CGN (gene)

From Wikipedia, the free encyclopedia

Cingulin

Identifiers

CGN; DKFZp779N1112; FLJ39281; KIAA1319

External IDs

OMIM: 609473 MGI: 1927237 HomoloGene: 41394

Gene ontology
Molecular Function:	• motor activity • actin binding • protein binding
Cellular Component:	• tight junction • myosin complex
Biological Process:	• biological_process

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_020770 (mRNA)
NP_065821 (protein)

XM_001001375 (mRNA)
XP_001001375 (protein)

Location

Chr 1: 149.75 - 149.78 Mb

n/a

Pubmed search

[1]

[2]

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

[edit] References

^ Entrez Gene: CGN cingulin.

[edit] 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.