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Baculoviral IAP repeat containing 2
Protein BIRC2 PDB 1qbh.png
PDB rendering based on 1qbh.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols BIRC2 ; API1; HIAP2; Hiap-2; MIHB; RNF48; c-IAP1; cIAP1
External IDs OMIM601712 MGI1197009 HomoloGene900 ChEMBL: 5462 GeneCards: BIRC2 Gene
RNA expression pattern
PBB GE BIRC2 202076 at tn.png
More reference expression data
Species Human Mouse
Entrez 329 11797
Ensembl ENSG00000110330 ENSMUSG00000057367
UniProt Q13490 Q62210
RefSeq (mRNA) NM_001166 NM_007465
RefSeq (protein) NP_001157 NP_031491
Location (UCSC) Chr 11:
102.22 – 102.25 Mb
Chr 9:
7.82 – 7.84 Mb
PubMed search [1] [2]

Baculoviral IAP repeat-containing protein 2 (also known as cIAP1) is a protein that in humans is encoded by the BIRC2 gene.[1][2]


cIAP1 is a member of the Inhibitor of Apoptosis family that inhibit apoptosis by interfering with the activation of caspases.


BIRC2 has been shown to interact with:


  1. ^ Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G et al. (February 1996). "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes". Nature 379 (6563): 349–53. doi:10.1038/379349a0. PMID 8552191. 
  2. ^ Rothe M, Pan M, Henzel W, Ayres T, Goeddel D (February 1996). "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins". Cell 83 (7): 1243–52. doi:10.1016/0092-8674(95)90149-3. PMID 8548810. 
  3. ^ Deveraux Q, Roy N, Stennicke H, Van Arsdale T, Zhou Q, Srinivasula S et al. (1998). "IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases". EMBO J. 17 (8): 2215–23. doi:10.1093/emboj/17.8.2215. PMC 1170566. PMID 9545235. 
  4. ^ a b c Hegde R, Srinivasula S, Datta P, Madesh M, Wassell R, Zhang Z et al. (2003). "The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein". J. Biol. Chem. 278 (40): 38699–706. doi:10.1074/jbc.M303179200. PMID 12865429. 
  5. ^ Verhagen A, Ekert P, Pakusch M, Silke J, Connolly L, Reid G et al. (2000). "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins". Cell 102 (1): 43–53. doi:10.1016/S0092-8674(00)00009-X. PMID 10929712. 
  6. ^ a b Didelot C, Lanneau D, Brunet M, Bouchot A, Cartier J, Jacquel A et al. (2008). "Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation". Cell Death Differ. 15 (5): 859–66. doi:10.1038/cdd.2008.5. PMID 18239673. 
  7. ^ Verhagen A, Silke J, Ekert P, Pakusch M, Kaufmann H, Connolly L et al. (2002). "HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins". J. Biol. Chem. 277 (1): 445–54. doi:10.1074/jbc.M109891200. PMID 11604410. 
  8. ^ a b Bertrand M, Milutinovic S, Dickson K, Ho W, Boudreault A, Durkin J et al. (2008). "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell 30 (6): 689–700. doi:10.1016/j.molcel.2008.05.014. PMID 18570872. 
  9. ^ McCarthy J, Ni J, Dixit V (1998). "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase". J. Biol. Chem. 273 (27): 16968–75. doi:10.1074/jbc.273.27.16968. PMID 9642260. 
  10. ^ Thome M, Hofmann K, Burns K, Martinon F, Bodmer J, Mattmann C et al. (1998). "Identification of CARDIAK, a RIP-like kinase that associates with caspase-1". Curr. Biol. 8 (15): 885–8. doi:10.1016/S0960-9822(07)00352-1. PMID 9705938. 
  11. ^ Kuai J, Nickbarg E, Wooters J, Qiu Y, Wang J, Lin L (2003). "Endogenous association of TRAF2, TRAF3, cIAP1, and Smac with lymphotoxin beta receptor reveals a novel mechanism of apoptosis". J. Biol. Chem. 278 (16): 14363–9. doi:10.1074/jbc.M208672200. PMID 12571250. 
  12. ^ a b Roy N, Deveraux Q, Takahashi R, Salvesen G, Reed J (1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571. 
  13. ^ a b Shu H, Takeuchi M, Goeddel D (1996). "The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13973–8. doi:10.1073/pnas.93.24.13973. PMC 19479. PMID 8943045. 
  14. ^ a b Li X, Yang Y, Ashwell J (2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature 416 (6878): 345–7. doi:10.1038/416345a. PMID 11907583. 
  15. ^ Rual J, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  16. ^ Uren A, Pakusch M, Hawkins C, Puls K, Vaux D (1996). "Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 4974–8. doi:10.1073/pnas.93.10.4974. PMC 39390. PMID 8643514. 
  17. ^ Yoneda T, Imaizumi K, Maeda M, Yui D, Manabe T, Katayama T et al. (2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. 275 (15): 11114–20. doi:10.1074/jbc.275.15.11114. PMID 10753917. 
  18. ^ Sekine K, Takubo K, Kikuchi R, Nishimoto M, Kitagawa M, Abe F et al. (2008). "Small molecules destabilize cIAP1 by activating auto-ubiquitylation". J. Biol. Chem. 283 (14): 8961–8. doi:10.1074/jbc.M709525200. PMID 18230607. 

Further reading[edit]