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Q8WNW3

- PLAK_PIG

UniProt

Q8WNW3 - PLAK_PIG

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Protein

Junction plakoglobin

Gene
Jup
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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.

GO - Molecular functioni

  1. transcription coactivator activity Source: Ensembl

GO - Biological processi

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

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_221864. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Junction plakoglobin
Gene namesi
Name:Jup
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 12

Subcellular locationi

Cell junctionadherens junction By similarity. Cell junctiondesmosome By similarity. Cytoplasmcytoskeleton By similarity. Membrane; Peripheral membrane protein By similarity
Note: Cytoplasmic in a soluble and membrane-associated form By similarity.

GO - Cellular componenti

  1. catenin complex Source: Ensembl
  2. cell-cell adherens junction Source: Ensembl
  3. cytosol Source: Ensembl
  4. desmosome Source: UniProtKB-SubCell
  5. gamma-catenin-TCF7L2 complex Source: Ensembl
  6. intercalated disc Source: Ensembl
  7. intermediate filament Source: Ensembl
  8. protein-DNA complex Source: Ensembl
  9. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Junction plakoglobinPRO_0000064280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Glycosylationi14 – 141O-linked (GlcNAc) By similarity
Modified residuei182 – 1821Phosphoserine By similarity
Modified residuei665 – 6651Phosphoserine By similarity

Post-translational modificationi

May be phosphorylated by FER By similarity.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ8WNW3.
PRIDEiQ8WNW3.

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.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000018469.

Structurei

3D structure databases

ProteinModelPortaliQ8WNW3.
SMRiQ8WNW3. Positions 118-672.

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 DSG1 By similarityAdd
BLAST
Regioni574 – 66188Interaction with DSC1 By 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.

Sequence similaritiesi

Belongs to the beta-catenin family.
Contains 12 ARM repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
HOGENOMiHOG000230958.
HOVERGENiHBG000919.
KOiK10056.
OMAiMNLIEQP.
OrthoDBiEOG7X9G6B.
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.

Q8WNW3-1 [UniParc]FASTAAdd to Basket

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MEVMNLIEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GLMEEDEACG    50
RQYTLKKTTT YTQAVPQSQG DLEYQMSTTA RAKRVREAMC PGVTGEDSSL 100
LLATQVEGQT 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 ASVIPRLVQL LVKAHQDAQR HVAAGTQQPY 550
TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI 600
QRVAAGVLCE LAQDKEAADA IDAEGASSPL MELLHSRNEG TATYAAAVLF 650
RISEDKNPDY RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT 700
YRPMYSSDVP LDPLEMHMDM DGDYPMDTYS DGLRPPYPAA DHMLA 745
Length:745
Mass (Da):81,850
Last modified:March 1, 2002 - v1
Checksum:i53F19D385AB19F60
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB046172 mRNA. Translation: BAB82985.1.
RefSeqiNP_999488.1. NM_214323.1.
XP_005668876.1. XM_005668819.1.
XP_005668877.1. XM_005668820.1.
XP_005668878.1. XM_005668821.1.
XP_005668879.1. XM_005668822.1.
UniGeneiSsc.42011.

Genome annotation databases

EnsembliENSSSCT00000018974; ENSSSCP00000018469; ENSSSCG00000017428.
GeneIDi397592.
KEGGissc:397592.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB046172 mRNA. Translation: BAB82985.1 .
RefSeqi NP_999488.1. NM_214323.1.
XP_005668876.1. XM_005668819.1.
XP_005668877.1. XM_005668820.1.
XP_005668878.1. XM_005668821.1.
XP_005668879.1. XM_005668822.1.
UniGenei Ssc.42011.

3D structure databases

ProteinModelPortali Q8WNW3.
SMRi Q8WNW3. Positions 118-672.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000018469.

Proteomic databases

PaxDbi Q8WNW3.
PRIDEi Q8WNW3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000018974 ; ENSSSCP00000018469 ; ENSSSCG00000017428 .
GeneIDi 397592.
KEGGi ssc:397592.

Organism-specific databases

CTDi 3728.

Phylogenomic databases

eggNOGi NOG297695.
GeneTreei ENSGT00730000110821.
HOGENOMi HOG000230958.
HOVERGENi HBG000919.
KOi K10056.
OMAi MNLIEQP.
OrthoDBi EOG7X9G6B.
TreeFami TF317997.

Enzyme and pathway databases

Reactomei REACT_221864. Adherens junctions interactions.

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. "Transcriptional upregulation of p27Kip1 during contact-induced growth arrest in endothelial cells."
    Hirano M., Hirano K., Nishimura J., Kanaide H.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Aortic endothelium.

Entry informationi

Entry nameiPLAK_PIG
AccessioniPrimary (citable) accession number: Q8WNW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 84 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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