Full text data of DLG1
DLG1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Disks large homolog 1 (Synapse-associated protein 97; SAP-97; SAP97; hDlg)
Disks large homolog 1 (Synapse-associated protein 97; SAP-97; SAP97; hDlg)
UniProt
Q12959
ID DLG1_HUMAN Reviewed; 904 AA.
AC Q12959; A5YKK7; B4DGU1; B4DGZ8; B7ZMM0; B9EIQ5; D3DXB8; D3DXB9;
read moreAC E7EWL7; E9PG21; Q12958;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 22-JAN-2014, entry version 160.
DE RecName: Full=Disks large homolog 1;
DE AltName: Full=Synapse-associated protein 97;
DE Short=SAP-97;
DE Short=SAP97;
DE AltName: Full=hDlg;
GN Name=DLG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EPB41, AND VARIANT
RP GLN-278.
RX PubMed=7937897; DOI=10.1073/pnas.91.21.9818;
RA Lue R.A., Marfatia S.M., Branton D., Chishti A.H.;
RT "Cloning and characterization of hdlg: the human homologue of the
RT Drosophila discs large tumor suppressor binds to protein 4.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9), AND VARIANT
RP GLN-278.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH KCNA1; KCNA2; KCNA3 AND KCNA4.
RX PubMed=7477295; DOI=10.1038/378085a0;
RA Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.;
RT "Clustering of Shaker-type K+ channels by interaction with a family of
RT membrane-associated guanylate kinases.";
RL Nature 378:85-88(1995).
RN [8]
RP INTERACTION WITH EPB41, AND SUBCELLULAR LOCATION.
RX PubMed=8922391; DOI=10.1083/jcb.135.4.1125;
RA Lue R.A., Brandin E., Chan E.P., Branton D.;
RT "Two independent domains of hDlg are sufficient for subcellular
RT targeting: the PDZ1-2 conformational unit and an alternatively spliced
RT domain.";
RL J. Cell Biol. 135:1125-1137(1996).
RN [9]
RP INTERACTION WITH APC.
RX PubMed=8638125; DOI=10.1126/science.272.5264.1020;
RA Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H.,
RA Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.;
RT "Binding of APC to the human homolog of the Drosophila discs large
RT tumor suppressor protein.";
RL Science 272:1020-1023(1996).
RN [10]
RP INTERACTION WITH VIRAL ONCOPROTEIN TAX AND HPV-18 E6.
RX PubMed=9192623; DOI=10.1073/pnas.94.13.6670;
RA Lee S.S., Weiss R.S., Javier R.T.;
RT "Binding of human virus oncoproteins to hDlg/SAP97, a mammalian
RT homolog of the Drosophila discs large tumor suppressor protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997).
RN [11]
RP INTERACTION WITH HTLV-1 TAX-1.
RX PubMed=10557085; DOI=10.1038/sj.onc.1203008;
RA Suzuki T., Ohsugi Y., Uchida-Toita M., Akiyama T., Yoshida M.;
RT "Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila
RT discs large tumor suppressor protein, hDLG, and perturbs its function
RT in cell growth control.";
RL Oncogene 18:5967-5972(1999).
RN [12]
RP INTERACTION WITH KIF13B, AND SUBCELLULAR LOCATION.
RX PubMed=10859302; DOI=10.1074/jbc.M000715200;
RA Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H.;
RT "GAKIN, a novel kinesin-like protein associates with the human
RT homologue of the Drosophila discs large tumor suppressor in T
RT lymphocytes.";
RL J. Biol. Chem. 275:28774-28784(2000).
RN [13]
RP INTERACTION WITH APC, AND FUNCTION IN CELL PROLIFERATION.
RX PubMed=10656683; DOI=10.1038/sj.onc.1203309;
RA Ishidate T., Matsumine A., Toyoshima K., Akiyama T.;
RT "The APC-hDLG complex negatively regulates cell cycle progression from
RT the G0/G1 to S phase.";
RL Oncogene 19:365-372(2000).
RN [14]
RP INTERACTION WITH TOPK.
RX PubMed=10779557; DOI=10.1073/pnas.090102397;
RA Gaudet S., Branton D., Lue R.A.;
RT "Characterization of PDZ-binding kinase, a mitotic kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000).
RN [15]
RP POSSIBLE INTERACTION WITH TJAP1.
RX PubMed=11602598; DOI=10.1074/jbc.M107335200;
RA Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K.,
RA Takeuchi M., Takai Y.;
RT "Pilt, a novel peripheral membrane protein at tight junctions in
RT epithelial cells.";
RL J. Biol. Chem. 276:48350-48355(2001).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH KCNF1.
RX PubMed=12445884; DOI=10.1016/S0008-6363(02)00602-8;
RA Godreau D., Vranckx R., Maguy A., Rucker-Martin C., Goyenvalle C.,
RA Abdelshafy S., Tessier S., Couetil J.P., Hatem S.N.;
RT "Expression, regulation and role of the MAGUK protein SAP-97 in human
RT atrial myocardium.";
RL Cardiovasc. Res. 56:433-442(2002).
RN [17]
RP ALTERNATIVE SPLICING (ISOFORMS 5; 6 AND 7), AND SUBCELLULAR LOCATION.
RX PubMed=11723125; DOI=10.1074/jbc.M108724200;
RA McLaughlin M., Hale R., Ellston D., Gaudet S., Lue R.A., Viel A.;
RT "The distribution and function of alternatively spliced insertions in
RT hDlg.";
RL J. Biol. Chem. 277:6406-6412(2002).
RN [18]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 38-ILE--ILE-40.
RX PubMed=12807908; DOI=10.1074/jbc.M305209200;
RA Hanada T., Takeuchi A., Sondarva G., Chishti A.H.;
RT "Protein 4.1-mediated membrane targeting of human discs large in
RT epithelial cells.";
RL J. Biol. Chem. 278:34445-34450(2003).
RN [19]
RP INTERACTION WITH PIK3R1 AND CDH1, AND FUNCTION IN ADHERENS JUNCTION
RP ASSEMBLY.
RX PubMed=14699157; DOI=10.1074/jbc.M309843200;
RA Laprise P., Viel A., Rivard N.;
RT "Human homolog of disc-large is required for adherens junction
RT assembly and differentiation of human intestinal epithelial cells.";
RL J. Biol. Chem. 279:10157-10166(2004).
RN [20]
RP FUNCTION IN T-CELL ACTIVATION.
RX PubMed=15263016; DOI=10.1083/jcb.200309044;
RA Xavier R., Rabizadeh S., Ishiguro K., Andre N., Ortiz J.B.,
RA Wachtel H., Morris D.G., Lopez-Ilasaca M., Shaw A.C., Swat W.,
RA Seed B.;
RT "Discs large (Dlg1) complexes in lymphocyte activation.";
RL J. Cell Biol. 166:173-178(2004).
RN [21]
RP INTERACTION WITH GPR124 AND GPR125.
RX PubMed=15021905; DOI=10.1038/sj.onc.1207495;
RA Yamamoto Y., Irie K., Asada M., Mino A., Mandai K., Takai Y.;
RT "Direct binding of the human homologue of the Drosophila disc large
RT tumor suppressor gene to seven-pass transmembrane proteins, tumor
RT endothelial marker 5 (TEM5), and a novel TEM5-like protein.";
RL Oncogene 23:3889-3897(2004).
RN [22]
RP REVIEW.
RX PubMed=12766944; DOI=10.1002/bies.10286;
RA Humbert P., Russell S., Richardson H.;
RT "Dlg, Scribble and Lgl in cell polarity, cell proliferation and
RT cancer.";
RL Bioessays 25:542-553(2003).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [24]
RP INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
RA Kaang B.-K., Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the
RT differentiation of excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [25]
RP INTERACTION WITH LIN7A; LIN7C AND MPP7.
RX PubMed=17237226; DOI=10.1074/jbc.M610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7
RT and DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [26]
RP INTERACTION WITH MPP7.
RX PubMed=17332497; DOI=10.1091/mbc.E06-11-0980;
RA Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.;
RT "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and
RT facilitates epithelial tight junction formation.";
RL Mol. Biol. Cell 18:1744-1755(2007).
RN [27]
RP INTERACTION WITH FRMPD4.
RX PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
RA Kang G.B., Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575;
RP SER-684 AND SER-687, AND MASS SPECTROMETRY.
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 [30]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH KCND2 AND KCND3.
RX PubMed=19213956; DOI=10.1161/CIRCRESAHA.108.191007;
RA El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
RA Coulombe A., Jeromin A., Hatem S.N.;
RT "Kv4 potassium channels form a tripartite complex with the anchoring
RT protein SAP97 and CaMKII in cardiac myocytes.";
RL Circ. Res. 104:758-769(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [32]
RP PHOSPHORYLATION BY MAPK12, INTERACTION WITH SFPQ, AND FUNCTION.
RX PubMed=20605917; DOI=10.1242/jcs.066514;
RA Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A.,
RA Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A.;
RT "p38gamma regulates interaction of nuclear PSF and RNA with the
RT tumour-suppressor hDlg in response to osmotic shock.";
RL J. Cell Sci. 123:2596-2604(2010).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-568; SER-575
RP AND SER-687, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 460-555.
RX PubMed=8757139; DOI=10.1038/382649a0;
RA Cabral J.H., Petosa C., Sutcliffe M.J., Raza S., Byron O., Poy F.,
RA Marfatia S.M., Chishti A.H., Liddington R.C.;
RT "Crystal structure of a PDZ domain.";
RL Nature 382:649-652(1996).
CC -!- FUNCTION: Essential multidomain scaffolding protein required for
CC normal development (By similarity). Recruits channels, receptors
CC and signaling molecules to discrete plasma membrane domains in
CC polarized cells. May play a role in adherens junction assembly,
CC signal transduction, cell proliferation, synaptogenesis and
CC lymphocyte activation. Regulates the excitability of cardiac
CC myocytes by modulating the functional expression of Kv4 channels.
CC Functional regulator of Kv1.5 channel.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts through its guanylate
CC kinase-like domain with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A.
CC May interact with HTR2A (By similarity). Interacts with LRFN1 (By
CC similarity). Interacts through its PDZ domains with GRIN2A, KCNA1,
CC KCNA2, KCNA3, KCNA4, KCNA5, KCND2, KCND3, GRIA1, GPR124 and
CC GPR125. Interacts with KCNF1. Interacts with CAMK2 (By
CC similarity). Interacts with cytoskeleton-associated proteins EPB41
CC and EZR. Found in a complex with KCNA5 and CAV3. Found in a
CC complex with APC and CTNNB1. Interacts with CDH1 through binding
CC to PIK3R1. Forms multiprotein complexes with CASK, LIN7A, LIN7B,
CC LIN7C, APBA1, and KCNJ12. Interacts through its guanylate kinase-
CC like domain with KIF13B. Forms a tripartite complex composed of
CC DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with TJAP1.
CC Interacts with TOPK and the HTLV-1 viral Tax and HPV-18 E6
CC papillomavirus (HPV) oncoproteins. Interacts with PTEN (By
CC similarity). Interacts with FRMPD4 (via C-terminus). Interacts
CC with LRFN1, LRFN2, LRFN4 and SFPQ.
CC -!- INTERACTION:
CC P78536:ADAM17; NbExp=7; IntAct=EBI-357481, EBI-78188;
CC P31016:Dlg4 (xeno); NbExp=9; IntAct=EBI-357500, EBI-375655;
CC O57125:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-7461590;
CC P03126:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-1177242;
CC P06463:E6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-1186926;
CC P36799:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-7363822;
CC Q9NQT8:KIF13B; NbExp=3; IntAct=EBI-357500, EBI-766408;
CC O60333-3:KIF1B; NbExp=4; IntAct=EBI-357481, EBI-465669;
CC P36507:MAP2K2; NbExp=10; IntAct=EBI-357481, EBI-1056930;
CC Q9ICL1:se6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-7461477;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity). Basolateral cell membrane (By similarity).
CC Endoplasmic reticulum membrane (By similarity). Cell junction,
CC synapse, postsynaptic cell membrane, postsynaptic density (By
CC similarity). Cell junction, synapse. Cell membrane, sarcolemma.
CC Note=Colocalizes with EPB41 at regions of intercellular contacts.
CC Basolateral in epithelial cells. May also associate with
CC endoplasmic reticulum membranes. Mainly found in neurons soma,
CC moderately found at postsynaptic densities (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q12959-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12959-2; Sequence=VSP_003150;
CC Note=Contains a phosphoserine at position 698 (By similarity);
CC Name=3;
CC IsoId=Q12959-3; Sequence=VSP_012862;
CC Name=4;
CC IsoId=Q12959-4; Sequence=VSP_012862, VSP_003150;
CC Note=Contains a phosphoserine at position 665 (By similarity).
CC Ref.6 (AAI44652) sequence is in conflict in position:
CC 636:Q->Missing;
CC Name=5;
CC IsoId=Q12959-5; Sequence=VSP_012862, VSP_012863;
CC Name=6;
CC IsoId=Q12959-6; Sequence=VSP_012864;
CC Name=7;
CC IsoId=Q12959-7; Sequence=VSP_012865;
CC Name=8;
CC IsoId=Q12959-8; Sequence=VSP_045896, VSP_045897;
CC Note=No experimental confirmation available;
CC Name=9;
CC IsoId=Q12959-9; Sequence=VSP_045896, VSP_045897, VSP_012865,
CC VSP_045898;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in atrial myocardium (at
CC protein level). Expressed in lung fibroblasts, cervical epithelial
CC and B-cells (at protein level). Widely expressed, with isoforms
CC displaying different expression profiles.
CC -!- DOMAIN: The alternatively spliced domain I3 corresponding to amino
CC acids (636-669) of isoform 4 is an EPB41 binding site mediating
CC association to membranes in polarized and non-polarized cells.
CC -!- DOMAIN: The PDZ domains may also mediate association to membranes
CC by binding to EPB41 and GPR124 together with the L27 domain that
CC binds CASK and DLG2.
CC -!- DOMAIN: The L27 domain may regulate DLG1 self-association. The N-
CC terminal alternatively spliced region is capable of binding
CC several SH3 domains and also moderates the level of protein
CC oligomerization.
CC -!- PTM: Phosphorylated by MAPK12. Phosphorylation of Ser-232
CC regulates association with GRIN2A. Isoform 2 is phosphorylated on
CC Ser-698. Isoform 3 is phosphorylated on Ser-665 (By similarity).
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC -!- SIMILARITY: Contains 1 L27 domain.
CC -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DLG1ID40333ch3q29.html";
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DR EMBL; U13896; AAA50598.1; -; mRNA.
DR EMBL; U13897; AAA50599.1; -; mRNA.
DR EMBL; AK294772; BAG57902.1; -; mRNA.
DR EMBL; AK294855; BAG57959.1; -; mRNA.
DR EMBL; EF553524; ABQ66269.1; -; mRNA.
DR EMBL; AC068302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471191; EAW53610.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53611.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53612.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53614.1; -; Genomic_DNA.
DR EMBL; BC140841; AAI40842.1; -; mRNA.
DR EMBL; BC144651; AAI44652.1; -; mRNA.
DR PIR; I38756; I38756.
DR PIR; I38757; I38757.
DR RefSeq; NP_001091894.1; NM_001098424.1.
DR RefSeq; NP_001191315.1; NM_001204386.1.
DR RefSeq; NP_001191316.1; NM_001204387.1.
DR RefSeq; NP_001191317.1; NM_001204388.1.
DR RefSeq; NP_004078.2; NM_004087.2.
DR RefSeq; XP_005269346.1; XM_005269289.1.
DR RefSeq; XP_005269347.1; XM_005269290.1.
DR RefSeq; XP_005269348.1; XM_005269291.1.
DR RefSeq; XP_005269349.1; XM_005269292.1.
DR RefSeq; XP_005269350.1; XM_005269293.1.
DR RefSeq; XP_005269351.1; XM_005269294.1.
DR RefSeq; XP_005269352.1; XM_005269295.1.
DR RefSeq; XP_005269353.1; XM_005269296.1.
DR RefSeq; XP_005269355.1; XM_005269298.1.
DR RefSeq; XP_005269356.1; XM_005269299.1.
DR UniGene; Hs.292549; -.
DR PDB; 1PDR; X-ray; 2.80 A; A=457-552.
DR PDB; 2M3M; NMR; -; A=318-406.
DR PDB; 2OQS; NMR; -; A=318-405.
DR PDB; 2X7Z; X-ray; 2.00 A; A=311-407.
DR PDB; 3LRA; X-ray; 2.95 A; A=2-65.
DR PDB; 3RL7; X-ray; 2.30 A; A/B/C/D/E/F=220-317.
DR PDB; 3RL8; X-ray; 2.20 A; A/B/C/D/E=315-410.
DR PDB; 3W9Y; X-ray; 2.20 A; A=712-904.
DR PDB; 4AMH; X-ray; 2.30 A; A/B=315-405.
DR PDB; 4G69; X-ray; 2.00 A; A=310-407.
DR PDBsum; 1PDR; -.
DR PDBsum; 2M3M; -.
DR PDBsum; 2OQS; -.
DR PDBsum; 2X7Z; -.
DR PDBsum; 3LRA; -.
DR PDBsum; 3RL7; -.
DR PDBsum; 3RL8; -.
DR PDBsum; 3W9Y; -.
DR PDBsum; 4AMH; -.
DR PDBsum; 4G69; -.
DR ProteinModelPortal; Q12959; -.
DR SMR; Q12959; 2-65, 220-904.
DR IntAct; Q12959; 28.
DR MINT; MINT-107690; -.
DR STRING; 9606.ENSP00000345731; -.
DR PhosphoSite; Q12959; -.
DR DMDM; 223590196; -.
DR PaxDb; Q12959; -.
DR PRIDE; Q12959; -.
DR Ensembl; ENST00000314062; ENSP00000321087; ENSG00000075711.
DR Ensembl; ENST00000346964; ENSP00000345731; ENSG00000075711.
DR Ensembl; ENST00000357674; ENSP00000350303; ENSG00000075711.
DR Ensembl; ENST00000392382; ENSP00000376187; ENSG00000075711.
DR Ensembl; ENST00000419354; ENSP00000407531; ENSG00000075711.
DR Ensembl; ENST00000422288; ENSP00000413238; ENSG00000075711.
DR Ensembl; ENST00000443183; ENSP00000396658; ENSG00000075711.
DR Ensembl; ENST00000448528; ENSP00000391732; ENSG00000075711.
DR Ensembl; ENST00000450955; ENSP00000411278; ENSG00000075711.
DR Ensembl; ENST00000452595; ENSP00000398939; ENSG00000075711.
DR GeneID; 1739; -.
DR KEGG; hsa:1739; -.
DR UCSC; uc011bub.2; human.
DR CTD; 1739; -.
DR GeneCards; GC03M196769; -.
DR HGNC; HGNC:2900; DLG1.
DR HPA; CAB016307; -.
DR MIM; 601014; gene.
DR neXtProt; NX_Q12959; -.
DR PharmGKB; PA27356; -.
DR eggNOG; COG0194; -.
DR HOVERGEN; HBG107814; -.
DR KO; K12076; -.
DR OMA; QHITSNA; -.
DR OrthoDB; EOG79GT6P; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_13685; Neuronal System.
DR EvolutionaryTrace; Q12959; -.
DR GeneWiki; DLG1; -.
DR GenomeRNAi; 1739; -.
DR NextBio; 7051; -.
DR PMAP-CutDB; A5YKK7; -.
DR PRO; PR:Q12959; -.
DR ArrayExpress; Q12959; -.
DR Bgee; Q12959; -.
DR CleanEx; HS_DLG1; -.
DR Genevestigator; Q12959; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; TAS:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; TAS:BHF-UCL.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:tight junction; IDA:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; NAS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0016337; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0001771; P:immunological synapse formation; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0031579; P:membrane raft organization; IEA:Ensembl.
DR GO; GO:0007093; P:mitotic cell cycle checkpoint; NAS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; TAS:BHF-UCL.
DR GO; GO:0048608; P:reproductive structure development; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR GO; GO:0002369; P:T cell cytokine production; IEA:Ensembl.
DR GO; GO:0070830; P:tight junction assembly; IDA:BHF-UCL.
DR InterPro; IPR016313; DLG1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR004172; L27.
DR InterPro; IPR015143; L27_1.
DR InterPro; IPR019590; MAGUK_PEST_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR019583; PDZ_assoc.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23119; PTHR23119; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Complete proteome; Endoplasmic reticulum; Host-virus interaction;
KW Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
KW Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1 904 Disks large homolog 1.
FT /FTId=PRO_0000094548.
FT DOMAIN 4 64 L27.
FT DOMAIN 224 310 PDZ 1.
FT DOMAIN 319 405 PDZ 2.
FT DOMAIN 466 546 PDZ 3.
FT DOMAIN 581 651 SH3.
FT DOMAIN 714 889 Guanylate kinase-like.
FT REGION 162 212 Interaction with SH3 domains.
FT MOD_RES 115 115 Phosphothreonine.
FT MOD_RES 122 122 Phosphoserine.
FT MOD_RES 158 158 Phosphoserine.
FT MOD_RES 232 232 Phosphoserine (By similarity).
FT MOD_RES 399 399 Phosphotyrosine (By similarity).
FT MOD_RES 568 568 Phosphoserine.
FT MOD_RES 575 575 Phosphoserine.
FT MOD_RES 619 619 Phosphoserine.
FT MOD_RES 684 684 Phosphoserine.
FT MOD_RES 687 687 Phosphoserine.
FT VAR_SEQ 1 77 MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIF
FT QSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQ -> M
FT NYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSD
FT ELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSST (in
FT isoform 8 and isoform 9).
FT /FTId=VSP_045896.
FT VAR_SEQ 78 193 Missing (in isoform 8 and isoform 9).
FT /FTId=VSP_045897.
FT VAR_SEQ 162 194 Missing (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_012862.
FT VAR_SEQ 195 212 Missing (in isoform 5).
FT /FTId=VSP_012863.
FT VAR_SEQ 669 680 EIPDDMGSKGLK -> QSFNDKRKKNLFSRKFPFYKNKDQS
FT EQETSDADQ (in isoform 2 and isoform 4).
FT /FTId=VSP_003150.
FT VAR_SEQ 681 693 Missing (in isoform 6).
FT /FTId=VSP_012864.
FT VAR_SEQ 693 693 Y -> YLILITDEYGCSKG (in isoform 7 and
FT isoform 9).
FT /FTId=VSP_012865.
FT VAR_SEQ 694 694 Missing (in isoform 9).
FT /FTId=VSP_045898.
FT VARIANT 140 140 K -> R (in dbSNP:rs1802668).
FT /FTId=VAR_054334.
FT VARIANT 278 278 R -> Q (in dbSNP:rs1134986).
FT /FTId=VAR_054335.
FT VARIANT 899 899 P -> L (in dbSNP:rs34492126).
FT /FTId=VAR_054336.
FT MUTAGEN 38 40 INI->ANA: Loss of membrane association
FT and DLG2-binding.
FT CONFLICT 237 237 S -> N (in Ref. 2; BAG57902).
FT CONFLICT 801 801 E -> G (in Ref. 1; AAA50598/AAA50599).
FT HELIX 5 20
FT STRAND 24 26
FT HELIX 30 42
FT HELIX 44 55
FT TURN 60 62
FT STRAND 221 228
FT STRAND 233 239
FT STRAND 254 258
FT HELIX 263 267
FT STRAND 275 279
FT HELIX 289 298
FT STRAND 301 309
FT STRAND 317 323
FT STRAND 331 337
FT STRAND 348 353
FT HELIX 358 362
FT STRAND 370 374
FT STRAND 377 382
FT HELIX 384 392
FT STRAND 396 403
FT STRAND 465 470
FT STRAND 472 474
FT STRAND 477 482
FT STRAND 484 487
FT STRAND 489 494
FT HELIX 499 503
FT STRAND 510 515
FT HELIX 525 533
FT STRAND 537 545
FT HELIX 547 554
FT STRAND 717 721
FT HELIX 724 734
FT TURN 736 738
FT TURN 756 758
FT HELIX 766 774
FT STRAND 778 784
FT STRAND 787 792
FT HELIX 793 800
FT TURN 801 803
FT STRAND 805 808
FT HELIX 813 820
FT STRAND 826 830
FT HELIX 855 864
FT HELIX 865 867
FT STRAND 869 872
FT HELIX 877 892
FT HELIX 900 902
SQ SEQUENCE 904 AA; 100455 MW; 6722993A84D0F761 CRC64;
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL
LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH
ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP
VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG
SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH
KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT
NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI
VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT
IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL
PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF
NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYRGQEEYV LSYEPVNQQE VNYTRPVIIL
GPMKDRINDD LISEFPDKFG SCVPHTTRPK RDYEVDGRDY HFVTSREQME KDIQEHKFIE
AGQYNNHLYG TSVQSVREVA EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME
MNKRLTEEQA RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGSYIWVPA
KEKL
//
ID DLG1_HUMAN Reviewed; 904 AA.
AC Q12959; A5YKK7; B4DGU1; B4DGZ8; B7ZMM0; B9EIQ5; D3DXB8; D3DXB9;
read moreAC E7EWL7; E9PG21; Q12958;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 22-JAN-2014, entry version 160.
DE RecName: Full=Disks large homolog 1;
DE AltName: Full=Synapse-associated protein 97;
DE Short=SAP-97;
DE Short=SAP97;
DE AltName: Full=hDlg;
GN Name=DLG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EPB41, AND VARIANT
RP GLN-278.
RX PubMed=7937897; DOI=10.1073/pnas.91.21.9818;
RA Lue R.A., Marfatia S.M., Branton D., Chishti A.H.;
RT "Cloning and characterization of hdlg: the human homologue of the
RT Drosophila discs large tumor suppressor binds to protein 4.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9), AND VARIANT
RP GLN-278.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH KCNA1; KCNA2; KCNA3 AND KCNA4.
RX PubMed=7477295; DOI=10.1038/378085a0;
RA Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.;
RT "Clustering of Shaker-type K+ channels by interaction with a family of
RT membrane-associated guanylate kinases.";
RL Nature 378:85-88(1995).
RN [8]
RP INTERACTION WITH EPB41, AND SUBCELLULAR LOCATION.
RX PubMed=8922391; DOI=10.1083/jcb.135.4.1125;
RA Lue R.A., Brandin E., Chan E.P., Branton D.;
RT "Two independent domains of hDlg are sufficient for subcellular
RT targeting: the PDZ1-2 conformational unit and an alternatively spliced
RT domain.";
RL J. Cell Biol. 135:1125-1137(1996).
RN [9]
RP INTERACTION WITH APC.
RX PubMed=8638125; DOI=10.1126/science.272.5264.1020;
RA Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H.,
RA Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.;
RT "Binding of APC to the human homolog of the Drosophila discs large
RT tumor suppressor protein.";
RL Science 272:1020-1023(1996).
RN [10]
RP INTERACTION WITH VIRAL ONCOPROTEIN TAX AND HPV-18 E6.
RX PubMed=9192623; DOI=10.1073/pnas.94.13.6670;
RA Lee S.S., Weiss R.S., Javier R.T.;
RT "Binding of human virus oncoproteins to hDlg/SAP97, a mammalian
RT homolog of the Drosophila discs large tumor suppressor protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997).
RN [11]
RP INTERACTION WITH HTLV-1 TAX-1.
RX PubMed=10557085; DOI=10.1038/sj.onc.1203008;
RA Suzuki T., Ohsugi Y., Uchida-Toita M., Akiyama T., Yoshida M.;
RT "Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila
RT discs large tumor suppressor protein, hDLG, and perturbs its function
RT in cell growth control.";
RL Oncogene 18:5967-5972(1999).
RN [12]
RP INTERACTION WITH KIF13B, AND SUBCELLULAR LOCATION.
RX PubMed=10859302; DOI=10.1074/jbc.M000715200;
RA Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H.;
RT "GAKIN, a novel kinesin-like protein associates with the human
RT homologue of the Drosophila discs large tumor suppressor in T
RT lymphocytes.";
RL J. Biol. Chem. 275:28774-28784(2000).
RN [13]
RP INTERACTION WITH APC, AND FUNCTION IN CELL PROLIFERATION.
RX PubMed=10656683; DOI=10.1038/sj.onc.1203309;
RA Ishidate T., Matsumine A., Toyoshima K., Akiyama T.;
RT "The APC-hDLG complex negatively regulates cell cycle progression from
RT the G0/G1 to S phase.";
RL Oncogene 19:365-372(2000).
RN [14]
RP INTERACTION WITH TOPK.
RX PubMed=10779557; DOI=10.1073/pnas.090102397;
RA Gaudet S., Branton D., Lue R.A.;
RT "Characterization of PDZ-binding kinase, a mitotic kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000).
RN [15]
RP POSSIBLE INTERACTION WITH TJAP1.
RX PubMed=11602598; DOI=10.1074/jbc.M107335200;
RA Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K.,
RA Takeuchi M., Takai Y.;
RT "Pilt, a novel peripheral membrane protein at tight junctions in
RT epithelial cells.";
RL J. Biol. Chem. 276:48350-48355(2001).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH KCNF1.
RX PubMed=12445884; DOI=10.1016/S0008-6363(02)00602-8;
RA Godreau D., Vranckx R., Maguy A., Rucker-Martin C., Goyenvalle C.,
RA Abdelshafy S., Tessier S., Couetil J.P., Hatem S.N.;
RT "Expression, regulation and role of the MAGUK protein SAP-97 in human
RT atrial myocardium.";
RL Cardiovasc. Res. 56:433-442(2002).
RN [17]
RP ALTERNATIVE SPLICING (ISOFORMS 5; 6 AND 7), AND SUBCELLULAR LOCATION.
RX PubMed=11723125; DOI=10.1074/jbc.M108724200;
RA McLaughlin M., Hale R., Ellston D., Gaudet S., Lue R.A., Viel A.;
RT "The distribution and function of alternatively spliced insertions in
RT hDlg.";
RL J. Biol. Chem. 277:6406-6412(2002).
RN [18]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 38-ILE--ILE-40.
RX PubMed=12807908; DOI=10.1074/jbc.M305209200;
RA Hanada T., Takeuchi A., Sondarva G., Chishti A.H.;
RT "Protein 4.1-mediated membrane targeting of human discs large in
RT epithelial cells.";
RL J. Biol. Chem. 278:34445-34450(2003).
RN [19]
RP INTERACTION WITH PIK3R1 AND CDH1, AND FUNCTION IN ADHERENS JUNCTION
RP ASSEMBLY.
RX PubMed=14699157; DOI=10.1074/jbc.M309843200;
RA Laprise P., Viel A., Rivard N.;
RT "Human homolog of disc-large is required for adherens junction
RT assembly and differentiation of human intestinal epithelial cells.";
RL J. Biol. Chem. 279:10157-10166(2004).
RN [20]
RP FUNCTION IN T-CELL ACTIVATION.
RX PubMed=15263016; DOI=10.1083/jcb.200309044;
RA Xavier R., Rabizadeh S., Ishiguro K., Andre N., Ortiz J.B.,
RA Wachtel H., Morris D.G., Lopez-Ilasaca M., Shaw A.C., Swat W.,
RA Seed B.;
RT "Discs large (Dlg1) complexes in lymphocyte activation.";
RL J. Cell Biol. 166:173-178(2004).
RN [21]
RP INTERACTION WITH GPR124 AND GPR125.
RX PubMed=15021905; DOI=10.1038/sj.onc.1207495;
RA Yamamoto Y., Irie K., Asada M., Mino A., Mandai K., Takai Y.;
RT "Direct binding of the human homologue of the Drosophila disc large
RT tumor suppressor gene to seven-pass transmembrane proteins, tumor
RT endothelial marker 5 (TEM5), and a novel TEM5-like protein.";
RL Oncogene 23:3889-3897(2004).
RN [22]
RP REVIEW.
RX PubMed=12766944; DOI=10.1002/bies.10286;
RA Humbert P., Russell S., Richardson H.;
RT "Dlg, Scribble and Lgl in cell polarity, cell proliferation and
RT cancer.";
RL Bioessays 25:542-553(2003).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [24]
RP INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
RA Kaang B.-K., Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the
RT differentiation of excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [25]
RP INTERACTION WITH LIN7A; LIN7C AND MPP7.
RX PubMed=17237226; DOI=10.1074/jbc.M610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7
RT and DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [26]
RP INTERACTION WITH MPP7.
RX PubMed=17332497; DOI=10.1091/mbc.E06-11-0980;
RA Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.;
RT "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and
RT facilitates epithelial tight junction formation.";
RL Mol. Biol. Cell 18:1744-1755(2007).
RN [27]
RP INTERACTION WITH FRMPD4.
RX PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
RA Kang G.B., Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575;
RP SER-684 AND SER-687, AND MASS SPECTROMETRY.
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 [30]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH KCND2 AND KCND3.
RX PubMed=19213956; DOI=10.1161/CIRCRESAHA.108.191007;
RA El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
RA Coulombe A., Jeromin A., Hatem S.N.;
RT "Kv4 potassium channels form a tripartite complex with the anchoring
RT protein SAP97 and CaMKII in cardiac myocytes.";
RL Circ. Res. 104:758-769(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [32]
RP PHOSPHORYLATION BY MAPK12, INTERACTION WITH SFPQ, AND FUNCTION.
RX PubMed=20605917; DOI=10.1242/jcs.066514;
RA Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A.,
RA Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A.;
RT "p38gamma regulates interaction of nuclear PSF and RNA with the
RT tumour-suppressor hDlg in response to osmotic shock.";
RL J. Cell Sci. 123:2596-2604(2010).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-568; SER-575
RP AND SER-687, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 460-555.
RX PubMed=8757139; DOI=10.1038/382649a0;
RA Cabral J.H., Petosa C., Sutcliffe M.J., Raza S., Byron O., Poy F.,
RA Marfatia S.M., Chishti A.H., Liddington R.C.;
RT "Crystal structure of a PDZ domain.";
RL Nature 382:649-652(1996).
CC -!- FUNCTION: Essential multidomain scaffolding protein required for
CC normal development (By similarity). Recruits channels, receptors
CC and signaling molecules to discrete plasma membrane domains in
CC polarized cells. May play a role in adherens junction assembly,
CC signal transduction, cell proliferation, synaptogenesis and
CC lymphocyte activation. Regulates the excitability of cardiac
CC myocytes by modulating the functional expression of Kv4 channels.
CC Functional regulator of Kv1.5 channel.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts through its guanylate
CC kinase-like domain with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A.
CC May interact with HTR2A (By similarity). Interacts with LRFN1 (By
CC similarity). Interacts through its PDZ domains with GRIN2A, KCNA1,
CC KCNA2, KCNA3, KCNA4, KCNA5, KCND2, KCND3, GRIA1, GPR124 and
CC GPR125. Interacts with KCNF1. Interacts with CAMK2 (By
CC similarity). Interacts with cytoskeleton-associated proteins EPB41
CC and EZR. Found in a complex with KCNA5 and CAV3. Found in a
CC complex with APC and CTNNB1. Interacts with CDH1 through binding
CC to PIK3R1. Forms multiprotein complexes with CASK, LIN7A, LIN7B,
CC LIN7C, APBA1, and KCNJ12. Interacts through its guanylate kinase-
CC like domain with KIF13B. Forms a tripartite complex composed of
CC DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with TJAP1.
CC Interacts with TOPK and the HTLV-1 viral Tax and HPV-18 E6
CC papillomavirus (HPV) oncoproteins. Interacts with PTEN (By
CC similarity). Interacts with FRMPD4 (via C-terminus). Interacts
CC with LRFN1, LRFN2, LRFN4 and SFPQ.
CC -!- INTERACTION:
CC P78536:ADAM17; NbExp=7; IntAct=EBI-357481, EBI-78188;
CC P31016:Dlg4 (xeno); NbExp=9; IntAct=EBI-357500, EBI-375655;
CC O57125:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-7461590;
CC P03126:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-1177242;
CC P06463:E6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-1186926;
CC P36799:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-7363822;
CC Q9NQT8:KIF13B; NbExp=3; IntAct=EBI-357500, EBI-766408;
CC O60333-3:KIF1B; NbExp=4; IntAct=EBI-357481, EBI-465669;
CC P36507:MAP2K2; NbExp=10; IntAct=EBI-357481, EBI-1056930;
CC Q9ICL1:se6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-7461477;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity). Basolateral cell membrane (By similarity).
CC Endoplasmic reticulum membrane (By similarity). Cell junction,
CC synapse, postsynaptic cell membrane, postsynaptic density (By
CC similarity). Cell junction, synapse. Cell membrane, sarcolemma.
CC Note=Colocalizes with EPB41 at regions of intercellular contacts.
CC Basolateral in epithelial cells. May also associate with
CC endoplasmic reticulum membranes. Mainly found in neurons soma,
CC moderately found at postsynaptic densities (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q12959-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12959-2; Sequence=VSP_003150;
CC Note=Contains a phosphoserine at position 698 (By similarity);
CC Name=3;
CC IsoId=Q12959-3; Sequence=VSP_012862;
CC Name=4;
CC IsoId=Q12959-4; Sequence=VSP_012862, VSP_003150;
CC Note=Contains a phosphoserine at position 665 (By similarity).
CC Ref.6 (AAI44652) sequence is in conflict in position:
CC 636:Q->Missing;
CC Name=5;
CC IsoId=Q12959-5; Sequence=VSP_012862, VSP_012863;
CC Name=6;
CC IsoId=Q12959-6; Sequence=VSP_012864;
CC Name=7;
CC IsoId=Q12959-7; Sequence=VSP_012865;
CC Name=8;
CC IsoId=Q12959-8; Sequence=VSP_045896, VSP_045897;
CC Note=No experimental confirmation available;
CC Name=9;
CC IsoId=Q12959-9; Sequence=VSP_045896, VSP_045897, VSP_012865,
CC VSP_045898;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in atrial myocardium (at
CC protein level). Expressed in lung fibroblasts, cervical epithelial
CC and B-cells (at protein level). Widely expressed, with isoforms
CC displaying different expression profiles.
CC -!- DOMAIN: The alternatively spliced domain I3 corresponding to amino
CC acids (636-669) of isoform 4 is an EPB41 binding site mediating
CC association to membranes in polarized and non-polarized cells.
CC -!- DOMAIN: The PDZ domains may also mediate association to membranes
CC by binding to EPB41 and GPR124 together with the L27 domain that
CC binds CASK and DLG2.
CC -!- DOMAIN: The L27 domain may regulate DLG1 self-association. The N-
CC terminal alternatively spliced region is capable of binding
CC several SH3 domains and also moderates the level of protein
CC oligomerization.
CC -!- PTM: Phosphorylated by MAPK12. Phosphorylation of Ser-232
CC regulates association with GRIN2A. Isoform 2 is phosphorylated on
CC Ser-698. Isoform 3 is phosphorylated on Ser-665 (By similarity).
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC -!- SIMILARITY: Contains 1 L27 domain.
CC -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DLG1ID40333ch3q29.html";
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DR EMBL; U13896; AAA50598.1; -; mRNA.
DR EMBL; U13897; AAA50599.1; -; mRNA.
DR EMBL; AK294772; BAG57902.1; -; mRNA.
DR EMBL; AK294855; BAG57959.1; -; mRNA.
DR EMBL; EF553524; ABQ66269.1; -; mRNA.
DR EMBL; AC068302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471191; EAW53610.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53611.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53612.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53614.1; -; Genomic_DNA.
DR EMBL; BC140841; AAI40842.1; -; mRNA.
DR EMBL; BC144651; AAI44652.1; -; mRNA.
DR PIR; I38756; I38756.
DR PIR; I38757; I38757.
DR RefSeq; NP_001091894.1; NM_001098424.1.
DR RefSeq; NP_001191315.1; NM_001204386.1.
DR RefSeq; NP_001191316.1; NM_001204387.1.
DR RefSeq; NP_001191317.1; NM_001204388.1.
DR RefSeq; NP_004078.2; NM_004087.2.
DR RefSeq; XP_005269346.1; XM_005269289.1.
DR RefSeq; XP_005269347.1; XM_005269290.1.
DR RefSeq; XP_005269348.1; XM_005269291.1.
DR RefSeq; XP_005269349.1; XM_005269292.1.
DR RefSeq; XP_005269350.1; XM_005269293.1.
DR RefSeq; XP_005269351.1; XM_005269294.1.
DR RefSeq; XP_005269352.1; XM_005269295.1.
DR RefSeq; XP_005269353.1; XM_005269296.1.
DR RefSeq; XP_005269355.1; XM_005269298.1.
DR RefSeq; XP_005269356.1; XM_005269299.1.
DR UniGene; Hs.292549; -.
DR PDB; 1PDR; X-ray; 2.80 A; A=457-552.
DR PDB; 2M3M; NMR; -; A=318-406.
DR PDB; 2OQS; NMR; -; A=318-405.
DR PDB; 2X7Z; X-ray; 2.00 A; A=311-407.
DR PDB; 3LRA; X-ray; 2.95 A; A=2-65.
DR PDB; 3RL7; X-ray; 2.30 A; A/B/C/D/E/F=220-317.
DR PDB; 3RL8; X-ray; 2.20 A; A/B/C/D/E=315-410.
DR PDB; 3W9Y; X-ray; 2.20 A; A=712-904.
DR PDB; 4AMH; X-ray; 2.30 A; A/B=315-405.
DR PDB; 4G69; X-ray; 2.00 A; A=310-407.
DR PDBsum; 1PDR; -.
DR PDBsum; 2M3M; -.
DR PDBsum; 2OQS; -.
DR PDBsum; 2X7Z; -.
DR PDBsum; 3LRA; -.
DR PDBsum; 3RL7; -.
DR PDBsum; 3RL8; -.
DR PDBsum; 3W9Y; -.
DR PDBsum; 4AMH; -.
DR PDBsum; 4G69; -.
DR ProteinModelPortal; Q12959; -.
DR SMR; Q12959; 2-65, 220-904.
DR IntAct; Q12959; 28.
DR MINT; MINT-107690; -.
DR STRING; 9606.ENSP00000345731; -.
DR PhosphoSite; Q12959; -.
DR DMDM; 223590196; -.
DR PaxDb; Q12959; -.
DR PRIDE; Q12959; -.
DR Ensembl; ENST00000314062; ENSP00000321087; ENSG00000075711.
DR Ensembl; ENST00000346964; ENSP00000345731; ENSG00000075711.
DR Ensembl; ENST00000357674; ENSP00000350303; ENSG00000075711.
DR Ensembl; ENST00000392382; ENSP00000376187; ENSG00000075711.
DR Ensembl; ENST00000419354; ENSP00000407531; ENSG00000075711.
DR Ensembl; ENST00000422288; ENSP00000413238; ENSG00000075711.
DR Ensembl; ENST00000443183; ENSP00000396658; ENSG00000075711.
DR Ensembl; ENST00000448528; ENSP00000391732; ENSG00000075711.
DR Ensembl; ENST00000450955; ENSP00000411278; ENSG00000075711.
DR Ensembl; ENST00000452595; ENSP00000398939; ENSG00000075711.
DR GeneID; 1739; -.
DR KEGG; hsa:1739; -.
DR UCSC; uc011bub.2; human.
DR CTD; 1739; -.
DR GeneCards; GC03M196769; -.
DR HGNC; HGNC:2900; DLG1.
DR HPA; CAB016307; -.
DR MIM; 601014; gene.
DR neXtProt; NX_Q12959; -.
DR PharmGKB; PA27356; -.
DR eggNOG; COG0194; -.
DR HOVERGEN; HBG107814; -.
DR KO; K12076; -.
DR OMA; QHITSNA; -.
DR OrthoDB; EOG79GT6P; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_13685; Neuronal System.
DR EvolutionaryTrace; Q12959; -.
DR GeneWiki; DLG1; -.
DR GenomeRNAi; 1739; -.
DR NextBio; 7051; -.
DR PMAP-CutDB; A5YKK7; -.
DR PRO; PR:Q12959; -.
DR ArrayExpress; Q12959; -.
DR Bgee; Q12959; -.
DR CleanEx; HS_DLG1; -.
DR Genevestigator; Q12959; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; TAS:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; TAS:BHF-UCL.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:tight junction; IDA:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; NAS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0016337; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0001771; P:immunological synapse formation; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0031579; P:membrane raft organization; IEA:Ensembl.
DR GO; GO:0007093; P:mitotic cell cycle checkpoint; NAS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; TAS:BHF-UCL.
DR GO; GO:0048608; P:reproductive structure development; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR GO; GO:0002369; P:T cell cytokine production; IEA:Ensembl.
DR GO; GO:0070830; P:tight junction assembly; IDA:BHF-UCL.
DR InterPro; IPR016313; DLG1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR004172; L27.
DR InterPro; IPR015143; L27_1.
DR InterPro; IPR019590; MAGUK_PEST_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR019583; PDZ_assoc.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23119; PTHR23119; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Complete proteome; Endoplasmic reticulum; Host-virus interaction;
KW Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
KW Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1 904 Disks large homolog 1.
FT /FTId=PRO_0000094548.
FT DOMAIN 4 64 L27.
FT DOMAIN 224 310 PDZ 1.
FT DOMAIN 319 405 PDZ 2.
FT DOMAIN 466 546 PDZ 3.
FT DOMAIN 581 651 SH3.
FT DOMAIN 714 889 Guanylate kinase-like.
FT REGION 162 212 Interaction with SH3 domains.
FT MOD_RES 115 115 Phosphothreonine.
FT MOD_RES 122 122 Phosphoserine.
FT MOD_RES 158 158 Phosphoserine.
FT MOD_RES 232 232 Phosphoserine (By similarity).
FT MOD_RES 399 399 Phosphotyrosine (By similarity).
FT MOD_RES 568 568 Phosphoserine.
FT MOD_RES 575 575 Phosphoserine.
FT MOD_RES 619 619 Phosphoserine.
FT MOD_RES 684 684 Phosphoserine.
FT MOD_RES 687 687 Phosphoserine.
FT VAR_SEQ 1 77 MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIF
FT QSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQ -> M
FT NYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSD
FT ELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSST (in
FT isoform 8 and isoform 9).
FT /FTId=VSP_045896.
FT VAR_SEQ 78 193 Missing (in isoform 8 and isoform 9).
FT /FTId=VSP_045897.
FT VAR_SEQ 162 194 Missing (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_012862.
FT VAR_SEQ 195 212 Missing (in isoform 5).
FT /FTId=VSP_012863.
FT VAR_SEQ 669 680 EIPDDMGSKGLK -> QSFNDKRKKNLFSRKFPFYKNKDQS
FT EQETSDADQ (in isoform 2 and isoform 4).
FT /FTId=VSP_003150.
FT VAR_SEQ 681 693 Missing (in isoform 6).
FT /FTId=VSP_012864.
FT VAR_SEQ 693 693 Y -> YLILITDEYGCSKG (in isoform 7 and
FT isoform 9).
FT /FTId=VSP_012865.
FT VAR_SEQ 694 694 Missing (in isoform 9).
FT /FTId=VSP_045898.
FT VARIANT 140 140 K -> R (in dbSNP:rs1802668).
FT /FTId=VAR_054334.
FT VARIANT 278 278 R -> Q (in dbSNP:rs1134986).
FT /FTId=VAR_054335.
FT VARIANT 899 899 P -> L (in dbSNP:rs34492126).
FT /FTId=VAR_054336.
FT MUTAGEN 38 40 INI->ANA: Loss of membrane association
FT and DLG2-binding.
FT CONFLICT 237 237 S -> N (in Ref. 2; BAG57902).
FT CONFLICT 801 801 E -> G (in Ref. 1; AAA50598/AAA50599).
FT HELIX 5 20
FT STRAND 24 26
FT HELIX 30 42
FT HELIX 44 55
FT TURN 60 62
FT STRAND 221 228
FT STRAND 233 239
FT STRAND 254 258
FT HELIX 263 267
FT STRAND 275 279
FT HELIX 289 298
FT STRAND 301 309
FT STRAND 317 323
FT STRAND 331 337
FT STRAND 348 353
FT HELIX 358 362
FT STRAND 370 374
FT STRAND 377 382
FT HELIX 384 392
FT STRAND 396 403
FT STRAND 465 470
FT STRAND 472 474
FT STRAND 477 482
FT STRAND 484 487
FT STRAND 489 494
FT HELIX 499 503
FT STRAND 510 515
FT HELIX 525 533
FT STRAND 537 545
FT HELIX 547 554
FT STRAND 717 721
FT HELIX 724 734
FT TURN 736 738
FT TURN 756 758
FT HELIX 766 774
FT STRAND 778 784
FT STRAND 787 792
FT HELIX 793 800
FT TURN 801 803
FT STRAND 805 808
FT HELIX 813 820
FT STRAND 826 830
FT HELIX 855 864
FT HELIX 865 867
FT STRAND 869 872
FT HELIX 877 892
FT HELIX 900 902
SQ SEQUENCE 904 AA; 100455 MW; 6722993A84D0F761 CRC64;
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL
LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH
ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP
VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG
SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH
KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT
NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI
VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT
IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL
PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF
NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYRGQEEYV LSYEPVNQQE VNYTRPVIIL
GPMKDRINDD LISEFPDKFG SCVPHTTRPK RDYEVDGRDY HFVTSREQME KDIQEHKFIE
AGQYNNHLYG TSVQSVREVA EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME
MNKRLTEEQA RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGSYIWVPA
KEKL
//
MIM
601014
*RECORD*
*FIELD* NO
601014
*FIELD* TI
*601014 DISCS LARGE, DROSOPHILA, HOMOLOG OF, 1; DLG1
;;SYNAPSE-ASSOCIATED PROTEIN 97; SAP97
read more*FIELD* TX
CLONING
Azim et al. (1995) noted that in Drosophila more than 50 genes have been
identified that lead to loss of cell proliferation control, indicating
that they are tumor suppressor genes. Many of these genes have been
cloned and sequenced, and most have clear mammalian homologs. The
Drosophila 'discs large' tumor suppressor protein, Dlg, is the prototype
of a family of proteins termed MAGUKs (membrane-associated guanylate
kinase homologs). MAGUKs are localized at the membrane-cytoskeleton
interface, usually at cell-cell junctions, where they appear to have
both structural and signaling roles. They contain several distinct
domains, including a modified guanylate kinase domain, an SH3 motif, and
1 or 3 copies of the DHR (GLGF/PDZ) domain. Recessive lethal mutations
in the 'discs large' tumor suppressor gene interfere with the formation
of septate junctions (thought to be the arthropod equivalent of tight
junctions) between epithelial cells, and they also cause neoplastic
overgrowth of imaginal discs, suggesting a role for cell junctions in
proliferation control.
A homolog of the Drosophila Dlg protein was isolated from human B
lymphocytes (Lue et al., 1994) and shown to bind directly to the
membrane cytoskeletal protein 4.1 (130500). The presence of human DLG
isoforms with or without the protein 4.1-binding domain suggested that
the tissue-specific cytoskeletal interactions of the protein may be
regulated by alternative splicing of its transcripts. Mori et al. (1998)
identified a number of novel splicing variants, some of which were
transcribed in a tissue-specific manner, as well as alteration of
splicing patterns in cell lines from neuroblastomas.
GENE FUNCTION
Hanada et al. (1997) showed by immunoblot analysis that
immunoprecipitates of DLG1 in T lymphocytes contain the Src family
tyrosine kinase p56(lck) (LCK; 153390) but not p59(fyn) (FYN; 137025) or
PIK3 (see PIK3CA, 171834). Binding analysis demonstrated that LCK
interacts with the proline-rich N-terminal domain of DLG1. Additionally,
DLG1 interacts with the Kv1.3 channel (see KCNAB1, 601141). Hanada et
al. (1997) suggested that DLG1 may function as a coupler of tyrosine
kinase and a voltage-gated potassium channel in T lymphocytes.
Ohshiro et al. (2000) demonstrated in Drosophila that lethal giant
larvae (Lgl) (LLGL1; 600966) is essential for asymmetric cortical
localization of all basal determinants in mitotic neuroblasts, and is
therefore indispensable for neural fate decisions. Lgl, which itself is
uniformly cortical, interacts with several types of myosin to localize
the determinants. Dlg, another tumor suppressor gene, participates in
this process by regulating the localization of Lgl. The localization of
the apical components is unaffected in Lgl or Dlg mutants. Thus, Lgl and
Dlg act in a common process that differentially mediates cortical
protein targeting in mitotic neuroblasts, and creates intrinsic
differences between daughter cells.
Peng et al. (2000) showed that Drosophila Lgl and Dlg regulate basal
protein targeting, but not apical complex formation or spindle
orientation, in both embryonic and larval neuroblasts. Dlg protein is
apically enriched and is required for maintaining cortical localization
of Lgl protein. Basal protein targeting requires microfilament and
myosin function, yet the Lgl phenotype is strongly suppressed by
reducing levels of myosin II. Peng et al. (2000) concluded that Dlg and
Lgl promote, and myosin II inhibits, actomyosin-dependent basal protein
targeting in neuroblasts.
Bonilha and Rodriguez-Boulan (2001) identified EBP50 (604990) and SAP97
as binding partners for ezrin (123900), an actin-binding protein crucial
for morphogenesis of apical microvilli and basolateral infoldings in
retinal pigment epithelial (RPE) cells. Immunofluorescence microscopy
detected a polarized distribution of EBP50 at apical microvilli and of
SAP97 at the basolateral surface of RPE cells, which overlapped with
ezrin.
Willatt et al. (2005) pointed out that the DLG1 and PAK2 (605022) genes
are deleted in the 3q29 microdeletion syndrome (609425) and raised the
possibility that loss of one of these genes may contribute to the
phenotype since PAK2 and DLG1 are autosomal homologs of 2 X-linked
mental retardation genes, PAK3 (300142) and DLG3 (300189).
Bohl et al. (2007) found that MPP7 (610973) formed a tripartite complex
with DLG1 and LIN7A (603380) or LIN7C in vitro and in vivo. MPP7
dimerized with the LIN7 proteins through its L27C domain. The LIN7/MPP7
dimer then linked to DLG1 though the L27N domain of MPP7. This complex
localized to epithelial adherens junctions in transfected Madin-Darby
canine kidney cells. Expression of an MPP7 construct lacking either the
PDZ or SH3 domain redistributed MPP7, DLG1, and LIN7 into the soluble
cytoplasmic fraction.
Stucke et al. (2007) showed that the L27N domain of endogenous MPP7
bound DLG1 in human epithelial cells. MPP7 and DLG1 colocalized at the
lateral surface of epithelial cells, and they overlapped with markers of
adherens junctions and tight junctions. Recruitment of MPP7 to the
plasma membrane was dependent on its interaction with DLG1. Loss of
either DLG1 or MPP7 from epithelial cells resulted in a significant
defect in assembly and maintenance of functional tight junctions. Stucke
et al. (2007) concluded that formation of the DLG1-MPP7 complex promotes
epithelial cell polarity and tight junction formation.
Cotter et al. (2010) showed that, in Schwann cells, mammalian disks
large homolog 1 (Dlg1) interacts with Pten (601728) to inhibit axonal
stimulation of myelination. This mechanism limits myelin sheath
thickness and prevents overmyelination in mouse sciatic nerves. Removing
this brake results in myelin outfoldings and demyelination,
characteristics of some peripheral neuropathies. Indeed, the Dlg1 brake
is no longer functional in a mouse model of Charcot-Marie-Tooth disease
(CMT4B1; 601382). Cotter et al. (2010) concluded that negative
regulation of myelination appears to be essential for optimization of
nerve conduction velocity and myelin maintenance.
MAPPING
By analysis of human/rodent somatic cell hybrids and by fluorescence in
situ hybridization, Azim et al. (1995) mapped the DLG1 gene to 3q29. The
authors stated that no tumor suppressor gene had previously been
localized to 3q29. By interspecific backcross mapping, Peters et al.
(1996) and Burgess et al. (1996) determined that the mouse gene
corresponding to human DLG1, Dlgh1, maps to chromosome 16.
ANIMAL MODEL
Mahoney et al. (2006) stated that mutant mice expressing a truncated
Dlgh1 protein retaining the 3 PDZ domains exhibit growth retardation,
craniofacial abnormalities, neonatal lethality, increased proliferation
in the lens, and small kidneys associated with impaired ureteric bud
branching and reduced nephron formation. Mahoney et al. (2006) developed
Dlgh1-null mice and found that they were born at the expected mendelian
ratio but exhibited respiratory distress and died shortly after birth.
In addition to the phenotypes described above, all Dlgh1 -/- mice had
severely shortened ureters. Unilateral renal agenesis was found in 20%
of Dlgh1-null embryos, and unilateral/bilateral perinatal hydronephrosis
was found in 35% of Dlgh1-null embryos. Hydronephrosis was associated
with a defect in ureteric smooth muscle orientation that dramatically
impaired efficient peristalsis.
*FIELD* RF
1. Azim, A. C.; Knoll, J. H. M.; Marfatia, S. M.; Peel, D. J.; Bryant,
P. J.; Chishti, A. H.: DLG1: chromosome location of the closest human
homologue of the Drosophila discs large tumor suppressor gene. Genomics 30:
613-616, 1995.
2. Bohl, J.; Brimer, N.; Lyons, C.; Vande Pol, S. B.: The Stardust
family protein MPP7 forms a tripartite complex with LIN7 and DLG1
that regulates the stability and localization of DLG1 to cell junctions. J.
Biol. Chem. 282: 9392-9400, 2007.
3. Bonilha, V. L.; Rodriguez-Boulan, E.: Polarity and developmental
regulation of two PDZ proteins in the retinal pigment epithelium. Invest.
Ophthal. Vis. Sci. 42: 3274-3282, 2001.
4. Burgess, D. L.; Rafael, J. A.; Meisler, M. H.; Chamberlain, J.
S.: Dlgh1, a mouse homolog of the Drosophila discs-large gene, is
located on chromosome 16. Mammalian Genome 7: 623-624, 1996.
5. Cotter, L.; Ozcelik, M.; Jacob, C.; Pereira, J. A.; Locher, V.;
Baumann, R.; Relvas, J. B.; Suter, U.; Tricaud, N.: Dlg1-PTEN interaction
regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328:
1415-1418, 2010.
6. Hanada, T.; Lin, L.; Chandy, K. G.; Oh, S. S.; Chishti, A. H.:
Human homologue of the Drosophila discs large tumor suppressor binds
to p56lck tyrosine kinase and Shaker type Kv1.3 potassium channel
in T lymphocytes. J. Biol. Chem. 272: 26899-26904, 1997.
7. Lue, R. A.; Marfatia, S. M.; Branton, D.; Chishti, A. H.: Cloning
and characterization of hdlg: the human homologue of the Drosophila
discs large tumor suppressor binds to protein 4.1. Proc. Nat. Acad.
Sci. 91: 9818-9822, 1994.
8. Mahoney, Z. X.; Sammut, B.; Xavier, R. J.; Cunninham, J.; Go, G.;
Brim, K. L.; Stappenbeck, T. S.; Miner, J. H.; Swat, W.: Discs-large
homolog 1 regulates smooth muscle orientation in the mouse ureter. Proc.
Nat. Acad. Sci. 103: 19872-19877, 2006.
9. Mori, K.; Iwao, K.; Miyoshi, Y.; Nakagawara, A.; Kofu, K.; Akiyama,
T.; Arita, N.; Hayakawa, T.; Nakamura, Y.: Identification of brain-specific
splicing variants of the hDLG1 gene and altered splicing in neuroblastoma
cell lines. J. Hum. Genet. 43: 123-127, 1998.
10. Ohshiro, T.; Yagami, T.; Zhang, C.; Matsuzaki, F.: Role of cortical
tumour-suppressor proteins in asymmetric division of Drosophila neuroblast. Nature 408:
593-596, 2000.
11. Peng, C.-Y.; Manning, L.; Albertson, R.; Doe, C. Q.: The tumour-suppressor
genes lgl and dlg regulate basal protein targeting in Drosophila neuroblasts. Nature 408:
596-600, 2000.
12. Peters, L. L.; Ciciotte, S. L.; Lin, L.; Chishti, A. H.: The
mouse homolog of the Drosophila discs large tumor suppressor gene
maps to chromosome 16. Mammalian Genome 7: 619-620, 1996.
13. Stucke, V. M.; Timmerman, E.; Vandekerckhove, J.; Gevaert, K.;
Hall, A.: The MAGUK protein MPP7 binds to the polarity protein hDlg1
and facilitates epithelial tight junction formation. Molec. Biol.
Cell 18: 1744-1755, 2007.
14. Willatt, L.; Cox, J.; Barber, J.; Cabanas, E. D.; Collins, A.;
Donnai, D.; FitzPatrick, D. R.; Maher, E.; Martin, H.; Parnau, J.;
Pindar, L.; Ramsay, J.; Shaw-Smith, C.; Sistermans, E. A.; Tettenborn,
M.; Trump, D.; de Vries, B. B. A.; Walker, K.; Raymond, F. L.: 3q29
microdeletion syndrome: clinical and molecular characterization of
a new syndrome. Am. J. Hum. Genet. 77: 154-160, 2005.
*FIELD* CN
Ada Hamosh - updated: 6/30/2010
Alan F. Scott - updated: 4/25/2007
Patricia A. Hartz - updated: 4/23/2007
Victor A. McKusick - updated: 6/17/2005
Jane Kelly - updated: 7/2/2002
Ada Hamosh - updated: 11/29/2000
Paul J. Converse - updated: 6/7/2000
Clair A. Francomano - updated: 6/25/1998
*FIELD* CD
Victor A. McKusick: 1/23/1996
*FIELD* ED
alopez: 07/01/2010
terry: 6/30/2010
mgross: 4/25/2007
wwang: 4/23/2007
alopez: 6/21/2005
terry: 6/17/2005
mgross: 7/2/2002
terry: 1/22/2001
carol: 11/29/2000
carol: 6/7/2000
alopez: 5/7/1999
carol: 11/12/1998
carol: 8/12/1998
carol: 6/26/1998
dholmes: 6/25/1998
terry: 9/11/1997
terry: 11/14/1996
terry: 3/26/1996
mark: 1/23/1996
*RECORD*
*FIELD* NO
601014
*FIELD* TI
*601014 DISCS LARGE, DROSOPHILA, HOMOLOG OF, 1; DLG1
;;SYNAPSE-ASSOCIATED PROTEIN 97; SAP97
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CLONING
Azim et al. (1995) noted that in Drosophila more than 50 genes have been
identified that lead to loss of cell proliferation control, indicating
that they are tumor suppressor genes. Many of these genes have been
cloned and sequenced, and most have clear mammalian homologs. The
Drosophila 'discs large' tumor suppressor protein, Dlg, is the prototype
of a family of proteins termed MAGUKs (membrane-associated guanylate
kinase homologs). MAGUKs are localized at the membrane-cytoskeleton
interface, usually at cell-cell junctions, where they appear to have
both structural and signaling roles. They contain several distinct
domains, including a modified guanylate kinase domain, an SH3 motif, and
1 or 3 copies of the DHR (GLGF/PDZ) domain. Recessive lethal mutations
in the 'discs large' tumor suppressor gene interfere with the formation
of septate junctions (thought to be the arthropod equivalent of tight
junctions) between epithelial cells, and they also cause neoplastic
overgrowth of imaginal discs, suggesting a role for cell junctions in
proliferation control.
A homolog of the Drosophila Dlg protein was isolated from human B
lymphocytes (Lue et al., 1994) and shown to bind directly to the
membrane cytoskeletal protein 4.1 (130500). The presence of human DLG
isoforms with or without the protein 4.1-binding domain suggested that
the tissue-specific cytoskeletal interactions of the protein may be
regulated by alternative splicing of its transcripts. Mori et al. (1998)
identified a number of novel splicing variants, some of which were
transcribed in a tissue-specific manner, as well as alteration of
splicing patterns in cell lines from neuroblastomas.
GENE FUNCTION
Hanada et al. (1997) showed by immunoblot analysis that
immunoprecipitates of DLG1 in T lymphocytes contain the Src family
tyrosine kinase p56(lck) (LCK; 153390) but not p59(fyn) (FYN; 137025) or
PIK3 (see PIK3CA, 171834). Binding analysis demonstrated that LCK
interacts with the proline-rich N-terminal domain of DLG1. Additionally,
DLG1 interacts with the Kv1.3 channel (see KCNAB1, 601141). Hanada et
al. (1997) suggested that DLG1 may function as a coupler of tyrosine
kinase and a voltage-gated potassium channel in T lymphocytes.
Ohshiro et al. (2000) demonstrated in Drosophila that lethal giant
larvae (Lgl) (LLGL1; 600966) is essential for asymmetric cortical
localization of all basal determinants in mitotic neuroblasts, and is
therefore indispensable for neural fate decisions. Lgl, which itself is
uniformly cortical, interacts with several types of myosin to localize
the determinants. Dlg, another tumor suppressor gene, participates in
this process by regulating the localization of Lgl. The localization of
the apical components is unaffected in Lgl or Dlg mutants. Thus, Lgl and
Dlg act in a common process that differentially mediates cortical
protein targeting in mitotic neuroblasts, and creates intrinsic
differences between daughter cells.
Peng et al. (2000) showed that Drosophila Lgl and Dlg regulate basal
protein targeting, but not apical complex formation or spindle
orientation, in both embryonic and larval neuroblasts. Dlg protein is
apically enriched and is required for maintaining cortical localization
of Lgl protein. Basal protein targeting requires microfilament and
myosin function, yet the Lgl phenotype is strongly suppressed by
reducing levels of myosin II. Peng et al. (2000) concluded that Dlg and
Lgl promote, and myosin II inhibits, actomyosin-dependent basal protein
targeting in neuroblasts.
Bonilha and Rodriguez-Boulan (2001) identified EBP50 (604990) and SAP97
as binding partners for ezrin (123900), an actin-binding protein crucial
for morphogenesis of apical microvilli and basolateral infoldings in
retinal pigment epithelial (RPE) cells. Immunofluorescence microscopy
detected a polarized distribution of EBP50 at apical microvilli and of
SAP97 at the basolateral surface of RPE cells, which overlapped with
ezrin.
Willatt et al. (2005) pointed out that the DLG1 and PAK2 (605022) genes
are deleted in the 3q29 microdeletion syndrome (609425) and raised the
possibility that loss of one of these genes may contribute to the
phenotype since PAK2 and DLG1 are autosomal homologs of 2 X-linked
mental retardation genes, PAK3 (300142) and DLG3 (300189).
Bohl et al. (2007) found that MPP7 (610973) formed a tripartite complex
with DLG1 and LIN7A (603380) or LIN7C in vitro and in vivo. MPP7
dimerized with the LIN7 proteins through its L27C domain. The LIN7/MPP7
dimer then linked to DLG1 though the L27N domain of MPP7. This complex
localized to epithelial adherens junctions in transfected Madin-Darby
canine kidney cells. Expression of an MPP7 construct lacking either the
PDZ or SH3 domain redistributed MPP7, DLG1, and LIN7 into the soluble
cytoplasmic fraction.
Stucke et al. (2007) showed that the L27N domain of endogenous MPP7
bound DLG1 in human epithelial cells. MPP7 and DLG1 colocalized at the
lateral surface of epithelial cells, and they overlapped with markers of
adherens junctions and tight junctions. Recruitment of MPP7 to the
plasma membrane was dependent on its interaction with DLG1. Loss of
either DLG1 or MPP7 from epithelial cells resulted in a significant
defect in assembly and maintenance of functional tight junctions. Stucke
et al. (2007) concluded that formation of the DLG1-MPP7 complex promotes
epithelial cell polarity and tight junction formation.
Cotter et al. (2010) showed that, in Schwann cells, mammalian disks
large homolog 1 (Dlg1) interacts with Pten (601728) to inhibit axonal
stimulation of myelination. This mechanism limits myelin sheath
thickness and prevents overmyelination in mouse sciatic nerves. Removing
this brake results in myelin outfoldings and demyelination,
characteristics of some peripheral neuropathies. Indeed, the Dlg1 brake
is no longer functional in a mouse model of Charcot-Marie-Tooth disease
(CMT4B1; 601382). Cotter et al. (2010) concluded that negative
regulation of myelination appears to be essential for optimization of
nerve conduction velocity and myelin maintenance.
MAPPING
By analysis of human/rodent somatic cell hybrids and by fluorescence in
situ hybridization, Azim et al. (1995) mapped the DLG1 gene to 3q29. The
authors stated that no tumor suppressor gene had previously been
localized to 3q29. By interspecific backcross mapping, Peters et al.
(1996) and Burgess et al. (1996) determined that the mouse gene
corresponding to human DLG1, Dlgh1, maps to chromosome 16.
ANIMAL MODEL
Mahoney et al. (2006) stated that mutant mice expressing a truncated
Dlgh1 protein retaining the 3 PDZ domains exhibit growth retardation,
craniofacial abnormalities, neonatal lethality, increased proliferation
in the lens, and small kidneys associated with impaired ureteric bud
branching and reduced nephron formation. Mahoney et al. (2006) developed
Dlgh1-null mice and found that they were born at the expected mendelian
ratio but exhibited respiratory distress and died shortly after birth.
In addition to the phenotypes described above, all Dlgh1 -/- mice had
severely shortened ureters. Unilateral renal agenesis was found in 20%
of Dlgh1-null embryos, and unilateral/bilateral perinatal hydronephrosis
was found in 35% of Dlgh1-null embryos. Hydronephrosis was associated
with a defect in ureteric smooth muscle orientation that dramatically
impaired efficient peristalsis.
*FIELD* RF
1. Azim, A. C.; Knoll, J. H. M.; Marfatia, S. M.; Peel, D. J.; Bryant,
P. J.; Chishti, A. H.: DLG1: chromosome location of the closest human
homologue of the Drosophila discs large tumor suppressor gene. Genomics 30:
613-616, 1995.
2. Bohl, J.; Brimer, N.; Lyons, C.; Vande Pol, S. B.: The Stardust
family protein MPP7 forms a tripartite complex with LIN7 and DLG1
that regulates the stability and localization of DLG1 to cell junctions. J.
Biol. Chem. 282: 9392-9400, 2007.
3. Bonilha, V. L.; Rodriguez-Boulan, E.: Polarity and developmental
regulation of two PDZ proteins in the retinal pigment epithelium. Invest.
Ophthal. Vis. Sci. 42: 3274-3282, 2001.
4. Burgess, D. L.; Rafael, J. A.; Meisler, M. H.; Chamberlain, J.
S.: Dlgh1, a mouse homolog of the Drosophila discs-large gene, is
located on chromosome 16. Mammalian Genome 7: 623-624, 1996.
5. Cotter, L.; Ozcelik, M.; Jacob, C.; Pereira, J. A.; Locher, V.;
Baumann, R.; Relvas, J. B.; Suter, U.; Tricaud, N.: Dlg1-PTEN interaction
regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328:
1415-1418, 2010.
6. Hanada, T.; Lin, L.; Chandy, K. G.; Oh, S. S.; Chishti, A. H.:
Human homologue of the Drosophila discs large tumor suppressor binds
to p56lck tyrosine kinase and Shaker type Kv1.3 potassium channel
in T lymphocytes. J. Biol. Chem. 272: 26899-26904, 1997.
7. Lue, R. A.; Marfatia, S. M.; Branton, D.; Chishti, A. H.: Cloning
and characterization of hdlg: the human homologue of the Drosophila
discs large tumor suppressor binds to protein 4.1. Proc. Nat. Acad.
Sci. 91: 9818-9822, 1994.
8. Mahoney, Z. X.; Sammut, B.; Xavier, R. J.; Cunninham, J.; Go, G.;
Brim, K. L.; Stappenbeck, T. S.; Miner, J. H.; Swat, W.: Discs-large
homolog 1 regulates smooth muscle orientation in the mouse ureter. Proc.
Nat. Acad. Sci. 103: 19872-19877, 2006.
9. Mori, K.; Iwao, K.; Miyoshi, Y.; Nakagawara, A.; Kofu, K.; Akiyama,
T.; Arita, N.; Hayakawa, T.; Nakamura, Y.: Identification of brain-specific
splicing variants of the hDLG1 gene and altered splicing in neuroblastoma
cell lines. J. Hum. Genet. 43: 123-127, 1998.
10. Ohshiro, T.; Yagami, T.; Zhang, C.; Matsuzaki, F.: Role of cortical
tumour-suppressor proteins in asymmetric division of Drosophila neuroblast. Nature 408:
593-596, 2000.
11. Peng, C.-Y.; Manning, L.; Albertson, R.; Doe, C. Q.: The tumour-suppressor
genes lgl and dlg regulate basal protein targeting in Drosophila neuroblasts. Nature 408:
596-600, 2000.
12. Peters, L. L.; Ciciotte, S. L.; Lin, L.; Chishti, A. H.: The
mouse homolog of the Drosophila discs large tumor suppressor gene
maps to chromosome 16. Mammalian Genome 7: 619-620, 1996.
13. Stucke, V. M.; Timmerman, E.; Vandekerckhove, J.; Gevaert, K.;
Hall, A.: The MAGUK protein MPP7 binds to the polarity protein hDlg1
and facilitates epithelial tight junction formation. Molec. Biol.
Cell 18: 1744-1755, 2007.
14. Willatt, L.; Cox, J.; Barber, J.; Cabanas, E. D.; Collins, A.;
Donnai, D.; FitzPatrick, D. R.; Maher, E.; Martin, H.; Parnau, J.;
Pindar, L.; Ramsay, J.; Shaw-Smith, C.; Sistermans, E. A.; Tettenborn,
M.; Trump, D.; de Vries, B. B. A.; Walker, K.; Raymond, F. L.: 3q29
microdeletion syndrome: clinical and molecular characterization of
a new syndrome. Am. J. Hum. Genet. 77: 154-160, 2005.
*FIELD* CN
Ada Hamosh - updated: 6/30/2010
Alan F. Scott - updated: 4/25/2007
Patricia A. Hartz - updated: 4/23/2007
Victor A. McKusick - updated: 6/17/2005
Jane Kelly - updated: 7/2/2002
Ada Hamosh - updated: 11/29/2000
Paul J. Converse - updated: 6/7/2000
Clair A. Francomano - updated: 6/25/1998
*FIELD* CD
Victor A. McKusick: 1/23/1996
*FIELD* ED
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