Plakophilin-3

PKP3
Identifiers
Aliases	PKP3, plakophilin 3
External IDs	OMIM: 605561; MGI: 1891830; HomoloGene: 5200; GeneCards: PKP3; OMA:PKP3 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11p15.5 Start 392,614 bp End 404,908 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 F5 Start 140,658,131 bp End 140,670,423 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen skin of leg mucosa of pharynx human penis skin of arm mucosa of transverse colon mucosa of ileum nipple vulva gums Top expressed in lip epidermis hair follicle esophagus skin of external ear corneal stroma skin of abdomen skin of back saccule crypt of lieberkuhn of small intestine More reference expression data BioGPS More reference expression data
Gene ontology Molecular function alpha-catenin binding cell adhesion molecule binding cadherin binding involved in cell-cell adhesion RNA binding protein binding enzyme binding translation regulator activity cadherin binding Cellular component desmosome nucleus cell-cell junction cornified envelope nucleoplasm plasma membrane cell junction messenger ribonucleoprotein complex cytoplasm Biological process desmosome assembly cell adhesion keratinization cornification regulation of translation positive regulation of gene expression negative regulation of mRNA catabolic process protein localization to plasma membrane cell-cell adhesion cell-cell junction assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11187 56460 Ensembl ENSG00000184363 ENSMUSG00000054065 UniProt Q9Y446 Q9QY23 RefSeq (mRNA) NM_007183 NM_001303029 NM_001162924 NM_019762 RefSeq (protein) NP_001289958 NP_009114 NP_001156396 NP_062736 Location (UCSC) Chr 11: 0.39 – 0.4 Mb Chr 7: 140.66 – 140.67 Mb PubMed search
Wikidata
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Plakophilin-3 is a protein that in humans is encoded by the PKP3 gene.

Function

This gene encodes a member of the arm-repeat (armadillo) and plakophilin gene families. Plakophilin proteins contain numerous armadillo repeats, localize to cell desmosomes and nuclei, and participate in linking cadherins to intermediate filaments in the cytoskeleton. This protein may act in cellular desmosome-dependent adhesion and signaling pathways.

Interactions

PKP3 has been shown to interact with:

• DSC3,
• DSG1,
• DSG2 and
• DSG3.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Bonné S, van Hengel J, Nollet F, Kools P, van Roy F (1999). "Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells". J. Cell. Sci. 112 (14): 2265–76. PMID 10381383.
• Hofmann I, Mertens C, Brettel M, Nimmrich V, Schnölzer M, Herrmann H (2000). "Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis". J. Cell. Sci. 113 (13): 2471–83. PMID 10852826.
• Bonné S, Gilbert B, Hatzfeld M, Chen X, Green KJ, van Roy F (2003). "Defining desmosomal plakophilin-3 interactions". J. Cell Biol. 161 (2): 403–16. doi:10.1083/jcb.200303036. PMC 2172904. PMID 12707304.
• Papagerakis S, Shabana AH, Depondt J, Gehanno P, Forest N (2003). "Immunohistochemical localization of plakophilins (PKP1, PKP2, PKP3, and p0071) in primary oropharyngeal tumors: correlation with clinical parameters". Hum. Pathol. 34 (6): 565–72. doi:10.1016/S0046-8177(03)00174-6. PMID 12827610.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell Proteomics. 4 (9): 1240–50. doi:10.1074/mcp.M500089-MCP200. PMID 15951569.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Hofmann I, Casella M, Schnölzer M, Schlechter T, Spring H, Franke WW (2006). "Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules". Mol. Biol. Cell. 17 (3): 1388–98. doi:10.1091/mbc.E05-08-0708. PMC 1382326. PMID 16407409.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Aigner K, Descovich L, Mikula M, Sultan A, Dampier B, Bonné S, van Roy F, Mikulits W, Schreiber M, Brabletz T, Sommergruber W, Schweifer N, Wernitznig A, Beug H, Foisner R, Eger A (2007). "The transcription factor ZEB1 (deltaEF1) represses Plakophilin 3 during human cancer progression". FEBS Lett. 581 (8): 1617–24. doi:10.1016/j.febslet.2007.03.026. PMC 2938730. PMID 17391671.