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 27-MAR-2024, entry version 212. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 175. 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; 58. DR MINT; Q8TDM6; -. DR STRING; 9606.ENSP00000361467; -. DR GlyCosmos; Q8TDM6; 3 sites, 1 glycan. DR GlyGen; Q8TDM6; 7 sites, 2 O-linked glycans (7 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; 9606-ENSP00000361467; -. DR PeptideAtlas; 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 Pumba; Q8TDM6; -. DR Antibodypedia; 618; 128 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 AGR; HGNC:2904; -. 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; 2877432at2759; -. 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 SIGNOR; Q8TDM6; -. DR BioGRID-ORCS; 9231; 108 hits in 1167 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 99 other cell types or tissues. DR ExpressionAtlas; Q8TDM6; baseline and differential. DR GO; GO:0005912; C:adherens junction; NAS:ComplexPortal. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. 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; NAS: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:0099173; P:postsynapse organization; IEA:Ensembl. 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; cd00992; PDZ_signaling; 4. DR CDD; cd11860; SH3_DLG5; 1. DR Gene3D; 2.30.42.10; -; 4. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001315; CARD. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR006907; DLG5_N. DR InterPro; IPR035537; DLG5_SH3. 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 PANTHER; PTHR46360; DISKS LARGE HOMOLOG 5; 1. DR PANTHER; PTHR46360:SF1; DISKS LARGE HOMOLOG 5; 1. DR Pfam; PF16610; dbPDZ_assoc; 1. 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; DEATH domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 4. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50209; CARD; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 4. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q8TDM6; HS. 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 //