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Gene Review

BIRC2  -  baculoviral IAP repeat containing 2

Gallus gallus

Synonyms: IAP1, ITA
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Disease relevance of BIRC2

  • Like other IAPs, ch-IAP1 contains the N-terminal baculovirus IAP repeats and C-terminal RING finger motifs [1].
  • In contrast, ch-IAP1 expression levels were low in chicken cell lines transformed by several other unrelated tumor viruses. ch-IAP1 was expressed predominantly in the cytoplasm of the v-Rel-transformed cells. ch-IAP1 suppressed mammalian cell apoptosis induced by the overexpression of the interleukin-1-converting enzyme [1].
  • The sperm IAP substrates displayed similar protease digest patterns to alpha i of mouse S-49 lymphoma cells [2].
  • The involvement of GTP binding proteins in muscarinic acetylcholine receptor (mAChR) mediated responses of cultured chick embryonic cardiac muscle cells was studied by using islet activating protein (IAP) from Bordetella pertussis [3].

High impact information on BIRC2

  • The avian ITA is homologous to the baculoviral and mammalian inhibitor of apoptosis (IAP) proteins, which can prevent apoptosis by inhibition of specific caspases [4].
  • We investigated the role of ITA in embryonic chick sympathetic and dorsal root ganglionic neurons, which depend on nerve growth factor (NGF) for their survival [4].
  • Thus the induction of ITA expression seems to be an essential signaling event for survival of sympathetic and dorsal root ganglionic sensory neurons in response to NGF [4].
  • The 25-kD inhibitor of actin polymerization (25-kD IAP), isolated from turkey smooth muscle (Miron, T., M. Wilchek, and B. Geiger, 1988. Eur. J. Biochem. 178:543-553), is shown here to be a low molecular mass heat shock protein (HSP) [5].
  • Immunofluorescent microscopic localization indicated that after heat treatment, the levels of the 25-kD IAP were markedly increased and the protein was apparently associated with cytoplasmic granules [5].

Biological context of BIRC2

  • Expression of exogenous ch-IAP1 in temperature-sensitive v-Rel transformed spleen cells inhibited apoptosis of these cells at the nonpermissive temperature [1].
  • These apoptotic pathways are likely regulated by the concurrent expression of prosurvival molecules, including Bcl-2 and Bcl-x(L); phosphorylation of Bad; and high expression of inhibitor of apoptosis proteins chicken IAP1, IAP3, and survivin [6].
  • This study is the first to demonstrate the association of SNPs for caspase-1, IAP-1, and PSAP genes with SE vaccine and with pathogen challenge response in chickens [7].
  • The sire IAP-1 gene was significantly associated with spleen bacterial load (P=0.04) in the three combined dam-line crosses, and interacted with dam-line genetics (P = 0.01) for cecum content bacterial load [7].

Anatomical context of BIRC2


Associations of BIRC2 with chemical compounds

  • Membrane fractions were incubated with either islet-activating protein (IAP) or cholera toxin and analyzed by sodium dodecyl sulfate SDS-polyacrylamide gel electrophoresis for the presence of toxin-catalyzed ADP-ribosylated proteins [2].
  • The supernatant from a Lubrol PX-extracted 48,000 X g pellet fraction contained a Mr = 41,000 IAP substrate [2].
  • Inhibition of forskolin-stimulated cAMP accumulation by the muscarinic agonist carbachol was abolished in cultures pretreated with IAP [3].
  • Overexpression of the full-length ch-IAP1 suppresses mammalian cell apoptosis induced by the interleukin-1-converting enzyme (ICE), a member of the mammalian caspase family of cysteine proteases [9].
  • In the transcriptional level, the expressions of bcl-2 and IAP were decreased in these cell lines during actinomycin D-induced apoptosis, but no change was detected in the expression level of p53 [10].

Analytical, diagnostic and therapeutic context of BIRC2


  1. ch-IAP1, a member of the inhibitor-of-apoptosis protein family, is a mediator of the antiapoptotic activity of the v-Rel oncoprotein. You, M., Ku, P.T., Hrdlicková, R., Bose, H.R. Mol. Cell. Biol. (1997) [Pubmed]
  2. Evidence for a guanine nucleotide-binding regulatory protein in invertebrate and mammalian sperm. Identification by islet-activating protein-catalyzed ADP-ribosylation and immunochemical methods. Kopf, G.S., Woolkalis, M.J., Gerton, G.L. J. Biol. Chem. (1986) [Pubmed]
  3. Islet activating protein inhibits physiological responses evoked by cardiac muscarinic acetylcholine receptors. Role of guanosine triphosphate binding proteins in regulation of potassium permeability. Martin, J.M., Hunter, D.D., Nathanson, N.M. Biochemistry (1985) [Pubmed]
  4. The anti-apoptotic protein ITA is essential for NGF-mediated survival of embryonic chick neurons. Wiese, S., Digby, M.R., Gunnersen, J.M., Götz, R., Pei, G., Holtmann, B., Lowenthal, J., Sendtner, M. Nat. Neurosci. (1999) [Pubmed]
  5. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. Miron, T., Vancompernolle, K., Vandekerckhove, J., Wilchek, M., Geiger, B. J. Cell Biol. (1991) [Pubmed]
  6. The canonical intrinsic mitochondrial death pathway has a non-apoptotic role in signaling lens cell differentiation. Weber, G.F., Menko, A.S. J. Biol. Chem. (2005) [Pubmed]
  7. Candidate gene approach: potentional association of caspase-1, inhibitor of apoptosis protein-1, and prosaposin gene polymorphisms with response to Salmonella enteritidis challenge or vaccination in young chicks. Liu, W., Lamont, S.J. Anim. Biotechnol. (2003) [Pubmed]
  8. ITA, a vertebrate homologue of IAP that is expressed in T lymphocytes. Digby, M.R., Kimpton, W.G., York, J.J., Connick, T.E., Lowenthal, J.W. DNA Cell Biol. (1996) [Pubmed]
  9. Identification of v-Rel oncogene-induced inhibitor of apoptosis by differential display. You, M., Bose, H.R. Methods (1998) [Pubmed]
  10. The presence of a short form of p53 in chicken lymphoblastoid cell lines during apoptosis. Takagi, M., Takeda, T., Asada, Y., Sugimoto, C., Onuma, M., Ohashi, K. J. Vet. Med. Sci. (2006) [Pubmed]
  11. Linkage mapping of inhibitor of apoptosis protein-1 (IAP 1) to chicken chromosome 1. Goodenbour, J.M., Kaiser, M.G., Lamont, S.J. Anim. Genet. (2004) [Pubmed]
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