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TJP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2OSG, 3E17
Identifiers
Aliases	TJP2, C9DUPq21.11, DFNA51, DUP9q21.11, PFIC4, X104, ZO2, Tight junction protein 2, FHCA1
External IDs	OMIM: 607709; MGI: 1341872; HomoloGene: 3541; GeneCards: TJP2; OMA:TJP2 - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9q21.11 Start 69,121,264 bp End 69,274,615 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 B Start 24,071,869 bp End 24,202,394 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus callosum Descending thoracic aorta ascending aorta right coronary artery C1 segment right lung subcutaneous adipose tissue duodenum right lobe of liver right lobe of thyroid gland Top expressed in otic vesicle saccule otic placode vestibular membrane of cochlear duct Paneth cell sciatic nerve conjunctival fornix left lung lobe epithelium of stomach cornea More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein-macromolecule adaptor activity protein domain specific binding guanylate kinase activity protein binding cadherin binding Cellular component membrane bicellular tight junction adherens junction plasma membrane cell junction nucleus cytosol nucleoplasm Biological process establishment of endothelial intestinal barrier hippo signaling regulation of membrane permeability intestinal absorption GMP metabolic process GDP metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9414 21873 Ensembl ENSG00000119139 ENSMUSG00000024812 UniProt Q9UDY2 Q9Z0U1 RefSeq (mRNA) NM_001170414 NM_001170415 NM_001170416 NM_001170630 NM_004817 NM_201629 NM_001369870 NM_001369871 NM_001369872 NM_001369873 NM_001369874 NM_001369875 NM_001198985 NM_011597 NM_001360391 NM_001360392 NM_001376368 RefSeq (protein) NP_001163885 NP_001163886 NP_001163887 NP_004808 NP_963923 NP_001185914 NP_035727 NP_001347320 NP_001347321 Location (UCSC) Chr 9: 69.12 – 69.27 Mb Chr 19: 24.07 – 24.2 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Tight junction protein ZO-2 is a protein that in humans is encoded by the TJP2 gene.

Tight junction proteins (TJPs) belong to a family of membrane-associated guanylate kinase (MAGUK) homologs that are involved in the organization of epithelial and endothelial intercellular junctions. TJPs bind to the cytoplasmic C termini of junctional transmembrane proteins and link them to the actin cytoskeleton .

Interactions

Tight junction protein 2 has been shown to interact with tight junction protein 1, band 4.1, occludin and USP53.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000119139 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000024812 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Duclos F, Rodius F, Wrogemann K, Mandel JL, Koenig M (November 1994). "The Friedreich ataxia region: characterization of two novel genes and reduction of the critical region to 300 kb". Hum Mol Genet. 3 (6): 909–914. doi:10.1093/hmg/3.6.909. PMID 7951235.
6. "Entrez Gene: TJP2 tight junction protein 2 (zona occludens 2)".
7. ^ Itoh, M; Morita K; Tsukita S (February 1999). "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin". J. Biol. Chem. 274 (9): 5981–5986. doi:10.1074/jbc.274.9.5981. ISSN 0021-9258. PMID 10026224.
8. ^ Wittchen, E S; Haskins J; Stevenson B R (December 1999). "Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3". J. Biol. Chem. 274 (49): 35179–35185. doi:10.1074/jbc.274.49.35179. ISSN 0021-9258. PMID 10575001.
9. Fanning, A S; Jameson B J; Jesaitis L A; Anderson J M (November 1998). "The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton". J. Biol. Chem. 273 (45): 29745–29753. doi:10.1074/jbc.273.45.29745. ISSN 0021-9258. PMID 9792688.
10. Mattagajasingh, S N; Huang S C; Hartenstein J S; Benz E J (September 2000). "Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton". J. Biol. Chem. 275 (39): 30573–30585. doi:10.1074/jbc.M004578200. ISSN 0021-9258. PMID 10874042.
11. Peng, Bi-Hung; Lee J Ching; Campbell Gerald A (December 2003). "In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis". J. Biol. Chem. 278 (49): 49644–49651. doi:10.1074/jbc.M302782200. ISSN 0021-9258. PMID 14512431.
12. Kazmierczak M, Harris SL, Kazmierczak P, Shah P, Starovoytov V, Ohlemiller KK, Schwander M (November 2015). "Progressive Hearing Loss in Mice Carrying a Mutation in Usp53". The Journal of Neuroscience. 35 (47): 15582–98. doi:10.1523/JNEUROSCI.1965-15.2015. PMC 4659823. PMID 26609154.

Further reading

• Denker BM, Nigam SK (1998). "Molecular structure and assembly of the tight junction". Am. J. Physiol. 274 (1 Pt 2): F1–9. doi:10.1152/ajprenal.1998.274.1.F1. PMID 9458817.
• González-Mariscal L, Betanzos A, Avila-Flores A (2000). "MAGUK proteins: structure and role in the tight junction". Semin. Cell Dev. Biol. 11 (4): 315–324. doi:10.1006/scdb.2000.0178. PMID 10966866.
• King JE, Eugenin EA, Buckner CM, Berman JW (2006). "HIV tat and neurotoxicity". Microbes Infect. 8 (5): 1347–1357. doi:10.1016/j.micinf.2005.11.014. PMID 16697675.
• Van Itallie CM, Balda MS, Anderson JM (1995). "Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells". J. Cell Sci. 108 (4): 1735–42. doi:10.1242/jcs.108.4.1735. PMID 7542259.
• Beatch M, Jesaitis LA, Gallin WJ, et al. (1996). "The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced region". J. Biol. Chem. 271 (42): 25723–25726. doi:10.1074/jbc.271.42.25723. PMID 8824195.
• Itoh M, Morita K, Tsukita S (1999). "Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin". J. Biol. Chem. 274 (9): 5981–5986. doi:10.1074/jbc.274.9.5981. PMID 10026224.
• Chlenski A, Ketels KV, Tsao MS, et al. (1999). "Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma". Int. J. Cancer. 82 (1): 137–144. doi:10.1002/(SICI)1097-0215(19990702)82:1<137::AID-IJC23>3.0.CO;2-F. PMID 10360833. S2CID 11349543.
• Chlenski A, Ketels KV, Engeriser JL, et al. (1999). "zo-2 gene alternative promoters in normal and neoplastic human pancreatic duct cells". Int. J. Cancer. 83 (3): 349–358. doi:10.1002/(SICI)1097-0215(19991029)83:3<349::AID-IJC10>3.0.CO;2-C. PMID 10495427.
• Wittchen ES, Haskins J, Stevenson BR (2000). "Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3". J. Biol. Chem. 274 (49): 35179–35185. doi:10.1074/jbc.274.49.35179. PMID 10575001.
• Itoh M, Furuse M, Morita K, et al. (2000). "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins". J. Cell Biol. 147 (6): 1351–1363. doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID 10601346.
• Cordenonsi M, D'Atri F, Hammar E, et al. (2000). "Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3, and myosin". J. Cell Biol. 147 (7): 1569–1582. doi:10.1083/jcb.147.7.1569. PMC 2174252. PMID 10613913.
• Mattagajasingh SN, Huang SC, Hartenstein JS, Benz EJ (2000). "Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton". J. Biol. Chem. 275 (39): 30573–30585. doi:10.1074/jbc.M004578200. PMID 10874042.
• Chlenski A, Ketels KV, Korovaitseva GI, et al. (2000). "Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues". Biochim. Biophys. Acta. 1493 (3): 319–24. doi:10.1016/S0167-4781(00)00185-8. PMID 11018256.
• Citi S, D'Atri F, Parry DA (2000). "Human and Xenopus cingulin share a modular organization of the coiled-coil rod domain: predictions for intra- and intermolecular assembly". J. Struct. Biol. 131 (2): 135–145. doi:10.1006/jsbi.2000.4284. PMID 11042084.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–1795. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Glaunsinger BA, Weiss RS, Lee SS, Javier R (2001). "Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2". EMBO J. 20 (20): 5578–5586. doi:10.1093/emboj/20.20.5578. PMC 125668. PMID 11598001.
• Islas S, Vega J, Ponce L, González-Mariscal L (2002). "Nuclear localization of the tight junction protein ZO-2 in epithelial cells". Exp. Cell Res. 274 (1): 138–148. doi:10.1006/excr.2001.5457. PMID 11855865.

• Genes on human chromosome 9