ZO1_HUMAN
ID ZO1_HUMAN Reviewed; 1748 AA.
AC Q07157; B4E3K1; Q2NKP3; Q4ZGJ6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Tight junction protein ZO-1;
DE AltName: Full=Tight junction protein 1;
DE AltName: Full=Zona occludens protein 1;
DE AltName: Full=Zonula occludens protein 1;
GN Name=TJP1; Synonyms=ZO1;
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], AND VARIANT VAL-790.
RC TISSUE=Liver;
RX PubMed=8395056; DOI=10.1073/pnas.90.16.7834;
RA Willott E., Balda M.S., Fanning A.S., Jameson B., van Itallie C.,
RA Anderson J.M.;
RT "The tight junction protein ZO-1 is homologous to the Drosophila discs-
RT large tumor suppressor protein of septate junctions.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7834-7838(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT VAL-790.
RC TISSUE=Uterus;
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 [GENOMIC DNA], AND VARIANTS SER-471; VAL-790; LEU-930;
RP ARG-1110; ALA-1347 AND SER-1605.
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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 [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH OCLN, AND FUNCTION.
RX PubMed=7798316; DOI=10.1083/jcb.127.6.1617;
RA Furuse M., Itoh M., Hirase T., Nagafuchi A., Yonemura S., Tsukita S.,
RA Tsukita S.;
RT "Direct association of occludin with ZO-1 and its possible involvement in
RT the localization of occludin at tight junctions.";
RL J. Cell Biol. 127:1617-1626(1994).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=7542259; DOI=10.1242/jcs.108.4.1735;
RA Van Itallie C.M., Balda M.S., Anderson J.M.;
RT "Epidermal growth factor induces tyrosine phosphorylation and
RT reorganization of the tight junction protein ZO-1 in A431 cells.";
RL J. Cell Sci. 108:1735-1742(1995).
RN [8]
RP FUNCTION, DOMAIN, AND INTERACTION WITH ACTIN; TJP2 AND OCLN.
RX PubMed=9792688; DOI=10.1074/jbc.273.45.29745;
RA Fanning A.S., Jameson B.J., Jesaitis L.A., Anderson J.M.;
RT "The tight junction protein ZO-1 establishes a link between the
RT transmembrane protein occludin and the actin cytoskeleton.";
RL J. Biol. Chem. 273:29745-29753(1998).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CXADR.
RX PubMed=11734628; DOI=10.1073/pnas.261452898;
RA Cohen C.J., Shieh J.T.C., Pickles R.J., Okegawa T., Hsieh J.-T.,
RA Bergelson J.M.;
RT "The coxsackievirus and adenovirus receptor is a transmembrane component of
RT the tight junction.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15191-15196(2001).
RN [10]
RP DOMAIN, AND INTERACTION WITH ACTIN.
RX PubMed=12354695; DOI=10.1096/fj.02-0121fje;
RA Fanning A.S., Ma T.Y., Anderson J.M.;
RT "Isolation and functional characterization of the actin binding region in
RT the tight junction protein ZO-1.";
RL FASEB J. 16:1835-1837(2002).
RN [11]
RP INTERACTION WITH CGN.
RX PubMed=12023291; DOI=10.1074/jbc.m203717200;
RA D'Atri F., Nadalutti F., Citi S.;
RT "Evidence for a functional interaction between cingulin and ZO-1 in
RT cultured cells.";
RL J. Biol. Chem. 277:27757-27764(2002).
RN [12]
RP INTERACTION WITH GJD3.
RX PubMed=12154091; DOI=10.1074/jbc.m205348200;
RA Nielsen P.A., Beahm D.L., Giepmans B.N., Baruch A., Hall J.E., Kumar N.M.;
RT "Molecular cloning, functional expression, and tissue distribution of a
RT novel human gap junction-forming protein, connexin-31.9. Interaction with
RT zona occludens protein-1.";
RL J. Biol. Chem. 277:38272-38283(2002).
RN [13]
RP INTERACTION WITH GJA12.
RX PubMed=15183511; DOI=10.1016/j.neuroscience.2004.03.063;
RA Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M.,
RA Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.;
RT "Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes
RT and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain.";
RL Neuroscience 126:611-630(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-1366, AND
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 [15]
RP INTERACTION WITH DNMBP.
RX PubMed=17015620; DOI=10.1083/jcb.200605012;
RA Otani T., Ichii T., Aono S., Takeichi M.;
RT "Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial
RT cells.";
RL J. Cell Biol. 175:135-146(2006).
RN [16]
RP INTERACTION WITH TJP2.
RX PubMed=17897942; DOI=10.1074/jbc.m703826200;
RA Wu J., Yang Y., Zhang J., Ji P., Du W., Jiang P., Xie D., Huang H., Wu M.,
RA Zhang G., Wu J., Shi Y.;
RT "Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a
RT structural basis for the polymerization of claudins.";
RL J. Biol. Chem. 282:35988-35999(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-912, AND
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-277; SER-329;
RP SER-617; SER-912; SER-968 AND SER-1545, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-912 (ISOFORM SHORT), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP INTERACTION WITH UBN1.
RX PubMed=18823282; DOI=10.1042/bc20080072;
RA Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P.,
RA Sergeant A., Manet E., Boyer V., Gruffat H.;
RT "Characterization of the ubinuclein protein as a new member of the nuclear
RT and adhesion complex components (NACos).";
RL Biol. Cell 101:319-334(2009).
RN [21]
RP PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPRJ.
RX PubMed=19332538; DOI=10.1074/jbc.m901901200;
RA Sallee J.L., Burridge K.;
RT "Density-enhanced phosphatase 1 regulates phosphorylation of tight junction
RT proteins and enhances barrier function of epithelial cells.";
RL J. Biol. Chem. 284:14997-15006(2009).
RN [22]
RP INTERACTION WITH MYZAP.
RX PubMed=20093627; DOI=10.1161/circresaha.109.213256;
RA Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R.,
RA Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A.,
RA Olson E.N., Frey N.;
RT "Myozap, a novel intercalated disc protein, activates serum response
RT factor-dependent signaling and is required to maintain cardiac function in
RT vivo.";
RL Circ. Res. 106:880-890(2010).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-337; SER-353;
RP SER-617; SER-968; SER-1366 AND SER-1617, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-912 (ISOFORM SHORT), AND IDENTIFICATION BY MASS
RP 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 [24]
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 [25]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND ACTIN-BINDING.
RX PubMed=20930113; DOI=10.1096/fj.10-155598;
RA Kremerskothen J., Stoelting M., Wiesner C., Korb-Pap A., van Vliet V.,
RA Linder S., Huber T.B., Rottiers P., Reuzeau E., Genot E., Pavenstaedt H.;
RT "Zona occludens proteins modulate podosome formation and function.";
RL FASEB J. 25:505-514(2011).
RN [26]
RP INTERACTION WITH ANKRD2.
RX PubMed=22016770; DOI=10.1371/journal.pone.0025519;
RA Belgrano A., Rakicevic L., Mittempergher L., Campanaro S., Martinelli V.C.,
RA Mouly V., Valle G., Kojic S., Faulkner G.;
RT "Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling
RT network of striated muscle.";
RL PLoS ONE 6:E25519-E25519(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-178;
RP SER-179; THR-185; SER-297; SER-300; SER-329; SER-334; SER-337; SER-617;
RP SER-622 AND SER-1366, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912
RP (ISOFORM SHORT), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-212; SER-329;
RP THR-354; SER-617; SER-837; SER-912; SER-968; SER-1111; SER-1413 AND
RP SER-1617, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-179;
RP THR-267; SER-275; SER-277; SER-280; SER-284; SER-290; SER-294; SER-297;
RP SER-300; SER-617; THR-809; SER-821; THR-854; THR-861; THR-868; SER-912;
RP SER-968 AND SER-1617, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912
RP (ISOFORM SHORT), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [30]
RP SUBCELLULAR LOCATION.
RX PubMed=28169360; DOI=10.1038/srep42125;
RA Liu J., Li J., Li P., Wang Y., Liang Z., Jiang Y., Li J., Feng C., Wang R.,
RA Chen H., Zhou C., Zhang J., Yang J., Liu P.;
RT "Loss of DLG5 promotes breast cancer malignancy by inhibiting the Hippo
RT signaling pathway.";
RL Sci. Rep. 7:42125-42125(2017).
RN [31]
RP INTERACTION WITH SPEF1, AND SUBCELLULAR LOCATION.
RX PubMed=31473225; DOI=10.1053/j.gastro.2019.08.031;
RA Tapia R., Perez-Yepez E.A., Carlino M.J., Karandikar U.C., Kralicek S.E.,
RA Estes M.K., Hecht G.A.;
RT "Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and
RT Contributes to Formation of Filopodia and Lamellipodia.";
RL Gastroenterology 157:1544-1555(2019).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-110, AND SUBUNIT.
RX PubMed=16737969; DOI=10.1074/jbc.m602901200;
RA Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J.,
RA Sidhu S.S., Wiesmann C.;
RT "Comparative structural analysis of the erbin PDZ domain and the first PDZ
RT domain of ZO-1. Insights into determinants of PDZ domain specificity.";
RL J. Biol. Chem. 281:22312-22320(2006).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 185-264, AND SUBUNIT.
RX PubMed=17928286; DOI=10.1074/jbc.m707255200;
RA Fanning A.S., Lye M.F., Anderson J.M., Lavie A.;
RT "Domain swapping within PDZ2 is responsible for dimerization of ZO
RT proteins.";
RL J. Biol. Chem. 282:37710-37716(2007).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 182-273 IN COMPLEX WITH GJA1
RP PEPTIDE, SUBUNIT, MUTAGENESIS OF ARG-201 AND LYS-209, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH GJA1.
RX PubMed=18636092; DOI=10.1038/emboj.2008.138;
RA Chen J., Pan L., Wei Z., Zhao Y., Zhang M.;
RT "Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory
RT connexin43-binding sites.";
RL EMBO J. 27:2113-2123(2008).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 516-803, AND INTERACTION WITH
RP CALM.
RX PubMed=20200156; DOI=10.1074/jbc.m109.093674;
RA Lye M.F., Fanning A.S., Su Y., Anderson J.M., Lavie A.;
RT "Insights into regulated ligand binding sites from the structure of ZO-1
RT Src homology 3-guanylate kinase module.";
RL J. Biol. Chem. 285:13907-13917(2010).
RN [36]
RP STRUCTURE BY NMR OF 1631-1748 OF MUTANT 1699-MET-CYS-1700 IN COMPLEX WITH
RP MYZAP, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1699-MET-CYS-1700 AND
RP PHE-1748, AND INTERACTION WITH MYZAP AND CDC42BPB.
RX PubMed=21240187; DOI=10.1038/emboj.2010.353;
RA Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.;
RT "Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge
RT controls cell migration.";
RL EMBO J. 30:665-678(2011).
RN [37]
RP STRUCTURE BY NMR OF 185-264.
RX PubMed=21387411; DOI=10.1002/prot.22955;
RA Ji P., Yang G., Zhang J., Wu J., Chen Z., Gong Q., Wu J., Shi Y.;
RT "Solution structure of the second PDZ domain of Zonula Occludens 1.";
RL Proteins 79:1342-1346(2011).
CC -!- FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins
CC that link tight junction (TJ) transmembrane proteins such as claudins,
CC junctional adhesion molecules, and occludin to the actin cytoskeleton
CC (PubMed:7798316, PubMed:9792688). The tight junction acts to limit
CC movement of substances through the paracellular space and as a boundary
CC between the compositionally distinct apical and basolateral plasma
CC membrane domains of epithelial and endothelial cells. Necessary for
CC lumenogenesis, and particularly efficient epithelial polarization and
CC barrier formation (By similarity). Plays a role in the regulation of
CC cell migration by targeting CDC42BPB to the leading edge of migrating
CC cells (PubMed:21240187). Plays an important role in podosome formation
CC and associated function, thus regulating cell adhesion and matrix
CC remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the
CC junctional retention and stability of the transcription factor DBPA,
CC but is not involved in its shuttling to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O97758, ECO:0000269|PubMed:20930113,
CC ECO:0000269|PubMed:21240187}.
CC -!- SUBUNIT: Homodimer (PubMed:17928286). Forms heterodimers (via the PDZ2
CC domain) with TJP2 and TJP3 (PubMed:9792688, PubMed:17928286,
CC PubMed:16737969, PubMed:17897942). Interacts with OCLN, CALM, claudins,
CC CGN/cingulin, CXADR, GJA12, GJD3 and UBN1 (PubMed:7798316,
CC PubMed:11734628, PubMed:12023291, PubMed:12154091, PubMed:15183511,
CC PubMed:18823282, PubMed:20200156). Interacts (via ZU5 domain) with
CC CDC42BPB and MYZAP (PubMed:20093627, PubMed:21240187). Interacts (via
CC PDZ domain) with GJA1 (PubMed:18636092). Interacts (via PDZ domains)
CC with ANKRD2 (PubMed:22016770). Interacts with BVES (via the C-terminus
CC cytoplasmic tail) (By similarity). Interacts with HSPA4 and KIRREL1 (By
CC similarity). Interacts with DLL1 (By similarity). Interacts with USP53
CC (via the C-terminal region) (By similarity). Interacts (via ABR region)
CC with F-actin (PubMed:9792688, PubMed:12354695, PubMed:20930113).
CC Interacts with DNMBP (via C-terminal domain); required for the apical
CC cell-cell junction localization of DNMBP (PubMed:17015620). Interacts
CC with SPEF1 (PubMed:31473225). {ECO:0000250|UniProtKB:O97758,
CC ECO:0000250|UniProtKB:P39447, ECO:0000269|PubMed:11734628,
CC ECO:0000269|PubMed:12023291, ECO:0000269|PubMed:12154091,
CC ECO:0000269|PubMed:12354695, ECO:0000269|PubMed:15183511,
CC ECO:0000269|PubMed:16737969, ECO:0000269|PubMed:17015620,
CC ECO:0000269|PubMed:17897942, ECO:0000269|PubMed:17928286,
CC ECO:0000269|PubMed:18636092, ECO:0000269|PubMed:18823282,
CC ECO:0000269|PubMed:20093627, ECO:0000269|PubMed:20200156,
CC ECO:0000269|PubMed:20930113, ECO:0000269|PubMed:21240187,
CC ECO:0000269|PubMed:22016770, ECO:0000269|PubMed:31473225,
CC ECO:0000269|PubMed:9792688}.
CC -!- INTERACTION:
CC Q07157; O43707: ACTN4; NbExp=4; IntAct=EBI-79553, EBI-351526;
CC Q07157; P17302: GJA1; NbExp=3; IntAct=EBI-79553, EBI-1103439;
CC Q07157; Q8N144: GJD3; NbExp=2; IntAct=EBI-79553, EBI-2629520;
CC Q07157; Q96J84: KIRREL1; NbExp=7; IntAct=EBI-79553, EBI-3988456;
CC Q07157; Q9EPK5: Wwtr1; Xeno; NbExp=4; IntAct=EBI-79553, EBI-1211920;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7798316};
CC Peripheral membrane protein {ECO:0000269|PubMed:7798316}; Cytoplasmic
CC side {ECO:0000269|PubMed:7798316}. Cell junction, tight junction
CC {ECO:0000269|PubMed:7798316}. Cell junction
CC {ECO:0000269|PubMed:28169360}. Cell junction, gap junction. Cell
CC projection, podosome {ECO:0000269|PubMed:20930113}. Note=Moves from the
CC cytoplasm to the cell membrane concurrently with cell-cell contact
CC (PubMed:7798316). At podosomal sites, is predominantly localized in the
CC ring structure surrounding the actin core (PubMed:20930113).
CC Colocalizes with SPEF1 at sites of cell-cell contact in intestinal
CC epithelial cells (PubMed:31473225). {ECO:0000269|PubMed:20930113,
CC ECO:0000269|PubMed:31473225, ECO:0000269|PubMed:7798316}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q07157-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q07157-2; Sequence=VSP_003148;
CC -!- TISSUE SPECIFICITY: The alpha-containing isoform is found in most
CC epithelial cell junctions. The short isoform is found both in
CC endothelial cells and the highly specialized epithelial junctions of
CC renal glomeruli and Sertoli cells of the seminiferous tubules.
CC -!- DOMAIN: The 244-aa domain between residues 633 and 876 is the primary
CC occludin (OCLN)-binding site and is required for stable association
CC with the tight junction (PubMed:9792688). {ECO:0000269|PubMed:9792688}.
CC -!- DOMAIN: The C-terminal region (residues 1151-1372) is an actin-binding
CC region (ABR) that interacts directly with F-actin and plays an
CC important role in the localization of TJP1 at junctions
CC (PubMed:9792688, PubMed:12354695, PubMed:20930113). The ABR is also
CC required for the localization to puncta at the free edge of cells
CC before initiation of cell-cell contact (PubMed:12354695). The ABR is
CC also necessary for TJP1 recruitment to podosomes (PubMed:20930113).
CC {ECO:0000269|PubMed:12354695, ECO:0000269|PubMed:20930113,
CC ECO:0000269|PubMed:9792688}.
CC -!- DOMAIN: The second PDZ domain (PDZ2) mediates homodimerization and
CC heterodimerization with TJP2 and TJP3 (PubMed:9792688,
CC PubMed:17928286). {ECO:0000269|PubMed:17928286,
CC ECO:0000269|PubMed:9792688}.
CC -!- PTM: Phosphorylated at tyrosine redidues in response to epidermal
CC growth factor (EGF) (PubMed:19332538, PubMed:7542259). This response is
CC dependent on an intact actin microfilament system (PubMed:7542259).
CC Dephosphorylated by PTPRJ (PubMed:19332538).
CC {ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:7542259}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02891.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tjp1/";
CC ---------------------------------------------------------------------------
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DR EMBL; L14837; AAA02891.1; ALT_INIT; mRNA.
DR EMBL; AK304758; BAG65513.1; -; mRNA.
DR EMBL; DQ015919; AAY22179.1; -; Genomic_DNA.
DR EMBL; AC022613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111712; AAI11713.1; -; mRNA.
DR CCDS; CCDS42007.1; -. [Q07157-1]
DR CCDS; CCDS45199.1; -. [Q07157-2]
DR PIR; A47747; A47747.
DR RefSeq; NP_003248.3; NM_003257.4. [Q07157-1]
DR RefSeq; NP_783297.2; NM_175610.3. [Q07157-2]
DR PDB; 2H2B; X-ray; 1.60 A; A=18-110.
DR PDB; 2H2C; X-ray; 2.00 A; A=18-110.
DR PDB; 2H3M; X-ray; 2.90 A; A=18-110.
DR PDB; 2JWE; NMR; -; A/B=185-264.
DR PDB; 2KXR; NMR; -; A=1631-1748.
DR PDB; 2KXS; NMR; -; A=1631-1748.
DR PDB; 2RCZ; X-ray; 1.70 A; A/B=186-264.
DR PDB; 3CYY; X-ray; 2.40 A; A/B=182-273.
DR PDB; 3LH5; X-ray; 2.60 A; A=516-803.
DR PDB; 3SHU; X-ray; 2.75 A; A/B=421-512.
DR PDB; 3SHW; X-ray; 2.90 A; A=421-888.
DR PDB; 3TSV; X-ray; 1.99 A; A=417-516.
DR PDB; 3TSW; X-ray; 2.85 A; A/B/C/D=417-803.
DR PDB; 3TSZ; X-ray; 2.50 A; A=417-803.
DR PDB; 4OEO; X-ray; 1.90 A; A/B/C=18-110.
DR PDB; 4OEP; X-ray; 2.35 A; A/B=18-110.
DR PDB; 4Q2Q; X-ray; 1.45 A; A=419-504.
DR PDB; 4YYX; X-ray; 1.79 A; A/B=18-110.
DR PDBsum; 2H2B; -.
DR PDBsum; 2H2C; -.
DR PDBsum; 2H3M; -.
DR PDBsum; 2JWE; -.
DR PDBsum; 2KXR; -.
DR PDBsum; 2KXS; -.
DR PDBsum; 2RCZ; -.
DR PDBsum; 3CYY; -.
DR PDBsum; 3LH5; -.
DR PDBsum; 3SHU; -.
DR PDBsum; 3SHW; -.
DR PDBsum; 3TSV; -.
DR PDBsum; 3TSW; -.
DR PDBsum; 3TSZ; -.
DR PDBsum; 4OEO; -.
DR PDBsum; 4OEP; -.
DR PDBsum; 4Q2Q; -.
DR PDBsum; 4YYX; -.
DR AlphaFoldDB; Q07157; -.
DR BMRB; Q07157; -.
DR SMR; Q07157; -.
DR BioGRID; 112937; 246.
DR CORUM; Q07157; -.
DR ELM; Q07157; -.
DR IntAct; Q07157; 84.
DR MINT; Q07157; -.
DR STRING; 9606.ENSP00000281537; -.
DR ChEMBL; CHEMBL4296026; -.
DR TCDB; 8.A.24.1.9; the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family.
DR GlyGen; Q07157; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q07157; -.
DR PhosphoSitePlus; Q07157; -.
DR BioMuta; TJP1; -.
DR DMDM; 85700443; -.
DR EPD; Q07157; -.
DR jPOST; Q07157; -.
DR MassIVE; Q07157; -.
DR MaxQB; Q07157; -.
DR PaxDb; Q07157; -.
DR PeptideAtlas; Q07157; -.
DR PRIDE; Q07157; -.
DR ProteomicsDB; 58506; -. [Q07157-1]
DR ProteomicsDB; 58507; -. [Q07157-2]
DR Antibodypedia; 783; 448 antibodies from 41 providers.
DR DNASU; 7082; -.
DR Ensembl; ENST00000346128.10; ENSP00000281537.7; ENSG00000104067.17. [Q07157-1]
DR Ensembl; ENST00000545208.6; ENSP00000441202.2; ENSG00000104067.17. [Q07157-2]
DR Ensembl; ENST00000621049.4; ENSP00000484535.2; ENSG00000277401.4.
DR GeneID; 7082; -.
DR KEGG; hsa:7082; -.
DR UCSC; uc001zcr.4; human. [Q07157-1]
DR CTD; 7082; -.
DR DisGeNET; 7082; -.
DR GeneCards; TJP1; -.
DR HGNC; HGNC:11827; TJP1.
DR HPA; ENSG00000104067; Low tissue specificity.
DR MIM; 601009; gene.
DR neXtProt; NX_Q07157; -.
DR OpenTargets; ENSG00000104067; -.
DR PharmGKB; PA36532; -.
DR VEuPathDB; HostDB:ENSG00000104067; -.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000155164; -.
DR InParanoid; Q07157; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q07157; -.
DR TreeFam; TF315957; -.
DR PathwayCommons; Q07157; -.
DR Reactome; R-HSA-191650; Regulation of gap junction activity.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-HSA-8935964; RUNX1 regulates expression of components of tight junctions.
DR Reactome; R-HSA-9705677; SARS-CoV-2 targets PDZ proteins in cell-cell junction.
DR SignaLink; Q07157; -.
DR SIGNOR; Q07157; -.
DR BioGRID-ORCS; 7082; 19 hits in 1086 CRISPR screens.
DR ChiTaRS; TJP1; human.
DR EvolutionaryTrace; Q07157; -.
DR GeneWiki; Tight_junction_protein_1; -.
DR GenomeRNAi; 7082; -.
DR Pharos; Q07157; Tbio.
DR PRO; PR:Q07157; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q07157; protein.
DR Bgee; ENSG00000104067; Expressed in corpus callosum and 95 other tissues.
DR ExpressionAtlas; Q07157; baseline and differential.
DR Genevisible; Q07157; HS.
DR GO; GO:0005912; C:adherens junction; TAS:ProtInc.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005921; C:gap junction; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:ARUK-UCL.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:ProtInc.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:ARUK-UCL.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:UniProtKB.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:2000250; P:negative regulation of actin cytoskeleton reorganization; IMP:ARUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ARUK-UCL.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:ARUK-UCL.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IMP:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IMP:ARUK-UCL.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:ARUK-UCL.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:ARUK-UCL.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; IMP:ARUK-UCL.
DR GO; GO:0150105; P:protein localization to cell-cell junction; IMP:ARUK-UCL.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:1901888; P:regulation of cell junction assembly; IMP:ARUK-UCL.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:ARUK-UCL.
DR CDD; cd12026; SH3_ZO-1; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR005417; ZO.
DR InterPro; IPR005418; ZO-1.
DR InterPro; IPR035597; ZO-1_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR13865:SF25; PTHR13865:SF25; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01598; ZONOCCLUDNS1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calmodulin-binding; Cell junction;
KW Cell membrane; Cell projection; Gap junction; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..1748
FT /note="Tight junction protein ZO-1"
FT /id="PRO_0000094540"
FT DOMAIN 23..110
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 186..264
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 421..502
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 516..584
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 598..779
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 1634..1748
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT REGION 102..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..876
FT /note="Occludin (OCLN)-binding region"
FT /evidence="ECO:0000269|PubMed:9792688"
FT REGION 825..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1371
FT /note="Actin-binding region (ABR)"
FT /evidence="ECO:0000269|PubMed:12354695"
FT COMPBIAS 134..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 809
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 848
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 854
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 868
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1165
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 922..1001
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_003148"
FT VARIANT 471
FT /note="N -> S (in dbSNP:rs2229517)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025153"
FT VARIANT 790
FT /note="I -> V (in dbSNP:rs2229515)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8395056, ECO:0000269|Ref.3"
FT /id="VAR_025154"
FT VARIANT 930
FT /note="P -> L (in dbSNP:rs45529137)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025155"
FT VARIANT 1110
FT /note="H -> R (in dbSNP:rs45567033)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025156"
FT VARIANT 1347
FT /note="D -> A (in dbSNP:rs2291166)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025157"
FT VARIANT 1605
FT /note="N -> S (in dbSNP:rs45578638)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025158"
FT MUTAGEN 201
FT /note="R->A: Strongly reduced interaction with GJA1."
FT /evidence="ECO:0000269|PubMed:18636092"
FT MUTAGEN 209
FT /note="K->A: Abolishes interaction with GJA1."
FT /evidence="ECO:0000269|PubMed:18636092"
FT MUTAGEN 1699..1700
FT /note="MC->AA: Abolishes interaction with CDC42BPB."
FT /evidence="ECO:0000269|PubMed:21240187"
FT MUTAGEN 1748
FT /note="Missing: Abolishes interaction with CDC42BPB and
FT MYZAP."
FT /evidence="ECO:0000269|PubMed:21240187"
FT CONFLICT 394..417
FT /note="QPDVDLPVSPSDGVLPNSTHEDGI -> NQMWIYLSVHLMVSYLIQLMKMGF
FT (in Ref. 1; AAA02891)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="V -> A (in Ref. 1; AAA02891)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="I -> Y (in Ref. 1; AAA02891)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="R -> A (in Ref. 1; AAA02891)"
FT /evidence="ECO:0000305"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:2H2B"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2H2B"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2H2B"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2H2B"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2H2B"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:4YYX"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2H2B"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:2H2B"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:2H2B"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2RCZ"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2JWE"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2JWE"
FT STRAND 200..211
FT /evidence="ECO:0007829|PDB:2RCZ"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:2RCZ"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2RCZ"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:2RCZ"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:3CYY"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2RCZ"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:3SHW"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT HELIX 480..489
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:4Q2Q"
FT HELIX 504..510
FT /evidence="ECO:0007829|PDB:3TSV"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 553..562
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 568..575
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 577..584
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 632..640
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 654..664
FT /evidence="ECO:0007829|PDB:3TSZ"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 691..698
FT /evidence="ECO:0007829|PDB:3TSZ"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 710..718
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 724..729
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 733..743
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 751..765
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 766..768
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:3TSZ"
FT HELIX 781..795
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 796..801
FT /evidence="ECO:0007829|PDB:3TSZ"
FT STRAND 1633..1640
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1645..1648
FT /evidence="ECO:0007829|PDB:2KXR"
FT TURN 1650..1652
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1655..1658
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1669..1677
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1679..1681
FT /evidence="ECO:0007829|PDB:2KXR"
FT TURN 1687..1689
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1701..1703
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1706..1715
FT /evidence="ECO:0007829|PDB:2KXR"
FT HELIX 1720..1723
FT /evidence="ECO:0007829|PDB:2KXS"
FT HELIX 1732..1734
FT /evidence="ECO:0007829|PDB:2KXR"
FT TURN 1735..1737
FT /evidence="ECO:0007829|PDB:2KXR"
FT STRAND 1738..1747
FT /evidence="ECO:0007829|PDB:2KXR"
FT MOD_RES Q07157-2:912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1748 AA; 195459 MW; 189E31617084C0CC CRC64;
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD
PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS ASRERSLSPR SDRRSVASSQ
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD
DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK
LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN LTNVRLEEPT
PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT KVYRKDPYPE EMMRQNHVLK
QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY
EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY
DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK
PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD
KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL
SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ
PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK
PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA
VEEDEDEDGH TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS
ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC
VSVLIDHF
