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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 DSG1. Interacts with DSC1 and DSC2. Ref.10 Ref.11 Ref.12 Ref.13 Ref.18 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.
Domain	the whole ARM repeats region mediate binding to CDH1/E-cadherin.
Post-translational modification	May be phosphorylated by FER. Ref.14
Involvement in disease	Naxos disease (NXD) [MIM:601214]: An 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Familial arrhythmogenic right ventricular dysplasia 12 (ARVD12) [MIM:611528]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.20 Ref.21
Sequence similarities	Belongs to the beta-catenin family. Contains 12 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)
Biological_process	adherens junction organization Traceable author statement. Source: Reactome atrioventricular valve morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome bundle of His cell to Purkinje myocyte communication Inferred from mutant phenotype Ref.20. Source: BHF-UCL cell migration Inferred from mutant phenotype PubMed 18937352. Source: BHF-UCL cell morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome cellular response to indole-3-methanol Inferred from direct assay PubMed 10868478. Source: UniProtKB cytoskeletal anchoring at plasma membrane Non-traceable author statement PubMed 22889254. Source: BHF-UCL desmosome assembly Inferred from direct assay PubMed 22889254. Source: BHF-UCL detection of mechanical stimulus Inferred from direct assay PubMed 18937352. 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 PubMed 14661054. Source: BHF-UCL positive regulation of protein import into nucleus Inferred from direct assay PubMed 10825188PubMed 14661054. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 14661054. Source: BHF-UCL protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from direct assay Ref.20. Source: BHF-UCL regulation of cell proliferation Inferred from direct assay Ref.20. Source: BHF-UCL regulation of heart rate by cardiac conduction Inferred from mutant phenotype Ref.20. Source: BHF-UCL regulation of ventricular cardiac muscle cell action potential Inferred from mutant phenotype Ref.20. Source: BHF-UCL skin development Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	Z disc Inferred from Biological aspect of Ancestor. Source: RefGenome actin cytoskeleton Inferred from Biological aspect of Ancestor. Source: RefGenome apicolateral plasma membrane Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome catenin complex Inferred from direct assay PubMed 7650039. Source: BHF-UCL cytosol Inferred from sequence or structural similarity. Source: BHF-UCL desmosome Inferred from direct assay PubMed 1639850. Source: BHF-UCL fascia adherens Inferred from Biological aspect of Ancestor. Source: RefGenome gamma-catenin-TCF7L2 complex Inferred from direct assay PubMed 14661054. Source: BHF-UCL intermediate filament Inferred from electronic annotation. Source: Compara internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL lateral plasma membrane Inferred from electronic annotation. Source: Compara protein-DNA complex Inferred from direct assay PubMed 14661054. Source: BHF-UCL zonula adherens Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	protein homodimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome structural constituent of cell wall Inferred by curator PubMed 7650039. Source: BHF-UCL transcription coactivator activity Inferred from direct assay PubMed 14661054. 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

172 – 215

44

ARM 2

Repeat

216 – 255

40

ARM 3

Repeat

258 – 297

40

ARM 4

Repeat

298 – 341

44

ARM 5

Repeat

342 – 381

40

ARM 6

Repeat

383 – 420

38

ARM 7

Repeat

423 – 464

42

ARM 8

Repeat

470 – 510

41

ARM 9

Repeat

512 – 551

40

ARM 10

Repeat

574 – 613

40

ARM 11

Repeat

615 – 661

47

ARM 12

Region

132 – 297

166

Interaction with DSC1 and DSG1

Region

574 – 661

88

Interaction with DSC1

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8

Modified residue

182

1

Phosphoserine Ref.15

Modified residue

665

1

Phosphoserine Ref.15 Ref.16

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 – 180

8

Helix

183 – 193

11

Helix

199 – 212

14

Helix

216 – 224

9

Helix

227 – 233

7

Helix

234 – 236

3

Helix

240 – 256

17

Helix

260 – 266

7

Helix

269 – 272

4

Helix

274 – 278

5

Helix

282 – 296

15

Helix

300 – 308

9

Helix

311 – 321

11

Helix

325 – 338

14

Helix

344 – 350

7

Helix

353 – 358

6

Helix

359 – 362

4

Helix

366 – 380

15

Helix

390 – 397

8

Turn

398 – 401

4

Helix

405 – 418

14

Turn

419 – 421

3

Helix

423 – 429

7

Turn

430 – 433

4

Helix

434 – 445

12

Helix

449 – 462

14

Beta strand

464 – 466

3

Helix

469 – 477

9

Turn

478 – 480

3

Helix

481 – 487

7

Helix

488 – 490

3

Helix

495 – 508

14

Helix

512 – 514

3

Helix

515 – 520

6

Helix

523 – 543

21

Helix

556 – 570

15

Helix

574 – 582

9

Helix

586 – 592

7

Helix

598 – 611

14

Helix

615 – 623

9

Turn

624 – 626

3

Helix

627 – 633

7

Helix

639 – 651

13

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] [Europe PMC] [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] [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 (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] [Europe PMC] [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] [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 (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] [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(1994) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPRJ.
[14]	"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(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY FER.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DSC2.
[19]	"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(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 124-676 IN COMPLEX WITH PHOSPHORYLATED MOUSE E-CADHERIN, ARM REPEATS, INTERACTION WITH DSC1 AND DSG1.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

ModBase

Search...

Protein-protein interaction databases

IntAct

P14923. 24 interactions.

MINT

MINT-105053.

STRING

9606.ENSP00000311113.

PTM databases

PhosphoSite

P14923.

Polymorphism databases

DMDM

205371866.

Proteomic databases

PaxDb

P14923.

PRIDE

P14923.

Protocols and materials databases

DNASU

3728.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310706; ENSP00000311113; ENSG00000173801.
ENST00000393930; ENSP00000377507; ENSG00000173801.
ENST00000393931; ENSP00000377508; ENSG00000173801.
ENST00000562805; ENSP00000456867; ENSG00000261577.
ENST00000565220; ENSP00000454630; ENSG00000261577.
ENST00000565780; ENSP00000457186; ENSG00000261577.

GeneID

3728.

KEGG

hsa:3728.

UCSC

uc002hxq.2. human.

Organism-specific databases

CTD

3728.

GeneCards

GC17M039776.

HGNC

HGNC:6207. JUP.

HPA

CAB002139.

MIM

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

neXtProt

NX_P14923.

Orphanet

293899. 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.
34217. Naxos disease.

PharmGKB

PA30009.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG297695.

HOVERGEN

HBG000919.

InParanoid

P14923.

KO

K10056.

OMA

MNLIEQP.

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

Gene3D

1.25.10.10. 1 hit.

InterPro

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

Pfam

PF00514. Arm. 3 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

Search...

Other

ChiTaRS

JUP. human.

EvolutionaryTrace

P14923.

GenomeRNAi

3728.

NextBio

14595.

PMAP-CutDB

P14923.

SOURCE

Search...

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:	May 1, 2013
This is version 139 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.