ID DLG1_HUMAN Reviewed; 904 AA. AC Q12959; A5YKK7; B4DGU1; B4DGZ8; B7ZMM0; B9EIQ5; D3DXB8; D3DXB9; E7EWL7; AC E9PG21; Q12958; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 27-MAR-2024, entry version 247. DE RecName: Full=Disks large homolog 1 {ECO:0000305}; DE AltName: Full=Synapse-associated protein 97; DE Short=SAP-97; DE Short=SAP97; DE AltName: Full=hDlg; GN Name=DLG1 {ECO:0000312|HGNC:HGNC:2900}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, INTERACTION WITH EPB41, AND VARIANT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., 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., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 targeting: RT the PDZ1-2 conformational unit and an alternatively spliced 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 tumor RT suppressor protein."; RL Science 272:1020-1023(1996). RN [10] RP INTERACTION WITH HPV-18 PROTEIN E6 (MICROBIAL INFECTION). 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 homolog of RT 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 (MICROBIAL INFECTION). 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 discs RT large tumor suppressor protein, hDLG, and perturbs its function in cell RT 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 homologue of RT the Drosophila discs large tumor suppressor in T 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 the RT 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., Takeuchi M., RA Takai Y.; RT "Pilt, a novel peripheral membrane protein at tight junctions in epithelial RT cells."; RL J. Biol. Chem. 276:48350-48355(2001). RN [16] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH RP 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 epithelial RT 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 assembly and RT 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., Wachtel H., RA Morris D.G., Lopez-Ilasaca M., Shaw A.C., Swat W., Seed B.; RT "Discs large (Dlg1) complexes in lymphocyte activation."; RL J. Cell Biol. 166:173-178(2004). RN [21] RP INTERACTION WITH ADGRA2 AND ADGRA3. 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 tumor RT suppressor gene to seven-pass transmembrane proteins, tumor endothelial RT 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 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [24] RP INTERACTION WITH MPP3. RC TISSUE=Retina; RX PubMed=16519681; DOI=10.1111/j.1742-4658.2006.05140.x; RA Kantardzhieva A., Alexeeva S., Versteeg I., Wijnholds J.; RT "MPP3 is recruited to the MPP5 protein scaffold at the retinal outer RT limiting membrane."; RL FEBS J. 273:1152-1165(2006). RN [25] 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., Kaang B.-K., RA Kim E.; RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of RT excitatory synapses."; RL Neuron 50:233-245(2006). RN [26] 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 and RT DLG1 that regulates the stability and localization of DLG1 to cell RT junctions."; RL J. Biol. Chem. 282:9392-9400(2007). RN [27] 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 facilitates RT epithelial tight junction formation."; RL Mol. Biol. Cell 18:1744-1755(2007). RN [28] RP INTERACTION WITH MARCHF2, AND UBIQUITINATION. RX PubMed=17980554; DOI=10.1016/j.cellsig.2007.08.019; RA Cao Z., Huett A., Kuballa P., Giallourakis C., Xavier R.J.; RT "DLG1 is an anchor for the E3 ligase MARCH2 at sites of cell-cell RT contact."; RL Cell. Signal. 20:73-82(2008). RN [29] 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., Kang G.B., RA 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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575; RP SER-684 AND SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [32] 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 [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [34] 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 tumour- RT suppressor hDlg in response to osmotic shock."; RL J. Cell Sci. 123:2596-2604(2010). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-568; SER-575 AND RP SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [36] 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., Buerckstuemmer T., RA 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 [37] RP FUNCTION, INTERACTION WITH ADAM10, AND TISSUE SPECIFICITY. RX PubMed=23676497; DOI=10.1172/jci65401; RA Marcello E., Saraceno C., Musardo S., Vara H., de la Fuente A.G., RA Pelucchi S., Di Marino D., Borroni B., Tramontano A., Perez-Otano I., RA Padovani A., Giustetto M., Gardoni F., Di Luca M.; RT "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's RT disease."; RL J. Clin. Invest. 123:2523-2538(2013). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-579, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-573, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 (ISOFORM 4), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [40] RP INTERACTION WITH MPP3. RX PubMed=24503895; DOI=10.1371/journal.pone.0082894; RA Murakami S., Sakurai-Yageta M., Maruyama T., Murakami Y.; RT "Trans-homophilic interaction of CADM1 activates PI3K by forming a complex RT with MAGuK-family proteins MPP3 and Dlg."; RL PLoS ONE 9:e82894-e82894(2014). RN [41] RP ERRATUM OF PUBMED:24503895. RX PubMed=25268382; DOI=10.1371/journal.pone.0110062; RA Murakami S., Sakurai-Yageta M., Maruyama T., Murakami Y.; RT "Trans-homophilic interaction of CADM1 activates PI3K by forming a complex RT with MAGuK-family proteins MPP3 and Dlg."; RL PLoS ONE 9:e110062-e110062(2014). RN [42] RP INTERACTION WITH ADGRA2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25558062; DOI=10.1016/j.celrep.2014.12.020; RA Posokhova E., Shukla A., Seaman S., Volate S., Hilton M.B., Wu B., RA Morris H., Swing D.A., Zhou M., Zudaire E., Rubin J.S., St Croix B.; RT "GPR124 functions as a WNT7-specific coactivator of canonical beta-catenin RT signaling."; RL Cell Rep. 10:123-130(2015). RN [43] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [44] 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). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-65 IN COMPLEX WITH MPP7 AND RP LIN7C, AND SUBUNIT. RX PubMed=20702775; DOI=10.1096/fj.10-163857; RA Yang X., Xie X., Chen L., Zhou H., Wang Z., Zhao W., Tian R., Zhang R., RA Tian C., Long J., Shen Y.; RT "Structural basis for tandem L27 domain-mediated polymerization."; RL FASEB J. 24:4806-4815(2010). CC -!- FUNCTION: Essential multidomain scaffolding protein required for normal CC development (By similarity). Recruits channels, receptors and signaling CC molecules to discrete plasma membrane domains in polarized cells. May CC play a role in adherens junction assembly, signal transduction, cell CC proliferation, synaptogenesis and lymphocyte activation. Regulates the CC excitability of cardiac myocytes by modulating the functional CC expression of Kv4 channels. Functional regulator of Kv1.5 channel. CC During long-term depression in hippocampal neurons, it recruits ADAM10 CC to the plasma membrane (PubMed:23676497). {ECO:0000250, CC ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:12445884, CC ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15263016, CC ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917, CC ECO:0000269|PubMed:23676497}. CC -!- SUBUNIT: Homotetramer (Probable). Interacts (via guanylate kinase-like CC domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A (By similarity). CC Interacts (via guanylate kinase-like domain) with KIF13B CC (PubMed:10859302). May interact with HTR2A (By similarity). Interacts CC (via PDZ domains) with GRIA1 (By similarity). Interacts (via PDZ CC domains) with GRIN2A (By similarity). Interacts (via PDZ domains) with CC KCND2 and KCND3 (PubMed:19213956). Interacts (via PDZ domains) with CC KCNA1, KCNA2, KCNA3 and KCNA4 (PubMed:7477295). Interacts (via PDZ CC domains) with ADGRA3 (PubMed:15021905). Interacts with KCNF1 CC (PubMed:12445884). Interacts with CAMK2 (By similarity). Interacts with CC cytoskeleton-associated protein EPB41 (PubMed:7937897, PubMed:8922391). CC Interacts with cytoskeleton-associated protein EZR (By similarity). CC Found in a complex with KCNA5 and CAV3 (By similarity). Found in a CC complex with APC and CTNNB1 (PubMed:8638125, PubMed:10656683). CC Interacts (via PDZ domains) with APC (PubMed:8638125). Interacts with CC CDH1 through binding to PIK3R1 (PubMed:14699157). Forms multiprotein CC complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12 (By CC similarity). Interacts with TOPK (PubMed:10779557). Forms a tripartite CC complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) CC (PubMed:17237226, PubMed:17332497, PubMed:20702775). May interact with CC TJAP1 (PubMed:11602598). Interacts with PTEN (By similarity). Interacts CC with FRMPD4 (via C-terminus) (PubMed:19118189). Interacts with LRFN1, CC LRFN2 and LRFN4 (PubMed:16630835). Interacts with SFPQ CC (PubMed:20605917). Interacts (via PDZ domains) with ADGRA2 (via PDZ- CC binding motif) (PubMed:15021905, PubMed:25558062). Interacts with CC ADAM10; this interaction recruits ADAM10 to the cell membrane during CC long-term depression in hippocampal neurons (PubMed:23676497). CC Interacts with DGKI (via PDZ-binding motif) (By similarity). Interacts CC (via PDZ domains) with MARCHF2 (via PDZ domain); the interaction leads CC to DLG1 ubiqtuitination and degradation (PubMed:17980554). Interacts CC (via N-terminus) with MPP3; this interaction connects CADM1 with DLG1 CC and links CADM1 with the regulatory subunit of phosphoinositide-3- CC kinase (PI3K) by forming a multiprotein complex and participates in CC cell spreading (PubMed:24503895, PubMed:16519681). CC {ECO:0000250|UniProtKB:Q62696, ECO:0000250|UniProtKB:Q811D0, CC ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:10779557, CC ECO:0000269|PubMed:10859302, ECO:0000269|PubMed:11602598, CC ECO:0000269|PubMed:12445884, ECO:0000269|PubMed:14699157, CC ECO:0000269|PubMed:15021905, ECO:0000269|PubMed:16519681, CC ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:17237226, CC ECO:0000269|PubMed:17332497, ECO:0000269|PubMed:17980554, CC ECO:0000269|PubMed:19118189, ECO:0000269|PubMed:19213956, CC ECO:0000269|PubMed:20605917, ECO:0000269|PubMed:20702775, CC ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:24503895, CC ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:7477295, CC ECO:0000269|PubMed:7937897, ECO:0000269|PubMed:8638125, CC ECO:0000269|PubMed:8922391, ECO:0000305}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 protein Tax. CC {ECO:0000269|PubMed:10557085}. CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus CC 18/HPV-18 protein E6. {ECO:0000269|PubMed:9192623}. CC -!- INTERACTION: CC Q12959; P78536: ADAM17; NbExp=7; IntAct=EBI-357481, EBI-78188; CC Q12959; Q96PE1: ADGRA2; NbExp=2; IntAct=EBI-357481, EBI-10893263; CC Q12959; Q9NQ90: ANO2; NbExp=2; IntAct=EBI-357481, EBI-20731422; CC Q12959; A1A5B4: ANO9; NbExp=2; IntAct=EBI-357481, EBI-3843564; CC Q12959; P25054: APC; NbExp=2; IntAct=EBI-357481, EBI-727707; CC Q12959; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-357481, EBI-1057448; CC Q12959; Q9Y297: BTRC; NbExp=2; IntAct=EBI-357481, EBI-307461; CC Q12959; Q86XJ0: CALHM3; NbExp=2; IntAct=EBI-357481, EBI-20731541; CC Q12959; P15813: CD1D; NbExp=2; IntAct=EBI-357481, EBI-15643544; CC Q12959; P34998: CRHR1; NbExp=2; IntAct=EBI-357481, EBI-3870393; CC Q12959; Q9UQB3: CTNND2; NbExp=2; IntAct=EBI-357481, EBI-7266482; CC Q12959; Q9NS75: CYSLTR2; NbExp=7; IntAct=EBI-357481, EBI-3843579; CC Q12959; O60447: EVI5; NbExp=2; IntAct=EBI-357481, EBI-852291; CC Q12959; P0C2L3: FAM163B; NbExp=3; IntAct=EBI-357481, EBI-11793223; CC Q12959; Q14CM0: FRMPD4; NbExp=4; IntAct=EBI-357481, EBI-311279; CC Q12959; Q13224: GRIN2B; NbExp=4; IntAct=EBI-357481, EBI-2256942; CC Q12959; Q14957: GRIN2C; NbExp=2; IntAct=EBI-357481, EBI-8285963; CC Q12959; P33402: GUCY1A2; NbExp=2; IntAct=EBI-357481, EBI-6911715; CC Q12959; Q9P2D3: HEATR5B; NbExp=2; IntAct=EBI-357481, EBI-2832021; CC Q12959; O60333-3: KIF1B; NbExp=4; IntAct=EBI-357481, EBI-465669; CC Q12959; P36507: MAP2K2; NbExp=10; IntAct=EBI-357481, EBI-1056930; CC Q12959; P53778: MAPK12; NbExp=2; IntAct=EBI-357481, EBI-602406; CC Q12959; Q7Z628: NET1; NbExp=5; IntAct=EBI-357481, EBI-2511306; CC Q12959; Q99569: PKP4; NbExp=3; IntAct=EBI-357481, EBI-726447; CC Q12959; P85299: PRR5; NbExp=2; IntAct=EBI-357481, EBI-1387467; CC Q12959; Q15311: RALBP1; NbExp=5; IntAct=EBI-357481, EBI-749285; CC Q12959; O15427: SLC16A3; NbExp=2; IntAct=EBI-357481, EBI-7600166; CC Q12959; Q9C0D5: TANC1; NbExp=3; IntAct=EBI-357481, EBI-11023211; CC Q12959; Q9ULK5: VANGL2; NbExp=2; IntAct=EBI-357481, EBI-1054279; CC Q12959; O57125: E6; Xeno; NbExp=2; IntAct=EBI-357481, EBI-7461590; CC Q12959; P03126: E6; Xeno; NbExp=3; IntAct=EBI-357481, EBI-1177242; CC Q12959; P06427: E6; Xeno; NbExp=3; IntAct=EBI-357481, EBI-11737184; CC Q12959; P06463: E6; Xeno; NbExp=4; IntAct=EBI-357481, EBI-1186926; CC Q12959; P17386: E6; Xeno; NbExp=2; IntAct=EBI-357481, EBI-8516807; CC Q12959; P21735: E6; Xeno; NbExp=2; IntAct=EBI-357481, EBI-11793794; CC Q12959; P24835: E6; Xeno; NbExp=3; IntAct=EBI-357481, EBI-11793707; CC Q12959; P27228: E6; Xeno; NbExp=2; IntAct=EBI-357481, EBI-11793748; CC Q12959; P36799: E6; Xeno; NbExp=2; IntAct=EBI-357481, EBI-7363822; CC Q12959; P50804: E6; Xeno; NbExp=3; IntAct=EBI-357481, EBI-11793696; CC Q12959; P54667: E6; Xeno; NbExp=2; IntAct=EBI-357481, EBI-11793910; CC Q12959; Q9ICL1: se6; Xeno; NbExp=3; IntAct=EBI-357481, EBI-7461477; CC Q12959; P09708: US32; Xeno; NbExp=2; IntAct=EBI-357481, EBI-11793940; CC Q12959-2; Q96PE1: ADGRA2; NbExp=2; IntAct=EBI-357500, EBI-10893263; CC Q12959-2; Q8IWK6-3: ADGRA3; NbExp=2; IntAct=EBI-357500, EBI-10949249; CC Q12959-2; Q9NQT8: KIF13B; NbExp=3; IntAct=EBI-357500, EBI-766408; CC Q12959-2; P31016: Dlg4; Xeno; NbExp=9; IntAct=EBI-357500, EBI-375655; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10859302, CC ECO:0000269|PubMed:11723125, ECO:0000269|PubMed:8922391}; Peripheral CC membrane protein {ECO:0000269|PubMed:8922391}. Basolateral cell CC membrane {ECO:0000269|PubMed:12807908}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q62696}. Postsynaptic density CC {ECO:0000250|UniProtKB:Q62696}. Synapse {ECO:0000250|UniProtKB:Q62696}. CC Cell membrane, sarcolemma {ECO:0000269|PubMed:12445884}. Apical cell CC membrane {ECO:0000269|PubMed:12445884}. Cell junction CC {ECO:0000269|PubMed:10859302, ECO:0000269|PubMed:11723125, CC ECO:0000269|PubMed:7937897}. Cytoplasm {ECO:0000269|PubMed:10859302}. CC Note=Colocalizes with EPB41 at regions of intercellular contacts. CC Basolateral in epithelial cells (PubMed:12807908). May also associate CC with endoplasmic reticulum membranes. Mainly found in neurons soma, CC moderately found at postsynaptic densities (By similarity). CC {ECO:0000250|UniProtKB:Q62696, ECO:0000269|PubMed:10859302, CC ECO:0000269|PubMed:12807908, ECO:0000269|PubMed:8922391, CC ECO:0000269|PubMed:9192623}. 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 Name=3; CC IsoId=Q12959-3; Sequence=VSP_012862; CC Name=4; CC IsoId=Q12959-4; Sequence=VSP_012862, VSP_003150; 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 Name=9; CC IsoId=Q12959-9; Sequence=VSP_045896, VSP_045897, VSP_012865, CC VSP_045898; CC -!- TISSUE SPECIFICITY: Abundantly expressed in atrial myocardium (at CC protein level). Expressed in lung fibroblasts, cervical epithelial and CC B-cells (at protein level). Expressed in the brain (at protein level) CC (PubMed:23676497). Widely expressed, with isoforms displaying different CC expression profiles. {ECO:0000269|PubMed:12445884, CC ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:23676497, CC ECO:0000269|PubMed:7937897}. 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 by CC binding to EPB41 and ADGRA2 together with the L27 domain that binds CC CASK and DLG2. CC -!- DOMAIN: The L27 domain may regulate DLG1 self-association. The N- CC terminal alternatively spliced region is capable of binding several SH3 CC domains and also moderates the level of protein oligomerization. CC -!- PTM: Phosphorylated by MAPK12. Phosphorylation of Ser-232 regulates CC association with GRIN2A (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated; by MARCHF2 which results in its degradation. CC {ECO:0000269|PubMed:17980554}. CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40333/DLG1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 CCDS; CCDS3327.1; -. [Q12959-2] DR CCDS; CCDS43194.1; -. [Q12959-1] DR CCDS; CCDS56300.1; -. [Q12959-8] DR CCDS; CCDS56301.1; -. [Q12959-9] DR CCDS; CCDS87192.1; -. [Q12959-4] DR CCDS; CCDS93449.1; -. [Q12959-5] DR CCDS; CCDS93452.1; -. [Q12959-3] DR PIR; I38756; I38756. DR PIR; I38757; I38757. DR RefSeq; NP_001091894.1; NM_001098424.1. [Q12959-1] DR RefSeq; NP_001191315.1; NM_001204386.1. DR RefSeq; NP_001191316.1; NM_001204387.1. [Q12959-9] DR RefSeq; NP_001191317.1; NM_001204388.1. [Q12959-8] DR RefSeq; NP_001277912.1; NM_001290983.1. [Q12959-1] DR RefSeq; NP_004078.2; NM_004087.2. [Q12959-2] DR RefSeq; XP_005269346.1; XM_005269289.3. [Q12959-2] DR RefSeq; XP_011510804.1; XM_011512502.2. [Q12959-1] DR RefSeq; XP_011510805.1; XM_011512503.1. DR RefSeq; XP_011510807.1; XM_011512505.1. DR RefSeq; XP_011510808.1; XM_011512506.1. DR RefSeq; XP_016861289.1; XM_017005800.1. [Q12959-2] DR RefSeq; XP_016861290.1; XM_017005801.1. [Q12959-2] DR RefSeq; XP_016861291.1; XM_017005802.1. [Q12959-2] DR RefSeq; XP_016861292.1; XM_017005803.1. [Q12959-2] DR RefSeq; XP_016861294.1; XM_017005805.1. DR RefSeq; XP_016861295.1; XM_017005806.1. DR RefSeq; XP_016861296.1; XM_017005807.1. DR RefSeq; XP_016861297.1; XM_017005808.1. DR RefSeq; XP_016861298.1; XM_017005809.1. DR RefSeq; XP_016861299.1; XM_017005810.1. DR RefSeq; XP_016861305.1; XM_017005816.1. DR RefSeq; XP_016861306.1; XM_017005817.1. DR RefSeq; XP_016861307.1; XM_017005818.1. DR RefSeq; XP_016861308.1; XM_017005819.1. DR RefSeq; XP_016861309.1; XM_017005820.1. DR PDB; 1PDR; X-ray; 2.80 A; A=457-555. DR PDB; 2M3M; NMR; -; A=318-406. DR PDB; 2OQS; NMR; -; A=318-406. 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 PDB; 7PC3; X-ray; 1.95 A; A=314-413. DR PDB; 8CN1; X-ray; 2.09 A; A/B/C/D/E/F/G/H/I/J/K/L=219-311. DR PDB; 8CN3; X-ray; 2.71 A; A/B=311-422. 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 PDBsum; 7PC3; -. DR PDBsum; 8CN1; -. DR PDBsum; 8CN3; -. DR AlphaFoldDB; Q12959; -. DR SMR; Q12959; -. DR BioGRID; 108083; 193. DR ComplexPortal; CPX-6168; Scribble cell polarity complex, DLG1-LLGL2-SCRIB variant. DR ComplexPortal; CPX-6192; Scribble cell polarity complex, DLG1-LLGL1-SCRIB variant. DR CORUM; Q12959; -. DR DIP; DIP-33957N; -. DR ELM; Q12959; -. DR IntAct; Q12959; 169. DR MINT; Q12959; -. DR STRING; 9606.ENSP00000345731; -. DR TCDB; 8.A.24.1.7; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family. DR GlyConnect; 1182; 1 N-Linked glycan (1 site). DR GlyCosmos; Q12959; 1 site, 1 glycan. DR GlyGen; Q12959; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; Q12959; -. DR PhosphoSitePlus; Q12959; -. DR SwissPalm; Q12959; -. DR BioMuta; DLG1; -. DR DMDM; 223590196; -. DR EPD; Q12959; -. DR jPOST; Q12959; -. DR MassIVE; Q12959; -. DR MaxQB; Q12959; -. DR PaxDb; 9606-ENSP00000345731; -. DR PeptideAtlas; Q12959; -. DR ProteomicsDB; 18869; -. DR ProteomicsDB; 20226; -. DR ProteomicsDB; 59049; -. [Q12959-1] DR ProteomicsDB; 59050; -. [Q12959-2] DR ProteomicsDB; 59051; -. [Q12959-3] DR ProteomicsDB; 59052; -. [Q12959-4] DR ProteomicsDB; 59053; -. [Q12959-5] DR ProteomicsDB; 59054; -. [Q12959-6] DR ProteomicsDB; 59055; -. [Q12959-7] DR Pumba; Q12959; -. DR ABCD; Q12959; 1 sequenced antibody. DR Antibodypedia; 4273; 330 antibodies from 41 providers. DR DNASU; 1739; -. DR Ensembl; ENST00000346964.6; ENSP00000345731.2; ENSG00000075711.21. [Q12959-2] DR Ensembl; ENST00000357674.9; ENSP00000350303.6; ENSG00000075711.21. [Q12959-4] DR Ensembl; ENST00000392382.6; ENSP00000376187.2; ENSG00000075711.21. [Q12959-3] DR Ensembl; ENST00000419354.5; ENSP00000407531.1; ENSG00000075711.21. [Q12959-1] DR Ensembl; ENST00000422288.6; ENSP00000413238.1; ENSG00000075711.21. [Q12959-5] DR Ensembl; ENST00000443183.5; ENSP00000396658.1; ENSG00000075711.21. [Q12959-9] DR Ensembl; ENST00000448528.6; ENSP00000391732.2; ENSG00000075711.21. [Q12959-1] DR Ensembl; ENST00000450955.5; ENSP00000411278.1; ENSG00000075711.21. [Q12959-4] DR Ensembl; ENST00000452595.5; ENSP00000398939.1; ENSG00000075711.21. [Q12959-8] DR Ensembl; ENST00000655488.1; ENSP00000499657.1; ENSG00000075711.21. [Q12959-3] DR Ensembl; ENST00000659716.1; ENSP00000499602.1; ENSG00000075711.21. [Q12959-3] DR Ensembl; ENST00000661453.1; ENSP00000499514.1; ENSG00000075711.21. [Q12959-3] DR Ensembl; ENST00000663148.1; ENSP00000499384.1; ENSG00000075711.21. [Q12959-3] DR Ensembl; ENST00000666007.1; ENSP00000499793.1; ENSG00000075711.21. [Q12959-5] DR Ensembl; ENST00000667157.1; ENSP00000499414.1; ENSG00000075711.21. [Q12959-4] DR Ensembl; ENST00000669565.1; ENSP00000499413.1; ENSG00000075711.21. [Q12959-4] DR Ensembl; ENST00000670455.1; ENSP00000499542.1; ENSG00000075711.21. [Q12959-4] DR Ensembl; ENST00000670935.1; ENSP00000499437.1; ENSG00000075711.21. [Q12959-1] DR Ensembl; ENST00000671185.1; ENSP00000499580.1; ENSG00000075711.21. [Q12959-3] DR GeneID; 1739; -. DR KEGG; hsa:1739; -. DR MANE-Select; ENST00000667157.1; ENSP00000499414.1; NM_001366207.1; NP_001353136.1. [Q12959-4] DR UCSC; uc003fxn.4; human. [Q12959-1] DR AGR; HGNC:2900; -. DR CTD; 1739; -. DR DisGeNET; 1739; -. DR GeneCards; DLG1; -. DR HGNC; HGNC:2900; DLG1. DR HPA; ENSG00000075711; Low tissue specificity. DR MalaCards; DLG1; -. DR MIM; 601014; gene. DR neXtProt; NX_Q12959; -. DR OpenTargets; ENSG00000075711; -. DR Orphanet; 199306; Cleft lip/palate. DR PharmGKB; PA27356; -. DR VEuPathDB; HostDB:ENSG00000075711; -. DR eggNOG; KOG0708; Eukaryota. DR GeneTree; ENSGT00940000159409; -. DR HOGENOM; CLU_001715_4_2_1; -. DR InParanoid; Q12959; -. DR OMA; WIASSDF; -. DR OrthoDB; 2879721at2759; -. DR PhylomeDB; Q12959; -. DR TreeFam; TF323171; -. DR BRENDA; 2.7.4.8; 2681. DR PathwayCommons; Q12959; -. DR Reactome; R-HSA-399719; Trafficking of AMPA receptors. DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor. DR Reactome; R-HSA-447038; NrCAM interactions. DR Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules. DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors. DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission. DR Reactome; R-HSA-9620244; Long-term potentiation. DR SignaLink; Q12959; -. DR SIGNOR; Q12959; -. DR BioGRID-ORCS; 1739; 215 hits in 1176 CRISPR screens. DR ChiTaRS; DLG1; human. DR EvolutionaryTrace; Q12959; -. DR GeneWiki; DLG1; -. DR GenomeRNAi; 1739; -. DR Pharos; Q12959; Tbio. DR PRO; PR:Q12959; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q12959; Protein. DR Bgee; ENSG00000075711; Expressed in endothelial cell and 211 other cell types or tissues. DR ExpressionAtlas; Q12959; baseline and differential. DR GO; GO:0005912; C:adherens junction; NAS:ComplexPortal. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IDA:BHF-UCL. DR GO; GO:0030054; C:cell junction; IDA:UniProtKB. DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 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:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB. 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; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. 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:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central. DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell. DR GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA: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:0019900; F:kinase binding; IEA:Ensembl. DR GO; GO:0097016; F:L27 domain binding; IPI:BHF-UCL. DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl. DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:UniProtKB. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0098919; F:structural constituent of postsynaptic density; IEA:Ensembl. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB. DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl. DR GO; GO:0042982; P:amyloid precursor protein metabolic process; IEA:Ensembl. DR GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB. DR GO; GO:0070830; P:bicellular tight junction assembly; IDA:BHF-UCL. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0043622; P:cortical microtubule organization; IMP: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:0051660; P:establishment of centrosome localization; IMP:UniProtKB. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central. 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:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:UniProtKB. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IBA:GO_Central. DR GO; GO:0030432; P:peristalsis; IEA:Ensembl. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL. DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL. DR GO; GO:0031503; P:protein-containing complex localization; IMP:UniProtKB. DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB. DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL. DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl. DR GO; GO:1903764; P:regulation of potassium ion export across plasma membrane; ISS:BHF-UCL. DR GO; GO:1903286; P:regulation of potassium ion import; ISS:BHF-UCL. DR GO; GO:1902473; P:regulation of protein localization to synapse; IDA:UniProtKB. DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; TAS:BHF-UCL. DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS:BHF-UCL. DR GO; GO:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISS: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:0042098; P:T cell proliferation; IEA:Ensembl. DR CDD; cd00071; GMPK; 1. DR CDD; cd00992; PDZ_signaling; 3. DR CDD; cd12031; SH3_DLG1; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 1.10.287.470; Helix hairpin bin; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR IDEAL; IID00513; -. DR InterPro; IPR019583; DLG1-4_PDZ_assoc. DR InterPro; IPR016313; DLG1-like. DR InterPro; IPR019590; DLG1_PEST_dom. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR015143; L27_1. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF5; DISKS LARGE HOMOLOG 1; 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; SM01277; MAGUK_N_PEST; 1. DR SMART; SM00228; PDZ; 3. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; L27 domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR SUPFAM; SSF50044; SH3-domain; 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. DR Genevisible; Q12959; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Cytoplasm; Endoplasmic reticulum; Host-virus interaction; Membrane; KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse; KW Ubl conjugation. FT CHAIN 1..904 FT /note="Disks large homolog 1" FT /id="PRO_0000094548" FT DOMAIN 4..64 FT /note="L27" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 224..310 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 319..405 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 466..546 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 581..651 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 714..889 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT REGION 162..212 FT /note="Interaction with SH3 domains" FT REGION 224..546 FT /note="Required for interaction with MARCHF2" FT /evidence="ECO:0000269|PubMed:17980554" FT REGION 662..693 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 662..676 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 115 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 122 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62696" FT MOD_RES 399 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q811D0" FT MOD_RES 568 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 573 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 575 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 579 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 598 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811D0" FT MOD_RES 619 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336" FT MOD_RES 684 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 687 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 834 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62696" FT VAR_SEQ 1..77 FT /note="MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDI FT QEFYEVTLLDNPKCIDRSKPSEPIQ -> MNYIFGNNTLLYSRGSRGGNTSSSHGSAGP FT KQKHWAKKGSSDELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSST (in isoform FT 8 and isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045896" FT VAR_SEQ 78..193 FT /note="Missing (in isoform 8 and isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045897" FT VAR_SEQ 162..194 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7937897" FT /id="VSP_012862" FT VAR_SEQ 195..212 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_012863" FT VAR_SEQ 669..680 FT /note="EIPDDMGSKGLK -> QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ FT (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7937897" FT /id="VSP_003150" FT VAR_SEQ 681..693 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_012864" FT VAR_SEQ 693 FT /note="Y -> YLILITDEYGCSKG (in isoform 7 and isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_012865" FT VAR_SEQ 694 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045898" FT VARIANT 140 FT /note="K -> R (in dbSNP:rs1802668)" FT /id="VAR_054334" FT VARIANT 278 FT /note="R -> Q (in dbSNP:rs1134986)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:7937897" FT /id="VAR_054335" FT VARIANT 899 FT /note="P -> L (in dbSNP:rs34492126)" FT /id="VAR_054336" FT MUTAGEN 38..40 FT /note="INI->ANA: Loss of membrane association and FT DLG2-binding." FT /evidence="ECO:0000269|PubMed:12807908" FT CONFLICT 237 FT /note="S -> N (in Ref. 2; BAG57902)" FT /evidence="ECO:0000305" FT CONFLICT 801 FT /note="E -> G (in Ref. 1; AAA50598/AAA50599)" FT /evidence="ECO:0000305" FT HELIX 5..20 FT /evidence="ECO:0007829|PDB:3LRA" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:3LRA" FT HELIX 30..42 FT /evidence="ECO:0007829|PDB:3LRA" FT HELIX 44..55 FT /evidence="ECO:0007829|PDB:3LRA" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:3LRA" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:3LRA" FT STRAND 220..228 FT /evidence="ECO:0007829|PDB:8CN1" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:8CN1" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:8CN1" FT HELIX 263..267 FT /evidence="ECO:0007829|PDB:8CN1" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:8CN1" FT HELIX 289..297 FT /evidence="ECO:0007829|PDB:8CN1" FT STRAND 301..310 FT /evidence="ECO:0007829|PDB:8CN1" FT STRAND 317..323 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 328..335 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 348..353 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:8CN3" FT HELIX 358..362 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 370..374 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 377..382 FT /evidence="ECO:0007829|PDB:2OQS" FT HELIX 384..392 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 396..403 FT /evidence="ECO:0007829|PDB:7PC3" FT STRAND 465..470 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 477..482 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 489..494 FT /evidence="ECO:0007829|PDB:1PDR" FT HELIX 499..503 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 510..515 FT /evidence="ECO:0007829|PDB:1PDR" FT HELIX 525..533 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 537..545 FT /evidence="ECO:0007829|PDB:1PDR" FT HELIX 547..554 FT /evidence="ECO:0007829|PDB:1PDR" FT STRAND 717..721 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 724..734 FT /evidence="ECO:0007829|PDB:3W9Y" FT TURN 736..738 FT /evidence="ECO:0007829|PDB:3W9Y" FT TURN 756..758 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 766..774 FT /evidence="ECO:0007829|PDB:3W9Y" FT STRAND 778..784 FT /evidence="ECO:0007829|PDB:3W9Y" FT STRAND 787..792 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 793..800 FT /evidence="ECO:0007829|PDB:3W9Y" FT TURN 801..803 FT /evidence="ECO:0007829|PDB:3W9Y" FT STRAND 805..808 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 813..820 FT /evidence="ECO:0007829|PDB:3W9Y" FT STRAND 826..830 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 855..864 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 865..867 FT /evidence="ECO:0007829|PDB:3W9Y" FT STRAND 869..872 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 877..892 FT /evidence="ECO:0007829|PDB:3W9Y" FT HELIX 900..902 FT /evidence="ECO:0007829|PDB:3W9Y" FT MOD_RES Q12959-2:709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q12959-4:676 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CONFLICT Q12959-4:636 FT /note="Missing (in Ref. 6; AAI44652)" FT /evidence="ECO:0000305" 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 //