ID ZO2_HUMAN Reviewed; 1190 AA. AC Q9UDY2; A2A3H9; B7Z2R8; B7Z7T6; F5H301; F5H886; Q15883; Q5VXL0; Q5VXL1; AC Q8N756; Q8NI14; Q99839; Q9UDY0; Q9UDY1; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 24-JAN-2024, entry version 231. DE RecName: Full=Tight junction protein ZO-2; DE AltName: Full=Tight junction protein 2; DE AltName: Full=Zona occludens protein 2; DE AltName: Full=Zonula occludens protein 2; GN Name=TJP2; Synonyms=X104, ZO2; 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] (ISOFORM A1), AND VARIANTS GLU-482; ASN-822 AND RP ASP-829. RC TISSUE=Brain; RX PubMed=7951235; DOI=10.1093/hmg/3.6.909; RA Duclos F., Rodius F., Wrogemann K., Mandel J.-L., Koenig M.; RT "The Friedreich ataxia region: characterization of two novel genes and RT reduction of the critical region to 300 kb."; RL Hum. Mol. Genet. 3:909-914(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1; C1; A2 AND C2), TISSUE RP SPECIFICITY, ALTERNATIVE PROMOTER USAGE, AND VARIANT GLU-482. RC TISSUE=Pancreas; RX PubMed=11018256; DOI=10.1016/s0167-4781(00)00185-8; RA Chlenski A., Ketels K.V., Korovaitseva G.I., Talamonti M.S., Oyasu R., RA Scarpelli D.G.; RT "Organization and expression of the human zo-2 gene (tjp-2) in normal and RT neoplastic tissues."; RL Biochim. Biophys. Acta 1493:319-324(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A3), AND VARIANT GLU-482. RA Yan H.H., Rong L., Qiang S., Jian W., Peng Z., Hua H., Hui Z.W.; RT "LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND VARIANTS RP GLU-482 AND ILE-668. RC TISSUE=Brain, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A1). RC TISSUE=Testis; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-166 (ISOFORMS A1/A2/A3), AND NUCLEOTIDE RP SEQUENCE [MRNA] OF 1-119 (ISOFORMS C1/C2). RC TISSUE=Pancreas; RX PubMed=10360833; RX DOI=10.1002/(sici)1097-0215(19990702)82:1<137::aid-ijc23>3.0.co;2-f; RA Chlenski A., Ketels K.V., Tsao M.-S., Talamonti M.S., Anderson M.R., RA Oyasu R., Scarpelli D.G.; RT "Tight junction protein ZO-2 is differentially expressed in normal RT pancreatic ducts compared to human pancreatic adenocarcinoma."; RL Int. J. Cancer 82:137-144(1999). RN [8] RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS A1 AND C1), AND ALTERNATIVE PROMOTER RP USAGE. RC TISSUE=Pancreas; RX PubMed=10495427; RX DOI=10.1002/(sici)1097-0215(19991029)83:3<349::aid-ijc10>3.0.co;2-c; RA Chlenski A., Ketels K.V., Engeriser J.L., Talamonti M.S., Tsao M.-S., RA Koutnikova H., Oyasu R., Scarpelli D.G.; RT "Zo-2 gene alternative promoters in normal and neoplastic human pancreatic RT duct cells."; RL Int. J. Cancer 83:349-358(1999). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1047-1167. RC TISSUE=Aortic smooth muscle; RA Adams L.D., Werny I., Schwartz S.M.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [10] RP INTERACTION WITH SCRIB. RX PubMed=15975580; DOI=10.1016/j.febslet.2005.05.062; RA Metais J.-Y., Navarro C., Santoni M.-J., Audebert S., Borg J.-P.; RT "hScrib interacts with ZO-2 at the cell-cell junctions of epithelial RT cells."; RL FEBS Lett. 579:3725-3730(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-244; SER-702; RP SER-966 AND SER-986, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-174; SER-244; RP SER-266; SER-400; THR-455; SER-920; THR-925; THR-933; SER-978; SER-986; RP SER-1067; SER-1068; THR-1131 AND SER-1159, 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [15] 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-1159, AND RP IDENTIFICATION BY 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-170; SER-174; RP SER-244; SER-920; THR-925; SER-986 AND SER-1159, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-153; SER-168; RP SER-174; SER-200; SER-220; SER-244; SER-430; SER-978; SER-986; SER-1067; RP SER-1068; SER-1147 AND SER-1159, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-130; SER-150; RP SER-170; SER-174; SER-232; SER-244; SER-266; SER-415; SER-424; SER-430; RP SER-431; THR-455; SER-499; SER-913; SER-966; SER-978; SER-986; SER-1067; RP TYR-1118 AND SER-1159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-325; SER-406; RP SER-431; SER-702; SER-966; SER-978; SER-986 AND SER-1159, 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 [22] RP INVOLVEMENT IN PFIC4. RX PubMed=24614073; DOI=10.1038/ng.2918; RA Sambrotta M., Strautnieks S., Papouli E., Rushton P., Clark B.E., RA Parry D.A., Logan C.V., Newbury L.J., Kamath B.M., Ling S., RA Grammatikopoulos T., Wagner B.E., Magee J.C., Sokol R.J., Mieli-Vergani G., RA Smith J.D., Johnson C.A., McClean P., Simpson M.A., Knisely A.S., RA Bull L.N., Thompson R.J.; RT "Mutations in TJP2 cause progressive cholestatic liver disease."; RL Nat. Genet. 46:326-328(2014). RN [23] RP STRUCTURE BY NMR OF 306-385, HOMODIMERIZATION, AND INTERACTION WITH TJP1. 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 [24] RP VARIANT FHCA1 ALA-48, CHARACTERIZATION OF VARIANT FHCA1 ALA-48, AND RP INTERACTION WITH CLDN1; CLDN2; CLDN3; CLDN5 AND CLDN7. RX PubMed=12704386; DOI=10.1038/ng1147; RA Carlton V.E.H., Harris B.Z., Puffenberger E.G., Batta A.K., Knisely A.S., RA Robinson D.L., Strauss K.A., Shneider B.L., Lim W.A., Salen G., RA Morton D.H., Bull L.N.; RT "Complex inheritance of familial hypercholanemia with associated mutations RT in TJP2 and BAAT."; RL Nat. Genet. 34:91-96(2003). RN [25] RP VARIANT [LARGE SCALE ANALYSIS] GLU-482, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: Plays a role in tight junctions and adherens junctions (By CC similarity). Acts as a positive regulator of RANKL-induced osteoclast CC differentiation, potentially via mediating downstream transcriptional CC activity (By similarity). {ECO:0000250|UniProtKB:Q9Z0U1}. CC -!- SUBUNIT: Homodimer (PubMed:17897942). Interacts (via PDZ2 domain) with CC TJP1/ZO1 (via PDZ2 domain) (PubMed:17897942). Interacts with OCLN (By CC similarity). Interacts with UBN1 (PubMed:18823282). Interacts with SAFB CC in the nucleus (By similarity). Interacts with SCRIB (PubMed:15975580). CC Interacts with USP53 (via the C-terminal region) (By similarity). CC Interacts with claudins, including CLDN1, CLDN2, CLDN3, CLDN5 and CLDN7 CC (PubMed:12704386). Interacts with CLDN18 (By similarity). Interacts CC (via N-terminus) with CTNNA1 (By similarity). CC {ECO:0000250|UniProtKB:Q95168, ECO:0000250|UniProtKB:Q9Z0U1, CC ECO:0000269|PubMed:12704386, ECO:0000269|PubMed:15975580, CC ECO:0000269|PubMed:17897942, ECO:0000269|PubMed:18823282}. CC -!- INTERACTION: CC Q9UDY2; Q14847: LASP1; NbExp=9; IntAct=EBI-1042602, EBI-742828; CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic CC side {ECO:0000250}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:Q9Z0U1}. Nucleus {ECO:0000250}. Note=Also CC nuclear under environmental stress conditions and in migratory CC endothelial cells and subconfluent epithelial cell cultures. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7; CC Name=A1; CC IsoId=Q9UDY2-1; Sequence=Displayed; CC Name=A2; CC IsoId=Q9UDY2-2; Sequence=VSP_003149; CC Name=A3; CC IsoId=Q9UDY2-5; Sequence=VSP_007835, VSP_007836; CC Name=C1; CC IsoId=Q9UDY2-3; Sequence=VSP_006953; CC Name=C2; CC IsoId=Q9UDY2-4; Sequence=VSP_006953, VSP_003149; CC Name=6; CC IsoId=Q9UDY2-6; Sequence=VSP_046115, VSP_046116; CC Name=7; CC IsoId=Q9UDY2-7; Sequence=VSP_046114; CC -!- TISSUE SPECIFICITY: This protein is found in epithelial cell junctions. CC Isoform A1 is abundant in the heart and brain. Detected in brain and CC skeletal muscle. It is present almost exclusively in normal tissues. CC Isoform C1 is expressed at high level in the kidney, pancreas, heart CC and placenta. Not detected in brain and skeletal muscle. Found in CC normal as well as in most neoplastic tissues. CC {ECO:0000269|PubMed:11018256}. CC -!- DISEASE: Hypercholanemia, familial, 1 (FHCA1) [MIM:607748]: A disorder CC characterized by elevated serum bile acid concentrations, itching, and CC fat malabsorption. {ECO:0000269|PubMed:12704386}. Note=The disease may CC be caused by variants affecting distinct genetic loci, including the CC gene represented in this entry. CC -!- DISEASE: Cholestasis, progressive familial intrahepatic, 4 (PFIC4) CC [MIM:615878]: A disorder characterized by early onset of cholestasis CC that progresses to hepatic fibrosis, cirrhosis, and end-stage liver CC disease before adulthood. PFIC4 inheritance is autosomal recessive. CC {ECO:0000269|PubMed:24614073}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform A1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform A2]: Produced by alternative splicing of CC isoform A1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform A3]: Produced by alternative splicing of CC isoform A1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform C1]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform C2]: Produced by alternative splicing of CC isoform C1. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA61300.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44347/TJP2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L27476; AAA61300.1; ALT_FRAME; mRNA. DR EMBL; AF177533; AAD20387.2; -; Genomic_DNA. DR EMBL; AF043195; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF043196; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF043197; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177518; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177519; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177520; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177521; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177522; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177523; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177524; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177525; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177526; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177527; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177528; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177529; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177530; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177531; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177532; AAD20387.2; JOINED; Genomic_DNA. DR EMBL; AF177533; AAC02527.2; -; Genomic_DNA. DR EMBL; AF043196; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF043197; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177518; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177519; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177520; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177521; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177522; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177523; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177524; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177525; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177526; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177527; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177528; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177529; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177530; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177531; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177532; AAC02527.2; JOINED; Genomic_DNA. DR EMBL; AF177533; AAD56218.2; -; Genomic_DNA. DR EMBL; AF043195; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF043196; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF043197; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177518; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177519; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177520; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177521; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177522; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177523; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177524; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177525; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177526; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177527; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177528; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177529; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177532; AAD56218.2; JOINED; Genomic_DNA. DR EMBL; AF177533; AAD56219.2; -; Genomic_DNA. DR EMBL; AF043196; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF043197; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177518; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177519; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177520; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177521; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177522; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177523; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177524; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177525; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177526; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177527; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177528; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177529; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF177532; AAD56219.2; JOINED; Genomic_DNA. DR EMBL; AF489824; AAM28524.1; -; mRNA. DR EMBL; AK295034; BAH11954.1; -; mRNA. DR EMBL; AK302483; BAH13722.1; -; mRNA. DR EMBL; AL162730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL358113; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590238; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC027592; AAH27592.1; -; mRNA. DR EMBL; AF083892; AAC33121.1; -; mRNA. DR EMBL; AF083893; AAC33122.1; -; mRNA. DR EMBL; U84581; AAB41794.1; -; mRNA. DR CCDS; CCDS55315.1; -. [Q9UDY2-6] DR CCDS; CCDS55316.1; -. [Q9UDY2-7] DR CCDS; CCDS6627.1; -. [Q9UDY2-1] DR CCDS; CCDS6628.1; -. [Q9UDY2-2] DR PIR; I54378; I54378. DR RefSeq; NP_001163886.1; NM_001170415.1. [Q9UDY2-6] DR RefSeq; NP_001163887.1; NM_001170416.1. [Q9UDY2-7] DR RefSeq; NP_004808.2; NM_004817.3. [Q9UDY2-1] DR RefSeq; XP_011517508.1; XM_011519206.2. [Q9UDY2-3] DR RefSeq; XP_011517509.1; XM_011519207.2. [Q9UDY2-3] DR RefSeq; XP_011517510.1; XM_011519208.2. [Q9UDY2-3] DR RefSeq; XP_011517511.1; XM_011519209.2. [Q9UDY2-3] DR PDB; 2OSG; NMR; -; A/B=306-385. DR PDB; 3E17; X-ray; 1.75 A; A/B=306-384. DR PDBsum; 2OSG; -. DR PDBsum; 3E17; -. DR AlphaFoldDB; Q9UDY2; -. DR BMRB; Q9UDY2; -. DR SMR; Q9UDY2; -. DR BioGRID; 114809; 299. DR ELM; Q9UDY2; -. DR IntAct; Q9UDY2; 70. DR MINT; Q9UDY2; -. DR STRING; 9606.ENSP00000438262; -. DR GlyGen; Q9UDY2; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9UDY2; -. DR MetOSite; Q9UDY2; -. DR PhosphoSitePlus; Q9UDY2; -. DR BioMuta; TJP2; -. DR DMDM; 317373313; -. DR EPD; Q9UDY2; -. DR jPOST; Q9UDY2; -. DR MassIVE; Q9UDY2; -. DR MaxQB; Q9UDY2; -. DR PaxDb; 9606-ENSP00000438262; -. DR PeptideAtlas; Q9UDY2; -. DR ProteomicsDB; 26127; -. DR ProteomicsDB; 27714; -. DR ProteomicsDB; 84127; -. [Q9UDY2-1] DR ProteomicsDB; 84128; -. [Q9UDY2-2] DR ProteomicsDB; 84129; -. [Q9UDY2-3] DR ProteomicsDB; 84130; -. [Q9UDY2-4] DR ProteomicsDB; 84131; -. [Q9UDY2-5] DR Pumba; Q9UDY2; -. DR Antibodypedia; 784; 451 antibodies from 37 providers. DR DNASU; 9414; -. DR Ensembl; ENST00000348208.9; ENSP00000345893.4; ENSG00000119139.21. [Q9UDY2-2] DR Ensembl; ENST00000377245.9; ENSP00000366453.4; ENSG00000119139.21. [Q9UDY2-1] DR Ensembl; ENST00000535702.6; ENSP00000442090.1; ENSG00000119139.21. [Q9UDY2-6] DR Ensembl; ENST00000539225.2; ENSP00000438262.1; ENSG00000119139.21. [Q9UDY2-7] DR GeneID; 9414; -. DR KEGG; hsa:9414; -. DR MANE-Select; ENST00000377245.9; ENSP00000366453.4; NM_004817.4; NP_004808.2. DR UCSC; uc004ahd.4; human. [Q9UDY2-1] DR AGR; HGNC:11828; -. DR CTD; 9414; -. DR DisGeNET; 9414; -. DR GeneCards; TJP2; -. DR HGNC; HGNC:11828; TJP2. DR HPA; ENSG00000119139; Low tissue specificity. DR MalaCards; TJP2; -. DR MIM; 607709; gene. DR MIM; 607748; phenotype. DR MIM; 615878; phenotype. DR neXtProt; NX_Q9UDY2; -. DR OpenTargets; ENSG00000119139; -. DR Orphanet; 238475; Familial hypercholanemia. DR Orphanet; 480483; Progressive familial intrahepatic cholestasis type 4. DR Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA. DR PharmGKB; PA36533; -. DR VEuPathDB; HostDB:ENSG00000119139; -. DR eggNOG; KOG3580; Eukaryota. DR GeneTree; ENSGT00940000158634; -. DR HOGENOM; CLU_006234_1_0_1; -. DR InParanoid; Q9UDY2; -. DR OrthoDB; 2904077at2759; -. DR PhylomeDB; Q9UDY2; -. DR TreeFam; TF315957; -. DR PathwayCommons; Q9UDY2; -. DR Reactome; R-HSA-2028269; Signaling by Hippo. DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013026; RHOB GTPase cycle. DR Reactome; R-HSA-9013106; RHOC GTPase cycle. DR SignaLink; Q9UDY2; -. DR SIGNOR; Q9UDY2; -. DR BioGRID-ORCS; 9414; 15 hits in 1157 CRISPR screens. DR ChiTaRS; TJP2; human. DR EvolutionaryTrace; Q9UDY2; -. DR GeneWiki; Tight_junction_protein_2; -. DR GenomeRNAi; 9414; -. DR Pharos; Q9UDY2; Tbio. DR PRO; PR:Q9UDY2; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9UDY2; Protein. DR Bgee; ENSG00000119139; Expressed in corpus callosum and 96 other cell types or tissues. DR ExpressionAtlas; Q9UDY2; baseline and differential. DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell. DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB. DR GO; GO:0044291; C:cell-cell contact zone; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central. DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0045216; P:cell-cell junction organization; IBA:GO_Central. DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:UniProtKB. DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:ARUK-UCL. DR GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB. DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IMP:ARUK-UCL. DR GO; GO:0150105; P:protein localization to cell-cell junction; IBA:GO_Central. DR GO; GO:0090559; P:regulation of membrane permeability; IMP:UniProtKB. DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl. DR CDD; cd00992; PDZ_signaling; 3. DR CDD; cd12027; SH3_ZO-2; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR005419; ZO-2. DR InterPro; IPR035598; ZO-2_SH3. DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1. DR PANTHER; PTHR13865:SF26; TIGHT JUNCTION PROTEIN ZO-2; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF00595; PDZ; 3. DR Pfam; PF07653; SH3_2; 1. DR PRINTS; PR01597; ZONOCCLUDNS. DR PRINTS; PR01599; ZONOCCLUDNS2. DR SMART; SM00072; GuKc; 1. DR SMART; SM00228; PDZ; 3. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 3. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9UDY2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative promoter usage; Alternative splicing; KW Cell junction; Cell membrane; Disease variant; Intrahepatic cholestasis; KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; SH3 domain; KW Tight junction. FT CHAIN 1..1190 FT /note="Tight junction protein ZO-2" FT /id="PRO_0000094543" FT DOMAIN 33..120 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 307..385 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 509..590 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 604..669 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 678..876 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT REGION 152..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 408..506 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 920..1079 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1105..1190 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1188..1190 FT /note="Interaction with SCRIB" FT /evidence="ECO:0000269|PubMed:15975580" FT COMPBIAS 162..296 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..445 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 927..941 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 956..970 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 997..1011 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1012..1027 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1157..1172 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 150 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 163 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1" FT MOD_RES 168 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 174 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 200 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 415 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 424 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 431 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 455 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 499 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 574 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:24275569" FT MOD_RES 902 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1" FT MOD_RES 905 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1" FT MOD_RES 913 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 920 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 925 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 933 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 966 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 978 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 986 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1006 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1" FT MOD_RES 1067 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1068 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1118 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1131 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1159 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..23 FT /note="Missing (in isoform C1 and isoform C2)" FT /evidence="ECO:0000305" FT /id="VSP_006953" FT VAR_SEQ 1..20 FT /note="MPVRGDRGFPPRRELSGWLR -> MKTAQALHRMWIQAVKKLRRWKGRVSPS FT ASSPLVFPNLSSWEGEGSKTILT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046114" FT VAR_SEQ 1..19 FT /note="MPVRGDRGFPPRRELSGWL -> MKTAQALHRMWIQAVKKLRRWKG (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046115" FT VAR_SEQ 961..1107 FT /note="Missing (in isoform A2 and isoform C2)" FT /evidence="ECO:0000305" FT /id="VSP_003149" FT VAR_SEQ 961..997 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046116" FT VAR_SEQ 961..993 FT /note="SIRKPSPEPRAQMRRAASSDQLRDNSPPPAFKP -> VRRGRPRAGTGEPGV FT FLALSWTAVCSGCCGRHS (in isoform A3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_007835" FT VAR_SEQ 994..1190 FT /note="Missing (in isoform A3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_007836" FT VARIANT 48 FT /note="V -> A (in FHCA1; affects the interaction with FT claudins; dbSNP:rs121918299)" FT /evidence="ECO:0000269|PubMed:12704386" FT /id="VAR_016004" FT VARIANT 482 FT /note="D -> E (in dbSNP:rs2309428)" FT /evidence="ECO:0000269|PubMed:11018256, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:7951235, FT ECO:0000269|Ref.3, ECO:0007744|PubMed:21269460" FT /id="VAR_030798" FT VARIANT 668 FT /note="M -> I (in dbSNP:rs34774441)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_046675" FT VARIANT 711 FT /note="S -> P (in dbSNP:rs35797487)" FT /id="VAR_046676" FT VARIANT 822 FT /note="K -> N (in dbSNP:rs1049624)" FT /evidence="ECO:0000269|PubMed:7951235" FT /id="VAR_046677" FT VARIANT 829 FT /note="N -> D (in dbSNP:rs1049625)" FT /evidence="ECO:0000269|PubMed:7951235" FT /id="VAR_046678" FT CONFLICT 411 FT /note="N -> T (in Ref. 1; AAA61300 and 3; AAM28524)" FT /evidence="ECO:0000305" FT CONFLICT 718 FT /note="A -> V (in Ref. 4; BAH13722)" FT /evidence="ECO:0000305" FT CONFLICT 782 FT /note="I -> V (in Ref. 1; AAA61300 and 3; AAM28524)" FT /evidence="ECO:0000305" FT CONFLICT 808 FT /note="P -> S (in Ref. 1; AAA61300)" FT /evidence="ECO:0000305" FT CONFLICT 812..814 FT /note="FFN -> SFT (in Ref. 1; AAA61300)" FT /evidence="ECO:0000305" FT CONFLICT 834 FT /note="K -> N (in Ref. 1; AAA61300)" FT /evidence="ECO:0000305" FT CONFLICT 842 FT /note="Q -> H (in Ref. 1; AAA61300)" FT /evidence="ECO:0000305" FT CONFLICT 996 FT /note="P -> S (in Ref. 1; AAA61300)" FT /evidence="ECO:0000305" FT CONFLICT 1093 FT /note="R -> G (in Ref. 1; AAA61300)" FT /evidence="ECO:0000305" FT CONFLICT 1110 FT /note="I -> L (in Ref. 4; BAH13722)" FT /evidence="ECO:0000305" FT CONFLICT 1136 FT /note="S -> N (in Ref. 9; AAB41794)" FT /evidence="ECO:0000305" FT CONFLICT 1155..1158 FT /note="GSYG -> RSFC (in Ref. 9; AAB41794)" FT /evidence="ECO:0000305" FT CONFLICT 1165..1167 FT /note="EYR -> IRS (in Ref. 9; AAB41794)" FT /evidence="ECO:0000305" FT STRAND 306..311 FT /evidence="ECO:0007829|PDB:3E17" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:2OSG" FT STRAND 321..332 FT /evidence="ECO:0007829|PDB:3E17" FT HELIX 337..341 FT /evidence="ECO:0007829|PDB:3E17" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:3E17" FT HELIX 363..372 FT /evidence="ECO:0007829|PDB:3E17" FT TURN 373..375 FT /evidence="ECO:0007829|PDB:3E17" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:3E17" SQ SEQUENCE 1190 AA; 133958 MW; 27305B723043BF6C CRC64; MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK VAAIVVKRPR KVQVAALQAS PPLDQDDRAF EVMDEFDGRS FRSGYSERSR LNSHGGRSRS WEDSPERGRP HERARSRERD LSRDRSRGRS LERGLDQDHA RTRDRSRGRS LERGLDHDFG PSRDRDRDRS RGRSIDQDYE RAYHRAYDPD YERAYSPEYR RGARHDARSR GPRSRSREHP HSRSPSPEPR GRPGPIGVLL MKSRANEEYG LRLGSQIFVK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI EKSRGKLQLV VLRDSQQTLI NIPSLNDSDS EIEDISEIES NRSFSPEERR HQYSDYDYHS SSEKLKERPS SREDTPSRLS RMGATPTPFK STGDIAGTVV PETNKEPRYQ EDPPAPQPKA APRTFLRPSP EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP QSLAFTRGEV FRVVDTLYDG KLGNWLAVRI GNELEKGLIP NKSRAEQMAS VQNAQRDNAG DRADFWRMRG QRSGVKKNLR KSREDLTAVV SVSTKFPAYE RVLLREAGFK RPVVLFGPIA DIAMEKLANE LPDWFQTAKT EPKDAGSEKS TGVVRLNTVR QIIEQDKHAL LDVTPKAVDL LNYTQWFPIV IFFNPDSRQG VKTMRQRLNP TSNKSSRKLF DQANKLKKTC AHLFTATINL NSANDSWFGS LKDTIQHQQG EAVWVSEGKM EGMDDDPEDR MSYLTAMGAD YLSCDSRLIS DFEDTDGEGG AYTDNELDEP AEEPLVSSIT RSSEPVQHEE SIRKPSPEPR AQMRRAASSD QLRDNSPPPA FKPEPPKAKT QNKEESYDFS KSYEYKSNPS AVAGNETPGA STKGYPPPVA AKPTFGRSIL KPSTPIPPQE GEEVGESSEE QDNAPKSVLG KVKIFEKMDH KARLQRMQEL QEAQNARIEI AQKHPDIYAV PIKTHKPDPG TPQHTSSRPP EPQKAPSRPY QDTRGSYGSD AEEEEYRQQL SEHSKRGYYG QSARYRDTEL //