BIRC2

From Wikipedia, the free encyclopedia

Baculoviral IAP repeat-containing 2

PDB rendering based on 1qbh.

Available structures: 1qbh

Identifiers

Symbol(s)

BIRC2; API1; HIAP2; Hiap-2; MIHB; RNF48; cIAP1

External IDs

OMIM: 601712 MGI: 1197009 HomoloGene: 900

Gene ontology
Molecular Function:	• signal transducer activity • protein binding • zinc ion binding • metal ion binding
Cellular Component:	• intracellular
Biological Process:	• anti-apoptosis • cell surface receptor linked signal transduction • regulation of apoptosis • positive regulation of I-kappaB kinase/NF-kappaB cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001166 (mRNA)
NP_001157 (protein)

NM_007465 (mRNA)
NP_031491 (protein)

Location

Chr 11: 101.72 - 101.75 Mb

Chr 9: 7.82 - 7.84 Mb

Pubmed search

[1]

[2]

Baculoviral IAP repeat-containing 2, also known as BIRC2, is a human gene.

The protein encoded by this gene is a member of a family of proteins that inhibits apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. This encoded protein inhibits apoptosis induced by serum deprivation and menadione, a potent inducer of free radicals.^[1]

[edit] References

^ Entrez Gene: BIRC2 baculoviral IAP repeat-containing 2.

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Rothe M, Pan MG, Henzel WJ, et al. (1996). "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins.". Cell 83 (7): 1243–52. PMID 8548810.
Liston P, Roy N, Tamai K, et al. (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.
Uren AG, Pakusch M, Hawkins CJ, et al. (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. PMID 8643514.
Rajcan-Separovic E, Liston P, Lefebvre C, Korneluk RG (1997). "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. doi:10.1006/geno.1996.0579. PMID 8938457.
Shu HB, Takeuchi M, Goeddel DV (1997). "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. PMID 8943045.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Roy N, Deveraux QL, Takahashi R, et al. (1998). "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. PMID 9384571.
Deveraux QL, Roy N, Stennicke HR, et al. (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. PMID 9545235.
McCarthy JV, Ni J, Dixit VM (1998). "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase.". J. Biol. Chem. 273 (27): 16968–75. PMID 9642260.
Young SS, Liston P, Xuan JY, et al. (1999). "Genomic organization and physical map of the human inhibitors of apoptosis: HIAP1 and HIAP2.". Mamm. Genome 10 (1): 44–8. PMID 9892732.
Hinds MG, Norton RS, Vaux DL, Day CL (1999). "Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat.". Nat. Struct. Biol. 6 (7): 648–51. doi:10.1038/10701. PMID 10404221.
Verhagen AM, Ekert PG, Pakusch M, et al. (2000). "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins.". Cell 102 (1): 43–53. PMID 10929712.
Vucic D, Stennicke HR, Pisabarro MT, et al. (2001). "ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas.". Curr. Biol. 10 (21): 1359–66. PMID 11084335.
Werneburg BG, Zoog SJ, Dang TT, et al. (2001). "Molecular characterization of CD40 signaling intermediates.". J. Biol. Chem. 276 (46): 43334–42. doi:10.1074/jbc.M104994200. PMID 11562359.
Suzuki Y, Imai Y, Nakayama H, et al. (2001). "A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death.". Mol. Cell 8 (3): 613–21. PMID 11583623.
Verhagen AM, Silke J, Ekert PG, et al. (2002). "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. doi:10.1074/jbc.M109891200. PMID 11604410.
Mellström B, Ceña V, Lamas M, et al. (2002). "Gas1 is induced during and participates in excitotoxic neuronal death.". Mol. Cell. Neurosci. 19 (3): 417–29. doi:10.1006/mcne.2001.1092. PMID 11906213.
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.
Imoto I, Tsuda H, Hirasawa A, et al. (2002). "Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy.". Cancer Res. 62 (17): 4860–6. PMID 12208731.