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P14923 (PLAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Junction plakoglobin
Alternative name(s):
Catenin gamma
Desmoplakin III
Desmoplakin-3
Gene names
Name:JUP
Synonyms:CTNNG, DP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton By similarity.

Subunit structure

Homodimer. Component of an E-cadherin/catenin adhesion complex composed of at least E-cadherin/CDH1 and gamma-catenin/JUP, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Interacts with MUC1. Interacts with CAV1 By similarity. Interacts with PTPRJ. Interacts with DSG1. Interacts with DSC1 and DSC2. Interacts with PKP2. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.20 Ref.21 Ref.23

Subcellular location

Cell junctionadherens junction. Cell junctiondesmosome. Cytoplasmcytoskeleton. Membrane; Peripheral membrane protein. Note: Cytoplasmic in a soluble and membrane-associated form. Ref.21

Domain

The entire ARM repeats region mediates binding to CDH1/E-cadherin. The N-terminus and first three ARM repeats are sufficient for binding to DSG1. The N-terminus and first ARM repeat are sufficient for association with CTNNA1. DSC1 association requires both ends of the ARM repeat region. Ref.11 Ref.23

Post-translational modification

May be phosphorylated by FER. Ref.16

Involvement in disease

Naxos disease (NXD) [MIM:601214]: An autosomal recessive disorder characterized by the association of diffuse non-epidermolytic palmoplantar keratoderma with woolly hair and cardiac abnormalities such as dilated cardiomyopathy and arrhythmogenic right ventricular dysplasia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Arrhythmogenic right ventricular dysplasia, familial, 12 (ARVD12) [MIM:611528]: A congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.24 Ref.25

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

Sequence caution

The sequence AAH00441.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCardiomyopathy
Disease mutation
Palmoplantar keratoderma
   DomainRepeat
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction organization

Traceable author statement. Source: Reactome

atrioventricular valve morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

bundle of His cell to Purkinje myocyte communication

Inferred from mutant phenotype Ref.24. Source: BHF-UCL

cell junction assembly

Traceable author statement. Source: Reactome

cell migration

Inferred from mutant phenotype PubMed 18937352. Source: BHF-UCL

cell morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell-cell junction organization

Traceable author statement. Source: Reactome

cellular response to indole-3-methanol

Inferred from direct assay PubMed 10868478. Source: UniProtKB

cytoskeletal anchoring at plasma membrane

Non-traceable author statement PubMed 22889254. Source: BHF-UCL

desmosome assembly

Inferred from direct assay PubMed 22889254. Source: BHF-UCL

detection of mechanical stimulus

Inferred from direct assay PubMed 18937352. Source: BHF-UCL

ectoderm development

Inferred from Biological aspect of Ancestor. Source: RefGenome

endothelial cell-cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

establishment of protein localization to plasma membrane

Inferred from mutant phenotype PubMed 20859650. Source: UniProt

gastrulation

Inferred from Biological aspect of Ancestor. Source: RefGenome

morphogenesis of embryonic epithelium

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of Wnt signaling pathway involved in heart development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of heart induction by canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

nervous system development

Inferred from Biological aspect of Ancestor. Source: RefGenome

oocyte development

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of canonical Wnt signaling pathway

Inferred by curator PubMed 14661054. Source: BHF-UCL

positive regulation of protein import into nucleus

Inferred from direct assay PubMed 10825188PubMed 14661054. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 14661054. Source: BHF-UCL

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from direct assay Ref.24. Source: BHF-UCL

regulation of heart rate by cardiac conduction

Inferred from mutant phenotype Ref.24. Source: BHF-UCL

single organismal cell-cell adhesion

Inferred from direct assay PubMed 18937352. Source: BHF-UCL

skin development

Inferred from Biological aspect of Ancestor. Source: RefGenome

ventricular cardiac muscle cell action potential

Inferred from mutant phenotype Ref.24. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

actin cytoskeleton

Inferred from Biological aspect of Ancestor. Source: RefGenome

apicolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

catenin complex

Inferred from direct assay PubMed 7650039. Source: BHF-UCL

cell-cell adherens junction

Inferred from direct assay PubMed 10403777. Source: UniProtKB

cell-cell junction

Inferred from direct assay PubMed 10460003. Source: UniProtKB

cytoplasm

Inferred from mutant phenotype PubMed 14661054. Source: BHF-UCL

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoskeleton

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

desmosome

Inferred from direct assay PubMed 1639850. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

fascia adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

gamma-catenin-TCF7L2 complex

Inferred from direct assay PubMed 14661054. Source: BHF-UCL

intercalated disc

Inferred from direct assay PubMed 22889254. Source: BHF-UCL

intermediate filament

Inferred from electronic annotation. Source: Ensembl

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from mutant phenotype PubMed 14661054. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 14661054. Source: BHF-UCL

protein-DNA complex

Inferred from direct assay PubMed 14661054. Source: BHF-UCL

zonula adherens

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionalpha-catenin binding

Inferred from physical interaction PubMed 7650039PubMed 7890674. Source: BHF-UCL

cadherin binding

Inferred from physical interaction PubMed 1639850PubMed 7650039. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein phosphatase binding

Inferred from physical interaction PubMed 8663237. Source: UniProtKB

structural constituent of cell wall

Inferred by curator PubMed 7650039. Source: BHF-UCL

structural molecule activity

Non-traceable author statement PubMed 22889254. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay PubMed 14661054. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745Junction plakoglobin
PRO_0000064278

Regions

Repeat132 – 17140ARM 1
Repeat172 – 21544ARM 2
Repeat216 – 25540ARM 3
Repeat258 – 29740ARM 4
Repeat298 – 34144ARM 5
Repeat342 – 38140ARM 6
Repeat383 – 42038ARM 7
Repeat423 – 46442ARM 8
Repeat470 – 51041ARM 9
Repeat512 – 55140ARM 10
Repeat574 – 61340ARM 11
Repeat615 – 66147ARM 12
Region132 – 297166Interaction with DSC1 and DSG1
Region574 – 66188Interaction with DSC1

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.22
Modified residue1821Phosphoserine Ref.17
Modified residue6651Phosphoserine Ref.17 Ref.18
Glycosylation141O-linked (GlcNAc) Ref.15

Natural variations

Natural variant191T → I in ARVD12. Ref.25
VAR_065698
Natural variant391S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. Ref.24
VAR_037803
Natural variant1421R → H. Ref.25 Ref.26
Corresponds to variant rs41283425 [ dbSNP | Ensembl ].
VAR_065699
Natural variant6481V → I. Ref.25
Corresponds to variant rs143043662 [ dbSNP | Ensembl ].
VAR_065700
Natural variant6971M → L. Ref.4 Ref.6 Ref.7 Ref.9 Ref.25 Ref.26
Corresponds to variant rs1126821 [ dbSNP | Ensembl ].
VAR_037804

Experimental info

Mutagenesis141T → A: Abolishes glycosylation. Does not affect binding to CDH1, DSC1 or DSG1. Ref.15
Mutagenesis191T → A: Reduces glycosylation. Ref.15
Mutagenesis211T → A: Does not affect glycosylation. Ref.15
Mutagenesis241S → A: Does not affect glycosylation. Ref.15
Mutagenesis281S → A: Does not affect glycosylation. Ref.15
Mutagenesis321T → A: Does not affect glycosylation. Ref.15
Sequence conflict911P → S in AAO85780. Ref.4
Sequence conflict264 – 2707VRLADGL → CAGRRA in AAA64895. Ref.1

Secondary structure

..................................................................................... 745
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14923 [UniParc].

Last modified September 2, 2008. Version 3.
Checksum: 3519A0973748BCF4

FASTA74581,745
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and amino acid sequence of human plakoglobin, the common junctional plaque protein."
Franke W.W., Goldschmidt M.D., Zimbelmann R., Mueller H.M., Schiller D.L., Cowin P.
Proc. Natl. Acad. Sci. U.S.A. 86:4027-4031(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Zimbelmann R.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic organization and amplification of the human plakoglobin gene (JUP)."
Whittock N.V., Eady R.A.J., McGrath J.A.
Exp. Dermatol. 9:323-326(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Homo sapiens gamma-catenin mRNA from human KB epidermoid adenocarcinoma cells."
Liang X.-J., Gottesman M.M.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-697.
Tissue: Epidermal carcinoma.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-697.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-697.
Tissue: Lung and Placenta.
[8]Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma and Lung carcinoma.
[9]"Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease)."
McKoy G., Protonotarios N., Crosby A., Tsatsopoulou A., Anastasakis A., Coonar A., Norman M., Baboonian C., Jeffery S., McKenna W.J.
Lancet 355:2119-2124(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-745, VARIANT LEU-697, INVOLVEMENT IN NAXOS DISEASE.
Tissue: Leukocyte.
[10]"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
Butz S., Kemler R.
FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[11]"Desmosomal cadherin binding domains of plakoglobin."
Witcher L.L., Collins R., Puttagunta S., Mechanic S.E., Munson M., Gumbiner B., Cowin P.
J. Biol. Chem. 271:10904-10909(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, INTERACTION WITH CTNNA1; DSC1 AND DSG1.
[12]"Interaction of the DF3/MUC1 breast carcinoma-associated antigen and beta-catenin in cell adhesion."
Yamamoto M., Bharti A., Li Y., Kufe D.
J. Biol. Chem. 272:12492-12494(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1.
[13]"Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin."
Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R., Wheelock M.J.
J. Cell Sci. 110:1013-1022(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNA1.
[14]"The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRJ.
[15]"Plakoglobin is O-glycosylated close to the N-terminal destruction box."
Hatsell S., Medina L., Merola J., Haltiwanger R., Cowin P.
J. Biol. Chem. 278:37745-37752(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-14, MUTAGENESIS OF THR-14; THR-19; THR-21; SER-24; SER-28 AND THR-32.
[16]"Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates beta-catenin-mediated transcription."
Miravet S., Piedra J., Castano J., Raurell I., Franci C., Dunach M., Garcia de Herreros A.
Mol. Cell. Biol. 23:7391-7402(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FER.
[17]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy caused by desmocollin-2 mutations."
Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A., Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C., Saffitz J.E., Protonotarios N., McKenna W.J.
Cardiovasc. Res. 90:77-87(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DSC2.
[21]"Molecular insights into arrhythmogenic right ventricular cardiomyopathy caused by plakophilin-2 missense mutations."
Kirchner F., Schuetz A., Boldt L.H., Martens K., Dittmar G., Haverkamp W., Thierfelder L., Heinemann U., Gerull B.
Circ. Cardiovasc. Genet. 5:400-411(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKP2, SUBCELLULAR LOCATION.
[22]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes."
Choi H.J., Gross J.C., Pokutta S., Weis W.I.
J. Biol. Chem. 284:31776-31788(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 124-676 IN COMPLEX WITH PHOSPHORYLATED MOUSE E-CADHERIN, DOMAIN ARM REPEATS, INTERACTION WITH DSC1 AND DSG1.
[24]"A novel dominant mutation in plakoglobin causes arrhythmogenic right ventricular cardiomyopathy."
Asimaki A., Syrris P., Wichter T., Matthias P., Saffitz J.E., McKenna W.J.
Am. J. Hum. Genet. 81:964-973(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARVD12 SER-39 INS, CHARACTERIZATION OF VARIANT ARVD12 SER-39 INS.
[25]"Comprehensive desmosome mutation analysis in North Americans with arrhythmogenic right ventricular dysplasia/cardiomyopathy."
den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A., Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D., Bluemke D.A., Calkins H., Dalal D., Judge D.P.
Circ. Cardiovasc. Genet. 2:428-435(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARVD12 ILE-19, VARIANTS HIS-142; ILE-648 AND LEU-697.
[26]"Role of genetic testing in arrhythmogenic right ventricular cardiomyopathy/dysplasia."
Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L., Robb L., Talajic M., Brugada R.
Clin. Genet. 77:37-48(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-142 AND LEU-697.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23410 mRNA. Translation: AAA64895.1.
Z68228 mRNA. Translation: CAA92522.1.
AF306723, AF233882 Genomic DNA. Translation: AAG16727.1.
AY243535 mRNA. Translation: AAO85780.1.
AC109319 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60762.1.
BC000441 mRNA. Translation: AAH00441.2. Different initiation.
BC011865 mRNA. Translation: AAH11865.1.
AJ249711 Genomic DNA. Translation: CAC04246.1.
CCDSCCDS11407.1.
PIRA32905.
RefSeqNP_002221.1. NM_002230.2.
NP_068831.1. NM_021991.2.
XP_006721936.1. XM_006721873.1.
XP_006721937.1. XM_006721874.1.
XP_006721938.1. XM_006721875.1.
XP_006721939.1. XM_006721876.1.
XP_006721940.1. XM_006721877.1.
XP_006721941.1. XM_006721878.1.
UniGeneHs.514174.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IFQX-ray2.80A/B124-676[»]
ProteinModelPortalP14923.
SMRP14923. Positions 111-673.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109931. 90 interactions.
IntActP14923. 35 interactions.
MINTMINT-105053.
STRING9606.ENSP00000311113.

PTM databases

PhosphoSiteP14923.

Polymorphism databases

DMDM205371866.

Proteomic databases

MaxQBP14923.
PaxDbP14923.
PRIDEP14923.

Protocols and materials databases

DNASU3728.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310706; ENSP00000311113; ENSG00000173801.
ENST00000393930; ENSP00000377507; ENSG00000173801.
ENST00000393931; ENSP00000377508; ENSG00000173801.
ENST00000562805; ENSP00000456867; ENSG00000261577.
ENST00000565220; ENSP00000454630; ENSG00000261577.
ENST00000565780; ENSP00000457186; ENSG00000261577.
GeneID3728.
KEGGhsa:3728.
UCSCuc002hxq.2. human.

Organism-specific databases

CTD3728.
GeneCardsGC17M039776.
GeneReviewsJUP.
HGNCHGNC:6207. JUP.
HPACAB002139.
HPA032047.
MIM173325. gene.
601214. phenotype.
611528. phenotype.
neXtProtNX_P14923.
Orphanet293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
158687. Lethal acantholytic epidermolysis bullosa.
34217. Naxos disease.
PharmGKBPA30009.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297695.
HOVERGENHBG000919.
InParanoidP14923.
KOK10056.
OMAMNLIEQP.
PhylomeDBP14923.
TreeFamTF317997.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkP14923.

Gene expression databases

ArrayExpressP14923.
BgeeP14923.
CleanExHS_JUP.
GenevestigatorP14923.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamPF00514. Arm. 3 hits.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSJUP. human.
EvolutionaryTraceP14923.
GeneWikiPlakoglobin.
GenomeRNAi3728.
NextBio14595.
PMAP-CutDBP14923.
PROP14923.
SOURCESearch...

Entry information

Entry namePLAK_HUMAN
AccessionPrimary (citable) accession number: P14923
Secondary accession number(s): Q15093 expand/collapse secondary AC list , Q15151, Q7L3S5, Q86W21, Q9BWC4, Q9HCX9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 2, 2008
Last modified: July 9, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM