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Baculoviral IAP repeat-containing protein 3

Protein-coding gene in the species Homo sapiens

Protein-coding gene in the species Homo sapiens

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

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.

Interactions

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

  • CASP9,
  • RIPK1,
  • TRAF1,
  • TRAF2, and
  • UBE2D2.

References

References

  1. (February 1996). "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes". Nature.
  2. (February 1996). "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins". Cell.
  3. "Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3".
  4. (1998). "IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases". EMBO J..
  5. (2008). "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell.
  6. (1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J..
  7. (2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature.
  8. (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..
  9. (2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem..
  10. (2008). "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". J. Biol. Chem..
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