DLG1_HUMAN
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 03-AUG-2022, entry version 238.
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 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 [25]
RP INTERACTION WITH LIN7A; LIN7C AND MPP7.
RX PubMed=17237226; DOI=10.1074/jbc.m610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7 and
RT DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [26]
RP INTERACTION WITH MPP7.
RX PubMed=17332497; DOI=10.1091/mbc.e06-11-0980;
RA Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.;
RT "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates
RT epithelial tight junction formation.";
RL Mol. Biol. Cell 18:1744-1755(2007).
RN [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 with CDH1 through binding to PIK3R1 (PubMed:14699157). Forms
CC multiprotein complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and
CC KCNJ12 (By similarity). Interacts with TOPK (PubMed:10779557). Forms a
CC tripartite 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).
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:16630835,
CC ECO:0000269|PubMed:17237226, ECO:0000269|PubMed:17332497,
CC ECO:0000269|PubMed:17980554, ECO:0000269|PubMed:19118189,
CC ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917,
CC ECO:0000269|PubMed:20702775, ECO:0000269|PubMed:23676497,
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=3; 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="http://atlasgeneticsoncology.org/Genes/DLG1ID40333ch3q29.html";
CC ---------------------------------------------------------------------------
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DR EMBL; U13896; AAA50598.1; -; mRNA.
DR EMBL; U13897; AAA50599.1; -; mRNA.
DR EMBL; AK294772; BAG57902.1; -; mRNA.
DR EMBL; AK294855; BAG57959.1; -; mRNA.
DR EMBL; EF553524; ABQ66269.1; -; mRNA.
DR EMBL; AC068302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471191; EAW53610.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53611.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53612.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53614.1; -; Genomic_DNA.
DR EMBL; BC140841; AAI40842.1; -; mRNA.
DR EMBL; BC144651; AAI44652.1; -; mRNA.
DR 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 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. [Q12959-3]
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 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 AlphaFoldDB; Q12959; -.
DR SMR; Q12959; -.
DR BioGRID; 108083; 170.
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; 157.
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 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; Q12959; -.
DR PeptideAtlas; Q12959; -.
DR PRIDE; 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 ABCD; Q12959; 1 sequenced antibody.
DR Antibodypedia; 4273; 293 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 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; TQHMENH; -.
DR OrthoDB; 807583at2759; -.
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; 214 hits in 1096 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 209 other tissues.
DR ExpressionAtlas; Q12959; baseline and differential.
DR Genevisible; Q12959; HS.
DR GO; GO:0005912; C:adherens junction; IC: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:0097016; F:L27 domain binding; IPI:BHF-UCL.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
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:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
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:0032147; P:activation of protein kinase activity; 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 protein kinase B signaling; 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: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:0043491; P:protein kinase B signaling; IEA:Ensembl.
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:0097120; P:receptor localization to synapse; 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 Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00513; -.
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; IPR019583; PDZ_assoc.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; 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; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW 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 DLG2-
FT 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 221..228
FT /evidence="ECO:0007829|PDB:3RL7"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3RL7"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3RL7"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:3RL7"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3RL7"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:3RL7"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:3RL7"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:2X7Z"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:2X7Z"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:2X7Z"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:2X7Z"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:2X7Z"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:2OQS"
FT HELIX 384..392
FT /evidence="ECO:0007829|PDB:2X7Z"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:2X7Z"
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
