Q99959 (PKP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plakophilin-2

Gene names

Name:

PKP2

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	881 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in junctional plaques.
Subunit structure	Interacts with DSC2. Ref.11
Subcellular location	Nucleus. Cell junction › desmosome. Note: Nuclear and associated with desmosomes.
Tissue specificity	Widely expressed. Found at desmosomal plaques in simple and stratified epithelia and in non-epithelial tissues such as myocardium and lymph node follicles. In most stratified epithelia found in the desmosomes of the basal cell layer and seems to be absent from suprabasal strata. Ref.5
Involvement in disease	Familial arrhythmogenic right ventricular dysplasia 9 (ARVD9) [MIM:609040]: 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.13 Ref.14 Ref.16
Sequence similarities	Belongs to the beta-catenin family. Contains 8 ARM repeats.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Nucleus
Coding sequence diversity	Alternative splicing
Disease	Cardiomyopathy Disease mutation
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction maintenance Inferred from sequence or structural similarity. Source: BHF-UCL bundle of His cell to Purkinje myocyte communication Inferred from mutant phenotype PubMed 22781308. Source: BHF-UCL cell communication by electrical coupling involved in cardiac conduction Inferred from sequence or structural similarity. Source: BHF-UCL cell-cell adhesion Non-traceable author statement Ref.1. Source: UniProtKB cell-cell signaling involved in cardiac conduction Inferred from mutant phenotype PubMed 22889254. Source: BHF-UCL desmosome assembly Inferred from mutant phenotype PubMed 18474624. Source: BHF-UCL gap junction assembly Inferred from sequence or structural similarity. Source: BHF-UCL intermediate filament bundle assembly Inferred from mutant phenotype PubMed 18474624. Source: BHF-UCL lipid homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL maintenance of organ identity Inferred from mutant phenotype PubMed 22889254. Source: BHF-UCL negative regulation of cell migration Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of sodium ion transport Inferred from sequence or structural similarity. Source: BHF-UCL regulation of heart rate by cardiac conduction Inferred from mutant phenotype PubMed 22781308PubMed 22889254. Source: BHF-UCL regulation of tight junction assembly Inferred from sequence or structural similarity. Source: BHF-UCL regulation of ventricular cardiac muscle cell action potential Inferred from mutant phenotype PubMed 22781308PubMed 22889254. Source: BHF-UCL ventricular cardiac muscle tissue morphogenesis Inferred from mutant phenotype PubMed 22889254. Source: BHF-UCL
Cellular_component	adherens junction Inferred from sequence or structural similarity. Source: BHF-UCL desmosome Non-traceable author statement Ref.1. Source: UniProtKB integral to membrane Traceable author statement Ref.1. Source: ProtInc intercalated disc Inferred from sequence or structural similarity. Source: BHF-UCL intermediate filament Inferred from sequence or structural similarity. Source: BHF-UCL nucleus Non-traceable author statement Ref.1. Source: UniProtKB plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	intermediate filament binding Inferred from direct assay PubMed 10852826. Source: BHF-UCL ion channel binding Inferred from sequence or structural similarity. Source: BHF-UCL protein complex scaffold Inferred from mutant phenotype PubMed 18474624. Source: BHF-UCL sodium channel regulator activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q99959-1)

Also known as: B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q99959-2)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     460-503: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 881

881

Plakophilin-2

PRO_0000064286

Regions

Repeat

341 – 383

43

ARM 1

Repeat

385 – 424

40

ARM 2

Repeat

427 – 467

41

ARM 3

Repeat

571 – 616

46

ARM 4

Repeat

671 – 711

41

ARM 5

Repeat

719 – 758

40

ARM 6

Repeat

763 – 804

42

ARM 7

Repeat

807 – 849

43

ARM 8

Amino acid modifications

Modified residue

44

1

Phosphoserine Ref.10

Modified residue

132

1

Phosphoserine Ref.6

Modified residue

151

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.12

Modified residue

154

1

Phosphoserine Ref.10 Ref.12

Modified residue

155

1

Phosphoserine Ref.10 Ref.12

Modified residue

169

1

Phosphoserine Ref.6

Modified residue

197

1

Phosphoserine Ref.8

Modified residue

251

1

Phosphoserine Ref.10 Ref.12

Modified residue

329

1

Phosphoserine Ref.8 Ref.10

Natural variations

Alternative sequence

460 – 503

44

Missing in isoform 1.

VSP_006736

Natural variant

26

1

D → N Associated with increased susceptibility to arrhythmogenic right ventricular cardiomyopathy. Ref.14 Ref.15

VAR_065701

Natural variant

58

1

E → D. Ref.15

VAR_065702

Natural variant

62

1

Q → K Found in patients with arrhythmogenic right ventricular cardiomyopathy. Ref.15

VAR_065703

Natural variant

70

1

S → I. Ref.14 Ref.15 Ref.16

VAR_065704

Natural variant

137

1

E → K in ARVD9. Ref.16

VAR_065705

Natural variant

140

1

S → F in ARVD9; uncertain pathological significance. Ref.13 Ref.14 Ref.15

VAR_021148

Natural variant

169

1

S → G in ARVD9. Ref.16

VAR_065706

Natural variant

195

1

A → V. Ref.14

VAR_065707

Natural variant

276

1

P → S. Ref.14

VAR_065708

Natural variant

338

1

T → A in a patient with arrhythmogenic right ventricular cardiomyopathy. Ref.15

VAR_065709

Natural variant

366

1

L → P. Ref.1 Ref.4 Ref.14 Ref.15 Ref.16
Corresponds to variant rs1046116 [ dbSNP | Ensembl ].

VAR_063108

Natural variant

372

1

A → P. Ref.11 Ref.14

VAR_065710

Natural variant

424

1

F → S in ARVD9. Ref.14

VAR_065711

Natural variant

489

1

G → R. Ref.15

VAR_065712

Natural variant

526

1

T → M. Ref.14

VAR_065713

Natural variant

531

1

I → S. Ref.14 Ref.15

VAR_065714

Natural variant

587

1

V → I Associated with increased susceptibility to arrhythmogenic right ventricular cardiomyopathy. Ref.14 Ref.15 Ref.16

VAR_065715

Natural variant

615

1

S → F in ARVD9. Ref.13

VAR_021149

Natural variant

631

1

Y → C in ARVD9. Ref.16

VAR_065716

Natural variant

654

1

K → Q in ARVD9. Ref.13

VAR_021150

Natural variant

673

1

G → V in a patient with arrhythmogenic right ventricular cardiomyopathy. Ref.15

VAR_065717

Natural variant

787

1

L → F in ARVD9. Ref.14

VAR_065718

Natural variant

796

1

C → R in ARVD9. Ref.13

VAR_021151

Secondary structure

1

.

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881

Helix Strand Turn

Details...

Helix

353 – 358

6

Helix

367 – 381

15

Helix

385 – 393

9

Helix

396 – 402

7

Helix

403 – 405

3

Helix

409 – 423

15

Helix

427 – 435

9

Helix

438 – 448

11

Helix

452 – 459

8

Helix

504 – 510

7

Helix

513 – 515

3

Helix

516 – 530

15

Helix

532 – 536

5

Helix

540 – 542

3

Helix

552 – 565

14

Helix

570 – 577

8

Helix

582 – 595

14

Helix

602 – 614

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (B) [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 947838B0C8275D5D	FASTA	881	97,415
	10 20 30 40 50 60 MAAPGAPAEY GYIRTVLGQQ ILGQLDSSSL ALPSEAKLKL AGSSGRGGQT VKSLRIQEQV 70 80 90 100 110 120 QQTLARKGRS SVGNGNLHRT SSVPEYVYNL HLVENDFVGG RSPVPKTYDM LKAGTTATYE 130 140 150 160 170 180 GRWGRGTAQY SSQKSVEERS LRHPLRRLEI SPDSSPERAH YTHSDYQYSQ RSQAGHTLHH 190 200 210 220 230 240 QESRRAALLV PPRYARSEIV GVSRAGTTSR QRHFDTYHRQ YQHGSVSDTV FDSIPANPAL 250 260 270 280 290 300 LTYPRPGTSR SMGNLLEKEN YLTAGLTVGQ VRPLVPLQPV TQNRASRSSW HQSSFHSTRT 310 320 330 340 350 360 LREAGPSVAV DSSGRRAHLT VGQAAAGGSG NLLTERSTFT DSQLGNADME MTLERAVSML 370 380 390 400 410 420 EADHMLPSRI SAAATFIQHE CFQKSEARKR VNQLRGILKL LQLLKVQNED VQRAVCGALR 430 440 450 460 470 480 NLVFEDNDNK LEVAELNGVP RLLQVLKQTR DLETKKQITD HTVNLRSRNG WPGAVAHACN 490 500 510 520 530 540 PSTLGGQGGR ITRSGVRDQP DQHGLLWNLS SNDKLKNLMI TEALLTLTEN IIIPFSGWPE 550 560 570 580 590 600 GDYPKANGLL DFDIFYNVTG CLRNMSSAGA DGRKAMRRCD GLIDSLVHYV RGTIADYQPD 610 620 630 640 650 660 DKATENCVCI LHNLSYQLEA ELPEKYSQNI YIQNRNIQTD NNKSIGCFGS RSRKVKEQYQ 670 680 690 700 710 720 DVPMPEEKSN PKGVEWLWHS IVIRMYLSLI AKSVRNYTQE ASLGALQNLT AGSGPMPTSV 730 740 750 760 770 780 AQTVVQKESG LQHTRKMLHV GDPSVKKTAI SLLRNLSRNL SLQNEIAKET LPDLVSIIPD 790 800 810 820 830 840 TVPSTDLLIE TTASACYTLN NIIQNSYQNA RDLLNTGGIQ KIMAISAGDA YASNKASKAA 850 860 870 880 SVLLYSLWAH TELHHAYKKA QFKKTDFVNS RTAKAYHSLK D
	Isoform 1 (A) [UniParc]. Checksum: 8E9553F9B820E8DF	FASTA	837	92,756
	10 20 30 40 50 60 MAAPGAPAEY GYIRTVLGQQ ILGQLDSSSL ALPSEAKLKL AGSSGRGGQT VKSLRIQEQV 70 80 90 100 110 120 QQTLARKGRS SVGNGNLHRT SSVPEYVYNL HLVENDFVGG RSPVPKTYDM LKAGTTATYE 130 140 150 160 170 180 GRWGRGTAQY SSQKSVEERS LRHPLRRLEI SPDSSPERAH YTHSDYQYSQ RSQAGHTLHH 190 200 210 220 230 240 QESRRAALLV PPRYARSEIV GVSRAGTTSR QRHFDTYHRQ YQHGSVSDTV FDSIPANPAL 250 260 270 280 290 300 LTYPRPGTSR SMGNLLEKEN YLTAGLTVGQ VRPLVPLQPV TQNRASRSSW HQSSFHSTRT 310 320 330 340 350 360 LREAGPSVAV DSSGRRAHLT VGQAAAGGSG NLLTERSTFT DSQLGNADME MTLERAVSML 370 380 390 400 410 420 EADHMLPSRI SAAATFIQHE CFQKSEARKR VNQLRGILKL LQLLKVQNED VQRAVCGALR 430 440 450 460 470 480 NLVFEDNDNK LEVAELNGVP RLLQVLKQTR DLETKKQITG LLWNLSSNDK LKNLMITEAL 490 500 510 520 530 540 LTLTENIIIP FSGWPEGDYP KANGLLDFDI FYNVTGCLRN MSSAGADGRK AMRRCDGLID 550 560 570 580 590 600 SLVHYVRGTI ADYQPDDKAT ENCVCILHNL SYQLEAELPE KYSQNIYIQN RNIQTDNNKS 610 620 630 640 650 660 IGCFGSRSRK VKEQYQDVPM PEEKSNPKGV EWLWHSIVIR MYLSLIAKSV RNYTQEASLG 670 680 690 700 710 720 ALQNLTAGSG PMPTSVAQTV VQKESGLQHT RKMLHVGDPS VKKTAISLLR NLSRNLSLQN 730 740 750 760 770 780 EIAKETLPDL VSIIPDTVPS TDLLIETTAS ACYTLNNIIQ NSYQNARDLL NTGGIQKIMA 790 800 810 820 830 ISAGDAYASN KASKAASVLL YSLWAHTELH HAYKKAQFKK TDFVNSRTAK AYHSLKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque." Mertens C., Kuhn C., Franke W.W. J. Cell Biol. 135:1009-1025(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT PRO-366.
[2]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORM 1), VARIANT PRO-366. Tissue: Brain and Placenta.
[5]	"Desmosomal plakophilin 2 as a differentiation marker in normal and malignant tissues." Mertens C., Kuhn C., Moll R., Schwetlick I., Franke W.W. Differentiation 64:277-290(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-169, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-329, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, MASS SPECTROMETRY.
[10]	"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-44; SER-151; SER-154; SER-155; SER-251 AND SER-329, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, VARIANT PRO-372.
[12]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-154; SER-155 AND SER-251, MASS SPECTROMETRY.
[13]	"Mutations in the desmosomal protein plakophilin-2 are common in arrhythmogenic right ventricular cardiomyopathy." Gerull B., Heuser A., Wichter T., Paul M., Basson C.T., McDermott D.A., Lerman B.B., Markowitz S.M., Ellinor P.T., MacRae C.A., Peters S., Grossmann K.S., Michely B., Sasse-Klaassen S., Birchmeier W., Dietz R., Breithardt G., Schulze-Bahr E., Thierfelder L. Nat. Genet. 36:1162-1164(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARVD9 PHE-140; PHE-615; GLN-654 AND ARG-796.
[14]	"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: VARIANTS ARVD9 PHE-140; SER-424 AND PHE-787, VARIANTS ASN-26; ILE-70; VAL-195; SER-276; PRO-366; PRO-372; MET-526; SER-531 AND ILE-587.
[15]	"Missense variants in plakophilin-2 in arrhythmogenic right ventricular cardiomyopathy patients -- disease-causing or innocent bystanders?" Christensen A.H., Benn M., Tybjaerg-Hansen A., Haunso S., Svendsen J.H. Cardiology 115:148-154(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASN-26; ASP-58; LYS-62; ILE-70; PHE-140; ALA-338; PRO-366; ARG-489; SER-531; ILE-587 AND VAL-673, DISCUSSION OF PATHOGENIC ROLE OF VARIANTS ASN-26; PHE-140 AND ILE-587.
[16]	"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 ARVD9 LYS-137; GLY-169 AND CYS-631, VARIANTS ILE-70; PRO-366 AND ILE-587.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97675 mRNA. Translation: CAA66264.1.
X97675 mRNA. Translation: CAA66265.1.
AC087311 Genomic DNA. No translation available.
AC087588 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88511.1.
CH471116 Genomic DNA. Translation: EAW88514.1.
CH471116 Genomic DNA. Translation: EAW88515.1.
BC094762 mRNA. Translation: AAH94762.1.
BC126199 mRNA. Translation: AAI26200.1.
BC143966 mRNA. Translation: AAI43967.1.

IPI

IPI00005264.
IPI00219688.

RefSeq

NP_001005242.2. NM_001005242.2.
NP_004563.2. NM_004572.3.

UniGene

Hs.164384.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TT9	X-ray	1.55	A	346-620	[»]

ProteinModelPortal

Q99959.

SMR

Q99959. Positions 346-854.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99959. 4 interactions.

MINT

MINT-5001916.

STRING

9606.ENSP00000070846.

PTM databases

PhosphoSite

Q99959.

Polymorphism databases

DMDM

296452867.

Proteomic databases

PaxDb

Q99959.

PRIDE

Q99959.

Protocols and materials databases

DNASU

5318.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000070846; ENSP00000070846; ENSG00000057294.
ENST00000340811; ENSP00000342800; ENSG00000057294.

GeneID

5318.

KEGG

hsa:5318.

UCSC

uc001rlj.4. human.

Organism-specific databases

CTD

5318.

GeneCards

GC12M032943.

HGNC

HGNC:9024. PKP2.

HPA

HPA014314.

MIM

602861. gene.
609040. phenotype.

neXtProt

NX_Q99959.

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.

PharmGKB

PA33357.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG273513.

HOGENOM

HOG000092312.

HOVERGEN

HBG009157.

InParanoid

Q99959.

KO

K12642.

OMA

SWHQSSF.

PhylomeDB

Q99959.

Gene expression databases

ArrayExpress

Q99959.

Bgee

Q99959.

CleanEx

HS_PKP2.

Genevestigator

Q99959.

GermOnline

ENSG00000057294. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 3 hits.

InterPro

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

Pfam

PF00514. Arm. 1 hit.
[Graphical view]

SMART

SM00185. ARM. 4 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50176. ARM_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PKP2. human.

GenomeRNAi

5318.

NextBio

20572.

SOURCE

Search...

Entry information

Entry name

PKP2_HUMAN

Accession

Primary (citable) accession number: Q99959
Secondary accession number(s): A0AV37 , D3DUW9, Q4VC01, Q99960

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 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.