Baculoviral IAP repeat-containing protein 3

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Baculoviral IAP repeat-containing protein 3

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Baculoviral IAP repeat containing 3

PDB rendering based on 2uvl.

Available structures

PDB

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 GeneCards: BIRC3 Gene

Gene Ontology
Molecular function	• ubiquitin-protein ligase activity • protein binding • zinc ion binding • metal ion binding
Cellular component	• intracellular • nucleus • cytoplasm
Biological process	• anti-apoptosis • cell surface receptor signaling pathway • regulation of toll-like receptor signaling pathway • NIK/NF-kappaB cascade • regulation of RIG-I signaling pathway • regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB cascade • regulation of innate immune response • regulation of inflammatory response • regulation of nucleotide-binding oligomerization domain containing signaling pathway • regulation of cysteine-type endopeptidase activity
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

[1]

[2]

Baculoviral IAP repeat-containing protein 3 (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 TRAF1,^[4]^[5] TRAF2,^[4]^[5]^[6]^[7] RIPK1,^[8] Caspase-9^[9] and UBE2D2.^[10]

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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=330.
^ ^a ^b Roy, N; Deveraux Q L, Takahashi R, Salvesen G S, Reed J C (December 1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. (ENGLAND) 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. ISSN 0261-4189. . PMID 9384571. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170295.
^ ^a ^b Li, Xiaoming; Yang Yili, Ashwell Jonathan D (March 2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature (England) 416 (6878): 345–7. doi:10.1038/416345a. ISSN 0028-0836. PMID 11907583.
^ Uren, A G; Pakusch M, Hawkins C J, Puls K L, Vaux D L (May. 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. (UNITED STATES) 93 (10): 4974–8. doi:10.1073/pnas.93.10.4974. ISSN 0027-8424. . PMID 8643514. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=39390.
^ 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 (April 2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. (UNITED STATES) 275 (15): 11114–20. doi:10.1074/jbc.275.15.11114. ISSN 0021-9258. PMID 10753917.
^ Bertrand, Mathieu J M; Milutinovic Snezana, Dickson Kathleen M, Ho Wai Chi, Boudreault Alain, Durkin Jon, Gillard John W, Jaquith James B, Morris Stephen J, Barker Philip A (June 2008). "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell (United States) 30 (6): 689–700. doi:10.1016/j.molcel.2008.05.014. PMID 18570872.
^ Deveraux, Q L; Roy N, Stennicke H R, Van Arsdale T, Zhou Q, Srinivasula S M, Alnemri E S, Salvesen G S, Reed J C (April 1998). "IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases". EMBO J. (ENGLAND) 17 (8): 2215–23. doi:10.1093/emboj/17.8.2215. ISSN 0261-4189. . PMID 9545235. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170566.
^ Mace, Peter D; Linke Katrin, Feltham Rebecca, Schumacher Frances-Rose, Smith Clyde A, Vaux David L, Silke John, Day Catherine L (November 2008). "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". J. Biol. Chem. (United States) 283 (46): 31633–40. doi:10.1074/jbc.M804753200. ISSN 0021-9258. 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. . PMID 8643514. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=39390.
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. . PMID 9384571. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170295.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170566.
Young SS, Liston P, Xuan JY, et al.; Xuan † (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)

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