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P14923

- PLAK_HUMAN

UniProt

P14923 - PLAK_HUMAN

Protein

Junction plakoglobin

Gene

JUP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (02 Sep 2008)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. alpha-catenin binding Source: BHF-UCL
    2. cadherin binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: BHF-UCL
    5. protein kinase binding Source: RefGenome
    6. protein phosphatase binding Source: UniProtKB
    7. structural constituent of cell wall Source: BHF-UCL
    8. structural molecule activity Source: BHF-UCL
    9. transcription coactivator activity Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_19195. Adherens junctions interactions.
    SignaLinkiP14923.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Junction plakoglobin
    Alternative name(s):
    Catenin gamma
    Desmoplakin III
    Desmoplakin-3
    Gene namesi
    Name:JUP
    Synonyms:CTNNG, DP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6207. JUP.

    Subcellular locationi

    Cell junctionadherens junction 1 Publication. Cell junctiondesmosome 1 Publication. Cytoplasmcytoskeleton 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication
    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. catenin complex Source: BHF-UCL
    5. cell-cell adherens junction Source: UniProtKB
    6. cell-cell junction Source: UniProtKB
    7. cytoplasm Source: BHF-UCL
    8. cytoplasmic side of plasma membrane Source: BHF-UCL
    9. cytoskeleton Source: BHF-UCL
    10. cytosol Source: BHF-UCL
    11. desmosome Source: BHF-UCL
    12. extracellular vesicular exosome Source: UniProt
    13. fascia adherens Source: RefGenome
    14. gamma-catenin-TCF7L2 complex Source: BHF-UCL
    15. intercalated disc Source: BHF-UCL
    16. intermediate filament Source: Ensembl
    17. lateral plasma membrane Source: Ensembl
    18. nucleus Source: BHF-UCL
    19. plasma membrane Source: BHF-UCL
    20. protein-DNA complex Source: BHF-UCL
    21. Z disc Source: RefGenome
    22. zonula adherens Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191T → I in ARVD12. 1 Publication
    VAR_065698
    Natural varianti39 – 391S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. 1 Publication
    VAR_037803

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141T → A: Abolishes glycosylation. Does not affect binding to CDH1, DSC1 or DSG1. 1 Publication
    Mutagenesisi19 – 191T → A: Reduces glycosylation. 1 Publication
    Mutagenesisi21 – 211T → A: Does not affect glycosylation. 1 Publication
    Mutagenesisi24 – 241S → A: Does not affect glycosylation. 1 Publication
    Mutagenesisi28 – 281S → A: Does not affect glycosylation. 1 Publication
    Mutagenesisi32 – 321T → A: Does not affect glycosylation. 1 Publication

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation, Palmoplantar keratoderma

    Organism-specific databases

    MIMi601214. phenotype.
    611528. phenotype.
    Orphaneti293899. 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.
    PharmGKBiPA30009.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Junction plakoglobinPRO_0000064278Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Glycosylationi14 – 141O-linked (GlcNAc)1 Publication
    Modified residuei182 – 1821Phosphoserine2 Publications
    Modified residuei665 – 6651Phosphoserine3 Publications

    Post-translational modificationi

    May be phosphorylated by FER.3 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP14923.
    PaxDbiP14923.
    PRIDEiP14923.

    PTM databases

    PhosphoSiteiP14923.

    Miscellaneous databases

    PMAP-CutDBP14923.

    Expressioni

    Gene expression databases

    ArrayExpressiP14923.
    BgeeiP14923.
    CleanExiHS_JUP.
    GenevestigatoriP14923.

    Organism-specific databases

    HPAiCAB002139.
    HPA032047.

    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 By similarity. Interacts with PTPRJ. Interacts with DSG1. Interacts with DSC1 and DSC2. Interacts with PKP2.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APCP250542EBI-702484,EBI-727707
    CTNNA1P352212EBI-702484,EBI-701918
    PECAM1P162847EBI-702484,EBI-716404
    PSEN1P497684EBI-702484,EBI-297277
    TCF7L2Q9NQB013EBI-702484,EBI-924724
    WDYHV1Q96HA83EBI-702484,EBI-741158

    Protein-protein interaction databases

    BioGridi109931. 89 interactions.
    IntActiP14923. 37 interactions.
    MINTiMINT-105053.
    STRINGi9606.ENSP00000311113.

    Structurei

    Secondary structure

    1
    745
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi127 – 1315
    Helixi133 – 14210
    Helixi144 – 1518
    Helixi156 – 16914
    Helixi173 – 1808
    Helixi183 – 19311
    Helixi199 – 21214
    Helixi216 – 2249
    Helixi227 – 2337
    Helixi234 – 2363
    Helixi240 – 25617
    Helixi260 – 2667
    Helixi269 – 2724
    Helixi274 – 2785
    Helixi282 – 29615
    Helixi300 – 3089
    Helixi311 – 32111
    Helixi325 – 33814
    Helixi344 – 3507
    Helixi353 – 3586
    Helixi359 – 3624
    Helixi366 – 38015
    Helixi390 – 3978
    Turni398 – 4014
    Helixi405 – 41814
    Turni419 – 4213
    Helixi423 – 4297
    Turni430 – 4334
    Helixi434 – 44512
    Helixi449 – 46214
    Beta strandi464 – 4663
    Helixi469 – 4779
    Turni478 – 4803
    Helixi481 – 4877
    Helixi488 – 4903
    Helixi495 – 50814
    Helixi512 – 5143
    Helixi515 – 5206
    Helixi523 – 54321
    Helixi556 – 57015
    Helixi574 – 5829
    Helixi586 – 5927
    Helixi598 – 61114
    Helixi615 – 6239
    Turni624 – 6263
    Helixi627 – 6337
    Helixi639 – 65113
    Helixi662 – 6676

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IFQX-ray2.80A/B124-676[»]
    ProteinModelPortaliP14923.
    SMRiP14923. Positions 111-673.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14923.

    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 DSG1Add
    BLAST
    Regioni574 – 66188Interaction with DSC1Add
    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.2 Publications

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG297695.
    HOVERGENiHBG000919.
    InParanoidiP14923.
    KOiK10056.
    OMAiMNLIEQP.
    PhylomeDBiP14923.
    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.

    P14923-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVMNLMEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GIMEEDEACG    50
    RQYTLKKTTT YTQGVPPSQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL 100
    LLATQVEGQA TNLQRLAEPS QLLKSAIVHL INYQDDAELA TRALPELTKL 150
    LNDEDPVVVT KAAMIVNQLS KKEASRRALM GSPQLVAAVV RTMQNTSDLD 200
    TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE SVLFYAITTL 250
    HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ 300
    ESKLIILANG GPQALVQIMR 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 EPYGDDMDAT 700
    YRPMYSSDVP LDPLEMHMDM DGDYPIDTYS DGLRPPYPTA DHMLA 745
    Length:745
    Mass (Da):81,745
    Last modified:September 2, 2008 - v3
    Checksum:i3519A0973748BCF4
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911P → S in AAO85780. 1 PublicationCurated
    Sequence conflicti264 – 2707VRLADGL → CAGRRA in AAA64895. (PubMed:2726765)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191T → I in ARVD12. 1 Publication
    VAR_065698
    Natural varianti39 – 391S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. 1 Publication
    VAR_037803
    Natural varianti142 – 1421R → H.2 Publications
    Corresponds to variant rs41283425 [ dbSNP | Ensembl ].
    VAR_065699
    Natural varianti648 – 6481V → I.1 Publication
    Corresponds to variant rs143043662 [ dbSNP | Ensembl ].
    VAR_065700
    Natural varianti697 – 6971M → L.6 Publications
    Corresponds to variant rs1126821 [ dbSNP | Ensembl ].
    VAR_037804

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11407.1.
    PIRiA32905.
    RefSeqiNP_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.
    UniGeneiHs.514174.

    Genome annotation databases

    EnsembliENST00000310706; ENSP00000311113; ENSG00000173801.
    ENST00000393930; ENSP00000377507; ENSG00000173801.
    ENST00000393931; ENSP00000377508; ENSG00000173801.
    GeneIDi3728.
    KEGGihsa:3728.
    UCSCiuc002hxq.2. human.

    Polymorphism databases

    DMDMi205371866.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11407.1.
    PIRi A32905.
    RefSeqi NP_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.
    UniGenei Hs.514174.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IFQ X-ray 2.80 A/B 124-676 [» ]
    ProteinModelPortali P14923.
    SMRi P14923. Positions 111-673.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109931. 89 interactions.
    IntActi P14923. 37 interactions.
    MINTi MINT-105053.
    STRINGi 9606.ENSP00000311113.

    PTM databases

    PhosphoSitei P14923.

    Polymorphism databases

    DMDMi 205371866.

    Proteomic databases

    MaxQBi P14923.
    PaxDbi P14923.
    PRIDEi P14923.

    Protocols and materials databases

    DNASUi 3728.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310706 ; ENSP00000311113 ; ENSG00000173801 .
    ENST00000393930 ; ENSP00000377507 ; ENSG00000173801 .
    ENST00000393931 ; ENSP00000377508 ; ENSG00000173801 .
    GeneIDi 3728.
    KEGGi hsa:3728.
    UCSCi uc002hxq.2. human.

    Organism-specific databases

    CTDi 3728.
    GeneCardsi GC17M039776.
    GeneReviewsi JUP.
    HGNCi HGNC:6207. JUP.
    HPAi CAB002139.
    HPA032047.
    MIMi 173325. gene.
    601214. phenotype.
    611528. phenotype.
    neXtProti NX_P14923.
    Orphaneti 293899. 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.
    PharmGKBi PA30009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297695.
    HOVERGENi HBG000919.
    InParanoidi P14923.
    KOi K10056.
    OMAi MNLIEQP.
    PhylomeDBi P14923.
    TreeFami TF317997.

    Enzyme and pathway databases

    Reactomei REACT_19195. Adherens junctions interactions.
    SignaLinki P14923.

    Miscellaneous databases

    ChiTaRSi JUP. human.
    EvolutionaryTracei P14923.
    GeneWikii Plakoglobin.
    GenomeRNAii 3728.
    NextBioi 14595.
    PMAP-CutDB P14923.
    PROi P14923.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14923.
    Bgeei P14923.
    CleanExi HS_JUP.
    Genevestigatori P14923.

    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. "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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiPLAK_HUMAN
    AccessioniPrimary (citable) accession number: P14923
    Secondary accession number(s): Q15093
    , Q15151, Q7L3S5, Q86W21, Q9BWC4, Q9HCX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3