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Q02257

- PLAK_MOUSE

UniProt

Q02257 - PLAK_MOUSE

Protein

Junction plakoglobin

Gene

Jup

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    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 heart induction by canonical Wnt signaling pathway Source: RefGenome
    14. negative regulation of Wnt signaling pathway involved in heart development 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

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

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Junction plakoglobinPRO_0000064279Add
    BLAST

    Amino acid modifications

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

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ02257.
    SMRiQ02257. Positions 68-673.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni132 – 297166Interaction with DSC1 and DSG1By similarityAdd
    BLAST
    Regioni574 – 66188Interaction with DSC1By similarityAdd
    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.By similarity

    Sequence similaritiesi

    Belongs to the beta-catenin family.Curated
    Contains 12 ARM repeats.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 128 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