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Q02257 (PLAK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Junction plakoglobin
Alternative name(s):
Desmoplakin III
Desmoplakin-3
Gene names
Name:Jup
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.7

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. Interacts with PTPRJ. Interacts with DSG1. Interacts with DSC1 and DSC2. Interacts with PKP2 By similarity. Ref.5

Subcellular location

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

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 By similarity.

Post-translational modification

May be phosphorylated by FER By similarity.

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processatrioventricular valve morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

bundle of His cell to Purkinje myocyte communication

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from direct assay PubMed 12847106. Source: MGI

cell migration

Inferred from electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to indole-3-methanol

Inferred from electronic annotation. Source: Ensembl

cytoskeletal anchoring at plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

desmosome assembly

Inferred from mutant phenotype PubMed 18496566PubMed 8954745PubMed 9847250. Source: MGI

detection of mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

ectoderm development

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate by cardiac conduction

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 8954745. Source: MGI

skin development

Inferred from mutant phenotype PubMed 8954745. Source: MGI

ventricular cardiac muscle cell action potential

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from direct assay PubMed 8821035. Source: MGI

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

beta-catenin destruction complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

catenin complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell-cell adherens junction

Inferred from direct assay PubMed 15775979PubMed 8582267. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 12847106PubMed 18816447PubMed 21296051. Source: MGI

cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from direct assay PubMed 12847106. Source: MGI

desmosome

Inferred from direct assay PubMed 10662781PubMed 14673151PubMed 15775979PubMed 9864371. Source: MGI

fascia adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

gamma-catenin-TCF7L2 complex

Inferred from electronic annotation. Source: Ensembl

intermediate filament

Inferred from direct assay PubMed 16917092. Source: BHF-UCL

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 16510873. Source: MGI

protein-DNA complex

Inferred from electronic annotation. Source: Ensembl

zonula adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-catenin binding

Inferred from physical interaction PubMed 14579029. Source: MGI

cadherin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 12847106PubMed 14579029PubMed 14673151PubMed 16973135. Source: MGI

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

structural molecule activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription coactivator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745Junction plakoglobin
PRO_0000064279

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 By similarity
Region574 – 66188Interaction with DSC1 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1821Phosphoserine By similarity
Modified residue6651Phosphoserine By similarity
Glycosylation141O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02257 [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: 9609619D94052FC5

FASTA74581,801
        10         20         30         40         50         60 
MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG RQYTLKKTTT 

        70         80         90        100        110        120 
YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQT 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 GPQGLVQIMR 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 EPYADDMDAT YRPMYSSDVP LDPLDMHMDL 

       730        740 
DGDYPMDTYS DGLRPPYPTA DHMLA 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[2]"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].
Strain: FVB/N.
Tissue: Colon and Mammary tumor.
[3]"Plakoglobin and beta-catenin: distinct but closely related."
Butz S., Stappert J., Weissig H., Kemler R.
Science 257:1142-1144(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-745.
[4]Butz S.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 418 AND 420.
[5]"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.
[6]"Deconstructing the cadherin-catenin-actin complex."
Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.
Cell 123:889-901(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[7]"VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF."
Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R., Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O., Bixel M.G., Butz S., Vestweber D.
J. Exp. Med. 205:2929-2945(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK170934 mRNA. Translation: BAE42126.1.
BC040757 mRNA. Translation: AAH40757.1.
BC094461 mRNA. Translation: AAH94461.1.
M90365 mRNA. Translation: AAB02885.1.
CCDSCCDS25420.1.
PIRS35092.
RefSeqNP_034723.1. NM_010593.2.
XP_006532378.1. XM_006532315.1.
XP_006532379.1. XM_006532316.1.
UniGeneMm.299774.

3D structure databases

ProteinModelPortalQ02257.
SMRQ02257. Positions 68-673.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200874. 11 interactions.
IntActQ02257. 10 interactions.
MINTMINT-4115765.

PTM databases

PhosphoSiteQ02257.

Proteomic databases

MaxQBQ02257.
PaxDbQ02257.
PRIDEQ02257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001592; ENSMUSP00000001592; ENSMUSG00000001552.
ENSMUST00000107403; ENSMUSP00000103026; ENSMUSG00000001552.
GeneID16480.
KEGGmmu:16480.
UCSCuc007lkz.2. mouse.

Organism-specific databases

CTD3728.
MGIMGI:96650. Jup.

Phylogenomic databases

eggNOGNOG297695.
GeneTreeENSGT00730000110821.
HOGENOMHOG000230958.
HOVERGENHBG000919.
InParanoidQ02257.
KOK10056.
OMAMNLIEQP.
OrthoDBEOG7X9G6B.
PhylomeDBQ02257.
TreeFamTF317997.

Gene expression databases

BgeeQ02257.
CleanExMM_JUP.
GenevestigatorQ02257.

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. mouse.
NextBio289775.
PROQ02257.
SOURCESearch...

Entry information

Entry namePLAK_MOUSE
AccessionPrimary (citable) accession number: Q02257
Secondary accession number(s): Q8CGD3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot