My watch list  


Baculoviral IAP repeat-containing 5 (survivin)
PDB rendering based on 1e31.
Available structures: 1e31, 1f3h, 1xox
Symbol(s) BIRC5; API4; EPR-1
External IDs OMIM: 603352 MGI: 1203517 Homologene: 37450
RNA expression pattern

More reference expression data

Human Mouse
Entrez 332 11799
Ensembl ENSG00000089685 ENSMUSG00000017716
Uniprot O15392 Q549P2
Refseq NM_001012270 (mRNA)
NP_001012270 (protein)
NM_001012273 (mRNA)
NP_001012273 (protein)
Location Chr 17: 73.72 - 73.73 Mb Chr 11: 117.67 - 117.67 Mb
Pubmed search [1] [2]

Baculoviral IAP repeat-containing 5 (survivin), also known as BIRC5, is a human gene.[1]

This gene is a member of the inhibitor of apoptosis (IAP) gene family, which encode negative regulatory proteins that prevent apoptotic cell death. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but this gene encodes proteins with only a single BIR domain. The encoded proteins also lack a C-terminus RING finger domain. Gene expression is high during fetal development and in most tumors yet low in adult tissues. Antisense transcripts are involved in the regulation of this gene's expression. At least four transcript variants encoding distinct isoforms have been found for this gene, but the full-length natures of only three of them have been determined.[1]

Survivin is a protein which is mostly known for its function as an inhibitor of programmed cell death (apoptosis). It is present during normal fetal development, but in an adult only detectable in rapidly proliferating cells. It is frequently detected in cancer cells and is believed to keep cancers alive by preventing apoptosis from occurring. High expressions of Survivin in cancer cells often correlates with a low survival rate in patients.[1]

Survivin has also been found to be a member of the chromosomal passenger complex and it plays an essential role in the proper progression through mitosis. Therefore, inhibiting Survivin is not a viable treatment for cancers, given that it would also disrupt proliferation of normal healthy cells. However, recent studies have indicated that survivin requires nuclear export for its anti-apoptotic function but not for its mitotic function. Cancer treatment by inhibiting the transport of survivin out of the nucleus remains a topic of interest.[2]


  1. ^ a b Entrez Gene: BIRC5 baculoviral IAP repeat-containing 5 (survivin).

Further reading

  • Ambrosini, G., Adida, C., Altieri, D.C. (1997) A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Abstract
  • Colnaghi, R., Connell, C.M., Barrett, R.M.A., Wheatley, S.P. (2006) Separating the Anti-apoptotic and Mitotic Roles of Survivin. Abstract
  • O'Driscoll L, Linehan R, Clynes M (2003). "Survivin: role in normal cells and in pathological conditions.". Current cancer drug targets 3 (2): 131-52. PMID 12678716.
  • Chiou SK, Jones MK, Tarnawski AS (2003). "Survivin - an anti-apoptosis protein: its biological roles and implications for cancer and beyond.". Med. Sci. Monit. 9 (4): PI25-9. PMID 12709681.
  • Ouhtit A, Matrougui K, Bengrine A, et al. (2007). "Survivin is not only a death encounter but also a survival protein for invading tumor cells.". Front. Biosci. 12: 1260-70. PMID 17127378.
  • Pennati M, Folini M, Zaffaroni N (2007). "Targeting survivin in cancer therapy: fulfilled promises and open questions.". Carcinogenesis 28 (6): 1133-9. doi:10.1093/carcin/bgm047. PMID 17341657.
  • Knauer SK, Mann W, Stauber RH (2007). "Survivin's dual role: an export's view.". Cell Cycle 6 (5): 518-21. PMID 17361097.
  • Wang TT, Qian XP, Liu BR (2007). "Survivin: potential role in diagnosis, prognosis and targeted therapy of gastric cancer.". World J. Gastroenterol. 13 (20): 2784-90. PMID 17569112.
  • Stauber RH, Mann W, Knauer SK (2007). "Nuclear and cytoplasmic survivin: molecular mechanism, prognostic, and therapeutic potential.". Cancer Res. 67 (13): 5999-6002. doi:10.1158/0008-5472.CAN-07-0494. PMID 17616652.
  • Bokarewa M, Tarkowski A, Magnusson M (2007). "Pathological survivin expression links viral infections with pathogenesis of erosive rheumatoid arthritis.". Scand. J. Immunol. 66 (2-3): 192-8. doi:10.1111/j.1365-3083.2007.01977.x. PMID 17635796.
  • Wolanin K, Piwocka K (2007). "[Role of survivin in mitosis]". Postepy Biochem. 53 (1): 10-8. PMID 17718383.
  • Altieri DC (1994). "Splicing of effector cell protease receptor-1 mRNA is modulated by an unusual retained intron.". Biochemistry 33 (46): 13848-55. PMID 7947793.
  • Altieri DC (1994). "Molecular cloning of effector cell protease receptor-1, a novel cell surface receptor for the protease factor Xa.". J. Biol. Chem. 269 (5): 3139-42. PMID 8106347.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
  • Ambrosini G, Adida C, Altieri DC (1997). "A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma.". Nat. Med. 3 (8): 917-21. PMID 9256286.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
  • Ambrosini G, Adida C, Sirugo G, Altieri DC (1998). "Induction of apoptosis and inhibition of cell proliferation by survivin gene targeting.". J. Biol. Chem. 273 (18): 11177-82. PMID 9556606.
  • Tamm I, Wang Y, Sausville E, et al. (1998). "IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs.". Cancer Res. 58 (23): 5315-20. PMID 9850056.
  • Li F, Ambrosini G, Chu EY, et al. (1999). "Control of apoptosis and mitotic spindle checkpoint by survivin.". Nature 396 (6711): 580-4. doi:10.1038/25141. PMID 9859993.
  • Mahotka C, Wenzel M, Springer E, et al. (2000). "Survivin-deltaEx3 and survivin-2B: two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties.". Cancer Res. 59 (24): 6097-102. PMID 10626797.
  • Suzuki A, Ito T, Kawano H, et al. (2000). "Survivin initiates procaspase 3/p21 complex formation as a result of interaction with Cdk4 to resist Fas-mediated cell death.". Oncogene 19 (10): 1346-53. doi:10.1038/sj.onc.1203429. PMID 10713676.
  • Verdecia MA, Huang H, Dutil E, et al. (2000). "Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement.". Nat. Struct. Biol. 7 (7): 602-8. doi:10.1038/76838. PMID 10876248.
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Survivin". A list of authors is available in Wikipedia.
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE