CALCOCO2

Calcium binding and coiled-coil domain 2, also known as CALCOCO2, is a human gene.cite web | title = Entrez Gene: CALCOCO2 calcium binding and coiled-coil domain 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10241| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: CALCOCO2 calcium binding and coiled-coil domain 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10241| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Korioth F, Gieffers C, Maul GG, Frey J |title=Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment. |journal=J. Cell Biol. |volume=130 |issue= 1 |pages= 1–13 |year= 1995 |pmid= 7540613 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Sternsdorf T, Jensen K, Züchner D, Will H |title=Cellular localization, expression, and structure of the nuclear dot protein 52. |journal=J. Cell Biol. |volume=138 |issue= 2 |pages= 435–48 |year= 1997 |pmid= 9230084 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Florin L, Schäfer F, Sotlar K, "et al." |title=Reorganization of nuclear domain 10 induced by papillomavirus capsid protein l2. |journal=Virology |volume=295 |issue= 1 |pages= 97–107 |year= 2002 |pmid= 12033769 |doi= 10.1006/viro.2002.1360
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Di Y, Li J, Zhang Y, "et al." |title=HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-finger proteins. |journal=J. Biochem. |volume=133 |issue= 6 |pages= 713–8 |year= 2004 |pmid= 12869526 |doi=
*cite journal | author=Everett RD, Sourvinos G, Leiper C, "et al." |title=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. |journal=J. Virol. |volume=78 |issue= 4 |pages= 1903–17 |year= 2004 |pmid= 14747555 |doi=
*cite journal | author=Colland F, Jacq X, Trouplin V, "et al." |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Morriswood B, Ryzhakov G, Puri C, "et al." |title=T6BP and NDP52 are myosin VI binding partners with potential roles in cytokine signalling and cell adhesion. |journal=J. Cell. Sci. |volume=120 |issue= Pt 15 |pages= 2574–85 |year= 2007 |pmid= 17635994 |doi= 10.1242/jcs.007005

PBB_Controls
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update_citations = yes