Biology:Baculoviral IAP repeat-containing protein 2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Baculoviral IAP repeat-containing protein 2 (also known as cIAP1) is a protein that in humans is encoded by the BIRC2 gene.[1][2]
Function
cIAP1 is a member of the Inhibitor of Apoptosis family that inhibit apoptosis by interfering with the activation of caspases.
Interactions
BIRC2 has been shown to interact with:
- CASP9,[3]
- DIABLO,[4][5]
- GSPT1,[4]
- HSP90B1,[6]
- HTRA2,[4][7]
- RIPK1,[8]
- RIPK2[9][10]
- TNFSF14,[11]
- TRAF1,[12][13][14]
- TRAF2,[12][13][14][15][16][17] and
- UBC.[6][8][18]
References
- ↑ "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. Bibcode: 1996Natur.379..349L.
- ↑ "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.
- ↑ "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.
- ↑ 4.0 4.1 4.2 "The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein". J. Biol. Chem. 278 (40): 38699–706. 2003. doi:10.1074/jbc.M303179200. PMID 12865429.
- ↑ "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins". Cell 102 (1): 43–53. 2000. doi:10.1016/S0092-8674(00)00009-X. PMID 10929712.
- ↑ 6.0 6.1 "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. 2008. doi:10.1038/cdd.2008.5. PMID 18239673.
- ↑ "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. 2002. doi:10.1074/jbc.M109891200. PMID 11604410.
- ↑ 8.0 8.1 "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.
- ↑ "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase". J. Biol. Chem. 273 (27): 16968–75. 1998. doi:10.1074/jbc.273.27.16968. PMID 9642260.
- ↑ "Identification of CARDIAK, a RIP-like kinase that associates with caspase-1". Curr. Biol. 8 (15): 885–8. 1998. doi:10.1016/S0960-9822(07)00352-1. PMID 9705938.
- ↑ "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. 2003. doi:10.1074/jbc.M208672200. PMID 12571250.
- ↑ 12.0 12.1 "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.
- ↑ 13.0 13.1 "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. 1996. doi:10.1073/pnas.93.24.13973. PMID 8943045. Bibcode: 1996PNAS...9313973S.
- ↑ 14.0 14.1 "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature 416 (6878): 345–7. 2002. doi:10.1038/416345a. PMID 11907583. Bibcode: 2002Natur.416..345L. https://zenodo.org/record/1233217.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "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. Bibcode: 1996PNAS...93.4974U.
- ↑ "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.
- ↑ "Small molecules destabilize cIAP1 by activating auto-ubiquitylation". J. Biol. Chem. 283 (14): 8961–8. 2008. doi:10.1074/jbc.M709525200. PMID 18230607.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "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. Bibcode: 1996PNAS...93.4974U.
- "Assignment of human inhibitor of apoptosis protein (IAP) genes xiap, hiap-1, and hiap-2 to chromosomes Xq25 and 11q22-q23 by fluorescence in situ hybridization.". Genomics 37 (3): 404–6. 1997. doi:10.1006/geno.1996.0579. PMID 8938457.
- "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. 1997. doi:10.1073/pnas.93.24.13973. PMID 8943045. Bibcode: 1996PNAS...9313973S.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases.". EMBO J. 16 (23): 6914–25. 1998. doi:10.1093/emboj/16.23.6914. PMID 9384571.
- "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.
- "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase.". J. Biol. Chem. 273 (27): 16968–75. 1998. doi:10.1074/jbc.273.27.16968. PMID 9642260.
- "Genomic organization and physical map of the human inhibitors of apoptosis: HIAP1 and HIAP2.". Mamm. Genome 10 (1): 44–8. 1999. doi:10.1007/s003359900940. PMID 9892732.
- "Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat.". Nat. Struct. Biol. 6 (7): 648–51. 1999. doi:10.1038/10701. PMID 10404221.
- "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins.". Cell 102 (1): 43–53. 2000. doi:10.1016/S0092-8674(00)00009-X. PMID 10929712.
- "ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas.". Curr. Biol. 10 (21): 1359–66. 2001. doi:10.1016/S0960-9822(00)00781-8. PMID 11084335.
- "Molecular characterization of CD40 signaling intermediates.". J. Biol. Chem. 276 (46): 43334–42. 2001. doi:10.1074/jbc.M104994200. PMID 11562359.
- "A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death.". Mol. Cell 8 (3): 613–21. 2001. doi:10.1016/S1097-2765(01)00341-0. PMID 11583623.
- "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. 2002. doi:10.1074/jbc.M109891200. PMID 11604410.
- "Gas1 is induced during and participates in excitotoxic neuronal death.". Mol. Cell. Neurosci. 19 (3): 417–29. 2002. doi:10.1006/mcne.2001.1092. PMID 11906213.
- "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2.". Nature 416 (6878): 345–7. 2002. doi:10.1038/416345a. PMID 11907583. Bibcode: 2002Natur.416..345L. https://zenodo.org/record/1233217.
- "Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy.". Cancer Res. 62 (17): 4860–6. 2002. PMID 12208731.
External links
- Human BIRC2 genome location and BIRC2 gene details page in the UCSC Genome Browser.
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