CALCOCO2
From Wikipedia, the free encyclopedia
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Calcium binding and coiled-coil domain 2
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| Identifiers | ||||||||||||||
| Symbol(s) | CALCOCO2; MGC17318; NDP52 | |||||||||||||
| External IDs | OMIM: 604587 HomoloGene: 31339 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 10241 | n/a | ||||||||||||
| Ensembl | ENSG00000136436 | n/a | ||||||||||||
| Refseq | NM_005831 (mRNA) NP_005822 (protein) |
n/a (mRNA) n/a (protein) |
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| Location | Chr 17: 44.26 - 44.3 Mb | n/a | ||||||||||||
| Pubmed search | [1] | n/a | ||||||||||||
Calcium binding and coiled-coil domain 2, also known as CALCOCO2, is a human gene.[1]
The protein encoded by this gene is a subunit of nuclear domain 10 (ND10) bodies. ND10 bodies are nuclear domains appearing immunohistochemically as ten dots per nucleus. They are believed to be associated with the nuclear matrix on the basis of their resistance to nuclease digestion and salt extraction. ND10 proteins are removed from the nucleus by herpes simplex virus-1 infection and may have a role in viral life cycles.[1]
[edit] References
[edit] Further reading
- Korioth F, Gieffers C, Maul GG, Frey J (1995). "Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment.". J. Cell Biol. 130 (1): 1–13. PMID 7540613.
- 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. PMID 8125298.
- Sternsdorf T, Jensen K, Züchner D, Will H (1997). "Cellular localization, expression, and structure of the nuclear dot protein 52.". J. Cell Biol. 138 (2): 435–48. PMID 9230084.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
- Florin L, Schäfer F, Sotlar K, et al. (2002). "Reorganization of nuclear domain 10 induced by papillomavirus capsid protein l2.". Virology 295 (1): 97–107. doi:. PMID 12033769.
- 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:. PMID 12477932.
- Di Y, Li J, Zhang Y, et al. (2004). "HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-finger proteins.". J. Biochem. 133 (6): 713–8. PMID 12869526.
- Everett RD, Sourvinos G, Leiper C, et al. (2004). "Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes.". J. Virol. 78 (4): 1903–17. PMID 14747555.
- Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:. PMID 15231748.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:. PMID 16189514.
- Morriswood B, Ryzhakov G, Puri C, et al. (2007). "T6BP and NDP52 are myosin VI binding partners with potential roles in cytokine signalling and cell adhesion.". J. Cell. Sci. 120 (Pt 15): 2574–85. doi:. PMID 17635994.

