Biology:Baculoviral IAP repeat-containing protein 3

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Baculoviral IAP repeat-containing protein3 (also known as cIAP2) is a protein that in humans is encoded by the BIRC3 gene.[1][2]

cIAP2 is a member of the inhibitor of apoptosis family that inhibit apoptosis by interfering with the activation of caspases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. The cIAP2 protein contains three BIR domains, a UBA domain, a CARD domain and a RING finger domain. Transcript variants encoding the same isoform have been identified.[3]

Interactions

Baculoviral IAP repeat-containing protein 3 has been shown to interact with:

References

  1. "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes". Nature 379 (6563): 349–53. February 1996. doi:10.1038/379349a0. PMID 8552191. Bibcode1996Natur.379..349L. 
  2. "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins". Cell 83 (7): 1243–52. February 1996. doi:10.1016/0092-8674(95)90149-3. PMID 8548810. 
  3. "Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=330. 
  4. "IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases". EMBO J. 17 (8): 2215–23. 1998. doi:10.1093/emboj/17.8.2215. PMID 9545235. 
  5. "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell 30 (6): 689–700. 2008. doi:10.1016/j.molcel.2008.05.014. PMID 18570872. 
  6. 6.0 6.1 "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. 16 (23): 6914–25. 1997. doi:10.1093/emboj/16.23.6914. PMID 9384571. 
  7. 7.0 7.1 "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature 416 (6878): 345–7. 2002. doi:10.1038/416345a. PMID 11907583. Bibcode2002Natur.416..345L. https://zenodo.org/record/1233217. 
  8. "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. 1996. doi:10.1073/pnas.93.10.4974. PMID 8643514. Bibcode1996PNAS...93.4974U. 
  9. "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. 275 (15): 11114–20. 2000. doi:10.1074/jbc.275.15.11114. PMID 10753917. 
  10. "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". J. Biol. Chem. 283 (46): 31633–40. 2008. doi:10.1074/jbc.M804753200. PMID 18784070. 

Further reading

External links