ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P14923


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PLAK_HUMAN
Primary accession number P14923
Secondary accession numbers Q15093 Q15151 Q7L3S5 Q86W21 Q9BWC4 Q9HCX9
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on September 2, 2008 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 93)
Name and origin of the protein
Protein name Junction plakoglobin
Synonyms Desmoplakin-3
Desmoplakin III
Catenin gamma
Gene name
Name: JUP
Synonyms: CTNNG, DP3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.86.11.4027; PubMed=2726765 [NCBI, ExPASy, EBI, Israel, Japan]
Franke W.W., Goldschmidt M.D., Zimbelmann R., Mueller H.M., Schiller D.L., Cowin P.;
"Molecular cloning and amino acid sequence of human plakoglobin, the common junctional plaque protein.";
Proc. Natl. Acad. Sci. U.S.A. 86:4027-4031(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Zimbelmann R.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1034/j.1600-0625.2000.009005323.x; PubMed=11016852 [NCBI, ExPASy, EBI, Israel, Japan]
Whittock N.V., Eady R.A.J., McGrath J.A.;
"Genomic organization and amplification of the human plakoglobin gene (JUP).";
Exp. Dermatol. 9:323-326(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-697.
TISSUE=Epidermal carcinoma;
Liang X.-J., Gottesman M.M.;
"Homo sapiens gamma-catenin mRNA from human KB epidermoid adenocarcinoma cells.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-697.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-697.
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 1-12; 116-142; 150-172; 177-203; 217-233; 273-279; 304-320; 327-333; 368-394; 427-460; 466-533; 583-602; 638-661 AND 664-674, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, and Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.;
Submitted (MAR-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-745, VARIANT LEU-697, AND INVOLVEMENT IN NAXOS DISEASE.
TISSUE=Leukocyte;
DOI=10.1016/S0140-6736(00)02379-5; PubMed=10902626 [NCBI, ExPASy, EBI, Israel, Japan]
McKoy G., Protonotarios N., Crosby A., Tsatsopoulou A., Anastasakis A., Coonar A., Norman M., Baboonian C., Jeffery S., McKenna W.J.;
"Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease).";
Lancet 355:2119-2124(2000).
[9]
INTERACTION WITH MUC1.
DOI=10.1074/jbc.272.19.12492; PubMed=9139698 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto M., Bharti A., Li Y., Kufe D.;
"Interaction of the DF3/MUC1 breast carcinoma-associated antigen and beta-catenin in cell adhesion.";
J. Biol. Chem. 272:12492-12494(1997).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-660, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[14]
VARIANT ARVD12 SER-39 INS, AND CHARACTERIZATION OF VARIANT ARVD12 SER-39 INS.
DOI=10.1086/521633; PubMed=17924338 [NCBI, ExPASy, EBI, Israel, Japan]
Asimaki A., Syrris P., Wichter T., Matthias P., Saffitz J.E., McKenna W.J.;
"A novel dominant mutation in plakoglobin causes arrhythmogenic right ventricular cardiomyopathy.";
Am. J. Hum. Genet. 81:964-973(2007).
Comments
  • FUNCTION: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques.
  • SUBUNIT: Homodimer. Interacts with MUC1.
  • INTERACTION:
    Q9NSA3:CTNNBIP1; NbExp=1; IntAct=EBI-702484, EBI-747082;
    P16284:PECAM1; NbExp=3; IntAct=EBI-702484, EBI-716404;
    Q99623:PHB2; NbExp=1; IntAct=EBI-702484, EBI-358348;
    P49768:PSEN1; NbExp=3; IntAct=EBI-702484, EBI-297277;
    P49769:Psen1 (xeno); NbExp=1; IntAct=EBI-702484, EBI-990067;
    Q9NQB0:TCF7L2; NbExp=1; IntAct=EBI-702484, EBI-924724;
  • SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell junction, desmosome. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Note=Cytoplasmic in a soluble and membrane-associated form.
  • DISEASE: Defects in JUP are the cause of Naxos disease (NXD) [MIM:601214]. NXD is an autosomal recessive disorder combining diffuse non-epidermolytic palmoplantar keratoderma with arrhythmogenic right ventricular dysplasia/cardiomyopathy and woolly hair.
  • DISEASE: Defects in JUP are the cause of familial arrhythmogenic right ventricular dysplasia type 12 (ARVD12) [MIM:611528]; also called arrhythmogenic right ventricular cardiomyopathy type 12 (ARVC12). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall.
  • SIMILARITY: Belongs to the beta-catenin family.
  • SIMILARITY: Contains 9 ARM repeats.
  • SEQUENCE CAUTION:
    • Sequence=AAH00441.2; Type=Erroneous initiation; Note=Translation N-terminally shortened
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=JUP";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M23410; AAA64895.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z68228; CAA92522.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF306723; AAG16727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF233882; AAG16727.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY243535; AAO85780.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471152; EAW60762.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000441; AAH00441.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011865; AAH11865.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ249711; CAC04246.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00554711; -.
PIR A32905; A32905.
RefSeq NP_002221.1; -.
NP_068831.1; -.
UniGene Hs.514174
3D structure databases
HSSP Q02248; 2BCT. [HSSP ENTRY / PDB]
SMR P14923; 140-652.
ModBase P14923.
Protein-protein interaction databases
IntAct P14923; 16.
PTM databases
PhosphoSite P14923; -.
Enzyme and pathway databases
Pathway_Interaction_DB arf6_traffickingpathway; Arf6 trafficking events.
Organism-specific databases
GeneCards GC17M037164; -.
HGNC HGNC:6207; JUP.
GenAtlas JUP.
HPA CAB002139; -.
MIM 173325; gene. [NCBI / EBI]
601214; phenotype. [NCBI / EBI]
611528; phenotype. [NCBI / EBI]
Orphanet 247; Arrhythmogenic right ventricular dysplasia.
34217; Naxos disease.
PharmGKB PA30009; -.
Gene expression databases
ArrayExpress P14923; -.
Bgee P14923; -.
CleanEx HS_JUP; -.
GermOnline ENSG00000173801; Homo sapiens.
Ontologies
GO
GO:0030057; Cellular component: desmosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0008092; Molecular function: cytoskeletal protein binding (traceable author statement from ProtInc).
GO:0019903; Molecular function: protein phosphatase binding (inferred from physical interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000225; Armadillo.
IPR013284; Beta-catenin.
IPR000357; HEAT.
Graphical view of domain structure.
Pfam PF00514; Arm; 6.
PF02985; HEAT; 1.
Pfam graphical view of domain structure.
PRINTS PR01869; BCATNINFAMLY.
SMART SM00185; ARM; 12.
SMART graphical view of domain structure.
PROSITE PS50176; ARM_REPEAT; 9.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P14923; -.
Genome annotation databases
Ensembl ENSG00000173801; Homo sapiens. [Contig view]
GeneID 3728; -.
KEGG hsa:3728; -.
Phylogenomic databases
HOVERGEN P14923; -.
OMA P14923; DDMDATY.
Other
PMAP-CutDB P14923; -.
SOURCE JUP; Homo sapiens.
ProtoNet P14923.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cardiomyopathy; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Membrane; Palmoplantar keratoderma; Phosphoprotein; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   745  745     Junction plakoglobin. PRO_0000064278
REPEAT   132   171  40     ARM 1. 
REPEAT   216   255  40     ARM 2. 
REPEAT   258   297  40     ARM 3. 
REPEAT   342   381  40     ARM 4. 
REPEAT   383   420  38     ARM 5. 
REPEAT   423   464  42     ARM 6. 
REPEAT   470   510  41     ARM 7. 
REPEAT   512   551  40     ARM 8. 
REPEAT   574   613  40     ARM 9. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   20    20        Phosphotyrosine. 
MOD_RES   182   182        Phosphoserine. 
MOD_RES   660   660        Phosphotyrosine. 
MOD_RES   665   665        Phosphoserine. 
VARIANT   39    39  1     S -> SS (in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions). VAR_037803
VARIANT   697   697  1     M -> L (in dbSNP:rs1126821 [NCBI]). VAR_037804 
CONFLICT   91    91        P -> S (in Ref. 4; AAO85780). 
CONFLICT   264   270        VRLADGL -> CAGRRA (in Ref. 1; AAA64895). 
Sequence information
Length: 745 AA [This is the length of the unprocessed precursor] Molecular weight: 81745 Da [This is the MW of the unprocessed precursor] CRC64: 3519A0973748BCF4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEVMNLMEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GIMEEDEACG RQYTLKKTTT 

        70         80         90        100        110        120 
YTQGVPPSQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQA TNLQRLAEPS 

       130        140        150        160        170        180 
QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM 

       190        200        210        220        230        240 
GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE 

       250        260        270        280        290        300 
SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ 

       310        320        330        340        350        360 
ESKLIILANG GPQALVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH 

       370        380        390        400        410        420 
LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC 

       430        440        450        460        470        480 
NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY 

       490        500        510        520        530        540 
GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR 

       550        560        570        580        590        600 
HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI 

       610        620        630        640        650        660 
QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY 

       670        680        690        700        710        720 
RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYGDDMDAT YRPMYSSDVP LDPLEMHMDM 

       730        740 
DGDYPIDTYS DGLRPPYPTA DHMLA 

P14923 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!