Biology:CDC23
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Cell division cycle 23 homolog (S. cerevisiae), also known as CDC23, is a protein that, in humans, is encoded by the CDC23 gene.[1]
Function
The CDC23 protein shares strong similarity with Saccharomyces cerevisiae Cdc23, a protein essential for cell cycle progression through the G2/M transition. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eukaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction.[1]
Interactions
CDC23 has been shown to interact with CDC27.[2][3]
References
- ↑ 1.0 1.1 "Entrez Gene: CDC23 cell division cycle 23 homolog (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8697.
- ↑ "TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1". Current Biology 13 (17): 1459–68. Sep 2003. doi:10.1016/S0960-9822(03)00581-5. PMID 12956947.
- ↑ "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex". Proceedings of the National Academy of Sciences of the United States of America 97 (16): 8973–8. Aug 2000. doi:10.1073/pnas.97.16.8973. PMID 10922056.
External links
- Human CDC23 genome location and CDC23 gene details page in the UCSC Genome Browser.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. Jan 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. Oct 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Identification of a cullin homology region in a subunit of the anaphase-promoting complex". Science 279 (5354): 1219–22. Feb 1998. doi:10.1126/science.279.5354.1219. PMID 9469815.
- "Human CDC23: cDNA cloning, mapping to 5q31, genomic structure, and evaluation as a candidate tumor suppressor gene in myeloid leukemias". Genomics 53 (2): 184–90. Oct 1998. doi:10.1006/geno.1998.5473. PMID 9790767.
- "Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex". The Journal of Biological Chemistry 274 (20): 14500–7. May 1999. doi:10.1074/jbc.274.20.14500. PMID 10318877.
- "Expression of the CDH1-associated form of the anaphase-promoting complex in postmitotic neurons". Proceedings of the National Academy of Sciences of the United States of America 96 (20): 11317–22. Sep 1999. doi:10.1073/pnas.96.20.11317. PMID 10500174.
- "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex". Proceedings of the National Academy of Sciences of the United States of America 97 (16): 8973–8. Aug 2000. doi:10.1073/pnas.97.16.8973. PMID 10922056.
- "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports 1 (3): 287–92. Sep 2000. doi:10.1093/embo-reports/kvd058. PMID 11256614.
- "Drug target discovery by gene expression analysis: cell cycle genes". Current Cancer Drug Targets 1 (1): 73–83. May 2001. doi:10.2174/1568009013334241. PMID 12188893.
- "Alterations of anaphase-promoting complex genes in human colon cancer cells". Oncogene 22 (10): 1486–90. Mar 2003. doi:10.1038/sj.onc.1206224. PMID 12629511.
- "TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1". Current Biology 13 (17): 1459–68. Sep 2003. doi:10.1016/S0960-9822(03)00581-5. PMID 12956947.
- "Mitotic regulation of the human anaphase-promoting complex by phosphorylation". The EMBO Journal 22 (24): 6598–609. Dec 2003. doi:10.1093/emboj/cdg627. PMID 14657031.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–5. Aug 2004. doi:10.1073/pnas.0404720101. PMID 15302935.
- "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics 3 (11): 1093–101. Nov 2004. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514.
- "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America 103 (14): 5391–6. Apr 2006. doi:10.1073/pnas.0507066103. PMID 16565220.
- "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology 24 (10): 1285–92. Oct 2006. doi:10.1038/nbt1240. PMID 16964243.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. Nov 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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