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Q02257

- PLAK_MOUSE

UniProt

Q02257 - PLAK_MOUSE

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Protein
Junction plakoglobin
Gene
Jup
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. alpha-catenin binding Source: MGI
  2. cadherin binding Source: RefGenome
  3. protein binding Source: MGI
  4. protein kinase binding Source: RefGenome
  5. structural molecule activity Source: RefGenome
  6. transcription coactivator activity Source: RefGenome

GO - Biological processi

  1. atrioventricular valve morphogenesis Source: RefGenome
  2. bundle of His cell to Purkinje myocyte communication Source: Ensembl
  3. cell adhesion Source: MGI
  4. cell migration Source: Ensembl
  5. cell morphogenesis Source: RefGenome
  6. cellular response to indole-3-methanol Source: Ensembl
  7. cytoskeletal anchoring at plasma membrane Source: RefGenome
  8. desmosome assembly Source: MGI
  9. detection of mechanical stimulus Source: Ensembl
  10. ectoderm development Source: RefGenome
  11. gastrulation Source: RefGenome
  12. morphogenesis of embryonic epithelium Source: RefGenome
  13. negative regulation of Wnt signaling pathway involved in heart development Source: RefGenome
  14. negative regulation of heart induction by canonical Wnt signaling pathway Source: RefGenome
  15. nervous system development Source: RefGenome
  16. oocyte development Source: RefGenome
  17. positive regulation of protein import into nucleus Source: Ensembl
  18. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  19. positive regulation of transcription from RNA polymerase II promoter Source: RefGenome
  20. protein heterooligomerization Source: Ensembl
  21. regulation of cell proliferation Source: Ensembl
  22. regulation of heart rate by cardiac conduction Source: Ensembl
  23. single organismal cell-cell adhesion Source: MGI
  24. skin development Source: MGI
  25. ventricular cardiac muscle cell action potential Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Junction plakoglobin
Alternative name(s):
Desmoplakin III
Desmoplakin-3
Gene namesi
Name:Jup
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:96650. Jup.

Subcellular locationi

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

GO - Cellular componenti

  1. Z disc Source: MGI
  2. actin cytoskeleton Source: RefGenome
  3. apicolateral plasma membrane Source: Ensembl
  4. basolateral plasma membrane Source: RefGenome
  5. beta-catenin destruction complex Source: RefGenome
  6. catenin complex Source: RefGenome
  7. cell-cell adherens junction Source: MGI
  8. cell-cell junction Source: MGI
  9. cytoplasmic side of plasma membrane Source: RefGenome
  10. cytosol Source: MGI
  11. desmosome Source: MGI
  12. fascia adherens Source: RefGenome
  13. gamma-catenin-TCF7L2 complex Source: Ensembl
  14. intermediate filament Source: BHF-UCL
  15. lateral plasma membrane Source: Ensembl
  16. membrane Source: MGI
  17. protein-DNA complex Source: Ensembl
  18. zonula adherens Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Junction plakoglobin
PRO_0000064279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Glycosylationi14 – 141O-linked (GlcNAc) By similarity
Modified residuei182 – 1821Phosphoserine By similarity
Modified residuei665 – 6651Phosphoserine By similarity

Post-translational modificationi

May be phosphorylated by FER By similarity.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ02257.
PaxDbiQ02257.
PRIDEiQ02257.

PTM databases

PhosphoSiteiQ02257.

Expressioni

Gene expression databases

BgeeiQ02257.
CleanExiMM_JUP.
GenevestigatoriQ02257.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi200874. 11 interactions.
IntActiQ02257. 10 interactions.
MINTiMINT-4115765.

Structurei

3D structure databases

ProteinModelPortaliQ02257.
SMRiQ02257. Positions 68-673.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati132 – 17140ARM 1
Add
BLAST
Repeati172 – 21544ARM 2
Add
BLAST
Repeati216 – 25540ARM 3
Add
BLAST
Repeati258 – 29740ARM 4
Add
BLAST
Repeati298 – 34144ARM 5
Add
BLAST
Repeati342 – 38140ARM 6
Add
BLAST
Repeati383 – 42038ARM 7
Add
BLAST
Repeati423 – 46442ARM 8
Add
BLAST
Repeati470 – 51041ARM 9
Add
BLAST
Repeati512 – 55140ARM 10
Add
BLAST
Repeati574 – 61340ARM 11
Add
BLAST
Repeati615 – 66147ARM 12
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 297166Interaction with DSC1 and DSG1 By similarity
Add
BLAST
Regioni574 – 66188Interaction with DSC1 By similarity
Add
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the beta-catenin family.
Contains 12 ARM repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
InParanoidiQ02257.
KOiK10056.
OMAiMNLIEQP.
OrthoDBiEOG7X9G6B.
PhylomeDBiQ02257.
TreeFamiTF317997.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 3 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02257-1 [UniParc]FASTAAdd to Basket

« Hide

MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG    50
RQYTLKKTTT YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL 100
LLATQVEGQT TNLQRLAEPS QLLKSAIVHL INYQDDAELA TRALPELTKL 150
LNDEDPVVVT KAAMIVNQLS KKEASRRALM GSPQLVAAVV RTMQNTSDLD 200
TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE SVLFYAITTL 250
HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ 300
ESKLIILANG GPQGLVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE 350
AGGMQALGKH LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL 400
SVDDVNVLTC ATGTLSNLTC NNSKNKTLVT QNSGVEALIH AILRAGDKDD 450
ITEPAVCALR HLTSRHPEAE MAQNSVRLNY GIPAIVKLLN QPNQWPLVKA 500
TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR HVAAGTQQPY 550
TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI 600
QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF 650
RISEDKNPDY RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT 700
YRPMYSSDVP LDPLDMHMDL DGDYPMDTYS DGLRPPYPTA DHMLA 745
Length:745
Mass (Da):81,801
Last modified:December 6, 2005 - v3
Checksum:i9609619D94052FC5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK170934 mRNA. Translation: BAE42126.1.
BC040757 mRNA. Translation: AAH40757.1.
BC094461 mRNA. Translation: AAH94461.1.
M90365 mRNA. Translation: AAB02885.1.
CCDSiCCDS25420.1.
PIRiS35092.
RefSeqiNP_034723.1. NM_010593.2.
XP_006532378.1. XM_006532315.1.
XP_006532379.1. XM_006532316.1.
UniGeneiMm.299774.

Genome annotation databases

EnsembliENSMUST00000001592; ENSMUSP00000001592; ENSMUSG00000001552.
ENSMUST00000107403; ENSMUSP00000103026; ENSMUSG00000001552.
GeneIDi16480.
KEGGimmu:16480.
UCSCiuc007lkz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK170934 mRNA. Translation: BAE42126.1 .
BC040757 mRNA. Translation: AAH40757.1 .
BC094461 mRNA. Translation: AAH94461.1 .
M90365 mRNA. Translation: AAB02885.1 .
CCDSi CCDS25420.1.
PIRi S35092.
RefSeqi NP_034723.1. NM_010593.2.
XP_006532378.1. XM_006532315.1.
XP_006532379.1. XM_006532316.1.
UniGenei Mm.299774.

3D structure databases

ProteinModelPortali Q02257.
SMRi Q02257. Positions 68-673.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200874. 11 interactions.
IntActi Q02257. 10 interactions.
MINTi MINT-4115765.

PTM databases

PhosphoSitei Q02257.

Proteomic databases

MaxQBi Q02257.
PaxDbi Q02257.
PRIDEi Q02257.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001592 ; ENSMUSP00000001592 ; ENSMUSG00000001552 .
ENSMUST00000107403 ; ENSMUSP00000103026 ; ENSMUSG00000001552 .
GeneIDi 16480.
KEGGi mmu:16480.
UCSCi uc007lkz.2. mouse.

Organism-specific databases

CTDi 3728.
MGIi MGI:96650. Jup.

Phylogenomic databases

eggNOGi NOG297695.
GeneTreei ENSGT00730000110821.
HOGENOMi HOG000230958.
HOVERGENi HBG000919.
InParanoidi Q02257.
KOi K10056.
OMAi MNLIEQP.
OrthoDBi EOG7X9G6B.
PhylomeDBi Q02257.
TreeFami TF317997.

Miscellaneous databases

ChiTaRSi JUP. mouse.
NextBioi 289775.
PROi Q02257.
SOURCEi Search...

Gene expression databases

Bgeei Q02257.
CleanExi MM_JUP.
Genevestigatori Q02257.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view ]
Pfami PF00514. Arm. 3 hits.
[Graphical view ]
PRINTSi PR01869. BCATNINFAMLY.
SMARTi SM00185. ARM. 12 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50176. ARM_REPEAT. 9 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPLAK_MOUSE
AccessioniPrimary (citable) accession number: Q02257
Secondary accession number(s): Q8CGD3
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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