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Disks large homolog 1 (Synapse-associated protein 97) (SAP-97) (SAP97) (hDlg)

 DLG1_HUMAN              Reviewed;         904 AA.
Q12959; A5YKK7; B4DGU1; B4DGZ8; B7ZMM0; B9EIQ5; D3DXB8; D3DXB9;
E7EWL7; E9PG21; Q12958;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
25-OCT-2017, entry version 203.
RecName: Full=Disks large homolog 1;
AltName: Full=Synapse-associated protein 97;
Short=SAP-97;
Short=SAP97;
AltName: Full=hDlg;
Name=DLG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EPB41, AND VARIANT
GLN-278.
PubMed=7937897; DOI=10.1073/pnas.91.21.9818;
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. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9), AND VARIANT
GLN-278.
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH KCNA1; KCNA2; KCNA3 AND KCNA4.
PubMed=7477295; DOI=10.1038/378085a0;
Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.;
"Clustering of Shaker-type K+ channels by interaction with a family of
membrane-associated guanylate kinases.";
Nature 378:85-88(1995).
[8]
INTERACTION WITH EPB41, AND SUBCELLULAR LOCATION.
PubMed=8922391; DOI=10.1083/jcb.135.4.1125;
Lue R.A., Brandin E., Chan E.P., Branton D.;
"Two independent domains of hDlg are sufficient for subcellular
targeting: the PDZ1-2 conformational unit and an alternatively spliced
domain.";
J. Cell Biol. 135:1125-1137(1996).
[9]
INTERACTION WITH APC.
PubMed=8638125; DOI=10.1126/science.272.5264.1020;
Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H.,
Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.;
"Binding of APC to the human homolog of the Drosophila discs large
tumor suppressor protein.";
Science 272:1020-1023(1996).
[10]
INTERACTION WITH VIRAL ONCOPROTEIN TAX AND HPV-18 E6.
PubMed=9192623; DOI=10.1073/pnas.94.13.6670;
Lee S.S., Weiss R.S., Javier R.T.;
"Binding of human virus oncoproteins to hDlg/SAP97, a mammalian
homolog of the Drosophila discs large tumor suppressor protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997).
[11]
INTERACTION WITH HTLV-1 TAX-1.
PubMed=10557085; DOI=10.1038/sj.onc.1203008;
Suzuki T., Ohsugi Y., Uchida-Toita M., Akiyama T., Yoshida M.;
"Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila
discs large tumor suppressor protein, hDLG, and perturbs its function
in cell growth control.";
Oncogene 18:5967-5972(1999).
[12]
INTERACTION WITH KIF13B, AND SUBCELLULAR LOCATION.
PubMed=10859302; DOI=10.1074/jbc.M000715200;
Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H.;
"GAKIN, a novel kinesin-like protein associates with the human
homologue of the Drosophila discs large tumor suppressor in T
lymphocytes.";
J. Biol. Chem. 275:28774-28784(2000).
[13]
INTERACTION WITH APC, AND FUNCTION IN CELL PROLIFERATION.
PubMed=10656683; DOI=10.1038/sj.onc.1203309;
Ishidate T., Matsumine A., Toyoshima K., Akiyama T.;
"The APC-hDLG complex negatively regulates cell cycle progression from
the G0/G1 to S phase.";
Oncogene 19:365-372(2000).
[14]
INTERACTION WITH TOPK.
PubMed=10779557; DOI=10.1073/pnas.090102397;
Gaudet S., Branton D., Lue R.A.;
"Characterization of PDZ-binding kinase, a mitotic kinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000).
[15]
POSSIBLE INTERACTION WITH TJAP1.
PubMed=11602598; DOI=10.1074/jbc.M107335200;
Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K.,
Takeuchi M., Takai Y.;
"Pilt, a novel peripheral membrane protein at tight junctions in
epithelial cells.";
J. Biol. Chem. 276:48350-48355(2001).
[16]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH KCNF1.
PubMed=12445884; DOI=10.1016/S0008-6363(02)00602-8;
Godreau D., Vranckx R., Maguy A., Rucker-Martin C., Goyenvalle C.,
Abdelshafy S., Tessier S., Couetil J.P., Hatem S.N.;
"Expression, regulation and role of the MAGUK protein SAP-97 in human
atrial myocardium.";
Cardiovasc. Res. 56:433-442(2002).
[17]
ALTERNATIVE SPLICING (ISOFORMS 5; 6 AND 7), AND SUBCELLULAR LOCATION.
PubMed=11723125; DOI=10.1074/jbc.M108724200;
McLaughlin M., Hale R., Ellston D., Gaudet S., Lue R.A., Viel A.;
"The distribution and function of alternatively spliced insertions in
hDlg.";
J. Biol. Chem. 277:6406-6412(2002).
[18]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 38-ILE--ILE-40.
PubMed=12807908; DOI=10.1074/jbc.M305209200;
Hanada T., Takeuchi A., Sondarva G., Chishti A.H.;
"Protein 4.1-mediated membrane targeting of human discs large in
epithelial cells.";
J. Biol. Chem. 278:34445-34450(2003).
[19]
INTERACTION WITH PIK3R1 AND CDH1, AND FUNCTION IN ADHERENS JUNCTION
ASSEMBLY.
PubMed=14699157; DOI=10.1074/jbc.M309843200;
Laprise P., Viel A., Rivard N.;
"Human homolog of disc-large is required for adherens junction
assembly and differentiation of human intestinal epithelial cells.";
J. Biol. Chem. 279:10157-10166(2004).
[20]
FUNCTION IN T-CELL ACTIVATION.
PubMed=15263016; DOI=10.1083/jcb.200309044;
Xavier R., Rabizadeh S., Ishiguro K., Andre N., Ortiz J.B.,
Wachtel H., Morris D.G., Lopez-Ilasaca M., Shaw A.C., Swat W.,
Seed B.;
"Discs large (Dlg1) complexes in lymphocyte activation.";
J. Cell Biol. 166:173-178(2004).
[21]
INTERACTION WITH ADGRA2 AND ADGRA3.
PubMed=15021905; DOI=10.1038/sj.onc.1207495;
Yamamoto Y., Irie K., Asada M., Mino A., Mandai K., Takai Y.;
"Direct binding of the human homologue of the Drosophila disc large
tumor suppressor gene to seven-pass transmembrane proteins, tumor
endothelial marker 5 (TEM5), and a novel TEM5-like protein.";
Oncogene 23:3889-3897(2004).
[22]
REVIEW.
PubMed=12766944; DOI=10.1002/bies.10286;
Humbert P., Russell S., Richardson H.;
"Dlg, Scribble and Lgl in cell polarity, cell proliferation and
cancer.";
Bioessays 25:542-553(2003).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[24]
INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
Kaang B.-K., Kim E.;
"SALM synaptic cell adhesion-like molecules regulate the
differentiation of excitatory synapses.";
Neuron 50:233-245(2006).
[25]
INTERACTION WITH LIN7A; LIN7C AND MPP7.
PubMed=17237226; DOI=10.1074/jbc.M610002200;
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).
[26]
INTERACTION WITH MPP7.
PubMed=17332497; DOI=10.1091/mbc.E06-11-0980;
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.";
Mol. Biol. Cell 18:1744-1755(2007).
[27]
INTERACTION WITH FRMPD4.
PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
Kang G.B., Eom S.H., Kim H., Kim E.;
"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
regulates dendritic spine morphogenesis.";
J. Neurosci. 28:14546-14556(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575;
SER-684 AND SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[30]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH KCND2 AND KCND3.
PubMed=19213956; DOI=10.1161/CIRCRESAHA.108.191007;
El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
Coulombe A., Jeromin A., Hatem S.N.;
"Kv4 potassium channels form a tripartite complex with the anchoring
protein SAP97 and CaMKII in cardiac myocytes.";
Circ. Res. 104:758-769(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[32]
PHOSPHORYLATION BY MAPK12, INTERACTION WITH SFPQ, AND FUNCTION.
PubMed=20605917; DOI=10.1242/jcs.066514;
Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A.,
Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A.;
"p38gamma regulates interaction of nuclear PSF and RNA with the
tumour-suppressor hDlg in response to osmotic shock.";
J. Cell Sci. 123:2596-2604(2010).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-568; SER-575
AND SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-579, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-573,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 (ISOFORM 4), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
INTERACTION WITH ADGRA2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25558062; DOI=10.1016/j.celrep.2014.12.020;
Posokhova E., Shukla A., Seaman S., Volate S., Hilton M.B., Wu B.,
Morris H., Swing D.A., Zhou M., Zudaire E., Rubin J.S., St Croix B.;
"GPR124 functions as a WNT7-specific coactivator of canonical beta-
catenin signaling.";
Cell Rep. 10:123-130(2015).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[39]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 460-555.
PubMed=8757139; DOI=10.1038/382649a0;
Cabral J.H., Petosa C., Sutcliffe M.J., Raza S., Byron O., Poy F.,
Marfatia S.M., Chishti A.H., Liddington R.C.;
"Crystal structure of a PDZ domain.";
Nature 382:649-652(1996).
[40]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-65 IN COMPLEX WITH MPP7
AND LIN7C, AND SUBUNIT.
PubMed=20702775; DOI=10.1096/fj.10-163857;
Yang X., Xie X., Chen L., Zhou H., Wang Z., Zhao W., Tian R.,
Zhang R., Tian C., Long J., Shen Y.;
"Structural basis for tandem L27 domain-mediated polymerization.";
FASEB J. 24:4806-4815(2010).
-!- FUNCTION: Essential multidomain scaffolding protein required for
normal development (By similarity). Recruits channels, receptors
and signaling molecules to discrete plasma membrane domains in
polarized cells. May play a role in adherens junction assembly,
signal transduction, cell proliferation, synaptogenesis and
lymphocyte activation. Regulates the excitability of cardiac
myocytes by modulating the functional expression of Kv4 channels.
Functional regulator of Kv1.5 channel. {ECO:0000250,
ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:12445884,
ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15263016,
ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917}.
-!- SUBUNIT: Homotetramer (Probable). Interacts (via guanylate kinase-
like domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A (By
similarity). Interacts (via guanylate kinase-like domain) with
KIF13B (PubMed:10859302). May interact with HTR2A (By similarity).
Interacts (via PDZ domains) with GRIA1 (By similarity). Interacts
(via PDZ domains) with GRIN2A (By similarity). Interacts (via PDZ
domains) with KCND2 and KCND3 (PubMed:19213956). Interacts (via
PDZ domains) with KCNA1, KCNA2, KCNA3 and KCNA4 (PubMed:7477295).
Interacts (via PDZ domains) with ADGRA3 (PubMed:15021905).
Interacts with KCNF1 (PubMed:12445884). Interacts with CAMK2 (By
similarity). Interacts with cytoskeleton-associated protein EPB41
(PubMed:7937897, PubMed:8922391). Interacts with cytoskeleton-
associated protein EZR (By similarity). Found in a complex with
KCNA5 and CAV3 (By similarity). Found in a complex with APC and
CTNNB1 (PubMed:8638125, PubMed:10656683). Interacts with CDH1
through binding to PIK3R1 (PubMed:14699157). Forms multiprotein
complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12 (By
similarity). Interacts with TOPK (PubMed:10779557). Forms a
tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or
LIN7C) (PubMed:17237226, PubMed:17332497, PubMed:20702775). May
interact with TJAP1 (PubMed:11602598). Interacts with PTEN (By
similarity). Interacts with FRMPD4 (via C-terminus)
(PubMed:19118189). Interacts with LRFN1, LRFN2 and LRFN4
(PubMed:16630835). Interacts with SFPQ (PubMed:20605917).
Interacts (via PDZ domains) with ADGRA2 (via PDZ-binding motif)
(PubMed:15021905, PubMed:25558062). Interacts with the HTLV-1
viral Tax and HPV-18 E6 papillomavirus (HPV) oncoproteins
(PubMed:9192623, PubMed:10557085). {ECO:0000250|UniProtKB:Q62696,
ECO:0000250|UniProtKB:Q811D0, ECO:0000269|PubMed:10557085,
ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:10779557,
ECO:0000269|PubMed:10859302, ECO:0000269|PubMed:12445884,
ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15021905,
ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:17237226,
ECO:0000269|PubMed:17332497, ECO:0000269|PubMed:19118189,
ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917,
ECO:0000269|PubMed:20702775, ECO:0000269|PubMed:25558062,
ECO:0000269|PubMed:7477295, ECO:0000269|PubMed:7937897,
ECO:0000269|PubMed:8638125, ECO:0000269|PubMed:8922391,
ECO:0000269|PubMed:9192623, ECO:0000305}.
-!- INTERACTION:
P78536:ADAM17; NbExp=7; IntAct=EBI-357481, EBI-78188;
Q96PE1:ADGRA2; NbExp=2; IntAct=EBI-357500, EBI-10893263;
Q8IWK6-3:ADGRA3; NbExp=2; IntAct=EBI-357500, EBI-10949249;
A1A5B4:ANO9; NbExp=2; IntAct=EBI-357481, EBI-3843564;
Q9Y297:BTRC; NbExp=2; IntAct=EBI-357481, EBI-307461;
Q9NS75:CYSLTR2; NbExp=3; IntAct=EBI-357481, EBI-3843579;
P31016:Dlg4 (xeno); NbExp=9; IntAct=EBI-357500, EBI-375655;
O57125:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-7461590;
P03126:E6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-1177242;
P06427:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-11737184;
P06463:E6 (xeno); NbExp=4; IntAct=EBI-357481, EBI-1186926;
P17386:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-8516807;
P21735:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-11793794;
P24835:E6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-11793707;
P27228:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-11793748;
P36799:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-7363822;
P50804:E6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-11793696;
P54667:E6 (xeno); NbExp=2; IntAct=EBI-357481, EBI-11793910;
Q9NQT8:KIF13B; NbExp=3; IntAct=EBI-357500, EBI-766408;
O60333-3:KIF1B; NbExp=4; IntAct=EBI-357481, EBI-465669;
P36507:MAP2K2; NbExp=10; IntAct=EBI-357481, EBI-1056930;
Q7Z628:NET1; NbExp=2; IntAct=EBI-357481, EBI-2511306;
Q9ICL1:se6 (xeno); NbExp=3; IntAct=EBI-357481, EBI-7461477;
P09708:US32 (xeno); NbExp=2; IntAct=EBI-357481, EBI-11793940;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}.
Endoplasmic reticulum membrane {ECO:0000250}. Cell junction,
synapse, postsynaptic cell membrane, postsynaptic density
{ECO:0000250}. Cell junction, synapse. Cell membrane, sarcolemma.
Note=Colocalizes with EPB41 at regions of intercellular contacts.
Basolateral in epithelial cells. May also associate with
endoplasmic reticulum membranes. Mainly found in neurons soma,
moderately found at postsynaptic densities (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1;
IsoId=Q12959-1; Sequence=Displayed;
Name=2;
IsoId=Q12959-2; Sequence=VSP_003150;
Note=Contains a phosphoserine at position 709.
{ECO:0000244|PubMed:24275569};
Name=3;
IsoId=Q12959-3; Sequence=VSP_012862;
Name=4;
IsoId=Q12959-4; Sequence=VSP_012862, VSP_003150;
Note=Ref.6 (AAI44652) sequence is in conflict in position:
636:Q->Missing. Contains a phosphoserine at position 676.
{ECO:0000244|PubMed:24275569, ECO:0000305};
Name=5;
IsoId=Q12959-5; Sequence=VSP_012862, VSP_012863;
Name=6;
IsoId=Q12959-6; Sequence=VSP_012864;
Name=7;
IsoId=Q12959-7; Sequence=VSP_012865;
Name=8;
IsoId=Q12959-8; Sequence=VSP_045896, VSP_045897;
Note=No experimental confirmation available.;
Name=9;
IsoId=Q12959-9; Sequence=VSP_045896, VSP_045897, VSP_012865,
VSP_045898;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Abundantly expressed in atrial myocardium (at
protein level). Expressed in lung fibroblasts, cervical epithelial
and B-cells (at protein level). Widely expressed, with isoforms
displaying different expression profiles.
{ECO:0000269|PubMed:12445884, ECO:0000269|PubMed:19213956,
ECO:0000269|PubMed:7937897}.
-!- DOMAIN: The alternatively spliced domain I3 corresponding to amino
acids (636-669) of isoform 4 is an EPB41 binding site mediating
association to membranes in polarized and non-polarized cells.
-!- DOMAIN: The PDZ domains may also mediate association to membranes
by binding to EPB41 and ADGRA2 together with the L27 domain that
binds CASK and DLG2.
-!- DOMAIN: The L27 domain may regulate DLG1 self-association. The N-
terminal alternatively spliced region is capable of binding
several SH3 domains and also moderates the level of protein
oligomerization.
-!- PTM: Phosphorylated by MAPK12. Phosphorylation of Ser-232
regulates association with GRIN2A (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DLG1ID40333ch3q29.html";
-----------------------------------------------------------------------
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EMBL; U13896; AAA50598.1; -; mRNA.
EMBL; U13897; AAA50599.1; -; mRNA.
EMBL; AK294772; BAG57902.1; -; mRNA.
EMBL; AK294855; BAG57959.1; -; mRNA.
EMBL; EF553524; ABQ66269.1; -; mRNA.
EMBL; AC068302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471191; EAW53610.1; -; Genomic_DNA.
EMBL; CH471191; EAW53611.1; -; Genomic_DNA.
EMBL; CH471191; EAW53612.1; -; Genomic_DNA.
EMBL; CH471191; EAW53614.1; -; Genomic_DNA.
EMBL; BC140841; AAI40842.1; -; mRNA.
EMBL; BC144651; AAI44652.1; -; mRNA.
CCDS; CCDS3327.1; -. [Q12959-2]
CCDS; CCDS43194.1; -. [Q12959-1]
CCDS; CCDS56300.1; -. [Q12959-8]
CCDS; CCDS56301.1; -. [Q12959-9]
PIR; I38756; I38756.
PIR; I38757; I38757.
RefSeq; NP_001091894.1; NM_001098424.1. [Q12959-1]
RefSeq; NP_001191315.1; NM_001204386.1.
RefSeq; NP_001191316.1; NM_001204387.1. [Q12959-9]
RefSeq; NP_001191317.1; NM_001204388.1. [Q12959-8]
RefSeq; NP_001277912.1; NM_001290983.1. [Q12959-1]
RefSeq; NP_004078.2; NM_004087.2. [Q12959-2]
RefSeq; XP_005269346.1; XM_005269289.3. [Q12959-2]
RefSeq; XP_011510804.1; XM_011512502.2. [Q12959-1]
RefSeq; XP_011510805.1; XM_011512503.1.
RefSeq; XP_011510807.1; XM_011512505.1. [Q12959-3]
RefSeq; XP_011510808.1; XM_011512506.1. [Q12959-5]
RefSeq; XP_016861289.1; XM_017005800.1. [Q12959-2]
RefSeq; XP_016861290.1; XM_017005801.1. [Q12959-2]
RefSeq; XP_016861291.1; XM_017005802.1. [Q12959-2]
RefSeq; XP_016861292.1; XM_017005803.1. [Q12959-2]
RefSeq; XP_016861294.1; XM_017005805.1. [Q12959-1]
RefSeq; XP_016861295.1; XM_017005806.1. [Q12959-4]
RefSeq; XP_016861296.1; XM_017005807.1. [Q12959-4]
RefSeq; XP_016861297.1; XM_017005808.1. [Q12959-4]
RefSeq; XP_016861298.1; XM_017005809.1. [Q12959-4]
RefSeq; XP_016861299.1; XM_017005810.1.
RefSeq; XP_016861305.1; XM_017005816.1. [Q12959-3]
RefSeq; XP_016861306.1; XM_017005817.1. [Q12959-3]
RefSeq; XP_016861307.1; XM_017005818.1. [Q12959-3]
RefSeq; XP_016861308.1; XM_017005819.1. [Q12959-3]
RefSeq; XP_016861309.1; XM_017005820.1. [Q12959-5]
UniGene; Hs.292549; -.
PDB; 1PDR; X-ray; 2.80 A; A=457-555.
PDB; 2M3M; NMR; -; A=318-406.
PDB; 2OQS; NMR; -; A=318-406.
PDB; 2X7Z; X-ray; 2.00 A; A=311-407.
PDB; 3LRA; X-ray; 2.95 A; A=2-65.
PDB; 3RL7; X-ray; 2.30 A; A/B/C/D/E/F=220-317.
PDB; 3RL8; X-ray; 2.20 A; A/B/C/D/E=315-410.
PDB; 3W9Y; X-ray; 2.20 A; A=712-904.
PDB; 4AMH; X-ray; 2.30 A; A/B=315-405.
PDB; 4G69; X-ray; 2.00 A; A=310-407.
PDBsum; 1PDR; -.
PDBsum; 2M3M; -.
PDBsum; 2OQS; -.
PDBsum; 2X7Z; -.
PDBsum; 3LRA; -.
PDBsum; 3RL7; -.
PDBsum; 3RL8; -.
PDBsum; 3W9Y; -.
PDBsum; 4AMH; -.
PDBsum; 4G69; -.
ProteinModelPortal; Q12959; -.
SMR; Q12959; -.
BioGrid; 108083; 66.
CORUM; Q12959; -.
DIP; DIP-33957N; -.
ELM; Q12959; -.
IntAct; Q12959; 96.
MINT; MINT-107690; -.
STRING; 9606.ENSP00000345731; -.
iPTMnet; Q12959; -.
PhosphoSitePlus; Q12959; -.
SwissPalm; Q12959; -.
BioMuta; DLG1; -.
DMDM; 223590196; -.
EPD; Q12959; -.
MaxQB; Q12959; -.
PaxDb; Q12959; -.
PeptideAtlas; Q12959; -.
PRIDE; Q12959; -.
Ensembl; ENST00000346964; ENSP00000345731; ENSG00000075711. [Q12959-2]
Ensembl; ENST00000392382; ENSP00000376187; ENSG00000075711. [Q12959-3]
Ensembl; ENST00000419354; ENSP00000407531; ENSG00000075711. [Q12959-1]
Ensembl; ENST00000422288; ENSP00000413238; ENSG00000075711. [Q12959-5]
Ensembl; ENST00000443183; ENSP00000396658; ENSG00000075711. [Q12959-9]
Ensembl; ENST00000448528; ENSP00000391732; ENSG00000075711. [Q12959-1]
Ensembl; ENST00000450955; ENSP00000411278; ENSG00000075711. [Q12959-4]
Ensembl; ENST00000452595; ENSP00000398939; ENSG00000075711. [Q12959-8]
GeneID; 1739; -.
KEGG; hsa:1739; -.
UCSC; uc003fxn.4; human. [Q12959-1]
CTD; 1739; -.
DisGeNET; 1739; -.
EuPathDB; HostDB:ENSG00000075711.20; -.
GeneCards; DLG1; -.
HGNC; HGNC:2900; DLG1.
HPA; CAB016307; -.
HPA; HPA069593; -.
MIM; 601014; gene.
neXtProt; NX_Q12959; -.
OpenTargets; ENSG00000075711; -.
PharmGKB; PA27356; -.
eggNOG; KOG0708; Eukaryota.
eggNOG; COG0194; LUCA.
GeneTree; ENSGT00760000118866; -.
HOGENOM; HOG000232102; -.
HOVERGEN; HBG107814; -.
InParanoid; Q12959; -.
KO; K12076; -.
OMA; NPKCIDH; -.
OrthoDB; EOG091G0BB1; -.
PhylomeDB; Q12959; -.
TreeFam; TF323171; -.
Reactome; R-HSA-399719; Trafficking of AMPA receptors.
Reactome; R-HSA-447038; NrCAM interactions.
Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
SIGNOR; Q12959; -.
ChiTaRS; DLG1; human.
EvolutionaryTrace; Q12959; -.
GeneWiki; DLG1; -.
GenomeRNAi; 1739; -.
PMAP-CutDB; A5YKK7; -.
PRO; PR:Q12959; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000075711; -.
CleanEx; HS_DLG1; -.
ExpressionAtlas; Q12959; baseline and differential.
Genevisible; Q12959; HS.
GO; GO:0005605; C:basal lamina; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:BHF-UCL.
GO; GO:0030054; C:cell junction; IDA:UniProtKB.
GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0014704; C:intercalated disc; TAS:BHF-UCL.
GO; GO:0043219; C:lateral loop; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
GO; GO:0097016; F:L27 domain binding; IPI:BHF-UCL.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:UniProtKB.
GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0032947; F:protein complex scaffold activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0042982; P:amyloid precursor protein metabolic process; IEA:Ensembl.
GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
GO; GO:0070830; P:bicellular tight junction assembly; IDA:BHF-UCL.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
GO; GO:0034629; P:cellular protein complex localization; IMP:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0051660; P:establishment of centrosome localization; IMP:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
GO; GO:0060022; P:hard palate development; IEA:Ensembl.
GO; GO:0001771; P:immunological synapse formation; IEA:Ensembl.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0031579; P:membrane raft organization; IEA:Ensembl.
GO; GO:0007093; P:mitotic cell cycle checkpoint; NAS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0030432; P:peristalsis; IEA:Ensembl.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
GO; GO:1903764; P:regulation of potassium ion export across plasma membrane; ISS:BHF-UCL.
GO; GO:1903286; P:regulation of potassium ion import; ISS:BHF-UCL.
GO; GO:1902305; P:regulation of sodium ion transmembrane transport; TAS:BHF-UCL.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISS:BHF-UCL.
GO; GO:0048608; P:reproductive structure development; IEA:Ensembl.
GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IEA:Ensembl.
GO; GO:0002369; P:T cell cytokine production; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR016313; DLG1-like.
InterPro; IPR019590; DLG1_PEST_dom.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR020590; Guanylate_kinase_CS.
InterPro; IPR015143; L27_1.
InterPro; IPR004172; L27_dom.
InterPro; IPR036892; L27_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR019583; PDZ_assoc.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF09058; L27_1; 1.
Pfam; PF10608; MAGUK_N_PEST; 1.
Pfam; PF00595; PDZ; 3.
Pfam; PF10600; PDZ_assoc; 1.
Pfam; PF07653; SH3_2; 1.
PIRSF; PIRSF001741; MAGUK_DLGH; 1.
SMART; SM00072; GuKc; 1.
SMART; SM00569; L27; 1.
SMART; SM01277; MAGUK_N_PEST; 1.
SMART; SM00228; PDZ; 3.
SMART; SM00326; SH3; 1.
SUPFAM; SSF101288; SSF101288; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS51022; L27; 1.
PROSITE; PS50106; PDZ; 3.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Endoplasmic reticulum; Host-virus interaction;
Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Reference proteome; Repeat; SH3 domain; Synapse.
CHAIN 1 904 Disks large homolog 1.
/FTId=PRO_0000094548.
DOMAIN 4 64 L27. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 224 310 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 319 405 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 466 546 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 581 651 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 714 889 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
REGION 162 212 Interaction with SH3 domains.
MOD_RES 115 115 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000250|UniProtKB:Q62696}.
MOD_RES 399 399 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q811D0}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000250|UniProtKB:Q811D0}.
MOD_RES 619 619 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000250|UniProtKB:Q62696}.
VAR_SEQ 1 77 MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIF
QSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQ -> M
NYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSD
ELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSST (in
isoform 8 and isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045896.
VAR_SEQ 78 193 Missing (in isoform 8 and isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045897.
VAR_SEQ 162 194 Missing (in isoform 3, isoform 4 and
isoform 5). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7937897}.
/FTId=VSP_012862.
VAR_SEQ 195 212 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_012863.
VAR_SEQ 669 680 EIPDDMGSKGLK -> QSFNDKRKKNLFSRKFPFYKNKDQS
EQETSDADQ (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7937897}.
/FTId=VSP_003150.
VAR_SEQ 681 693 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_012864.
VAR_SEQ 693 693 Y -> YLILITDEYGCSKG (in isoform 7 and
isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012865.
VAR_SEQ 694 694 Missing (in isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045898.
VARIANT 140 140 K -> R (in dbSNP:rs1802668).
/FTId=VAR_054334.
VARIANT 278 278 R -> Q (in dbSNP:rs1134986).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:7937897}.
/FTId=VAR_054335.
VARIANT 899 899 P -> L (in dbSNP:rs34492126).
/FTId=VAR_054336.
MUTAGEN 38 40 INI->ANA: Loss of membrane association
and DLG2-binding.
{ECO:0000269|PubMed:12807908}.
CONFLICT 237 237 S -> N (in Ref. 2; BAG57902).
{ECO:0000305}.
CONFLICT 801 801 E -> G (in Ref. 1; AAA50598/AAA50599).
{ECO:0000305}.
STRAND 221 228 {ECO:0000244|PDB:3RL7}.
STRAND 233 239 {ECO:0000244|PDB:3RL7}.
STRAND 254 258 {ECO:0000244|PDB:3RL7}.
HELIX 263 267 {ECO:0000244|PDB:3RL7}.
STRAND 275 279 {ECO:0000244|PDB:3RL7}.
HELIX 289 298 {ECO:0000244|PDB:3RL7}.
STRAND 301 309 {ECO:0000244|PDB:3RL7}.
STRAND 317 323 {ECO:0000244|PDB:2X7Z}.
STRAND 331 337 {ECO:0000244|PDB:2X7Z}.
STRAND 348 353 {ECO:0000244|PDB:2X7Z}.
HELIX 358 362 {ECO:0000244|PDB:2X7Z}.
STRAND 370 374 {ECO:0000244|PDB:2X7Z}.
STRAND 377 382 {ECO:0000244|PDB:2OQS}.
HELIX 384 392 {ECO:0000244|PDB:2X7Z}.
STRAND 396 403 {ECO:0000244|PDB:2X7Z}.
STRAND 465 470 {ECO:0000244|PDB:1PDR}.
STRAND 472 474 {ECO:0000244|PDB:1PDR}.
STRAND 477 482 {ECO:0000244|PDB:1PDR}.
STRAND 484 487 {ECO:0000244|PDB:1PDR}.
STRAND 489 494 {ECO:0000244|PDB:1PDR}.
HELIX 499 503 {ECO:0000244|PDB:1PDR}.
STRAND 510 515 {ECO:0000244|PDB:1PDR}.
HELIX 525 533 {ECO:0000244|PDB:1PDR}.
STRAND 537 545 {ECO:0000244|PDB:1PDR}.
HELIX 547 554 {ECO:0000244|PDB:1PDR}.
STRAND 717 721 {ECO:0000244|PDB:3W9Y}.
HELIX 724 734 {ECO:0000244|PDB:3W9Y}.
TURN 736 738 {ECO:0000244|PDB:3W9Y}.
TURN 756 758 {ECO:0000244|PDB:3W9Y}.
HELIX 766 774 {ECO:0000244|PDB:3W9Y}.
STRAND 778 784 {ECO:0000244|PDB:3W9Y}.
STRAND 787 792 {ECO:0000244|PDB:3W9Y}.
HELIX 793 800 {ECO:0000244|PDB:3W9Y}.
TURN 801 803 {ECO:0000244|PDB:3W9Y}.
STRAND 805 808 {ECO:0000244|PDB:3W9Y}.
HELIX 813 820 {ECO:0000244|PDB:3W9Y}.
STRAND 826 830 {ECO:0000244|PDB:3W9Y}.
HELIX 855 864 {ECO:0000244|PDB:3W9Y}.
HELIX 865 867 {ECO:0000244|PDB:3W9Y}.
STRAND 869 872 {ECO:0000244|PDB:3W9Y}.
HELIX 877 892 {ECO:0000244|PDB:3W9Y}.
HELIX 900 902 {ECO:0000244|PDB:3W9Y}.
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


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