ID PLAK_HUMAN Reviewed; 745 AA. AC P14923; Q15093; Q15151; Q7L3S5; Q86W21; Q9BWC4; Q9HCX9; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 3. DT 04-NOV-2026, entry version 239. DE RecName: Full=Junction plakoglobin; DE AltName: Full=Catenin gamma; DE AltName: Full=Desmoplakin III; DE AltName: Full=Desmoplakin-3; GN Name=JUP {ECO:0000312|HGNC:HGNC:6207}; GN Synonyms=CTNNG {ECO:0000312|HGNC:HGNC:6207}, DP3 GN {ECO:0000312|HGNC:HGNC:6207}; 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]. RX PubMed=2726765; DOI=10.1073/pnas.86.11.4027; RA Franke W.W., Goldschmidt M.D., Zimbelmann R., Mueller H.M., Schiller D.L., RA Cowin P.; RT "Molecular cloning and amino acid sequence of human plakoglobin, the common RT junctional plaque protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4027-4031(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zimbelmann R.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11016852; DOI=10.1034/j.1600-0625.2000.009005323.x; RA Whittock N.V., Eady R.A.J., McGrath J.A.; RT "Genomic organization and amplification of the human plakoglobin gene RT (JUP)."; RL Exp. Dermatol. 9:323-326(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-697. RC TISSUE=Epidermal carcinoma; RA Liang X.-J., Gottesman M.M.; RT "Homo sapiens gamma-catenin mRNA from human KB epidermoid adenocarcinoma RT cells."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-697. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-697. RC TISSUE=Lung, and Placenta; 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 [8] RP PROTEIN SEQUENCE OF 1-12; 116-142; 150-172; 177-203; 217-233; 273-279; RP 304-320; 327-333; 368-394; 427-460; 466-533; 583-602; 638-661 AND 664-674, RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma, and Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.; RL Submitted (MAR-2008) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-745, VARIANT LEU-697, AND RP INVOLVEMENT IN NAXOS DISEASE. RC TISSUE=Leukocyte; RX PubMed=10902626; DOI=10.1016/s0140-6736(00)02379-5; RA McKoy G., Protonotarios N., Crosby A., Tsatsopoulou A., Anastasakis A., RA Coonar A., Norman M., Baboonian C., Jeffery S., McKenna W.J.; RT "Identification of a deletion in plakoglobin in arrhythmogenic right RT ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair RT (Naxos disease)."; RL Lancet 355:2119-2124(2000). RN [10] RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX. RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9; RA Butz S., Kemler R.; RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell RT adhesion."; RL FEBS Lett. 355:195-200(1994). RN [11] RP DOMAIN, AND INTERACTION WITH CTNNA1; DSC1 AND DSG1. RX PubMed=8631907; DOI=10.1074/jbc.271.18.10904; RA Witcher L.L., Collins R., Puttagunta S., Mechanic S.E., Munson M., RA Gumbiner B., Cowin P.; RT "Desmosomal cadherin binding domains of plakoglobin."; RL J. Biol. Chem. 271:10904-10909(1996). RN [12] RP INTERACTION WITH MUC1. RX PubMed=9139698; DOI=10.1074/jbc.272.19.12492; RA Yamamoto M., Bharti A., Li Y., Kufe D.; RT "Interaction of the DF3/MUC1 breast carcinoma-associated antigen and beta- RT catenin in cell adhesion."; RL J. Biol. Chem. 272:12492-12494(1997). RN [13] RP INTERACTION WITH CTNNA1. RX PubMed=9152027; DOI=10.1242/jcs.110.8.1013; RA Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R., RA Wheelock M.J.; RT "Characterization of the interactions of alpha-catenin with alpha-actinin RT and beta-catenin/plakoglobin."; RL J. Cell Sci. 110:1013-1022(1997). RN [14] RP INTERACTION WITH PKP2, AND SUBCELLULAR LOCATION. RX PubMed=11790773; DOI=10.1074/jbc.m108765200; RA Chen X., Bonne S., Hatzfeld M., van Roy F., Green K.J.; RT "Protein binding and functional characterization of plakophilin 2. Evidence RT for its diverse roles in desmosomes and beta -catenin signaling."; RL J. Biol. Chem. 277:10512-10522(2002). RN [15] RP INTERACTION WITH PTPRJ. RX PubMed=12370829; DOI=10.1038/sj.onc.1205858; RA Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.; RT "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts RT with p120(ctn)."; RL Oncogene 21:7067-7076(2002). RN [16] RP GLYCOSYLATION AT THR-14, AND MUTAGENESIS OF THR-14; THR-19; THR-21; SER-24; RP SER-28 AND THR-32. RX PubMed=12847106; DOI=10.1074/jbc.m301346200; RA Hatsell S., Medina L., Merola J., Haltiwanger R., Cowin P.; RT "Plakoglobin is O-glycosylated close to the N-terminal destruction box."; RL J. Biol. Chem. 278:37745-37752(2003). RN [17] RP PHOSPHORYLATION BY FER. RX PubMed=14517306; DOI=10.1128/mcb.23.20.7391-7402.2003; RA Miravet S., Piedra J., Castano J., Raurell I., Franci C., Dunach M., RA Garcia de Herreros A.; RT "Tyrosine phosphorylation of plakoglobin causes contrary effects on its RT association with desmosomes and adherens junction components and modulates RT beta-catenin-mediated transcription."; RL Mol. Cell. Biol. 23:7391-7402(2003). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, 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 [19] RP INTERACTION WITH DSP. RX PubMed=16917092; DOI=10.1161/01.res.0000241482.19382.c6; RA Yang Z., Bowles N.E., Scherer S.E., Taylor M.D., Kearney D.L., Ge S., RA Nadvoretskiy V.V., DeFreitas G., Carabello B., Brandon L.I., Godsel L.M., RA Green K.J., Saffitz J.E., Li H., Danieli G.A., Calkins H., Marcus F., RA Towbin J.A.; RT "Desmosomal dysfunction due to mutations in desmoplakin causes RT arrhythmogenic right ventricular dysplasia/cardiomyopathy."; RL Circ. Res. 99:646-655(2006). RN [20] RP CLEAVAGE BY CASP3. RX PubMed=17559062; DOI=10.1002/jcb.21431; RA Cirillo N., Lanza M., De Rosa A., Cammarota M., La Gatta A., Gombos F., RA Lanza A.; RT "The most widespread desmosomal cadherin, desmoglein 2, is a novel target RT of caspase 3-mediated apoptotic machinery."; RL J. Cell. Biochem. 103:598-606(2008). RN [21] RP INTERACTION WITH DSG1. RX PubMed=19136012; DOI=10.1016/j.jmb.2008.12.054; RA Kami K., Chidgey M., Dafforn T., Overduin M.; RT "The desmoglein-specific cytoplasmic region is intrinsically disordered in RT solution and interacts with multiple desmosomal protein partners."; RL J. Mol. Biol. 386:531-543(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION BY RP 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 [23] 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 [24] RP INTERACTION WITH DSG4, AND SUBCELLULAR LOCATION. RX PubMed=21495994; DOI=10.1111/j.1365-2133.2011.10373.x; RA Farooq M., Ito M., Naito M., Shimomura Y.; RT "A case of monilethrix caused by novel compound heterozygous mutations in RT the desmoglein 4 (DSG4) gene."; RL Br. J. Dermatol. 165:425-431(2011). RN [25] RP INTERACTION WITH DSC2. RX PubMed=21062920; DOI=10.1093/cvr/cvq353; RA Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A., RA Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C., RA Saffitz J.E., Protonotarios N., McKenna W.J.; RT "Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy RT caused by desmocollin-2 mutations."; RL Cardiovasc. Res. 90:77-87(2011). RN [26] RP INTERACTION WITH PKP3, AND SUBCELLULAR LOCATION. RX PubMed=20859650; DOI=10.1007/s00018-010-0531-3; RA Gosavi P., Kundu S.T., Khapare N., Sehgal L., Karkhanis M.S., Dalal S.N.; RT "E-cadherin and plakoglobin recruit plakophilin3 to the cell border to RT initiate desmosome assembly."; RL Cell. Mol. Life Sci. 68:1439-1454(2011). RN [27] RP INTERACTION WITH PKP2, AND SUBCELLULAR LOCATION. RX PubMed=22781308; DOI=10.1161/circgenetics.111.961854; RA Kirchner F., Schuetz A., Boldt L.H., Martens K., Dittmar G., Haverkamp W., RA Thierfelder L., Heinemann U., Gerull B.; RT "Molecular insights into arrhythmogenic right ventricular cardiomyopathy RT caused by plakophilin-2 missense mutations."; RL Circ. Cardiovasc. Genet. 5:400-411(2012). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-125; SER-182 AND RP SER-730, AND 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 [30] RP SUBCELLULAR LOCATION. RX PubMed=25208567; DOI=10.1091/mbc.e14-05-0968; RA Todorovic V., Koetsier J.L., Godsel L.M., Green K.J.; RT "Plakophilin 3 mediates Rap1-dependent desmosome assembly and adherens RT junction maturation."; RL Mol. Biol. Cell 25:3749-3764(2014). RN [31] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=26604139; DOI=10.1093/hmg/ddv481; RA Boyden L.M., Kam C.Y., Hernandez-Martin A., Zhou J., Craiglow B.G., RA Sidbury R., Mathes E.F., Maguiness S.M., Crumrine D.A., Williams M.L., RA Hu R., Lifton R.P., Elias P.M., Green K.J., Choate K.A.; RT "Dominant de novo DSP mutations cause erythrokeratodermia-cardiomyopathy RT syndrome."; RL Hum. Mol. Genet. 25:348-357(2016). RN [32] RP TISSUE SPECIFICITY. RX PubMed=31845994; DOI=10.1093/europace/euz329; RA Vite A., Gandjbakhch E., Hery T., Fressart V., Gary F., Simon F., RA Varnous S., Hidden Lucet F., Charron P., Villard E.; RT "Desmoglein-2 mutations in propeptide cleavage-site causes arrhythmogenic RT right ventricular cardiomyopathy/dysplasia by impairing extracellular 1- RT dependent desmosomal interactions upon cellular stress."; RL Europace 22:320-329(2020). RN [33] RP TISSUE SPECIFICITY. RX PubMed=33784018; DOI=10.1002/ctm2.319; RA Moreau A., Reisqs J.B., Delanoe-Ayari H., Pierre M., Janin A., RA Deliniere A., Bessiere F., Meli A.C., Charrabi A., Lafont E., Valla C., RA Bauer D., Morel E., Gache V., Millat G., Nissan X., Faucherre A., RA Jopling C., Richard S., Mejat A., Chevalier P.; RT "Deciphering DSC2 arrhythmogenic cardiomyopathy electrical instability: RT From ion channels to ECG and tailored drug therapy."; RL Clin. Transl. Med. 11:e319-e319(2021). RN [34] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PHOSPHORYLATED MOUSE E-CADHERIN, RP DOMAIN ARM REPEATS, AND INTERACTION WITH DSC1 AND DSG1. RX PubMed=19759396; DOI=10.1074/jbc.m109.047928; RA Choi H.J., Gross J.C., Pokutta S., Weis W.I.; RT "Interactions of plakoglobin and beta-catenin with desmosomal cadherins: RT basis of selective exclusion of alpha- and beta-catenin from desmosomes."; RL J. Biol. Chem. 284:31776-31788(2009). RN [35] RP VARIANT ARVD12 SER-39 INS, AND CHARACTERIZATION OF VARIANT ARVD12 SER-39 RP INS. RX PubMed=17924338; DOI=10.1086/521633; RA Asimaki A., Syrris P., Wichter T., Matthias P., Saffitz J.E., McKenna W.J.; RT "A novel dominant mutation in plakoglobin causes arrhythmogenic right RT ventricular cardiomyopathy."; RL Am. J. Hum. Genet. 81:964-973(2007). RN [36] RP VARIANT ARVD12 ILE-19, AND VARIANTS HIS-142; ILE-648 AND LEU-697. RX PubMed=20031617; DOI=10.1161/circgenetics.109.858217; RA den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A., RA Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D., RA Bluemke D.A., Calkins H., Dalal D., Judge D.P.; RT "Comprehensive desmosome mutation analysis in North Americans with RT arrhythmogenic right ventricular dysplasia/cardiomyopathy."; RL Circ. Cardiovasc. Genet. 2:428-435(2009). RN [37] RP VARIANTS HIS-142 AND LEU-697. RX PubMed=19863551; DOI=10.1111/j.1399-0004.2009.01282.x; RA Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L., RA Robb L., Talajic M., Brugada R.; RT "Role of genetic testing in arrhythmogenic right ventricular RT cardiomyopathy/dysplasia."; RL Clin. Genet. 77:37-48(2010). CC -!- FUNCTION: Common junctional plaque protein. The membrane-associated CC plaques are architectural elements in an important strategic position CC to influence the arrangement and function of both the cytoskeleton and CC the cells within the tissue. The presence of plakoglobin in both the CC desmosomes and in the intermediate junctions suggests that it plays a CC central role in the structure and function of submembranous plaques. CC Acts as a substrate for VE-PTP and is required by it to stimulate VE- CC cadherin function in endothelial cells. Can replace beta-catenin in E- CC cadherin/catenin adhesion complexes which are proposed to couple CC cadherins to the actin cytoskeleton (By similarity). May promote axon CC outgrowth and motor fiber repair via DSP-mediated recruitment to CC outgrowth tips (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q02257}. CC -!- SUBUNIT: Homodimer. Component of an E-cadherin/catenin adhesion complex CC composed of at least E-cadherin/CDH1 and gamma-catenin/JUP, and CC possibly alpha-catenin/CTNNA1; the complex is located to adherens CC junctions. The stable association of CTNNA1 is controversial as CTNNA1 CC was shown not to bind to F-actin when assembled in the complex. CC Identified in a complex containing at least DSP, JUP, VIM and CDH2; the CC complex is more abundant following crush injury in regenerating motor CC neurons and may promote axon outgrowth and motor fiber repair (By CC similarity). Interacts with MUC1. Interacts with CAV1 (By similarity). CC Interacts with PTPRJ. Interacts with DSG1 (via cytoplasmic region) CC (PubMed:19136012, PubMed:19759396, PubMed:8631907). Interacts with DSC1 CC and DSC2. Interacts with PKP2 (PubMed:11790773, PubMed:22781308). CC Interacts with PKP3 (via N-terminus); the interaction is required for CC PKP3 localization to desmosome cell-cell junctions (PubMed:20859650). CC Interacts with DSG4 (PubMed:21495994). Interacts with DSP CC (PubMed:16917092). Interacts (via ARM repeats) to PGBDF; this CC interaction regulates JUN stability (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q02257, ECO:0000269|PubMed:11790773, CC ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:16917092, CC ECO:0000269|PubMed:19136012, ECO:0000269|PubMed:19759396, CC ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:21062920, CC ECO:0000269|PubMed:21495994, ECO:0000269|PubMed:22781308, CC ECO:0000269|PubMed:7982500, ECO:0000269|PubMed:8631907, CC ECO:0000269|PubMed:9139698, ECO:0000269|PubMed:9152027}. CC -!- INTERACTION: CC P14923; Q02410: APBA1; NbExp=2; IntAct=EBI-702484, EBI-368690; CC P14923; Q99767: APBA2; NbExp=2; IntAct=EBI-702484, EBI-81711; CC P14923; P25054: APC; NbExp=3; IntAct=EBI-702484, EBI-727707; CC P14923; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-702484, EBI-16429430; CC P14923; O15169: AXIN1; NbExp=4; IntAct=EBI-702484, EBI-710484; CC P14923; Q9HAW0: BRF2; NbExp=2; IntAct=EBI-702484, EBI-1055224; CC P14923; P19022: CDH2; NbExp=2; IntAct=EBI-702484, EBI-2256711; CC P14923; P35221: CTNNA1; NbExp=4; IntAct=EBI-702484, EBI-701918; CC P14923; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-702484, EBI-11962928; CC P14923; Q9NSA3: CTNNBIP1; NbExp=5; IntAct=EBI-702484, EBI-747082; CC P14923; P26196: DDX6; NbExp=4; IntAct=EBI-702484, EBI-351257; CC P14923; Q12959: DLG1; NbExp=2; IntAct=EBI-702484, EBI-357481; CC P14923; Q92796: DLG3; NbExp=3; IntAct=EBI-702484, EBI-80440; CC P14923; P78352: DLG4; NbExp=3; IntAct=EBI-702484, EBI-80389; CC P14923; Q02413: DSG1; NbExp=2; IntAct=EBI-702484, EBI-1045757; CC P14923; P00533: EGFR; NbExp=3; IntAct=EBI-702484, EBI-297353; CC P14923; Q14192: FHL2; NbExp=7; IntAct=EBI-702484, EBI-701903; CC P14923; Q68DX3: FRMPD2; NbExp=3; IntAct=EBI-702484, EBI-53993476; CC P14923; A4D2P6: GRID2IP; NbExp=2; IntAct=EBI-702484, EBI-15893226; CC P14923; Q9Y3R0: GRIP1; NbExp=5; IntAct=EBI-702484, EBI-5349621; CC P14923; Q9C0E4: GRIP2; NbExp=5; IntAct=EBI-702484, EBI-949557; CC P14923; P23327: HRC; NbExp=2; IntAct=EBI-702484, EBI-9639760; CC P14923; Q14005: IL16; NbExp=3; IntAct=EBI-702484, EBI-2831580; CC P14923; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-702484, EBI-739832; CC P14923; Q8N448: LNX2; NbExp=2; IntAct=EBI-702484, EBI-2340947; CC P14923; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-702484, EBI-924464; CC P14923; Q86UL8: MAGI2; NbExp=5; IntAct=EBI-702484, EBI-311035; CC P14923; O75970: MPDZ; NbExp=3; IntAct=EBI-702484, EBI-821405; CC P14923; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-702484, EBI-8744528; CC P14923; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-702484, EBI-741158; CC P14923; Q8NI35: PATJ; NbExp=9; IntAct=EBI-702484, EBI-724390; CC P14923; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-702484, EBI-349819; CC P14923; P16284: PECAM1; NbExp=7; IntAct=EBI-702484, EBI-716404; CC P14923; P0CG20: PRR35; NbExp=3; IntAct=EBI-702484, EBI-11986293; CC P14923; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-702484, EBI-748350; CC P14923; Q14160: SCRIB; NbExp=3; IntAct=EBI-702484, EBI-357345; CC P14923; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-702484, EBI-11746252; CC P14923; Q07157: TJP1; NbExp=2; IntAct=EBI-702484, EBI-79553; CC P14923; Q9P202: WHRN; NbExp=2; IntAct=EBI-702484, EBI-310886; CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction CC {ECO:0000269|PubMed:22781308}. Cell junction, desmosome CC {ECO:0000269|PubMed:21495994, ECO:0000269|PubMed:22781308, CC ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:26604139}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:22781308}. Cell membrane CC {ECO:0000269|PubMed:11790773, ECO:0000269|PubMed:20859650, CC ECO:0000269|PubMed:22781308}; Peripheral membrane protein CC {ECO:0000269|PubMed:22781308}. Cytoplasm CC {ECO:0000250|UniProtKB:Q9PVF7}. Cell junction CC {ECO:0000250|UniProtKB:Q9PVF7}. Nucleus {ECO:0000250|UniProtKB:Q9PVF7}. CC Cell projection, axon {ECO:0000250|UniProtKB:Q02257}. Note=Cytoplasmic CC in a soluble and membrane-associated form. Colocalizes with DSG4 at CC desmosomes (PubMed:21495994). {ECO:0000269|PubMed:21495994}. CC -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes in the heart (at CC protein level). Expressed by keratinocytes in the skin (at protein CC level) (PubMed:26604139). {ECO:0000269|PubMed:26604139, CC ECO:0000269|PubMed:31845994, ECO:0000269|PubMed:33784018}. CC -!- DOMAIN: The entire ARM repeats region mediates binding to CDH1/E- CC cadherin. The N-terminus and first three ARM repeats are sufficient for CC binding to DSG1. The N-terminus and first ARM repeat are sufficient for CC association with CTNNA1. DSC1 association requires both ends of the ARM CC repeat region. {ECO:0000269|PubMed:19759396, CC ECO:0000269|PubMed:8631907}. CC -!- PTM: Cleaved by CASP3 in response to apoptosis. CC {ECO:0000269|PubMed:17559062}. CC -!- PTM: May be phosphorylated by FER. {ECO:0000269|PubMed:14517306}. CC -!- DISEASE: Naxos disease (NXD) [MIM:601214]: An autosomal recessive CC disorder characterized by the association of diffuse non-epidermolytic CC palmoplantar keratoderma with woolly hair and cardiac abnormalities CC such as dilated cardiomyopathy and arrhythmogenic right ventricular CC dysplasia. {ECO:0000269|PubMed:10902626}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 12 CC (ARVD12) [MIM:611528]: A congenital heart disease characterized by CC infiltration of adipose and fibrous tissue into the right ventricle and CC loss of myocardial cells, resulting in ventricular and supraventricular CC arrhythmias. {ECO:0000269|PubMed:17924338, CC ECO:0000269|PubMed:20031617}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH00441.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M23410; AAA64895.1; -; mRNA. DR EMBL; Z68228; CAA92522.1; -; mRNA. DR EMBL; AF306723; AAG16727.1; -; Genomic_DNA. DR EMBL; AF233882; AAG16727.1; JOINED; Genomic_DNA. DR EMBL; AY243535; AAO85780.1; -; mRNA. DR EMBL; AC109319; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471152; EAW60762.1; -; Genomic_DNA. DR EMBL; BC000441; AAH00441.2; ALT_INIT; mRNA. DR EMBL; BC011865; AAH11865.1; -; mRNA. DR EMBL; AJ249711; CAC04246.1; -; Genomic_DNA. DR CCDS; CCDS11407.1; -. DR PIR; A32905; A32905. DR RefSeq; NP_001339702.1; NM_001352773.2. DR RefSeq; NP_001339703.1; NM_001352774.2. DR RefSeq; NP_001339704.1; NM_001352775.2. DR RefSeq; NP_001339705.1; NM_001352776.2. DR RefSeq; NP_001339706.1; NM_001352777.2. DR RefSeq; NP_002221.1; NM_002230.4. DR RefSeq; NP_068831.1; NM_021991.4. DR RefSeq; XP_006721937.1; XM_006721874.4. DR RefSeq; XP_006721938.1; XM_006721875.2. DR RefSeq; XP_011523060.1; XM_011524758.2. DR RefSeq; XP_016880079.1; XM_017024590.2. DR RefSeq; XP_047291894.1; XM_047435938.1. DR RefSeq; XP_047291895.1; XM_047435939.1. DR RefSeq; XP_047291896.1; XM_047435940.1. DR RefSeq; XP_047291897.1; XM_047435941.1. DR RefSeq; XP_047291898.1; XM_047435942.1. DR PDB; 3IFQ; X-ray; 2.80 A; A/B=124-676. DR AlphaFoldDB; P14923; -. DR SMR; P14923; -. DR BioGRID; 109931; 571. DR CORUM; P14923; -. DR DIP; DIP-36235N; -. DR FunCoup; P14923; 172. DR IntAct; P14923; 308. DR NDEx; IQUERY-CP-JUP; 11 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000377508; -. DR BindingDB; P14923; -. DR ChEMBL; CHEMBL6066271; -. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR GlyConnect; P14923; 10 N-Linked glycans (4 sites). DR GlyCosmos; P14923; 7 sites, 12 glycans. DR GlyGen; P14923; 7 sites, 11 N-linked glycans (4 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P14923; -. DR MetOSite; P14923; -. DR PhosphoSitePlus; P14923; -. DR SwissPalm; P14923; -. DR BioMuta; JUP; -. DR DMDM; 205371866; -. DR jPOST; P14923; -. DR MassIVE; P14923; -. DR PaxDb; 9606-ENSP00000377508; -. DR PeptideAtlas; P14923; -. DR PRIDE; P14923; -. DR ProteomicsDB; 53098; -. DR Antibodypedia; 80391; 1424 antibodies from 49 providers. DR DNASU; 3728; -. DR Ensembl; ENST00000310706.9; ENSP00000311113.5; ENSG00000173801.18. DR Ensembl; ENST00000393930.5; ENSP00000377507.1; ENSG00000173801.18. DR Ensembl; ENST00000393931.8; ENSP00000377508.3; ENSG00000173801.18. DR Ensembl; ENST00000885261.1; ENSP00000555320.1; ENSG00000173801.18. DR Ensembl; ENST00000885262.1; ENSP00000555321.1; ENSG00000173801.18. DR Ensembl; ENST00000885263.1; ENSP00000555322.1; ENSG00000173801.18. DR Ensembl; ENST00000885264.1; ENSP00000555323.1; ENSG00000173801.18. DR Ensembl; ENST00000885265.1; ENSP00000555324.1; ENSG00000173801.18. DR Ensembl; ENST00000885266.1; ENSP00000555325.1; ENSG00000173801.18. DR Ensembl; ENST00000885268.1; ENSP00000555327.1; ENSG00000173801.18. DR Ensembl; ENST00000885269.1; ENSP00000555328.1; ENSG00000173801.18. DR Ensembl; ENST00000885270.1; ENSP00000555329.1; ENSG00000173801.18. DR Ensembl; ENST00000885271.1; ENSP00000555330.1; ENSG00000173801.18. DR Ensembl; ENST00000885272.1; ENSP00000555331.1; ENSG00000173801.18. DR Ensembl; ENST00000885273.1; ENSP00000555332.1; ENSG00000173801.18. DR Ensembl; ENST00000885274.1; ENSP00000555333.1; ENSG00000173801.18. DR Ensembl; ENST00000885275.1; ENSP00000555334.1; ENSG00000173801.18. DR Ensembl; ENST00000885276.1; ENSP00000555335.1; ENSG00000173801.18. DR Ensembl; ENST00000885277.1; ENSP00000555336.1; ENSG00000173801.18. DR Ensembl; ENST00000885278.1; ENSP00000555337.1; ENSG00000173801.18. DR Ensembl; ENST00000918661.1; ENSP00000588720.1; ENSG00000173801.18. DR Ensembl; ENST00000918662.1; ENSP00000588721.1; ENSG00000173801.18. DR Ensembl; ENST00000918663.1; ENSP00000588722.1; ENSG00000173801.18. DR Ensembl; ENST00000918664.1; ENSP00000588723.1; ENSG00000173801.18. DR Ensembl; ENST00000918665.1; ENSP00000588724.1; ENSG00000173801.18. DR Ensembl; ENST00000918666.1; ENSP00000588725.1; ENSG00000173801.18. DR Ensembl; ENST00000918667.1; ENSP00000588726.1; ENSG00000173801.18. DR Ensembl; ENST00000918668.1; ENSP00000588727.1; ENSG00000173801.18. DR Ensembl; ENST00000955949.1; ENSP00000626008.1; ENSG00000173801.18. DR Ensembl; ENST00000955950.1; ENSP00000626009.1; ENSG00000173801.18. DR Ensembl; ENST00000955951.1; ENSP00000626010.1; ENSG00000173801.18. DR Ensembl; ENST00000955952.1; ENSP00000626011.1; ENSG00000173801.18. DR GeneID; 3728; -. DR KEGG; hsa:3728; -. DR MANE-Select; ENST00000393931.8; ENSP00000377508.3; NM_002230.4; NP_002221.1. DR UCSC; uc002hxq.3; human. DR AGR; HGNC:6207; -. DR ClinPGx; PA30009; -. DR CTD; 3728; -. DR DisGeNET; 3728; -. DR GeneCards; JUP; -. DR GeneReviews; JUP; -. DR HGNC; HGNC:6207; JUP. DR HPA; ENSG00000173801; Tissue enhanced (esophagus, skin). DR MalaCards; JUP; -. DR MIM; 173325; gene. DR MIM; 601214; phenotype. DR MIM; 611528; phenotype. DR OpenTargets; ENSG00000173801; -. DR Orphanet; 293888; Inherited isolated arrhythmogenic cardiomyopathy, dominant-left variant. DR Orphanet; 293910; Inherited isolated arrhythmogenic cardiomyopathy, dominant-right variant. DR Orphanet; 293899; Inherited isolated arrhythmogenic ventricular dysplasia, biventricular variant. DR Orphanet; 158687; Lethal acantholytic erosive disorder. DR Orphanet; 34217; Naxos disease. DR VEuPathDB; HostDB:ENSG00000173801; -. DR eggNOG; KOG4203; Eukaryota. DR GeneTree; ENSGT00940000156395; -. DR HOGENOM; CLU_008757_1_1_1; -. DR InParanoid; P14923; -. DR OMA; ACERQYM; -. DR OrthoDB; 195736at2759; -. DR PAN-GO; P14923; 12 GO annotations based on evolutionary models. DR PhylomeDB; P14923; -. DR PathwayCommons; P14923; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. 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 Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR Reactome; R-HSA-9013407; RHOH GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9762292; Regulation of CDH11 function. DR Reactome; R-HSA-9764302; Regulation of CDH19 Expression and Function. DR Reactome; R-HSA-9764561; Regulation of CDH1 Function. DR Reactome; R-HSA-9766229; Degradation of CDH1. DR Reactome; R-HSA-9768727; Regulation of CDH1 posttranslational processing and trafficking to plasma membrane. DR Reactome; R-HSA-9833576; CDH11 homotypic and heterotypic interactions. DR Reactome; R-HSA-9958810; SRC activates STAT3 in a quantitative manner, through Cadherin-11 (CDH11), RAC1 and gp130 (IL6ST). DR Reactome; R-HSA-9958825; Activation of STAT3 by cadherin engagement. DR SignaLink; P14923; -. DR SIGNOR; P14923; -. DR Agora; ENSG00000173801; -. DR BioGRID-ORCS; 3728; 21 hits in 1167 CRISPR screens. DR CD-CODE; B5B9A610; PML body. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; JUP; human. DR EvolutionaryTrace; P14923; -. DR GeneWiki; Plakoglobin; -. DR GenomeRNAi; 3728; -. DR Pharos; P14923; Tbio. DR PRO; PR:P14923; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P14923; protein. DR Bgee; ENSG00000173801; Expressed in lower esophagus mucosa and 202 other cell types or tissues. DR ExpressionAtlas; P14923; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0070161; C:anchoring junction; ISS:UniProtKB. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0016342; C:catenin complex; IDA:BHF-UCL. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0001533; C:cornified envelope; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IMP:BHF-UCL. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL. DR GO; GO:0005856; C:cytoskeleton; ISS:BHF-UCL. DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL. DR GO; GO:0030057; C:desmosome; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0071665; C:gamma-catenin-TCF7L2 complex; IDA:BHF-UCL. DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL. DR GO; GO:0005882; C:intermediate filament; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IMP:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:0005915; C:zonula adherens; ISS:BHF-UCL. DR GO; GO:0045294; F:alpha-catenin binding; IPI:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL. DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL. DR GO; GO:0086083; F:cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication; IC:BHF-UCL. DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IDA:BHF-UCL. DR GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; NAS:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL. DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IMP:BHF-UCL. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. DR GO; GO:0098609; P:cell-cell adhesion; IDA:BHF-UCL. DR GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB. DR GO; GO:0002159; P:desmosome assembly; IDA:BHF-UCL. DR GO; GO:0050982; P:detection of mechanical stimulus; IDA:BHF-UCL. DR GO; GO:0071603; P:endothelial cell-cell adhesion; ISS:BHF-UCL. DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IGI:BHF-UCL. DR GO; GO:0045766; P:positive regulation of angiogenesis; IGI:BHF-UCL. DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IC:BHF-UCL. DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IGI:BHF-UCL. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:BHF-UCL. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL. DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL. DR FunFam; 1.25.10.10:FF:000015; Catenin beta-1; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR IDEAL; IID00298; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR013284; Beta-catenin. DR PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1. DR Pfam; PF00514; Arm; 3. DR PRINTS; PR01869; BCATNINFAMLY. DR SMART; SM00185; ARM; 12. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 9. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cardiomyopathy; Cell adhesion; Cell junction; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Disease variant; Glycoprotein; Membrane; KW Nucleus; Palmoplantar keratoderma; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat. FT CHAIN 1..745 FT /note="Junction plakoglobin" FT /id="PRO_0000064278" FT REPEAT 132..171 FT /note="ARM 1" FT REPEAT 172..215 FT /note="ARM 2" FT REPEAT 216..255 FT /note="ARM 3" FT REPEAT 258..297 FT /note="ARM 4" FT REPEAT 298..341 FT /note="ARM 5" FT REPEAT 342..381 FT /note="ARM 6" FT REPEAT 383..420 FT /note="ARM 7" FT REPEAT 423..464 FT /note="ARM 8" FT REPEAT 470..510 FT /note="ARM 9" FT REPEAT 512..551 FT /note="ARM 10" FT REPEAT 574..613 FT /note="ARM 11" FT REPEAT 615..661 FT /note="ARM 12" FT REGION 132..297 FT /note="Interaction with DSC1 and DSG1" FT REGION 574..661 FT /note="Interaction with DSC1" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 665 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 730 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 14 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000269|PubMed:12847106" FT VARIANT 19 FT /note="T -> I (in ARVD12; uncertain significance; FT dbSNP:rs570878629)" FT /evidence="ECO:0000269|PubMed:20031617" FT /id="VAR_065698" FT VARIANT 39 FT /note="S -> SS (in ARVD12; affects the structure and FT distribution of mechanical and electrical cell junctions)" FT /evidence="ECO:0000269|PubMed:17924338" FT /id="VAR_037803" FT VARIANT 142 FT /note="R -> H (in dbSNP:rs41283425)" FT /evidence="ECO:0000269|PubMed:19863551, FT ECO:0000269|PubMed:20031617" FT /id="VAR_065699" FT VARIANT 648 FT /note="V -> I (in dbSNP:rs143043662)" FT /evidence="ECO:0000269|PubMed:20031617" FT /id="VAR_065700" FT VARIANT 697 FT /note="M -> L (in dbSNP:rs1126821)" FT /evidence="ECO:0000269|PubMed:10902626, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:19863551, FT ECO:0000269|PubMed:20031617, ECO:0000269|Ref.4, FT ECO:0000269|Ref.6" FT /id="VAR_037804" FT MUTAGEN 14 FT /note="T->A: Abolishes glycosylation. Does not affect FT binding to CDH1, DSC1 or DSG1." FT /evidence="ECO:0000269|PubMed:12847106" FT MUTAGEN 19 FT /note="T->A: Reduces glycosylation." FT /evidence="ECO:0000269|PubMed:12847106" FT MUTAGEN 21 FT /note="T->A: Does not affect glycosylation." FT /evidence="ECO:0000269|PubMed:12847106" FT MUTAGEN 24 FT /note="S->A: Does not affect glycosylation." FT /evidence="ECO:0000269|PubMed:12847106" FT MUTAGEN 28 FT /note="S->A: Does not affect glycosylation." FT /evidence="ECO:0000269|PubMed:12847106" FT MUTAGEN 32 FT /note="T->A: Does not affect glycosylation." FT /evidence="ECO:0000269|PubMed:12847106" FT CONFLICT 91 FT /note="P -> S (in Ref. 4; AAO85780)" FT /evidence="ECO:0000305" FT CONFLICT 264..270 FT /note="VRLADGL -> CAGRRA (in Ref. 1; AAA64895)" FT /evidence="ECO:0000305" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 133..142 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 144..151 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 156..169 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 183..193 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 199..212 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 216..224 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 227..233 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 240..256 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 260..266 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 282..296 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 300..308 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 311..321 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 325..338 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 344..350 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 353..358 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 359..362 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 366..380 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 390..397 FT /evidence="ECO:0007829|PDB:3IFQ" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 405..418 FT /evidence="ECO:0007829|PDB:3IFQ" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 423..429 FT /evidence="ECO:0007829|PDB:3IFQ" FT TURN 430..433 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 434..445 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 449..462 FT /evidence="ECO:0007829|PDB:3IFQ" FT STRAND 464..466 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 469..477 FT /evidence="ECO:0007829|PDB:3IFQ" FT TURN 478..480 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 481..487 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 488..490 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 495..508 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 512..514 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 515..520 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 523..543 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 556..570 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 574..582 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 586..592 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 598..611 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 615..623 FT /evidence="ECO:0007829|PDB:3IFQ" FT TURN 624..626 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 627..633 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 639..651 FT /evidence="ECO:0007829|PDB:3IFQ" FT HELIX 662..667 FT /evidence="ECO:0007829|PDB:3IFQ" SQ SEQUENCE 745 AA; 81745 MW; 3519A0973748BCF4 CRC64; MEVMNLMEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GIMEEDEACG RQYTLKKTTT YTQGVPPSQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQA TNLQRLAEPS QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ ESKLIILANG GPQALVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYGDDMDAT YRPMYSSDVP LDPLEMHMDM DGDYPIDTYS DGLRPPYPTA DHMLA //