CGN (gene)

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Cingulin
Identifiers
Symbols CGN ; DKFZp779N1112; FLJ39281; KIAA1319
External IDs Template:OMIM5 Template:MGI HomoloGene41394
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Cingulin, also known as CGN, is a human gene.[1]


References

  1. "Entrez Gene: CGN cingulin".

Further reading

  • Wolburg H, Lippoldt A (2003). "Tight junctions of the blood-brain barrier: development, composition and regulation". Vascul. Pharmacol. 38 (6): 323–37. PMID 12529927.
  • 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): 1569–82. PMID 10613913.
  • Nagase T, Kikuno R, Ishikawa KI; et al. (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. PMID 10718198.
  • Bazzoni G, Martinez-Estrada OM, Orsenigo F; et al. (2000). "Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin". J. Biol. Chem. 275 (27): 20520–6. doi:10.1074/jbc.M905251199. PMID 10877843.
  • 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): 135–45. doi:10.1006/jsbi.2000.4284. PMID 11042084.
  • D'Atri F, Nadalutti F, Citi S (2002). "Evidence for a functional interaction between cingulin and ZO-1 in cultured cells". J. Biol. Chem. 277 (31): 27757–64. doi:10.1074/jbc.M203717200. PMID 12023291.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
  • Benzinger A, Muster N, Koch HB; et al. (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.
  • Aijaz S, D'Atri F, Citi S; et al. (2005). "Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition". Dev. Cell. 8 (5): 777–86. doi:10.1016/j.devcel.2005.03.003. PMID 15866167.
  • Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells". J. Proteome Res. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
  • Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
  • Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.

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