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Protein

Junction plakoglobin

Gene

Jup

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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: MGI
  3. protein phosphatase binding Source: MGI
  4. structural molecule activity Source: Ensembl
  5. transcription coactivator activity Source: MGI

GO - Biological processi

  1. bundle of His cell to Purkinje myocyte communication Source: MGI
  2. cell adhesion Source: MGI
  3. cell migration Source: MGI
  4. cellular response to indole-3-methanol Source: MGI
  5. desmosome assembly Source: MGI
  6. detection of mechanical stimulus Source: MGI
  7. establishment of protein localization to plasma membrane Source: MGI
  8. positive regulation of protein import into nucleus Source: MGI
  9. positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  10. protein heterooligomerization Source: Ensembl
  11. regulation of cell fate specification Source: GO_Central
  12. regulation of cell proliferation Source: MGI
  13. regulation of heart rate by cardiac conduction Source: MGI
  14. single organismal cell-cell adhesion Source: MGI
  15. skin development Source: MGI
  16. ventricular cardiac muscle cell action potential Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_230395. Adherens junctions interactions.
REACT_261840. VEGFR2 mediated vascular permeability.

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: Ensembl
  2. apicolateral plasma membrane Source: Ensembl
  3. catenin complex Source: MGI
  4. cell-cell adherens junction Source: MGI
  5. cell-cell junction Source: MGI
  6. cytoplasm Source: MGI
  7. cytoplasmic side of plasma membrane Source: Ensembl
  8. cytosol Source: MGI
  9. desmosome Source: MGI
  10. extracellular vesicular exosome Source: MGI
  11. fascia adherens Source: Ensembl
  12. focal adhesion Source: MGI
  13. gamma-catenin-TCF7L2 complex Source: MGI
  14. intercalated disc Source: MGI
  15. intermediate filament Source: BHF-UCL
  16. lateral plasma membrane Source: Ensembl
  17. membrane Source: MGI
  18. nucleus Source: MGI
  19. plasma membrane Source: MGI
  20. protein-DNA complex Source: MGI
  21. Z disc Source: MGI
Complete GO annotation...

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

        10         20         30         40         50
MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG
60 70 80 90 100
RQYTLKKTTT YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL
110 120 130 140 150
LLATQVEGQT TNLQRLAEPS QLLKSAIVHL INYQDDAELA TRALPELTKL
160 170 180 190 200
LNDEDPVVVT KAAMIVNQLS KKEASRRALM GSPQLVAAVV RTMQNTSDLD
210 220 230 240 250
TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE SVLFYAITTL
260 270 280 290 300
HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ
310 320 330 340 350
ESKLIILANG GPQGLVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE
360 370 380 390 400
AGGMQALGKH LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL
410 420 430 440 450
SVDDVNVLTC ATGTLSNLTC NNSKNKTLVT QNSGVEALIH AILRAGDKDD
460 470 480 490 500
ITEPAVCALR HLTSRHPEAE MAQNSVRLNY GIPAIVKLLN QPNQWPLVKA
510 520 530 540 550
TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR HVAAGTQQPY
560 570 580 590 600
TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI
610 620 630 640 650
QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF
660 670 680 690 700
RISEDKNPDY RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT
710 720 730 740
YRPMYSSDVP LDPLDMHMDL DGDYPMDTYS DGLRPPYPTA DHMLA
Length:745
Mass (Da):81,801
Last modified:December 6, 2005 - v3
Checksum:i9609619D94052FC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ02257.

Proteomic databases

MaxQBiQ02257.
PaxDbiQ02257.
PRIDEiQ02257.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3728.
MGIiMGI:96650. Jup.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_230395. Adherens junctions interactions.
REACT_261840. VEGFR2 mediated vascular permeability.

Miscellaneous databases

ChiTaRSiJup. mouse.
NextBioi289775.
PROiQ02257.
SOURCEiSearch...

Gene expression databases

BgeeiQ02257.
CleanExiMM_JUP.
GenevestigatoriQ02257.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.