Baculoviral IAP repeat-containing protein 3

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Protein BIRC3 PDB 2uvl.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesBIRC3, AIP1, API2, CIAP2, HAIP1, HIAP1, MALT2, MIHC, RNF49, c-IAP2, baculoviral IAP repeat containing 3, IAP-1
External IDsOMIM: 601721 MGI: 1197007 HomoloGene: 899 GeneCards: BIRC3
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for BIRC3
Genomic location for BIRC3
Band11q22.2Start102,317,450 bp[1]
End102,339,403 bp[1]
RNA expression pattern
PBB GE BIRC3 210538 s at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 11: 102.32 – 102.34 MbChr 9: 7.85 – 7.87 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Baculoviral IAP repeat-containing protein3 (also known as cIAP2) is a protein that in humans is encoded by the BIRC3 gene.[5][6]

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.[7]


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


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000023445 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032000 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G, Farahani R, McLean M, Ikeda JE, MacKenzie A, Korneluk RG (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.
  6. ^ Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV (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.
  7. ^ "Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3".
  8. ^ Deveraux QL, Roy N, Stennicke HR, Van Arsdale T, Zhou Q, Srinivasula SM, Alnemri ES, Salvesen GS, Reed JC (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.
  9. ^ Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, Gillard JW, Jaquith JB, Morris SJ, Barker PA (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.
  10. ^ a b Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (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.
  11. ^ a b Li X, Yang Y, Ashwell JD (2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature. 416 (6878): 345–7. doi:10.1038/416345a. PMID 11907583.
  12. ^ Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL (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.
  13. ^ Yoneda T, Imaizumi K, Maeda M, Yui D, Manabe T, Katayama T, Sato N, Gomi F, Morihara T, Mori Y, Miyoshi K, Hitomi J, Ugawa S, Yamada S, Okabe M, Tohyama M (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.
  14. ^ Mace PD, Linke K, Feltham R, Schumacher FR, Smith CA, Vaux DL, Silke J, Day CL (2008). "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". J. Biol. Chem. 283 (46): 31633–40. doi:10.1074/jbc.M804753200. PMID 18784070.

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