=S97;
IsoId=P31007-8; Sequence=VSP_011406, VSP_011407, VSP_011415;
Note=Contains the N-terminal domain essential for correct
neuronal development.;
-!- 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. {ECO:0000269|PubMed:10884224,
ECO:0000269|PubMed:12657668, ECO:0000269|PubMed:1651169}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
throughout development. {ECO:0000269|PubMed:1651169}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL39553.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M73529; AAA28468.1; -; mRNA.
EMBL; AY332243; AAQ01226.1; -; mRNA.
EMBL; AE014298; AAF48037.2; -; Genomic_DNA.
EMBL; AE014298; AAF48038.2; -; Genomic_DNA.
EMBL; AE014298; AAF48039.2; -; Genomic_DNA.
EMBL; AE014298; AAN09630.1; -; Genomic_DNA.
EMBL; AE014298; AAS65308.1; -; Genomic_DNA.
EMBL; AE014298; AAS65309.1; -; Genomic_DNA.
EMBL; AE014298; AAS65310.1; -; Genomic_DNA.
EMBL; AE014298; AAS65311.1; -; Genomic_DNA.
EMBL; AE014298; AAS65312.1; -; Genomic_DNA.
EMBL; AE014298; AAS65313.1; -; Genomic_DNA.
EMBL; AE014298; ABW09394.1; -; Genomic_DNA.
EMBL; AE014298; ABW09395.1; -; Genomic_DNA.
EMBL; AY059433; AAL13339.1; -; mRNA.
EMBL; AY069408; AAL39553.1; ALT_INIT; mRNA.
EMBL; AY075410; AAL68235.1; -; mRNA.
EMBL; BT099726; ACV53090.1; -; mRNA.
PIR; A39651; A39651.
RefSeq; NP_001096955.1; NM_001103485.3. [P31007-9]
RefSeq; NP_001096956.1; NM_001103486.3. [P31007-8]
RefSeq; NP_001162719.1; NM_001169248.2. [P31007-1]
RefSeq; NP_001245623.1; NM_001258694.2. [P31007-5]
RefSeq; NP_001259447.1; NM_001272518.1. [P31007-1]
RefSeq; NP_511120.2; NM_078565.5. [P31007-1]
RefSeq; NP_727518.1; NM_167280.2. [P31007-7]
RefSeq; NP_727519.1; NM_167281.2. [P31007-4]
RefSeq; NP_727520.1; NM_167282.4. [P31007-3]
RefSeq; NP_996402.1; NM_206679.2. [P31007-7]
RefSeq; NP_996403.1; NM_206680.2. [P31007-7]
RefSeq; NP_996404.1; NM_206681.4. [P31007-6]
RefSeq; NP_996405.1; NM_206682.4. [P31007-5]
RefSeq; NP_996406.1; NM_206683.4. [P31007-2]
RefSeq; NP_996407.1; NM_206684.4. [P31007-1]
UniGene; Dm.4352; -.
PDB; 3TVT; X-ray; 1.60 A; A=618-970.
PDB; 4RP3; X-ray; 1.36 A; A/B=1-97.
PDB; 4RP4; X-ray; 1.42 A; A/B=1-97.
PDB; 4RP5; X-ray; 1.65 A; A/B=1-97.
PDBsum; 3TVT; -.
PDBsum; 4RP3; -.
PDBsum; 4RP4; -.
PDBsum; 4RP5; -.
ProteinModelPortal; P31007; -.
SMR; P31007; -.
BioGrid; 58494; 42.
DIP; DIP-31531N; -.
IntAct; P31007; 44.
MINT; MINT-287852; -.
STRING; 7227.FBpp0290503; -.
iPTMnet; P31007; -.
PaxDb; P31007; -.
PRIDE; P31007; -.
EnsemblMetazoa; FBtr0073483; FBpp0073339; FBgn0001624. [P31007-7]
EnsemblMetazoa; FBtr0073484; FBpp0073340; FBgn0001624. [P31007-4]
EnsemblMetazoa; FBtr0073485; FBpp0073341; FBgn0001624. [P31007-1]
EnsemblMetazoa; FBtr0073486; FBpp0073342; FBgn0001624. [P31007-3]
EnsemblMetazoa; FBtr0073487; FBpp0089350; FBgn0001624. [P31007-1]
EnsemblMetazoa; FBtr0073488; FBpp0089351; FBgn0001624. [P31007-2]
EnsemblMetazoa; FBtr0073489; FBpp0089352; FBgn0001624. [P31007-5]
EnsemblMetazoa; FBtr0073490; FBpp0089353; FBgn0001624. [P31007-6]
EnsemblMetazoa; FBtr0073491; FBpp0089348; FBgn0001624. [P31007-7]
EnsemblMetazoa; FBtr0073492; FBpp0089349; FBgn0001624. [P31007-7]
EnsemblMetazoa; FBtr0112812; FBpp0111724; FBgn0001624. [P31007-9]
EnsemblMetazoa; FBtr0112813; FBpp0111725; FBgn0001624. [P31007-8]
EnsemblMetazoa; FBtr0301289; FBpp0290504; FBgn0001624. [P31007-1]
EnsemblMetazoa; FBtr0308089; FBpp0300432; FBgn0001624. [P31007-5]
EnsemblMetazoa; FBtr0333261; FBpp0305459; FBgn0001624. [P31007-1]
GeneID; 32083; -.
KEGG; dme:Dmel_CG1725; -.
UCSC; CG1725-RE; d. melanogaster.
UCSC; CG1725-RI; d. melanogaster.
UCSC; CG1725-RK; d. melanogaster.
UCSC; CG1725-RL; d. melanogaster.
CTD; 1739; -.
FlyBase; FBgn0001624; dlg1.
eggNOG; KOG0708; Eukaryota.
eggNOG; COG0194; LUCA.
GeneTree; ENSGT00760000118866; -.
InParanoid; P31007; -.
KO; K12076; -.
OrthoDB; EOG091G0BB1; -.
PhylomeDB; P31007; -.
Reactome; R-DME-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-DME-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-DME-5625900; RHO GTPases activate CIT.
Reactome; R-DME-6794361; Neurexins and neuroligins.
Reactome; R-DME-8849932; Synaptic adhesion-like molecules.
SignaLink; P31007; -.
ChiTaRS; dlg1; fly.
GenomeRNAi; 32083; -.
PRO; PR:P31007; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0001624; -.
ExpressionAtlas; P31007; differential.
Genevisible; P31007; DM.
GO; GO:0045179; C:apical cortex; IDA:FlyBase.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
GO; GO:0016323; C:basolateral plasma membrane; TAS:FlyBase.
GO; GO:0005938; C:cell cortex; IDA:FlyBase.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
GO; GO:0016020; C:membrane; TAS:FlyBase.
GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IDA:FlyBase.
GO; GO:0005918; C:septate junction; IDA:FlyBase.
GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase.
GO; GO:0045202; C:synapse; IDA:FlyBase.
GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
GO; GO:0061689; C:tricellular tight junction; IDA:FlyBase.
GO; GO:0061174; C:type I terminal bouton; IDA:FlyBase.
GO; GO:0061176; C:type Ib terminal bouton; IDA:FlyBase.
GO; GO:0005154; F:epidermal growth factor receptor binding; TAS:FlyBase.
GO; GO:0004385; F:guanylate kinase activity; TAS:FlyBase.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; TAS:FlyBase.
GO; GO:0030714; P:anterior/posterior axis specification, follicular epithelium; IMP:BHF-UCL.
GO; GO:0008105; P:asymmetric protein localization; IMP:FlyBase.
GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; TAS:FlyBase.
GO; GO:0045175; P:basal protein localization; IMP:FlyBase.
GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060581; P:cell fate commitment involved in pattern specification; IMP:BHF-UCL.
GO; GO:0001708; P:cell fate specification; IMP:BHF-UCL.
GO; GO:0008283; P:cell proliferation; TAS:FlyBase.
GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
GO; GO:0007010; P:cytoskeleton organization; NAS:FlyBase.
GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:FlyBase.
GO; GO:0051294; P:establishment of spindle orientation; IMP:FlyBase.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; TAS:FlyBase.
GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; TAS:FlyBase.
GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; TAS:FlyBase.
GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IGI:FlyBase.
GO; GO:0016336; P:establishment or maintenance of polarity of larval imaginal disc epithelium; TAS:FlyBase.
GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0007617; P:mating behavior; IMP:FlyBase.
GO; GO:0001738; P:morphogenesis of a polarized epithelium; TAS:FlyBase.
GO; GO:0002009; P:morphogenesis of an epithelium; TAS:FlyBase.
GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
GO; GO:0016335; P:morphogenesis of larval imaginal disc epithelium; TAS:FlyBase.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:FlyBase.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0007399; P:nervous system development; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:BHF-UCL.
GO; GO:0007318; P:pole plasm protein localization; IMP:BHF-UCL.
GO; GO:0046956; P:positive phototaxis; IMP:FlyBase.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0008104; P:protein localization; IMP:FlyBase.
GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
GO; GO:0030710; P:regulation of border follicle cell delamination; TAS:FlyBase.
GO; GO:0051726; P:regulation of cell cycle; NAS:FlyBase.
GO; GO:0042127; P:regulation of cell proliferation; TAS:FlyBase.
GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:FlyBase.
GO; GO:0046425; P:regulation of JAK-STAT cascade; IMP:BHF-UCL.
GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:BHF-UCL.
GO; GO:0019991; P:septate junction assembly; TAS:FlyBase.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IMP:FlyBase.
InterPro; IPR016313; DLG1-like.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR020590; Guanylate_kinase_CS.
InterPro; IPR015143; L27_1.
InterPro; IPR004172; L27_dom.
InterPro; IPR036892; L27_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF09058; L27_1; 1.
Pfam; PF00595; PDZ; 3.
Pfam; PF00018; SH3_1; 1.
PIRSF; PIRSF001741; MAGUK_DLGH; 1.
SMART; SM00072; GuKc; 1.
SMART; SM00569; L27; 1.
SMART; SM00228; PDZ; 3.
SMART; SM00326; SH3; 1.
SUPFAM; SSF101288; SSF101288; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS51022; L27; 1.
PROSITE; PS50106; PDZ; 3.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Membrane; Neurogenesis;
Phosphoprotein; Reference proteome; Repeat; SH3 domain; Transducer.
CHAIN 1 970 Disks large 1 tumor suppressor protein.
/FTId=PRO_0000094538.
DOMAIN 4 64 L27. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 216 303 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 330 421 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 506 587 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 620 690 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 780 955 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 714 714 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1 92 MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIF
KSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWE
KDGQAVKIAD -> MIDWVSIVRHSRRRFSNYVGSRSPVRM
RRRRRQLTAPPPQQQQQQHYHQQQQQDQHQSRERQKKDKEK
EKETEKDNESGGGIGSRYACCCAN (in isoform K).
{ECO:0000305}.
/FTId=VSP_039402.
VAR_SEQ 1 37 MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERV ->
MTTRKKKRDGGGSGGGFIKKVSSLFNLDSLHKASSTK (in
isoform A). {ECO:0000305}.
/FTId=VSP_011403.
VAR_SEQ 1 29 MPVKKQEAHRALELLEDYHARLSEPQDRA -> MTTRKKKR
DGGGSGGGFIKKVSSLFNLDS (in isoform E and
isoform G). {ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:1651169,
ECO:0000303|Ref.6}.
/FTId=VSP_011402.
VAR_SEQ 1 7 MPVKKQE -> MDSDTDSEREKSSDPNEGLLSSDDKTFHDD
DEPAEDSSPADDEEEPEEEECLLPQKKAQIRCDQDQPPLVV
LVQPSAEAIEVRQEIDDTNPVAVAAKASDMDGDSQLEVMEH
QMETVTEPDPEPPKCPTSLRDSVRESVECFYSAQDLLEYGH
MLSSTSMVRTPDVESGYFEKSESDASRDEWEGPSSSSSGAA
RCRLLSGISGLSVSSSSRHSAEGLRMELSRFRTMIETLERE
SLEKSQSELQLKAKSKAKPKPKQRSHVQDAAGESGSEQGSE
RGFWSTIFGQAGLAISQDEEERIADIQK (in isoform
F). {ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12657668}.
/FTId=VSP_011401.
VAR_SEQ 30 205 Missing (in isoform E and isoform G).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:1651169,
ECO:0000303|Ref.6}.
/FTId=VSP_011404.
VAR_SEQ 38 205 Missing (in isoform A). {ECO:0000305}.
/FTId=VSP_011405.
VAR_SEQ 93 151 Missing (in isoform I, isoform H, isoform
K and isoform L).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12657668}.
/FTId=VSP_011406.
VAR_SEQ 205 205 T -> TLHKASSTK (in isoform L).
{ECO:0000303|PubMed:12657668}.
/FTId=VSP_011407.
VAR_SEQ 206 267 VNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIY
ITKLISGGAAAADGRLSINDI -> SQIQIQSLTQTYPNAH
QRKRVLVSLHPHQHQHQSQIQHQHHYQLRHNNGIQAKMLKR
AFEST (in isoform I).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12657668}.
/FTId=VSP_011408.
VAR_SEQ 268 970 Missing (in isoform I).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12657668}.
/FTId=VSP_011409.
VAR_SEQ 473 519 EPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGP
QGLGFN -> AFMLCYTQDDANAEGGEIIYRVELPDMEQIT
LIYLENNDADYRKSSI (in isoform F).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12657668}.
/FTId=VSP_011411.
VAR_SEQ 473 473 E -> GALNSMGQTVVDSPSIPQAAAAVAAAANASASASVI
ASNNTISNTTVTTVTATATASNSSSKLPPSLGANSSISISN
SNSNSNSNNINNINSINNNNSSSSSTTATVAAATPTAASAA
AAAASSPPANSFYNNASMPALPVESNQTNNRSQSPQPRQ
(in isoform A, isoform E and isoform G).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:1651169,
ECO:0000303|Ref.6}.
/FTId=VSP_011410.
VAR_SEQ 520 970 Missing (in isoform F).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12657668}.
/FTId=VSP_011412.
VAR_SEQ 746 746 P -> PNGVVSSTSEIDINNVNNNQSNEPQP (in
isoform G). {ECO:0000303|PubMed:12537569,
ECO:0000303|Ref.6}.
/FTId=VSP_011413.
VAR_SEQ 747 761 FMLCYTQDDANAEGA -> NGVVSSTSEIDINNVNNNQSNE
PQP (in isoform A and isoform E).
{ECO:0000303|PubMed:1651169}.
/FTId=VSP_011414.
VAR_SEQ 761 761 A -> GEIIYRVELPDMEQITLIYLENNDADYP (in
isoform L).
{ECO:0000303|PubMed:12657668}.
/FTId=VSP_011415.
CONFLICT 365 365 M -> T (in Ref. 1; AAA28468 and 2;
AAQ01226). {ECO:0000305}.
CONFLICT 369 369 A -> R (in Ref. 1; AAA28468 and 2;
AAQ01226). {ECO:0000305}.
CONFLICT 395 395 E -> G (in Ref. 6; ACV53090).
{ECO:0000305}.
HELIX 8 10 {ECO:0000244|PDB:4RP3}.
HELIX 11 21 {ECO:0000244|PDB:4RP3}.
HELIX 25 27 {ECO:0000244|PDB:4RP3}.
HELIX 28 58 {ECO:0000244|PDB:4RP3}.
TURN 59 61 {ECO:0000244|PDB:4RP3}.
HELIX 67 83 {ECO:0000244|PDB:4RP3}.
HELIX 84 86 {ECO:0000244|PDB:4RP3}.
STRAND 87 90 {ECO:0000244|PDB:4RP3}.
STRAND 624 627 {ECO:0000244|PDB:3TVT}.
STRAND 651 656 {ECO:0000244|PDB:3TVT}.
STRAND 659 665 {ECO:0000244|PDB:3TVT}.
STRAND 679 681 {ECO:0000244|PDB:3TVT}.
HELIX 683 691 {ECO:0000244|PDB:3TVT}.
STRAND 769 776 {ECO:0000244|PDB:3TVT}.
STRAND 783 787 {ECO:0000244|PDB:3TVT}.
HELIX 790 800 {ECO:0000244|PDB:3TVT}.
TURN 802 804 {ECO:0000244|PDB:3TVT}.
TURN 822 824 {ECO:0000244|PDB:3TVT}.
HELIX 832 840 {ECO:0000244|PDB:3TVT}.
STRAND 844 850 {ECO:0000244|PDB:3TVT}.
STRAND 853 858 {ECO:0000244|PDB:3TVT}.
HELIX 859 868 {ECO:0000244|PDB:3TVT}.
STRAND 871 874 {ECO:0000244|PDB:3TVT}.
HELIX 879 886 {ECO:0000244|PDB:3TVT}.
STRAND 892 896 {ECO:0000244|PDB:3TVT}.
HELIX 901 906 {ECO:0000244|PDB:3TVT}.
HELIX 915 930 {ECO:0000244|PDB:3TVT}.
TURN 931 933 {ECO:0000244|PDB:3TVT}.
STRAND 935 938 {ECO:0000244|PDB:3TVT}.
HELIX 943 957 {ECO:0000244|PDB:3TVT}.
STRAND 960 965 {ECO:0000244|PDB:3TVT}.
SEQUENCE 970 AA; 106673 MW; 544D1E1AD03B0674 CRC64;
MPVKKQEAHR ALELLEDYHA RLSEPQDRAL RIAIERVIRI FKSRLFQALL DIQEFYELTL
LDDSKSIQQK TAETLQIATK WEKDGQAVKI ADFIKSSNLN RNCAYEFNND ASSNQTNQSA
LNQNPIANNV SAQAQAEALS RTFKSELEEI LNQRMRIESD TENAKEPTVE QQQKQQQAQQ
RSSRSPQQQN PQQQQGSKSR SGSQTVNGDD SWLYEDIQLE RGNSGLGFSI AGGTDNPHIG
TDTSIYITKL ISGGAAAADG RLSINDIIVS VNDVSVVDVP HASAVDALKK AGNVVKLHVK
RKRGTATTPA AGSAAGDARD SAASGPKVIE IDLVKGGKGL GFSIAGGIGN QHIPGDNGIY
VTKLMDGGAA QVDGRLSIGD KLIAVRTNGS EKNLENVTHE LAVATLKSIT DKVTLIIGKT
QHLTTSASGG GGGGLSSGQQ LSQSQSQLAT SQSQSQVHQQ QHATPMVNSQ STEPGSRYAS
TNVLAAVPPG TPRAVSTEDI TREPRTITIQ KGPQGLGFNI VGGEDGQGIY VSFILAGGPA
DLGSELKRGD QLLSVNNVNL THATHEEAAQ ALKTSGGVVT LLAQYRPEEY NRFEARIQEL
KQQAALGAGG SGTLLRTTQK RSLYVRALFD YDPNRDDGLP SRGLPFKHGD ILHVTNASDD
EWWQARRVLG DNEDEQIGIV PSKRRWERKM RARDRSVKFQ GHAAANNNLD KQSTLDRKKK
NFTFSRKFPF MKSRDEKNED GSDQEPFMLC YTQDDANAEG ASEENVLSYE AVQRLSINYT
RPVIILGPLK DRINDDLISE YPDKFGSCVP HTTRPKREYE VDGRDYHFVS SREQMERDIQ
NHLFIEAGQY NDNLYGTSVA SVREVAEKGK HCILDVSGNA IKRLQVAQLY PVAVFIKPKS
VDSVMEMNRR MTEEQAKKTY ERAIKMEQEF GEYFTGVVQG DTIEEIYSKV KSMIWSQSGP
TIWVPSKESL


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