Baculoviral IAP repeat-containing protein 3

Baculoviral IAP repeat containing 3

PDB rendering based on 2uvl.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2UVL, 3EB5, 3EB6, 3M0A, 3M0D

Identifiers

Symbols

BIRC3 ; AIP1; API2; CIAP2; HAIP1; HIAP1; MALT2; MIHC; RNF49; c-IAP2

External IDs

OMIM: 601721 MGI: 1197007 HomoloGene: 899 IUPHAR: 2792 ChEMBL: 5335 GeneCards: BIRC3 Gene

Gene ontology
Molecular function	• ubiquitin-protein transferase activity • protein binding • zinc ion binding • ligase activity
Cellular component	• nucleus • nucleolus • cytoplasm • cytosol • protein complex • membrane raft
Biological process	• toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • apoptotic process • cell surface receptor signaling pathway • spermatogenesis • protein ubiquitination • positive regulation of protein ubiquitination • regulation of toll-like receptor signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • TRIF-dependent toll-like receptor signaling pathway • NIK/NF-kappaB signaling • regulation of RIG-I signaling pathway • negative regulation of phosphorylation • regulation of apoptotic process • negative regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB signaling • innate immune response • regulation of innate immune response • regulation of inflammatory response • protein heterooligomerization • regulation of necroptotic process • negative regulation of necroptotic process • necroptotic process • regulation of nucleotide-binding oligomerization domain containing signaling pathway • regulation of cysteine-type endopeptidase activity • negative regulation of reactive oxygen species metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
102.19 – 102.21 Mb

Chr 9:
7.85 – 7.87 Mb

PubMed search

Baculoviral IAP repeat-containing protein3 (also known as cIAP2) is a protein that in humans is encoded by the BIRC3 gene.^[1]^[2]

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.^[3]

Interactions

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

References

↑ 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.
↑ 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.
↑ "Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3".
↑ 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.
↑ 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.
↑ 6.0 6.1 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.
↑ 7.0 7.1 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.
↑ 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.
↑ 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.
↑ 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.

Bertoni F, Cavalli F, Cotter FE, Zucca E (2003). "Genetic alterations underlying the pathogenesis of MALT lymphoma". Hematol. J. 3 (1): 10–3. doi:10.1038/sj/thj/6200146. PMID 11960389.
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. doi:10.1073/pnas.93.10.4974. PMC 39390. 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.
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. PMC 1170295. 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. PMC 1170566. PMID 9545235.
Young SS, Liston P, Xuan JY; Xuan † et al. (1999). "Genomic organization and physical map of the human inhibitors of apoptosis: HIAP1 and HIAP2". Mamm. Genome 10 (1): 44–8. doi:10.1007/s003359900940. PMID 9892732.
Horrevoets AJ, Fontijn RD, van Zonneveld AJ et al. (1999). "Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes". Blood 93 (10): 3418–31. PMID 10233894.
Suzuki H, Motegi M, Akagi T et al. (1999). "API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue lymphoma with t(11;18)(q21;q21)". Blood 94 (9): 3270–1. PMID 10610122.
Huang H, Joazeiro CA, Bonfoco E et al. (2000). "The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7". J. Biol. Chem. 275 (35): 26661–4. doi:10.1074/jbc.C000199200. PMID 10862606.
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. doi:10.1016/S0092-8674(00)00009-X. PMID 10929712.
Baens M, Steyls A, Dierlamm J et al. (2001). "Structure of the MLT gene and molecular characterization of the genomic breakpoint junctions in the t(11;18)(q21;q21) of marginal zone B-cell lymphomas of MALT type". Genes Chromosomes Cancer 29 (4): 281–91. doi:10.1002/1098-2264(2000)9999:9999<::AID-GCC1036>3.0.CO;2-I. PMID 11066071.
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. doi:10.1016/S1097-2765(01)00341-0. PMID 11583623.
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.
Gordon GJ, Appasani K, Parcells JP et al. (2002). "Inhibitor of apoptosis protein-1 promotes tumor cell survival in mesothelioma". Carcinogenesis 23 (6): 1017–24. doi:10.1093/carcin/23.6.1017. PMID 12082024.
Sharief MK, Noori MA, Zoukos Y (2002). "Reduced expression of the inhibitor of apoptosis proteins in T cells from patients with multiple sclerosis following interferon-beta therapy". J. Neuroimmunol. 129 (1–2): 224–31. doi:10.1016/S0165-5728(02)00185-6. PMID 12161039.
Ekedahl J, Joseph B, Grigoriev MY et al. (2002). "Expression of inhibitor of apoptosis proteins in small- and non-small-cell lung carcinoma cells". Exp. Cell Res. 279 (2): 277–90. doi:10.1006/excr.2002.5608. PMID 12243753.

PDB gallery

2uvl: HUMAN BIR3 DOMAIN OF BACULOVIRAL INHIBITOR OF APOPTOSIS REPEAT-CONTAINING 3 (BIRC3)

Baculoviral IAP repeat-containing protein 3

Interactions

References

Further reading