P14923 (PLAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Junction plakoglobin

Alternative name(s):
Catenin gamma
Desmoplakin III
Desmoplakin-3

Gene names

Name:	JUP
Synonyms:	CTNNG, DP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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 DSC2. Ref.11 Ref.12 Ref.13 Ref.19
Subcellular location	Cell junction › adherens junction. Cell junction › desmosome. Cytoplasm › cytoskeleton. Membrane; Peripheral membrane protein. Note: Cytoplasmic in a soluble and membrane-associated form.
Involvement in disease	Defects in JUP are the cause of Naxos disease (NXD) [MIM:601214]. NXD is an autosomal recessive disorder combining diffuse non-epidermolytic palmoplantar keratoderma with arrhythmogenic right ventricular dysplasia/cardiomyopathy and woolly hair. Ref.9 Defects in JUP are the cause of familial arrhythmogenic right ventricular dysplasia type 12 (ARVD12) [MIM:611528]; also called arrhythmogenic right ventricular cardiomyopathy 12 (ARVC12). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall. Ref.9 Ref.20 Ref.21
Sequence similarities	Belongs to the beta-catenin family. Contains 9 ARM repeats.
Sequence caution	The sequence AAH00441.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Disease	Cardiomyopathy Disease mutation Palmoplantar keratoderma
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Uncategorized	specific RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Biological process	adherens junction organization Traceable author statement. Source: Reactome atrioventricular valve morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome cell junction assembly Traceable author statement. Source: Reactome cell migration Inferred from mutant phenotype. Source: BHF-UCL cell morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome cellular response to indole-3-methanol Inferred from direct assay. Source: UniProtKB cytoskeletal anchoring at plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome detection of mechanical stimulus Inferred from direct assay. Source: BHF-UCL ectoderm development Inferred from Biological aspect of Ancestor. Source: RefGenome endothelial cell-cell adhesion Inferred from sequence or structural similarity. Source: BHF-UCL gastrulation Inferred from Biological aspect of Ancestor. Source: RefGenome morphogenesis of embryonic epithelium Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of Wnt receptor signaling pathway involved in heart development Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of heart induction by canonical Wnt receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome nervous system development Inferred from Biological aspect of Ancestor. Source: RefGenome oocyte development Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of canonical Wnt receptor signaling pathway Inferred by curator. Source: BHF-UCL positive regulation of protein import into nucleus Inferred from direct assay. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: BHF-UCL skin development Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from Biological aspect of Ancestor. Source: RefGenome Z disc Inferred from Biological aspect of Ancestor. Source: RefGenome actin cytoskeleton Inferred from Biological aspect of Ancestor. Source: RefGenome basolateral plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome catenin complex Inferred from direct assay. Source: BHF-UCL desmosome Inferred from direct assay. Source: BHF-UCL fascia adherens Inferred from Biological aspect of Ancestor. Source: RefGenome gamma-catenin-TCF7L2 complex Inferred from direct assay. Source: BHF-UCL internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL nucleus Inferred from mutant phenotype. Source: BHF-UCL protein-DNA complex Inferred from direct assay. Source: BHF-UCL zonula adherens Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	RPTP-like protein binding Inferred from Biological aspect of Ancestor. Source: RefGenome alpha-catenin binding Inferred from physical interaction. Source: BHF-UCL cadherin binding Inferred from physical interaction. Source: BHF-UCL protein homodimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein phosphatase binding Inferred from physical interaction. Source: UniProtKB structural constituent of cell wall Inferred by curator. Source: BHF-UCL transcription coactivator activity Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PECAM1	P16284	7	EBI-702484,EBI-716404
PSEN1	P49768	4	EBI-702484,EBI-297277
TCF7L2	Q9NQB0	13	EBI-702484,EBI-924724
WDYHV1	Q96HA8	3	EBI-702484,EBI-741158

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 745

745

Junction plakoglobin

PRO_0000064278

Regions

Repeat

132 – 171

40

ARM 1

Repeat

216 – 255

40

ARM 2

Repeat

258 – 297

40

ARM 3

Repeat

342 – 381

40

ARM 4

Repeat

383 – 420

38

ARM 5

Repeat

423 – 464

42

ARM 6

Repeat

470 – 510

41

ARM 7

Repeat

512 – 551

40

ARM 8

Repeat

574 – 613

40

ARM 9

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8

Modified residue

20

1

Phosphotyrosine Ref.14

Modified residue

182

1

Phosphoserine Ref.15

Modified residue

660

1

Phosphotyrosine Ref.16 Ref.17

Modified residue

665

1

Phosphoserine Ref.15

Natural variations

Natural variant

19

1

T → I in ARVD12. Ref.21

VAR_065698

Natural variant

39

1

S → SS in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions. Ref.20

VAR_037803

Natural variant

142

1

R → H. Ref.21 Ref.22

VAR_065699

Natural variant

648

1

V → I. Ref.21

VAR_065700

Natural variant

697

1

M → L. Ref.4 Ref.6 Ref.7 Ref.9 Ref.21 Ref.22
Corresponds to variant rs1126821 [ dbSNP | Ensembl ].

VAR_037804

Experimental info

Sequence conflict

91

1

P → S in AAO85780. Ref.4

Sequence conflict

264 – 270

7

VRLADGL → CAGRRA in AAA64895. Ref.1

Secondary structure

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745

Helix Strand Turn

Details...

Helix

127 – 131

5

Helix

133 – 142

10

Helix

144 – 151

8

Helix

156 – 169

14

Helix

173 – 179

7

Helix

183 – 193

11

Helix

199 – 212

14

Helix

220 – 224

5

Helix

229 – 233

5

Helix

234 – 236

3

Helix

240 – 256

17

Helix

261 – 266

6

Turn

271 – 273

3

Helix

274 – 278

5

Helix

282 – 296

15

Helix

300 – 308

9

Helix

313 – 321

9

Helix

325 – 338

14

Helix

344 – 350

7

Helix

360 – 362

3

Helix

366 – 380

15

Helix

390 – 397

8

Turn

398 – 401

4

Helix

405 – 411

7

Helix

415 – 418

4

Turn

419 – 421

3

Helix

423 – 429

7

Helix

436 – 444

9

Helix

449 – 462

14

Beta strand

464 – 466

3

Helix

469 – 477

9

Helix

483 – 487

5

Helix

488 – 490

3

Helix

495 – 501

7

Helix

505 – 508

4

Helix

512 – 514

3

Helix

515 – 520

6

Helix

523 – 543

21

Helix

556 – 560

5

Helix

567 – 570

4

Helix

574 – 582

9

Helix

586 – 592

7

Helix

598 – 604

7

Helix

608 – 611

4

Helix

615 – 623

9

Helix

627 – 633

7

Helix

642 – 651

10

Helix

662 – 667

6

Sequences

	Sequence		Length	Mass (Da)
	P14923 [UniParc]. Last modified September 2, 2008. Version 3. Checksum: 3519A0973748BCF4	FASTA	745	81,745
	10 20 30 40 50 60 MEVMNLMEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GIMEEDEACG RQYTLKKTTT 70 80 90 100 110 120 YTQGVPPSQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQA TNLQRLAEPS 130 140 150 160 170 180 QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM 190 200 210 220 230 240 GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE 250 260 270 280 290 300 SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ 310 320 330 340 350 360 ESKLIILANG GPQALVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH 370 380 390 400 410 420 LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC 430 440 450 460 470 480 NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY 490 500 510 520 530 540 GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR 550 560 570 580 590 600 HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI 610 620 630 640 650 660 QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY 670 680 690 700 710 720 RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYGDDMDAT YRPMYSSDVP LDPLEMHMDM 730 740 DGDYPIDTYS DGLRPPYPTA DHMLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1989) [PubMed: 2726765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Zimbelmann R. Submitted (DEC-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(2000) [PubMed: 11016852] [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 (FEB-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(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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(2004) [PubMed: 15489334] [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 (MAR-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, 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(2000) [PubMed: 10902626] [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(1994) [PubMed: 7982500] [Abstract] Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[11]	"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(1997) [PubMed: 9139698] [Abstract] Cited for: INTERACTION WITH MUC1.
[12]	"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(1997) [PubMed: 9152027] [Abstract] Cited for: INTERACTION WITH CTNNA1.
[13]	"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(2002) [PubMed: 12370829] [Abstract] Cited for: INTERACTION WITH PTPRJ.
[14]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[15]	"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(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-660, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[17]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-660, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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(2011) [PubMed: 21062920] [Abstract] Cited for: INTERACTION WITH DSC2.
[20]	"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(2007) [PubMed: 17924338] [Abstract] Cited for: VARIANT ARVD12 SER-39 INS, CHARACTERIZATION OF VARIANT ARVD12 SER-39 INS.
[21]	"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(2009) [PubMed: 20031617] [Abstract] Cited for: VARIANT ARVD12 ILE-19, VARIANTS HIS-142; ILE-648 AND LEU-697.
[22]	"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(2010) [PubMed: 19863551] [Abstract] Cited for: VARIANTS HIS-142 AND LEU-697.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00554711.

PIR

A32905.

RefSeq

NP_002221.1. NM_002230.2.
NP_068831.1. NM_021991.2.

UniGene

Hs.514174.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IFQ	X-ray	2.80	A/B	124-676	[»]

ProteinModelPortal

P14923.

SMR

P14923. Positions 111-673.

ModBase

Search...

Protein-protein interaction databases

IntAct

P14923. 21 interactions.

MINT

MINT-105053.

STRING

P14923.

PTM databases

PhosphoSite

P14923.

Polymorphism databases

DMDM

205371866.

Proteomic databases

PRIDE

P14923.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310706; ENSP00000311113; ENSG00000173801.
ENST00000393930; ENSP00000377507; ENSG00000173801.
ENST00000393931; ENSP00000377508; ENSG00000173801.

GeneID

3728.

KEGG

hsa:3728.

Organism-specific databases

CTD

3728.

GeneCards

GC17M039776.

H-InvDB

HIX0013818.

HGNC

HGNC:6207. JUP.

HPA

CAB002139.

MIM

173325. gene.
601214. phenotype.
611528. phenotype.

neXtProt

NX_P14923.

Orphanet

217656. Familial isolated arrhythmogenic right ventricular dysplasia.
34217. Naxos disease.

PharmGKB

PA30009.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06428.

HOVERGEN

HBG000919.

InParanoid

P14923.

OMA

DDMDATY.

OrthoDB

EOG4FR0R3.

PhylomeDB

P14923.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

P14923.

Bgee

P14923.

CleanEx

HS_JUP.

Genevestigator

P14923.

GermOnline

ENSG00000173801. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

KO

K10056.

Pfam

PF00514. Arm. 4 hits.
[Graphical view]

PRINTS

PR01869. BCATNINFAMLY.

SMART

SM00185. ARM. 12 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50176. ARM_REPEAT. 9 hits.
[Graphical view]

ProtoNet

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Other

PMAP-CutDB

P14923.

SOURCE

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Entry information

Entry name

PLAK_HUMAN

Accession

Primary (citable) accession number: P14923
Secondary accession number(s): Q15093 , Q15151, Q7L3S5, Q86W21, Q9BWC4, Q9HCX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	September 2, 2008
Last modified:	January 25, 2012
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.