CDC27

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Cell division cycle 27
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CDC27 ; ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E; H-NUC; HNUC; NUC2
External IDs OMIM116946 MGI102685 HomoloGene960 GeneCards: CDC27 Gene
Orthologs
Species Human Mouse
Entrez 996 217232
Ensembl ENSG00000004897 ENSMUSG00000020687
UniProt P30260 A2A6Q5
RefSeq (mRNA) NM_001114091 NM_001285988
RefSeq (protein) NP_001107563 NP_001272917
Location (UCSC) Chr 17:
47.12 – 47.19 Mb
Chr 11:
104.5 – 104.55 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]

Function[edit]

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[edit]

CDC27 has been shown to interact with:

References[edit]

  1. ^ 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 47707. PMID 8234252. 
  2. ^ a b "Entrez Gene: CDC27 cell division cycle 27 homolog (S. cerevisiae)". 
  3. ^ 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. 
  4. ^ 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 16806. PMID 10922056. 
  5. ^ 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 2169443. PMID 11076961. 
  6. ^ 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 387753. PMID 15082755. 
  7. ^ 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 2132789. PMID 9628895. 
  8. ^ 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. 
  9. ^ 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. 
  10. ^ 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 218146. PMID 14561775. 
  11. ^ 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 2173153. PMID 12196507. 
  12. ^ 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 21618. PMID 9736712. 
  13. ^ 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 2635557. PMID 18997788. 
  14. ^ 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 1223613. PMID 12797865. 
  15. ^ 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 316589. PMID 9499405. 
  16. ^ 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. 

Further reading[edit]