DLG5_HUMAN
ID DLG5_HUMAN Reviewed; 1919 AA.
AC Q8TDM6; A6H8Y3; Q149N1; Q5T1H7; Q5T1H8; Q6DKG3; Q86WC0; Q8TDM7; Q9UE73;
AC Q9Y4E3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Disks large homolog 5;
DE AltName: Full=Discs large protein P-dlg;
DE AltName: Full=Placenta and prostate DLG;
GN Name=DLG5; Synonyms=KIAA0583, PDLG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, AND INTERACTION
RP WITH MPP1.
RC TISSUE=Fetal brain;
RX PubMed=9738934; DOI=10.1016/s0014-5793(98)00882-5;
RA Nakamura H., Sudo T., Tsuiki H., Miyake H., Morisaki T., Sasaki J.,
RA Masuko N., Kochi M., Ushio Y., Saya H.;
RT "Identification of a novel human homolog of the Drosophila dlg, P-dlg,
RT specifically expressed in the gland tissues and interacting with p55.";
RL FEBS Lett. 433:63-67(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4), TISSUE SPECIFICITY,
RP AND VARIANT ARG-140.
RX PubMed=11876824; DOI=10.1186/1471-2164-3-6;
RA Shah G., Brugada R., Gonzalez O., Czernuszewicz G., Gibbs R.A.,
RA Bachinski L., Roberts R.;
RT "The cloning, genomic organization and tissue expression profile of the
RT human DLG5 gene.";
RL BMC Genomics 3:6-6(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-140.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Ishikawa K.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1075-1919 (ISOFORM 3), AND VARIANTS ARG-140 AND
RP GLN-1481.
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-1919 (ISOFORM 1), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH SORBS3 AND CTNNB1.
RX PubMed=12657639; DOI=10.1074/jbc.m211004200;
RA Wakabayashi M., Ito T., Mitsushima M., Aizawa S., Ueda K., Amachi T.,
RA Kioka N.;
RT "Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase
RT family protein, with vinexin and beta-catenin at sites of cell-cell
RT contact.";
RL J. Biol. Chem. 278:21709-21714(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-900; THR-984;
RP SER-1000; THR-1011; SER-1021; THR-1183; SER-1209; SER-1263; SER-1334 AND
RP SER-1666, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, AND INTERACTION WITH STK3; STK4 AND MARK3.
RX PubMed=28087714; DOI=10.1101/gad.284539.116;
RA Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S.,
RA Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.;
RT "DLG5 connects cell polarity and Hippo signaling protein networks by
RT linking PAR-1 with MST1/2.";
RL Genes Dev. 30:2696-2709(2016).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SCRIB, AND TISSUE
RP SPECIFICITY.
RX PubMed=28169360; DOI=10.1038/srep42125;
RA Liu J., Li J., Li P., Wang Y., Liang Z., Jiang Y., Li J., Feng C., Wang R.,
RA Chen H., Zhou C., Zhang J., Yang J., Liu P.;
RT "Loss of DLG5 promotes breast cancer malignancy by inhibiting the Hippo
RT signaling pathway.";
RL Sci. Rep. 7:42125-42125(2017).
RN [14]
RP STRUCTURE BY NMR OF 1224-1330.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-006, the third PDZ domain of HDLG5
RT (KIAA0583) protein [Homo sapiens].";
RL Submitted (JAN-2004) to the PDB data bank.
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-140.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
CC -!- FUNCTION: Acts as a regulator of the Hippo signaling pathway
CC (PubMed:28087714, PubMed:28169360). Negatively regulates the Hippo
CC signaling pathway by mediating the interaction of MARK3 with STK3/4,
CC bringing them together to promote MARK3-dependent hyperphosphorylation
CC and inactivation of STK3 kinase activity toward LATS1
CC (PubMed:28087714). Positively regulates the Hippo signaling pathway by
CC mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is
CC important for the activation of the Hippo signaling pathway. Involved
CC in regulating cell proliferation, maintenance of epithelial polarity,
CC epithelial-mesenchymal transition (EMT), cell migration and invasion
CC (PubMed:28169360). Plays an important role in dendritic spine formation
CC and synaptogenesis in cortical neurons; regulates synaptogenesis by
CC enhancing the cell surface localization of N-cadherin. Acts as a
CC positive regulator of hedgehog (Hh) signaling pathway. Plays a critical
CC role in the early point of the SMO activity cycle by interacting with
CC SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at
CC the ciliary tip for GLI2 activation (By similarity).
CC {ECO:0000250|UniProtKB:E9Q9R9, ECO:0000269|PubMed:28087714,
CC ECO:0000269|PubMed:28169360}.
CC -!- SUBUNIT: Interacts with MPP1 (PubMed:9738934). Interacts with CTNNB1
CC and with the third SH3 domain of SORBS3 to form a ternary complex
CC (PubMed:12657639). Interacts (via coiled-coil domain) with MARK3.
CC Interacts (via PDZ domain 3) with STK3/MST2 and STK4/MST1
CC (PubMed:28087714). Interacts with SCRIB (PubMed:28169360). Interacts
CC with CTNB1, SMO and (via PDZ4 or guanylate kinase-like domain) with
CC KIF7 (By similarity). {ECO:0000250|UniProtKB:E9Q9R9,
CC ECO:0000269|PubMed:12657639, ECO:0000269|PubMed:28087714,
CC ECO:0000269|PubMed:28169360, ECO:0000269|PubMed:9738934}.
CC -!- INTERACTION:
CC Q8TDM6; Q64729: Tgfbr1; Xeno; NbExp=3; IntAct=EBI-715138, EBI-2899393;
CC Q8TDM6; Q62312: Tgfbr2; Xeno; NbExp=3; IntAct=EBI-715138, EBI-2899332;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:12657639,
CC ECO:0000269|PubMed:28169360}. Cell membrane
CC {ECO:0000269|PubMed:12657639}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12657639}. Postsynaptic density
CC {ECO:0000250|UniProtKB:E9Q9R9}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:E9Q9R9}. Note=Localized at sites of cell-
CC cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8TDM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDM6-2; Sequence=VSP_016349;
CC Name=3;
CC IsoId=Q8TDM6-3; Sequence=VSP_027199, VSP_027200, VSP_027201;
CC Name=4;
CC IsoId=Q8TDM6-4; Sequence=VSP_027197;
CC Name=5;
CC IsoId=Q8TDM6-5; Sequence=VSP_027198;
CC -!- TISSUE SPECIFICITY: Highly expressed in normal breast tissues and low-
CC grade breast cancer tissues (at protein level) (PubMed:28169360).
CC Highly expressed in the placenta and prostate. Expressed at a lower
CC level in the thyroid, spinal cord, trachea, adrenal gland, skeletal
CC muscle, pancreas, heart, brain, liver and kidney. A short splice
CC product shows more limited expression, being absent from at least the
CC brain. {ECO:0000269|PubMed:11876824, ECO:0000269|PubMed:12657639,
CC ECO:0000269|PubMed:28169360, ECO:0000269|PubMed:9738934}.
CC -!- DOMAIN: The guanylate kinase-like domain interacts with the SH3 domain.
CC {ECO:0000250|UniProtKB:E9Q9R9}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI17696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25509.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U61843; AAC61295.1; -; mRNA.
DR EMBL; AF352033; AAL83937.1; -; Genomic_DNA.
DR EMBL; AF352034; AAL83938.1; -; mRNA.
DR EMBL; AB011155; BAA25509.2; ALT_INIT; mRNA.
DR EMBL; AL391421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC073996; AAH73996.1; -; mRNA.
DR EMBL; BC117695; AAI17696.1; ALT_INIT; mRNA.
DR EMBL; BC146794; AAI46795.1; -; mRNA.
DR EMBL; AB091676; BAC65420.1; -; mRNA.
DR CCDS; CCDS7353.2; -. [Q8TDM6-1]
DR PIR; T00346; T00346.
DR RefSeq; NP_004738.3; NM_004747.3. [Q8TDM6-1]
DR RefSeq; XP_006718119.1; XM_006718056.3. [Q8TDM6-2]
DR RefSeq; XP_011538647.1; XM_011540345.1.
DR RefSeq; XP_016872403.1; XM_017016914.1. [Q8TDM6-4]
DR PDB; 1UIT; NMR; -; A=1336-1439.
DR PDBsum; 1UIT; -.
DR AlphaFoldDB; Q8TDM6; -.
DR SMR; Q8TDM6; -.
DR BioGRID; 114662; 144.
DR ComplexPortal; CPX-6187; Scribble cell polarity complex, DLG5-LLGL2-SCRIB variant.
DR ComplexPortal; CPX-6188; Scribble cell polarity complex, DLG5-LLGL1-SCRIB variant.
DR CORUM; Q8TDM6; -.
DR DIP; DIP-41450N; -.
DR IntAct; Q8TDM6; 45.
DR MINT; Q8TDM6; -.
DR STRING; 9606.ENSP00000361467; -.
DR GlyGen; Q8TDM6; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8TDM6; -.
DR PhosphoSitePlus; Q8TDM6; -.
DR BioMuta; DLG5; -.
DR DMDM; 158939323; -.
DR EPD; Q8TDM6; -.
DR jPOST; Q8TDM6; -.
DR MassIVE; Q8TDM6; -.
DR MaxQB; Q8TDM6; -.
DR PaxDb; Q8TDM6; -.
DR PeptideAtlas; Q8TDM6; -.
DR PRIDE; Q8TDM6; -.
DR ProteomicsDB; 74302; -. [Q8TDM6-1]
DR ProteomicsDB; 74303; -. [Q8TDM6-2]
DR ProteomicsDB; 74304; -. [Q8TDM6-3]
DR ProteomicsDB; 74305; -. [Q8TDM6-4]
DR ProteomicsDB; 74306; -. [Q8TDM6-5]
DR Antibodypedia; 618; 103 antibodies from 18 providers.
DR DNASU; 9231; -.
DR Ensembl; ENST00000372391.7; ENSP00000361467.2; ENSG00000151208.17. [Q8TDM6-1]
DR Ensembl; ENST00000614211.2; ENSP00000484894.1; ENSG00000274429.2. [Q8TDM6-1]
DR GeneID; 9231; -.
DR KEGG; hsa:9231; -.
DR MANE-Select; ENST00000372391.7; ENSP00000361467.2; NM_004747.4; NP_004738.3.
DR UCSC; uc001jzk.4; human. [Q8TDM6-1]
DR CTD; 9231; -.
DR DisGeNET; 9231; -.
DR GeneCards; DLG5; -.
DR HGNC; HGNC:2904; DLG5.
DR HPA; ENSG00000151208; Low tissue specificity.
DR MIM; 604090; gene.
DR neXtProt; NX_Q8TDM6; -.
DR OpenTargets; ENSG00000151208; -.
DR PharmGKB; PA27360; -.
DR VEuPathDB; HostDB:ENSG00000151208; -.
DR eggNOG; KOG0708; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155303; -.
DR HOGENOM; CLU_002448_1_0_1; -.
DR InParanoid; Q8TDM6; -.
DR OMA; QEHYMAD; -.
DR OrthoDB; 123652at2759; -.
DR PhylomeDB; Q8TDM6; -.
DR TreeFam; TF323171; -.
DR PathwayCommons; Q8TDM6; -.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q8TDM6; -.
DR BioGRID-ORCS; 9231; 102 hits in 1080 CRISPR screens.
DR ChiTaRS; DLG5; human.
DR EvolutionaryTrace; Q8TDM6; -.
DR GeneWiki; DLG5; -.
DR GenomeRNAi; 9231; -.
DR Pharos; Q8TDM6; Tbio.
DR PRO; PR:Q8TDM6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8TDM6; protein.
DR Bgee; ENSG00000151208; Expressed in ventricular zone and 97 other tissues.
DR ExpressionAtlas; Q8TDM6; baseline and differential.
DR Genevisible; Q8TDM6; HS.
DR GO; GO:0005912; C:adherens junction; IC:ComplexPortal.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IC:ComplexPortal.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0071896; P:protein localization to adherens junction; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0045186; P:zonula adherens assembly; IEA:Ensembl.
DR CDD; cd11860; SH3_DLG5; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.30.42.10; -; 4.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR035537; DLG5_SH3.
DR InterPro; IPR006907; DUF622.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF04822; Takusan; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 4.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 4.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 4.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1..1919
FT /note="Disks large homolog 5"
FT /id="PRO_0000094564"
FT DOMAIN 620..710
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 705..796
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1350..1429
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1501..1582
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1593..1661
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1722..1905
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 98..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..599
FT /evidence="ECO:0000255"
FT COMPBIAS 102..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1016
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 984
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1011
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1245
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9738934"
FT /id="VSP_027198"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11876824"
FT /id="VSP_027197"
FT VAR_SEQ 130..580
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027199"
FT VAR_SEQ 795..1134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_016349"
FT VAR_SEQ 1135
FT /note="E -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027200"
FT VAR_SEQ 1136..1919
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027201"
FT VARIANT 140
FT /note="Q -> R (in dbSNP:rs1248696)"
FT /evidence="ECO:0000269|PubMed:11876824,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18987736,
FT ECO:0000269|PubMed:9628581"
FT /id="VAR_027897"
FT VARIANT 1481
FT /note="P -> Q (in dbSNP:rs2289310)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027898"
FT VARIANT 1600
FT /note="A -> V (in dbSNP:rs4979794)"
FT /id="VAR_027899"
FT STRAND 1349..1354
FT /evidence="ECO:0007829|PDB:1UIT"
FT STRAND 1362..1366
FT /evidence="ECO:0007829|PDB:1UIT"
FT STRAND 1372..1377
FT /evidence="ECO:0007829|PDB:1UIT"
FT HELIX 1382..1386
FT /evidence="ECO:0007829|PDB:1UIT"
FT TURN 1402..1404
FT /evidence="ECO:0007829|PDB:1UIT"
FT HELIX 1407..1413
FT /evidence="ECO:0007829|PDB:1UIT"
FT STRAND 1419..1425
FT /evidence="ECO:0007829|PDB:1UIT"
SQ SEQUENCE 1919 AA; 213868 MW; CC19273380260C92 CRC64;
MEPQRRELLA QCQQSLAQAM TEVEAVLGLL EAAGALSPGE RRQLDEEAGG AKAELLLKLL
LAKERDHFQD LRAALEKTQP HLLPILYLNG VVGPPQPAEG AGSTYSVLST MPSDSESSSS
LSSVGTTGKA PSPPPLLTDQ QVNEKVENLS IQLRLMTRER NELRKRLAFA THGTAFDKRP
YHRLNPDYER LKIQCVRAMS DLQSLQNQHT NALKRCEEVA KETDFYHTLH SRLLSDQTRL
KDDVDMLRRE NGQLLRERNL LQQSWEDMKR LHEEDQKEIG DLRAQQQQVL KHNGSSEILN
KLYDTAMDKL EVVKKDYDAL RKRYSEKVAI HNADLSRLEQ LGEENQRLLK QTEMLTQQRD
TAIQLQHQCA LSLRRFEAIH HELNKATAQN KDLQWEMELL QSELTELRTT QVKTAKESEK
YREERDAVYS EYKLIMSERD QVISELDKLQ TEVELAESKL KSSTSEKKAA NEEMEALRQI
KDTVTMDAGR ANKEVEILRK QCKALCQELK EALQEADVAK CRRDWAFQER DKIVAERDSI
RTLCDNLRRE RDRAVSELAE ALRSLDDTRK QKNDVSRELK ELKEQMESQL EKEARFRQLM
AHSSHDSAID TDSMEWETEV VEFERETEDI DLKALGFDMA EGVNEPCFPG DCGIFVTKVD
KGSIADGRLR VNDWLLRIND VDLINKDKKQ AIKALLNGEG AINMVVRRRK SLGGKVVTPL
HINLSGQKDS GISLENGVYA AAVLPGSPAA KEGSLAVGDR IVAINGIALD NKSLNECESL
LRSCQDSLTL SLLKVFPQSS SWSGQNIFEN IKDSDKMLSF RAHGPEVQAH NKRNLIQHNN
STQTDIFYTD RLEDRKEPGP PGGSSSFLHK PFPGGPLQVC PQACPSASER SLSSFRSDAS
GDRGFGLVDV RGRRPLLPFE TEVGPCGVGE ASLDKADSEG SNSGGTWPKA MLSSTAVPEK
LSVYKKPKQR KSIFDPNTFK RPQTPPKIDY LLPGPGPAHS PQPSKRAGPL TPPKPPRRSD
SIKFQHRLET SSESEATLVG SSPSTSPPSA LPPDVDPGEP MHASPPRKAR VRIASSYYPE
GDGDSSHLPA KKSCDEDLTS QKVDELGQKR RRPKSAPSFR PKLAPVVIPA QFLEEQKCVP
ASGELSPELQ EWAPYSPGHS SRHSNPPLYP SRPSVGTVPR SLTPSTTVSS ILRNPIYTVR
SHRVGPCSSP PAARDAGPQG LHPSVQHQGR LSLDLSHRTC SDYSEMRATH GSNSLPSSAR
LGSSSNLQFK AERIKIPSTP RYPRSVVGSE RGSVSHSECS TPPQSPLNID TLSSCSQSQT
SASTLPRIAV NPASLGERRK DRPYVEEPRH VKVQKGSEPL GISIVSGEKG GIYVSKVTVG
SIAHQAGLEY GDQLLEFNGI NLRSATEQQA RLIIGQQCDT ITILAQYNPH VHQLSSHSRS
SSHLDPAGTH STLQGSGTTT PEHPSVIDPL MEQDEGPSTP PAKQSSSRIA GDANKKTLEP
RVVFIKKSQL ELGVHLCGGN LHGVFVAEVE DDSPAKGPDG LVPGDLILEY GSLDVRNKTV
EEVYVEMLKP RDGVRLKVQY RPEEFTKAKG LPGDSFYIRA LYDRLADVEQ ELSFKKDDIL
YVDDTLPQGT FGSWMAWQLD ENAQKIQRGQ IPSKYVMDQE FSRRLSMSEV KDDNSATKTL
SAAARRSFFR RKHKHKRSGS KDGKDLLALD AFSSDSIPLF EDSVSLAYQR VQKVDCTALR
PVLILGPLLD VVKEMLVNEA PGKFCRCPLE VMKASQQAIE RGVKDCLFVD YKRRSGHFDV
TTVASIKEIT EKNRHCLLDI APHAIERLHH MHIYPIVIFI HYKSAKHIKE QRDPIYLRDK
VTQRHSKEQF EAAQKLEQEY SRYFTGVIQG GALSSICTQI LAMVNQEQNK VLWIPACPL
