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Protein

Junction plakoglobin

Gene

JUP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

GO - Molecular functioni

  • alpha-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cell adhesion molecule binding Source: BHF-UCL
  • cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase binding Source: Ensembl
  • protein phosphatase binding Source: UniProtKB
  • structural constituent of cell wall Source: BHF-UCL
  • structural molecule activity Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL

GO - Biological processi

  • adherens junction organization Source: Reactome
  • bundle of His cell-Purkinje myocyte adhesion involved in cell communication Source: BHF-UCL
  • cell-cell adhesion Source: BHF-UCL
  • cell migration Source: BHF-UCL
  • cellular response to indole-3-methanol Source: UniProtKB
  • cornification Source: Reactome
  • cytoskeletal anchoring at plasma membrane Source: BHF-UCL
  • desmosome assembly Source: BHF-UCL
  • detection of mechanical stimulus Source: BHF-UCL
  • endothelial cell-cell adhesion Source: BHF-UCL
  • keratinization Source: Reactome
  • negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • neutrophil degranulation Source: Reactome
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • positive regulation of cell-matrix adhesion Source: BHF-UCL
  • positive regulation of DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of protein import into nucleus Source: BHF-UCL
  • protein heterooligomerization Source: Ensembl
  • protein localization to plasma membrane Source: UniProtKB
  • regulation of cell proliferation Source: BHF-UCL
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of ventricular cardiac muscle cell action potential Source: BHF-UCL

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-418990 Adherens junctions interactions
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-6798695 Neutrophil degranulation
R-HSA-6805567 Keratinization
R-HSA-6809371 Formation of the cornified envelope
SignaLinkiP14923
SIGNORiP14923

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000173801.16
HGNCiHGNC:6207 JUP
MIMi173325 gene
neXtProtiNX_P14923

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Naxos disease (NXD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:601214
Arrhythmogenic right ventricular dysplasia, familial, 12 (ARVD12)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:611528
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06569819T → I in ARVD12. 1 PublicationCorresponds to variant dbSNP:rs570878629EnsemblClinVar.1
Natural variantiVAR_03780339S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14T → A: Abolishes glycosylation. Does not affect binding to CDH1, DSC1 or DSG1. 1 Publication1
Mutagenesisi19T → A: Reduces glycosylation. 1 Publication1
Mutagenesisi21T → A: Does not affect glycosylation. 1 Publication1
Mutagenesisi24S → A: Does not affect glycosylation. 1 Publication1
Mutagenesisi28S → A: Does not affect glycosylation. 1 Publication1
Mutagenesisi32T → A: Does not affect glycosylation. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Palmoplantar keratoderma

Organism-specific databases

DisGeNETi3728
GeneReviewsiJUP
MalaCardsiJUP
MIMi601214 phenotype
611528 phenotype
OpenTargetsiENSG00000173801
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

Polymorphism and mutation databases

BioMutaiJUP
DMDMi205371866

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000642781 – 745Junction plakoglobinAdd BLAST745

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Glycosylationi14O-linked (GlcNAc) threonine1 Publication1
Modified residuei99PhosphoserineCombined sources1
Modified residuei125PhosphoserineCombined sources1
Modified residuei182PhosphoserineCombined sources1
Modified residuei665PhosphoserineCombined sources1
Modified residuei730PhosphoserineCombined sources1

Post-translational modificationi

May be phosphorylated by FER.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP14923
MaxQBiP14923
PaxDbiP14923
PeptideAtlasiP14923
PRIDEiP14923
ProteomicsDBi53098

PTM databases

iPTMnetiP14923
PhosphoSitePlusiP14923
SwissPalmiP14923

Miscellaneous databases

PMAP-CutDBiP14923

Expressioni

Gene expression databases

BgeeiENSG00000173801
CleanExiHS_JUP
ExpressionAtlasiP14923 baseline and differential
GenevisibleiP14923 HS

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

Show more details

GO - Molecular functioni

  • alpha-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cell adhesion molecule binding Source: BHF-UCL
  • cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase binding Source: Ensembl
  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109931, 157 interactors
CORUMiP14923
DIPiDIP-36235N
IntActiP14923, 81 interactors
MINTiP14923
STRINGi9606.ENSP00000311113

Structurei

Secondary structure

1745
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi127 – 131Combined sources5
Helixi133 – 142Combined sources10
Helixi144 – 151Combined sources8
Helixi156 – 169Combined sources14
Helixi173 – 180Combined sources8
Helixi183 – 193Combined sources11
Helixi199 – 212Combined sources14
Helixi216 – 224Combined sources9
Helixi227 – 233Combined sources7
Helixi234 – 236Combined sources3
Helixi240 – 256Combined sources17
Helixi260 – 266Combined sources7
Helixi269 – 272Combined sources4
Helixi274 – 278Combined sources5
Helixi282 – 296Combined sources15
Helixi300 – 308Combined sources9
Helixi311 – 321Combined sources11
Helixi325 – 338Combined sources14
Helixi344 – 350Combined sources7
Helixi353 – 358Combined sources6
Helixi359 – 362Combined sources4
Helixi366 – 380Combined sources15
Helixi390 – 397Combined sources8
Turni398 – 401Combined sources4
Helixi405 – 418Combined sources14
Turni419 – 421Combined sources3
Helixi423 – 429Combined sources7
Turni430 – 433Combined sources4
Helixi434 – 445Combined sources12
Helixi449 – 462Combined sources14
Beta strandi464 – 466Combined sources3
Helixi469 – 477Combined sources9
Turni478 – 480Combined sources3
Helixi481 – 487Combined sources7
Helixi488 – 490Combined sources3
Helixi495 – 508Combined sources14
Helixi512 – 514Combined sources3
Helixi515 – 520Combined sources6
Helixi523 – 543Combined sources21
Helixi556 – 570Combined sources15
Helixi574 – 582Combined sources9
Helixi586 – 592Combined sources7
Helixi598 – 611Combined sources14
Helixi615 – 623Combined sources9
Turni624 – 626Combined sources3
Helixi627 – 633Combined sources7
Helixi639 – 651Combined sources13
Helixi662 – 667Combined sources6

3D structure databases

ProteinModelPortaliP14923
SMRiP14923
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14923

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati132 – 171ARM 1Add BLAST40
Repeati172 – 215ARM 2Add BLAST44
Repeati216 – 255ARM 3Add BLAST40
Repeati258 – 297ARM 4Add BLAST40
Repeati298 – 341ARM 5Add BLAST44
Repeati342 – 381ARM 6Add BLAST40
Repeati383 – 420ARM 7Add BLAST38
Repeati423 – 464ARM 8Add BLAST42
Repeati470 – 510ARM 9Add BLAST41
Repeati512 – 551ARM 10Add BLAST40
Repeati574 – 613ARM 11Add BLAST40
Repeati615 – 661ARM 12Add BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 297Interaction with DSC1 and DSG1Add BLAST166
Regioni574 – 661Interaction with DSC1Add BLAST88

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4203 Eukaryota
COG0035 LUCA
GeneTreeiENSGT00730000110821
HOVERGENiHBG000919
InParanoidiP14923
KOiK10056
OMAiMNLIEQP
OrthoDBiEOG091G03A5
PhylomeDBiP14923
TreeFamiTF317997

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR013284 Beta-catenin
IPR030461 Plakoglobin/HMP-2
PANTHERiPTHR23315:SF12 PTHR23315:SF12, 1 hit
PfamiView protein in Pfam
PF00514 Arm, 3 hits
PRINTSiPR01869 BCATNINFAMLY
SMARTiView protein in SMART
SM00185 ARM, 12 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 9 hits

Sequencei

Sequence statusi: Complete.

P14923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVMNLMEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GIMEEDEACG
60 70 80 90 100
RQYTLKKTTT YTQGVPPSQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL
110 120 130 140 150
LLATQVEGQA 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 GPQALVQIMR 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 EPYGDDMDAT
710 720 730 740
YRPMYSSDVP LDPLEMHMDM DGDYPIDTYS DGLRPPYPTA DHMLA
Length:745
Mass (Da):81,745
Last modified:September 2, 2008 - v3
Checksum:i3519A0973748BCF4
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91P → S in AAO85780 (Ref. 4) Curated1
Sequence conflicti264 – 270VRLADGL → CAGRRA in AAA64895 (PubMed:2726765).Curated7

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06569819T → I in ARVD12. 1 PublicationCorresponds to variant dbSNP:rs570878629EnsemblClinVar.1
Natural variantiVAR_03780339S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. 1 Publication1
Natural variantiVAR_065699142R → H2 PublicationsCorresponds to variant dbSNP:rs41283425EnsemblClinVar.1
Natural variantiVAR_065700648V → I1 PublicationCorresponds to variant dbSNP:rs143043662EnsemblClinVar.1
Natural variantiVAR_037804697M → L6 PublicationsCorresponds to variant dbSNP:rs1126821EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006721873.2
XP_006721937.1, XM_006721874.2
XP_006721938.1, XM_006721875.1
XP_006721941.1, XM_006721878.1
XP_011523055.1, XM_011524753.2
XP_011523057.1, XM_011524755.1
XP_011523058.1, XM_011524756.1
XP_011523059.1, XM_011524757.2
XP_011523060.1, XM_011524758.1
XP_016880079.1, XM_017024590.1
UniGeneiHs.514174

Genome annotation databases

EnsembliENST00000310706; ENSP00000311113; ENSG00000173801
ENST00000393930; ENSP00000377507; ENSG00000173801
ENST00000393931; ENSP00000377508; ENSG00000173801
GeneIDi3728
KEGGihsa:3728
UCSCiuc002hxq.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPLAK_HUMAN
AccessioniPrimary (citable) accession number: P14923
Secondary accession number(s): Q15093
, Q15151, Q7L3S5, Q86W21, Q9BWC4, Q9HCX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 2, 2008
Last modified: July 18, 2018
This is version 194 of the entry and version 3 of the sequence. See 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

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