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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

  • alpha-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion 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 phosphatase binding Source: UniProtKB
  • signal transducer activity Source: InterPro
  • 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 assembly Source: InterPro
  • adherens junction organization Source: Reactome
  • bundle of His cell-Purkinje myocyte adhesion involved in cell communication Source: BHF-UCL
  • cell migration Source: BHF-UCL
  • cellular response to indole-3-methanol Source: UniProtKB
  • cytoskeletal anchoring at plasma membrane Source: BHF-UCL
  • desmosome assembly Source: UniProtKB
  • detection of mechanical stimulus Source: BHF-UCL
  • endothelial cell-cell adhesion Source: BHF-UCL
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • positive regulation of protein import into nucleus Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • protein heterooligomerization Source: Ensembl
  • 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
  • single organismal cell-cell adhesion Source: UniProtKB
  • skin development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173801-MONOMER.
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

HGNCiHGNC:6207. JUP.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • apicolateral plasma membrane Source: Ensembl
  • catenin complex Source: BHF-UCL
  • cell-cell adherens junction Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cytoplasm Source: BHF-UCL
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • cytoskeleton Source: BHF-UCL
  • cytosol Source: BHF-UCL
  • desmosome Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • fascia adherens Source: Ensembl
  • focal adhesion Source: UniProtKB
  • gamma-catenin-TCF7L2 complex Source: BHF-UCL
  • intercalated disc Source: BHF-UCL
  • intermediate filament Source: Ensembl
  • lateral plasma membrane Source: Ensembl
  • nucleus Source: BHF-UCL
  • plasma membrane Source: UniProtKB
  • protein-DNA complex Source: BHF-UCL
  • Z disc Source: Ensembl
  • 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06569819T → I in ARVD12. 1 PublicationCorresponds to variant rs570878629dbSNPEnsembl.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.
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)1 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.

PTM databases

iPTMnetiP14923.
PhosphoSitePlusiP14923.
SwissPalmiP14923.

Miscellaneous databases

PMAP-CutDBP14923.

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

WithEntry#Exp.IntActNotes
APCP250543EBI-702484,EBI-727707
CTNNA1P352212EBI-702484,EBI-701918
CTNNB1P352223EBI-702484,EBI-491549
CTNNBIP1Q9NSA33EBI-702484,EBI-747082
FHL2Q141923EBI-702484,EBI-701903
PECAM1P162847EBI-702484,EBI-716404
PSEN1P497684EBI-702484,EBI-297277
TCF7L2Q9NQB013EBI-702484,EBI-924724
WDYHV1Q96HA83EBI-702484,EBI-741158

GO - Molecular functioni

  • alpha-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion 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 phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109931. 140 interactors.
DIPiDIP-36235N.
IntActiP14923. 73 interactors.
MINTiMINT-105053.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IFQX-ray2.80A/B124-676[»]
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
Contains 12 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOVERGENiHBG000919.
InParanoidiP14923.
KOiK10056.
OMAiDPLDMHM.
OrthoDBiEOG091G03A5.
PhylomeDBiP14923.
TreeFamiTF317997.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
IPR030461. Plakoglobin/HMP-2.
[Graphical view]
PANTHERiPTHR23315:SF12. PTHR23315:SF12. 1 hit.
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 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 rs570878629dbSNPEnsembl.1
Natural variantiVAR_03780339S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. 1 Publication1
Natural variantiVAR_065699142R → H.2 PublicationsCorresponds to variant rs41283425dbSNPEnsembl.1
Natural variantiVAR_065700648V → I.1 PublicationCorresponds to variant rs143043662dbSNPEnsembl.1
Natural variantiVAR_037804697M → L.6 PublicationsCorresponds to variant rs1126821dbSNPEnsembl.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

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_006721873.2.
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi109931. 140 interactors.
DIPiDIP-36235N.
IntActiP14923. 73 interactors.
MINTiMINT-105053.
STRINGi9606.ENSP00000311113.

PTM databases

iPTMnetiP14923.
PhosphoSitePlusiP14923.
SwissPalmiP14923.

Polymorphism and mutation databases

BioMutaiJUP.
DMDMi205371866.

Proteomic databases

EPDiP14923.
MaxQBiP14923.
PaxDbiP14923.
PeptideAtlasiP14923.
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.3. human.

Organism-specific databases

CTDi3728.
DisGeNETi3728.
GeneCardsiJUP.
GeneReviewsiJUP.
HGNCiHGNC:6207. JUP.
HPAiCAB002139.
HPA032047.
MalaCardsiJUP.
MIMi173325. gene.
601214. phenotype.
611528. phenotype.
neXtProtiNX_P14923.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
GeneTreeiENSGT00730000110821.
HOVERGENiHBG000919.
InParanoidiP14923.
KOiK10056.
OMAiDPLDMHM.
OrthoDBiEOG091G03A5.
PhylomeDBiP14923.
TreeFamiTF317997.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173801-MONOMER.
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.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000173801.
CleanExiHS_JUP.
ExpressionAtlasiP14923. baseline and differential.
GenevisibleiP14923. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
IPR030461. Plakoglobin/HMP-2.
[Graphical view]
PANTHERiPTHR23315:SF12. PTHR23315:SF12. 1 hit.
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...

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: November 30, 2016
This is version 180 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

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 one 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.