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Available structures
PDB Ortholog search: PDBe RCSB
Aliases CDC27, ANAPC3, APC3, CDC27Hs, D0S1430E, D17S978E, H-NUC, HNUC, NUC2, cell division cycle 27
External IDs MGI: 102685 HomoloGene: 960 GeneCards: CDC27
Gene location (Human)
Chromosome 17 (human)
Chr. Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for CDC27
Genomic location for CDC27
Band 17q21.32 Start 47,117,703 bp[1]
End 47,189,422 bp[1]
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 17: 47.12 – 47.19 Mb Chr 17: 104.5 – 104.55 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Cell division cycle protein 27 homolog is a protein that in humans is encoded by the CDC27 gene.[5][6]


The protein encoded by this gene shares strong similarity with Saccharomyces cerevisiae protein Cdc27, and the gene product of Schizosaccharomyces pombe nuc 2. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eucaryotic 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. This protein was shown to interact with mitotic checkpoint proteins including Mad2, p55CDC and BUBR1, and thus may be involved in controlling the timing of mitosis.[6]


CDC27 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000004897 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020687 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Tugendreich S, Boguski MS, Seldin MS, Hieter P (Nov 1993). "Linking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data base". Proceedings of the National Academy of Sciences of the United States of America. 90 (21): 10031–5. doi:10.1073/pnas.90.21.10031. PMC 47707Freely accessible. PMID 8234252. 
  6. ^ a b "Entrez Gene: CDC27 cell division cycle 27 homolog (S. cerevisiae)". 
  7. ^ a b c d e f g h i j Vodermaier HC, Gieffers C, Maurer-Stroh S, Eisenhaber F, Peters JM (Sep 2003). "TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1". Current Biology. 13 (17): 1459–68. doi:10.1016/s0960-9822(03)00581-5. PMID 12956947. 
  8. ^ a b c d e f g Gmachl M, Gieffers C, Podtelejnikov AV, Mann M, Peters JM (Aug 2000). "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. doi:10.1073/pnas.97.16.8973. PMC 16806Freely accessible. PMID 10922056. 
  9. ^ Sumara I, Vorlaufer E, Gieffers C, Peters BH, Peters JM (Nov 2000). "Characterization of vertebrate cohesin complexes and their regulation in prophase". The Journal of Cell Biology. 151 (4): 749–62. doi:10.1083/jcb.151.4.749. PMC 2169443Freely accessible. PMID 11076961. 
  10. ^ Koloteva-Levine N, Pinchasi D, Pereman I, Zur A, Brandeis M, Elroy-Stein O (May 2004). "The Apc5 subunit of the anaphase-promoting complex/cyclosome interacts with poly(A) binding protein and represses internal ribosome entry site-mediated translation". Molecular and Cellular Biology. 24 (9): 3577–87. doi:10.1128/mcb.24.9.3577-3587.2004. PMC 387753Freely accessible. PMID 15082755. 
  11. ^ a b c Kallio M, Weinstein J, Daum JR, Burke DJ, Gorbsky GJ (Jun 1998). "Mammalian p55CDC mediates association of the spindle checkpoint protein Mad2 with the cyclosome/anaphase-promoting complex, and is involved in regulating anaphase onset and late mitotic events". The Journal of Cell Biology. 141 (6): 1393–406. doi:10.1083/jcb.141.6.1393. PMC 2132789Freely accessible. PMID 9628895. 
  12. ^ Ollendorff V, Donoghue DJ (Dec 1997). "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two tetratricopeptide repeat-containing subunits of the anaphase-promoting complex". The Journal of Biological Chemistry. 272 (51): 32011–8. doi:10.1074/jbc.272.51.32011. PMID 9405394. 
  13. ^ a b Kramer ER, Gieffers C, Hölzl G, Hengstschläger M, Peters JM (Nov 1998). "Activation of the human anaphase-promoting complex by proteins of the CDC20/Fizzy family". Current Biology. 8 (22): 1207–10. doi:10.1016/s0960-9822(07)00510-6. PMID 9811605. 
  14. ^ D'Angiolella V, Mari C, Nocera D, Rametti L, Grieco D (Oct 2003). "The spindle checkpoint requires cyclin-dependent kinase activity". Genes & Development. 17 (20): 2520–5. doi:10.1101/gad.267603. PMC 218146Freely accessible. PMID 14561775. 
  15. ^ Kallio MJ, Beardmore VA, Weinstein J, Gorbsky GJ (Sep 2002). "Rapid microtubule-independent dynamics of Cdc20 at kinetochores and centrosomes in mammalian cells". The Journal of Cell Biology. 158 (5): 841–7. doi:10.1083/jcb.200201135. PMC 2173153Freely accessible. PMID 12196507. 
  16. ^ a b Wassmann K, Benezra R (Sep 1998). "Mad2 transiently associates with an APC/p55Cdc complex during mitosis". Proceedings of the National Academy of Sciences of the United States of America. 95 (19): 11193–8. doi:10.1073/pnas.95.19.11193. PMC 21618Freely accessible. PMID 9736712. 
  17. ^ Nilsson J, Yekezare M, Minshull J, Pines J (Dec 2008). "The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for destruction". Nature Cell Biology. 10 (12): 1411–20. doi:10.1038/ncb1799. PMC 2635557Freely accessible. PMID 18997788. 
  18. ^ Zhou Y, Ching YP, Ng RW, Jin DY (Sep 2003). "Differential expression, localization and activity of two alternatively spliced isoforms of human APC regulator CDH1". The Biochemical Journal. 374 (Pt 2): 349–58. doi:10.1042/BJ20030600. PMC 1223613Freely accessible. PMID 12797865. 
  19. ^ Shen M, Stukenberg PT, Kirschner MW, Lu KP (Mar 1998). "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes & Development. 12 (5): 706–20. doi:10.1101/gad.12.5.706. PMC 316589Freely accessible. PMID 9499405. 
  20. ^ Lu PJ, Zhou XZ, Shen M, Lu KP (Feb 1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science. 283 (5406): 1325–8. doi:10.1126/science.283.5406.1325. PMID 10037602. 

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