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Protein

Junction plakoglobin

Gene

JUP

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Molecular functioni

  1. alpha-catenin binding Source: BHF-UCL
  2. cadherin binding Source: BHF-UCL
  3. cell adhesion molecule binding Source: BHF-UCL
  4. protein homodimerization activity Source: BHF-UCL
  5. protein phosphatase binding Source: UniProtKB
  6. signal transducer activity Source: InterPro
  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 assembly Source: InterPro
  2. adherens junction organization Source: Reactome
  3. bundle of His cell-Purkinje myocyte adhesion involved in cell communication Source: BHF-UCL
  4. cell-cell junction organization Source: Reactome
  5. cell junction assembly Source: Reactome
  6. cell migration Source: BHF-UCL
  7. cellular response to indole-3-methanol Source: UniProtKB
  8. cytoskeletal anchoring at plasma membrane Source: BHF-UCL
  9. desmosome assembly Source: UniProtKB
  10. detection of mechanical stimulus Source: BHF-UCL
  11. endothelial cell-cell adhesion Source: BHF-UCL
  12. establishment of protein localization to plasma membrane Source: UniProtKB
  13. positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
  14. positive regulation of protein import into nucleus Source: BHF-UCL
  15. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  16. protein heterooligomerization Source: Ensembl
  17. regulation of cell fate specification Source: GO_Central
  18. regulation of cell proliferation Source: BHF-UCL
  19. regulation of heart rate by cardiac conduction Source: BHF-UCL
  20. regulation of ventricular cardiac muscle cell action potential Source: BHF-UCL
  21. single organismal cell-cell adhesion Source: UniProtKB
  22. skin development Source: Ensembl
  23. vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_263991. VEGFR2 mediated vascular permeability.
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 Componenti: 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: Ensembl
  2. apicolateral plasma membrane Source: Ensembl
  3. catenin complex Source: BHF-UCL
  4. cell-cell adherens junction Source: UniProtKB
  5. cell-cell junction Source: UniProtKB
  6. cytoplasm Source: BHF-UCL
  7. cytoplasmic side of plasma membrane Source: BHF-UCL
  8. cytoskeleton Source: BHF-UCL
  9. cytosol Source: BHF-UCL
  10. desmosome Source: BHF-UCL
  11. extracellular vesicular exosome Source: UniProtKB
  12. fascia adherens Source: Ensembl
  13. focal adhesion Source: UniProtKB
  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: UniProtKB
  20. protein-DNA complex Source: BHF-UCL
  21. Z disc Source: Ensembl
  22. zonula adherens Source: BHF-UCL
Complete GO annotation...

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)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 residuei99 – 991Phosphoserine1 Publication
Modified residuei125 – 1251Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine2 Publications
Modified residuei665 – 6651Phosphoserine2 Publications
Modified residuei730 – 7301Phosphoserine1 Publication

Post-translational modificationi

May be phosphorylated by FER.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP14923.
PaxDbiP14923.
PRIDEiP14923.

PTM databases

PhosphoSiteiP14923.

Miscellaneous databases

PMAP-CutDBP14923.

Expressioni

Gene expression databases

BgeeiP14923.
CleanExiHS_JUP.
ExpressionAtlasiP14923. baseline and differential.
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. 101 interactions.
IntActiP14923. 38 interactions.
MINTiMINT-105053.
STRINGi9606.ENSP00000311113.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IFQX-ray2.80A/B124-676[»]
ProteinModelPortaliP14923.
SMRiP14923. Positions 71-673.
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.
GeneTreeiENSGT00730000110821.
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

        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 1, 2008 - v3
Checksum:i3519A0973748BCF4
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911P → S in AAO85780 (Ref. 4) Curated
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:
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_006721873.1.
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:
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_006721873.1.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IFQX-ray2.80A/B124-676[»]
ProteinModelPortaliP14923.
SMRiP14923. Positions 71-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109931. 101 interactions.
IntActiP14923. 38 interactions.
MINTiMINT-105053.
STRINGi9606.ENSP00000311113.

PTM databases

PhosphoSiteiP14923.

Polymorphism databases

DMDMi205371866.

Proteomic databases

MaxQBiP14923.
PaxDbiP14923.
PRIDEiP14923.

Protocols and materials databases

DNASUi3728.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3728.
GeneCardsiGC17M039776.
GeneReviewsiJUP.
HGNCiHGNC:6207. JUP.
HPAiCAB002139.
HPA032047.
MIMi173325. gene.
601214. phenotype.
611528. phenotype.
neXtProtiNX_P14923.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOVERGENiHBG000919.
InParanoidiP14923.
KOiK10056.
OMAiMNLIEQP.
PhylomeDBiP14923.
TreeFamiTF317997.

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_263991. VEGFR2 mediated vascular permeability.
SignaLinkiP14923.

Miscellaneous databases

ChiTaRSiJUP. human.
EvolutionaryTraceiP14923.
GeneWikiiPlakoglobin.
GenomeRNAii3728.
NextBioi14595.
PMAP-CutDBP14923.
PROiP14923.
SOURCEiSearch...

Gene expression databases

BgeeiP14923.
CleanExiHS_JUP.
ExpressionAtlasiP14923. baseline and differential.
GenevestigatoriP14923.

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. "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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Zimbelmann R.
    Submitted (NOV-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(1999) [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 (JAN-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(2005) [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(2003) [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 (FEB-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(1999) [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(1993) [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(1996) [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(1996) [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(2001) [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(2002) [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(2002) [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(2005) [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(2009) [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(2010) [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(2011) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-125; SER-182 AND SER-730, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "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(2008) [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.
  25. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARVD12 SER-39 INS, CHARACTERIZATION OF VARIANT ARVD12 SER-39 INS.
  26. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARVD12 ILE-19, VARIANTS HIS-142; ILE-648 AND LEU-697.
  27. "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(2009) [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: March 31, 1990
Last sequence update: September 1, 2008
Last modified: March 31, 2015
This is version 161 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

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.