PLAK_HUMAN
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 03-AUG-2022, entry version 219.
DE RecName: Full=Junction plakoglobin;
DE AltName: Full=Catenin gamma;
DE AltName: Full=Desmoplakin III;
DE AltName: Full=Desmoplakin-3;
GN Name=JUP; Synonyms=CTNNG, DP3;
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 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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 124-676 IN COMPLEX WITH
RP PHOSPHORYLATED MOUSE E-CADHERIN, DOMAIN ARM REPEATS, AND INTERACTION WITH
RP 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 [25]
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 [26]
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 [27]
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). {ECO:0000250}.
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 Interacts with MUC1. Interacts with CAV1 (By similarity). Interacts
CC with PTPRJ. Interacts with DSG1. Interacts with DSC1 and DSC2.
CC Interacts with PKP2. {ECO:0000250, ECO:0000269|PubMed:12370829,
CC ECO:0000269|PubMed:19759396, ECO:0000269|PubMed:21062920,
CC ECO:0000269|PubMed:22781308, ECO:0000269|PubMed:7982500,
CC ECO:0000269|PubMed:8631907, ECO:0000269|PubMed:9139698,
CC ECO:0000269|PubMed:9152027}.
CC -!- INTERACTION:
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; P19022: CDH2; NbExp=2; IntAct=EBI-702484, EBI-2256711;
CC P14923; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-702484, EBI-11962928;
CC P14923; Q9NSA3: CTNNBIP1; NbExp=4; IntAct=EBI-702484, EBI-747082;
CC P14923; P26196: DDX6; NbExp=3; IntAct=EBI-702484, EBI-351257;
CC P14923; Q02413: DSG1; NbExp=2; IntAct=EBI-702484, EBI-1045757;
CC P14923; Q14192: FHL2; NbExp=7; IntAct=EBI-702484, EBI-701903;
CC P14923; P23327: HRC; NbExp=2; IntAct=EBI-702484, EBI-9639760;
CC P14923; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-702484, EBI-741158;
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; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-702484, EBI-11746252;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:22781308}. Cell junction, desmosome
CC {ECO:0000269|PubMed:22781308}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22781308}. Membrane {ECO:0000269|PubMed:22781308};
CC Peripheral membrane protein {ECO:0000269|PubMed:22781308}.
CC Note=Cytoplasmic in a soluble and membrane-associated form.
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: 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};
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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_002221.1; NM_002230.2.
DR RefSeq; NP_068831.1; NM_021991.2.
DR RefSeq; XP_006721936.1; XM_006721873.2.
DR RefSeq; XP_006721937.1; XM_006721874.2.
DR RefSeq; XP_006721938.1; XM_006721875.1.
DR RefSeq; XP_006721941.1; XM_006721878.1.
DR RefSeq; XP_011523055.1; XM_011524753.2.
DR RefSeq; XP_011523057.1; XM_011524755.1.
DR RefSeq; XP_011523058.1; XM_011524756.1.
DR RefSeq; XP_011523059.1; XM_011524757.2.
DR RefSeq; XP_011523060.1; XM_011524758.1.
DR RefSeq; XP_016880079.1; XM_017024590.1.
DR PDB; 3IFQ; X-ray; 2.80 A; A/B=124-676.
DR PDBsum; 3IFQ; -.
DR AlphaFoldDB; P14923; -.
DR SMR; P14923; -.
DR BioGRID; 109931; 400.
DR CORUM; P14923; -.
DR DIP; DIP-36235N; -.
DR IntAct; P14923; 131.
DR MINT; P14923; -.
DR STRING; 9606.ENSP00000377508; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GlyConnect; 1950; 10 N-Linked glycans (4 sites).
DR GlyGen; P14923; 6 sites, 10 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P14923; -.
DR MetOSite; P14923; -.
DR PhosphoSitePlus; P14923; -.
DR SwissPalm; P14923; -.
DR BioMuta; JUP; -.
DR DMDM; 205371866; -.
DR EPD; P14923; -.
DR jPOST; P14923; -.
DR MassIVE; P14923; -.
DR MaxQB; P14923; -.
DR PaxDb; P14923; -.
DR PeptideAtlas; P14923; -.
DR PRIDE; P14923; -.
DR ProteomicsDB; 53098; -.
DR Antibodypedia; 80391; 1297 antibodies from 46 providers.
DR DNASU; 3728; -.
DR Ensembl; ENST00000310706.9; ENSP00000311113.5; ENSG00000173801.17.
DR Ensembl; ENST00000393930.5; ENSP00000377507.1; ENSG00000173801.17.
DR Ensembl; ENST00000393931.8; ENSP00000377508.3; ENSG00000173801.17.
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 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 neXtProt; NX_P14923; -.
DR OpenTargets; ENSG00000173801; -.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR Orphanet; 158687; Lethal acantholytic erosive disorder.
DR Orphanet; 34217; Naxos disease.
DR PharmGKB; PA30009; -.
DR VEuPathDB; HostDB:ENSG00000173801; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000156395; -.
DR HOGENOM; CLU_008757_1_1_1; -.
DR InParanoid; P14923; -.
DR OMA; PLDPMEM; -.
DR OrthoDB; 321213at2759; -.
DR PhylomeDB; P14923; -.
DR TreeFam; TF317997; -.
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 SignaLink; P14923; -.
DR SIGNOR; P14923; -.
DR BioGRID-ORCS; 3728; 21 hits in 1089 CRISPR screens.
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 200 other tissues.
DR ExpressionAtlas; P14923; baseline and differential.
DR Genevisible; P14923; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016342; C:catenin complex; IDA:BHF-UCL.
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:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
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:0016328; C:lateral plasma membrane; 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:0030018; C:Z disc; IEA:Ensembl.
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:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
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: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:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA: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; IBA:GO_Central.
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 GO; GO:0043588; P:skin development; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 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 InterPro; IPR030461; Plakoglobin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR PANTHER; PTHR45976:SF3; PTHR45976:SF3; 1.
DR Pfam; PF00514; Arm; 3.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cardiomyopathy; Cell adhesion; Cell junction;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant;
KW Glycoprotein; Membrane; Palmoplantar keratoderma; Phosphoprotein;
KW 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; unknown pathological
FT significance; 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
