CDC27

Cell division cycle 27 homolog (S. cerevisiae)
Identifiers
Symbols CDC27; ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E; HNUC; NUC2
External IDs OMIM: 116946 MGI: 102685 HomoloGene: 960 GeneCards: CDC27 Gene
Orthologs
Species Human Mouse
Entrez 996 217232
Ensembl ENSG00000004897 ENSMUSG00000020687
UniProt P30260 n/a
RefSeq (mRNA) NM_001114091.1 NM_145436.2
RefSeq (protein) NP_001107563.1 NP_663411.2
Location (UCSC) Chr 17:
45.2 – 45.27 Mb		 Chr 11:
104.36 – 104.41 Mb
PubMed search [1] [2]

Cell division cycle protein 27 homolog is a protein that in humans is encoded by the CDC27 gene.[1][2]

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.[2]

Interactions

CDC27 has been shown to interact with ANAPC1,[3][4] ANAPC4,[3][5] ANAPC5,[3][6][5] ANAPC11,[3][5] FZR1,[7][8] CDC20,[3][9][10][11][8][12][13] CDH1,[3] CDC23,[3][5] PIN1,[14][15] CDC16,[3][16][12][5] ANAPC7,[3][5] MAD2L1[11][12] and ANAPC10.[3][5]

References

  1. ^ Tugendreich S, Boguski MS, Seldin MS, Hieter P (Dec 1993). "Linking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data base". Proc Natl Acad Sci USA 90 (21): 10031–5. doi:10.1073/pnas.90.21.10031. PMC 47707. PMID 8234252. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47707. 
  2. ^ a b "Entrez Gene: CDC27 cell division cycle 27 homolog (S. cerevisiae)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=996. 
  3. ^ a b c d e f g h i j Vodermaier, Hartmut C; Gieffers Christian, Maurer-Stroh Sebastian, Eisenhaber Frank, Peters Jan-Michael (Sep. 2003). "TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1". Curr. Biol. (England) 13 (17): 1459–68. doi:10.1016/S0960-9822(03)00581-5. ISSN 0960-9822. PMID 12956947. 
  4. ^ Sumara, I; Vorlaufer E, Gieffers C, Peters B H, Peters J M (Nov. 2000). "Characterization of Vertebrate Cohesin Complexes and Their Regulation in Prophase". J. Cell Biol. (UNITED STATES) 151 (4): 749–62. doi:10.1083/jcb.151.4.749. ISSN 0021-9525. PMC 2169443. PMID 11076961. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2169443. 
  5. ^ a b c d e f g Gmachl, M; Gieffers C, Podtelejnikov A V, Mann M, Peters J M (Aug. 2000). "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (16): 8973–8. doi:10.1073/pnas.97.16.8973. ISSN 0027-8424. PMC 16806. PMID 10922056. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16806. 
  6. ^ Koloteva-Levine, Nadejda; Pinchasi Dalia, Pereman Idan, Zur Amit, Brandeis Michael, Elroy-Stein Orna (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". Mol. Cell. Biol. (United States) 24 (9): 3577–87. doi:10.1128/MCB.24.9.3577-3587.2004. ISSN 0270-7306. PMC 387753. PMID 15082755. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=387753. 
  7. ^ Zhou, Yuan; Ching Yick-Pang, Ng Raymond W M, Jin Dong-Yan (Sep. 2003). "Differential expression, localization and activity of two alternatively spliced isoforms of human APC regulator CDH1". Biochem. J. (England) 374 (Pt 2): 349–58. doi:10.1042/BJ20030600. PMC 1223613. PMID 12797865. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223613. 
  8. ^ a b Kramer, E R; Gieffers C, Hölzl G, Hengstschläger M, Peters J M (Nov. 1998). "Activation of the human anaphase-promoting complex by proteins of the CDC20/Fizzy family". Curr. Biol. (ENGLAND) 8 (22): 1207–10. doi:10.1016/S0960-9822(07)00510-6. ISSN 0960-9822. PMID 9811605. 
  9. ^ D'Angiolella, Vincenzo; Mari Cecilia, Nocera Donatella, Rametti Linda, Grieco Domenico (Oct. 2003). "The spindle checkpoint requires cyclin-dependent kinase activity". Genes Dev. (United States) 17 (20): 2520–5. doi:10.1101/gad.267603. ISSN 0890-9369. PMC 218146. PMID 14561775. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=218146. 
  10. ^ Kallio, Marko J; Beardmore Victoria A, Weinstein Jasminder, Gorbsky Gary J (Sep. 2002). "Rapid microtubule-independent dynamics of Cdc20 at kinetochores and centrosomes in mammalian cells". J. Cell Biol. (United States) 158 (5): 841–7. doi:10.1083/jcb.200201135. ISSN 0021-9525. PMC 2173153. PMID 12196507. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173153. 
  11. ^ a b Wassmann, K; Benezra R (Sep. 1998). "Mad2 transiently associates with an APC/p55Cdc complex during mitosis". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (19): 11193–8. doi:10.1073/pnas.95.19.11193. ISSN 0027-8424. PMC 21618. PMID 9736712. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21618. 
  12. ^ a b c Kallio, M; Weinstein J, Daum J R, Burke D J, Gorbsky G J (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". J. Cell Biol. (UNITED STATES) 141 (6): 1393–406. doi:10.1083/jcb.141.6.1393. ISSN 0021-9525. PMC 2132789. PMID 9628895. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132789. 
  13. ^ Nilsson, Jakob; Yekezare Mona, Minshull Jeremy, Pines Jonathon (Dec. 2008). "The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for destruction". Nat. Cell Biol. (England) 10 (12): 1411–20. doi:10.1038/ncb1799. PMC 2635557. PMID 18997788. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2635557. 
  14. ^ Shen, M; Stukenberg P T, Kirschner M W, Lu K P (Mar. 1998). "The essential mitotic peptidyl–prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes Dev. (UNITED STATES) 12 (5): 706–20. doi:10.1101/gad.12.5.706. ISSN 0890-9369. PMC 316589. PMID 9499405. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316589. 
  15. ^ Lu, P J; Zhou X Z, Shen M, Lu K P (Feb. 1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science (UNITED STATES) 283 (5406): 1325–8. doi:10.1126/science.283.5406.1325. ISSN 0036-8075. PMID 10037602. 
  16. ^ Ollendorff, V; Donoghue D J (Dec. 1997). "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two tetratricopeptide repeat-containing subunits of the anaphase-promoting complex". J. Biol. Chem. (UNITED STATES) 272 (51): 32011–8. doi:10.1074/jbc.272.51.32011. ISSN 0021-9258. PMID 9405394. 

Further reading