Baculoviral IAP repeat-containing protein 3: Difference between revisions

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{{Infobox gene}}
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'''Baculoviral IAP repeat-containing protein3''' (also known as '''cIAP2''') is a [[protein]] that in humans is encoded by the ''BIRC3'' [[gene]].<ref name="pmid8552191">{{cite journal | vauthors = Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G, Farahani R, McLean M, Ikeda JE, MacKenzie A, Korneluk RG | title = Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes | journal = Nature | volume = 379 | issue = 6563 | pages = 349–53 |date=February 1996 | pmid = 8552191 | pmc =  | doi = 10.1038/379349a0 }}</ref><ref name="pmid8548810">{{cite journal | vauthors = Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV | title = The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins | journal = Cell | volume = 83 | issue = 7 | pages = 1243–52 |date=February 1996 | pmid = 8548810 | pmc =  | doi =10.1016/0092-8674(95)90149-3 }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BIRC3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2uvl.
| PDB = {{PDB2|2uvl}}
| Name = Baculoviral IAP repeat-containing 3
| HGNCid = 591
| Symbol = BIRC3
| AltSymbols =; AIP1; API2; CIAP2; HAIP1; HIAP1; MALT2; MIHC; RNF49
| OMIM = 601721
| ECnumber =
| Homologene = 899
| MGIid = 1197007
  | GeneAtlas_image1 = PBB_GE_BIRC3_210538_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 330
    | Hs_Ensembl = ENSG00000023445
    | Hs_RefseqProtein = NP_001156
    | Hs_RefseqmRNA = NM_001165
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 101693404
    | Hs_GenLoc_end = 101713658
    | Hs_Uniprot = Q13489
    | Mm_EntrezGene = 11796
    | Mm_Ensembl =   
    | Mm_RefseqmRNA = NM_007464
    | Mm_RefseqProtein = NP_031490
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =   
  }}
}}
'''Baculoviral IAP repeat-containing 3''', also known as '''BIRC3''', is a human [[gene]].


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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. 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 amino acid sequence predicts three baculovirus IAP repeat domains and a ring finger domain. Transcript variants encoding the same isoform have been identified.<ref>{{cite web | title = Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=330| accessdate = }}</ref>
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=330| accessdate = }}</ref>
}}
}}
==Interactions==
Baculoviral IAP repeat-containing protein 3 has been shown to [[Protein-protein interaction|interact]] with:
* [[Caspase-9|CASP9]],<ref name = pmid9545235>{{cite journal | vauthors = Deveraux QL, Roy N, Stennicke HR, Van Arsdale T, Zhou Q, Srinivasula SM, Alnemri ES, Salvesen GS, Reed JC | title = IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases | journal = EMBO J. | volume = 17 | issue = 8 | pages = 2215–23 | year = 1998 | pmid = 9545235 | pmc = 1170566 | doi = 10.1093/emboj/17.8.2215 }}</ref>
* [[RIPK1]],<ref name = pmid18570872>{{cite journal | vauthors = Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, Gillard JW, Jaquith JB, Morris SJ, Barker PA | title = cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination | journal = Mol. Cell | volume = 30 | issue = 6 | pages = 689–700 | year = 2008 | pmid = 18570872 | doi = 10.1016/j.molcel.2008.05.014 }}</ref>
* [[TRAF1]],<ref name = pmid9384571>{{cite journal | vauthors = Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC | title = The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases | journal = EMBO J. | volume = 16 | issue = 23 | pages = 6914–25 | year = 1997 | pmid = 9384571 | pmc = 1170295 | doi = 10.1093/emboj/16.23.6914 }}</ref><ref name = pmid11907583>{{cite journal | vauthors = Li X, Yang Y, Ashwell JD | title = TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2 | journal = Nature | volume = 416 | issue = 6878 | pages = 345–7 | year = 2002 | pmid = 11907583 | doi = 10.1038/416345a }}</ref>
* [[TRAF2]],<ref name = pmid9384571/><ref name = pmid11907583/><ref name = pmid8643514>{{cite journal | vauthors = Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL | title = Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 10 | pages = 4974–8 | year = 1996 | pmid = 8643514 | pmc = 39390 | doi = 10.1073/pnas.93.10.4974}}</ref><ref name = pmid10753917>{{cite journal | vauthors = 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 | title = Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein | journal = J. Biol. Chem. | volume = 275 | issue = 15 | pages = 11114–20 | year = 2000 | pmid = 10753917 | doi = 10.1074/jbc.275.15.11114}}</ref>  and
* [[UBE2D2]].<ref name = pmid18784070>{{cite journal | vauthors = Mace PD, Linke K, Feltham R, Schumacher FR, Smith CA, Vaux DL, Silke J, Day CL | title = Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment | journal = J. Biol. Chem. | volume = 283 | issue = 46 | pages = 31633–40 | year = 2008 | pmid = 18784070 | doi = 10.1074/jbc.M804753200 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Bertoni F, Cavalli F, Cotter FE, Zucca E |title=Genetic alterations underlying the pathogenesis of MALT lymphoma. |journal=Hematol. J. |volume=3 |issue= 1 |pages= 10-3 |year= 2003 |pmid= 11960389 |doi= 10.1038/sj/thj/6200146 }}
*{{cite journal  | vauthors=Bertoni F, Cavalli F, Cotter FE, Zucca E |title=Genetic alterations underlying the pathogenesis of MALT lymphoma |journal=Hematol. J. |volume=3 |issue= 1 |pages= 10–3 |year= 2003 |pmid= 11960389 |doi= 10.1038/sj/thj/6200146 }}
*{{cite journal  | author=Rothe M, Pan MG, Henzel WJ, ''et al.'' |title=The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. |journal=Cell |volume=83 |issue= 7 |pages= 1243-52 |year= 1996 |pmid= 8548810 |doi=  }}
*{{cite journal  | vauthors=Uren AG, Pakusch M, Hawkins CJ |title=Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 4974–8 |year= 1996 |pmid= 8643514 |doi=10.1073/pnas.93.10.4974 | pmc=39390  |display-authors=etal}}
*{{cite journal  | author=Liston P, Roy N, Tamai K, ''et al.'' |title=Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes. |journal=Nature |volume=379 |issue= 6563 |pages= 349-53 |year= 1996 |pmid= 8552191 |doi= 10.1038/379349a0 }}
*{{cite journal  | vauthors=Rajcan-Separovic E, Liston P, Lefebvre C, Korneluk RG |title=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 |journal=Genomics |volume=37 |issue= 3 |pages= 404–6 |year= 1997 |pmid= 8938457 |doi= 10.1006/geno.1996.0579 }}
*{{cite journal  | author=Uren AG, Pakusch M, Hawkins CJ, ''et al.'' |title=Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 4974-8 |year= 1996 |pmid= 8643514 |doi=  }}
*{{cite journal  | vauthors=Roy N, Deveraux QL, Takahashi R |title=The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases |journal=EMBO J. |volume=16 |issue= 23 |pages= 6914–25 |year= 1998 |pmid= 9384571 |doi= 10.1093/emboj/16.23.6914 | pmc=1170295 |display-authors=etal}}
*{{cite journal  | author=Rajcan-Separovic E, Liston P, Lefebvre C, Korneluk RG |title=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. |journal=Genomics |volume=37 |issue= 3 |pages= 404-6 |year= 1997 |pmid= 8938457 |doi= 10.1006/geno.1996.0579 }}
*{{cite journal  | vauthors=Deveraux QL, Roy N, Stennicke HR |title=IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases |journal=EMBO J. |volume=17 |issue= 8 |pages= 2215–23 |year= 1998 |pmid= 9545235 |doi= 10.1093/emboj/17.8.2215  | pmc=1170566 |display-authors=etal}}
*{{cite journal  | author=Roy N, Deveraux QL, Takahashi R, ''et al.'' |title=The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. |journal=EMBO J. |volume=16 |issue= 23 |pages= 6914-25 |year= 1998 |pmid= 9384571 |doi= 10.1093/emboj/16.23.6914 }}
*{{cite journal  | vauthors=Young SS, Liston P, Xuan JY |title=Genomic organization and physical map of the human inhibitors of apoptosis: HIAP1 and HIAP2 |journal=Mamm. Genome |volume=10 |issue= 1 |pages= 44–8 |year= 1999 |pmid= 9892732 |doi=10.1007/s003359900940  |display-authors=etal}}
*{{cite journal  | author=Deveraux QL, Roy N, Stennicke HR, ''et al.'' |title=IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. |journal=EMBO J. |volume=17 |issue= 8 |pages= 2215-23 |year= 1998 |pmid= 9545235 |doi= 10.1093/emboj/17.8.2215 }}
*{{cite journal  | vauthors=Horrevoets AJ, Fontijn RD, van Zonneveld AJ |title=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 |journal=Blood |volume=93 |issue= 10 |pages= 3418–31 |year= 1999 |pmid= 10233894 |doi= |display-authors=etal}}
*{{cite journal  | author=Young SS, Liston P, Xuan JY, ''et al.'' |title=Genomic organization and physical map of the human inhibitors of apoptosis: HIAP1 and HIAP2. |journal=Mamm. Genome |volume=10 |issue= 1 |pages= 44-8 |year= 1999 |pmid= 9892732 |doi=  }}
*{{cite journal  | vauthors=Suzuki H, Motegi M, Akagi T |title=API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue lymphoma with t(11;18)(q21;q21) |journal=Blood |volume=94 |issue= 9 |pages= 3270–1 |year= 1999 |pmid= 10610122 |doi=  |display-authors=etal}}
*{{cite journal  | author=Horrevoets AJ, Fontijn RD, van Zonneveld AJ, ''et al.'' |title=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. |journal=Blood |volume=93 |issue= 10 |pages= 3418-31 |year= 1999 |pmid= 10233894 |doi= }}
*{{cite journal  | vauthors=Huang H, Joazeiro CA, Bonfoco E |title=The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7 |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 26661–4 |year= 2000 |pmid= 10862606 |doi= 10.1074/jbc.C000199200 |display-authors=etal}}
*{{cite journal  | author=Suzuki H, Motegi M, Akagi T, ''et al.'' |title=API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue lymphoma with t(11;18)(q21;q21) |journal=Blood |volume=94 |issue= 9 |pages= 3270-1 |year= 1999 |pmid= 10610122 |doi=  }}
*{{cite journal  | vauthors=Verhagen AM, Ekert PG, Pakusch M |title=Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins |journal=Cell |volume=102 |issue= 1 |pages= 43–53 |year= 2000 |pmid= 10929712 |doi=10.1016/S0092-8674(00)00009-X |display-authors=etal}}
*{{cite journal  | author=Huang H, Joazeiro CA, Bonfoco E, ''et al.'' |title=The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 26661-4 |year= 2000 |pmid= 10862606 |doi= 10.1074/jbc.C000199200 }}
*{{cite journal  | vauthors=Baens M, Steyls A, Dierlamm J |title=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 |journal=Genes Chromosomes Cancer |volume=29 |issue= 4 |pages= 281–91 |year= 2001 |pmid= 11066071 |doi=10.1002/1098-2264(2000)9999:9999<::AID-GCC1036>3.0.CO;2-I  |display-authors=etal}}
*{{cite journal  | author=Verhagen AM, Ekert PG, Pakusch M, ''et al.'' |title=Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. |journal=Cell |volume=102 |issue= 1 |pages= 43-53 |year= 2000 |pmid= 10929712 |doi= }}
*{{cite journal  | vauthors=Werneburg BG, Zoog SJ, Dang TT |title=Molecular characterization of CD40 signaling intermediates |journal=J. Biol. Chem. |volume=276 |issue= 46 |pages= 43334–42 |year= 2001 |pmid= 11562359 |doi= 10.1074/jbc.M104994200 |display-authors=etal}}
*{{cite journal  | author=Baens M, Steyls A, Dierlamm J, ''et al.'' |title=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. |journal=Genes Chromosomes Cancer |volume=29 |issue= 4 |pages= 281-91 |year= 2001 |pmid= 11066071 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Imai Y, Nakayama H |title=A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death |journal=Mol. Cell |volume=8 |issue= 3 |pages= 613–21 |year= 2001 |pmid= 11583623 |doi=10.1016/S1097-2765(01)00341-0 |display-authors=etal}}
*{{cite journal  | author=Werneburg BG, Zoog SJ, Dang TT, ''et al.'' |title=Molecular characterization of CD40 signaling intermediates. |journal=J. Biol. Chem. |volume=276 |issue= 46 |pages= 43334-42 |year= 2001 |pmid= 11562359 |doi= 10.1074/jbc.M104994200 }}
*{{cite journal  | vauthors=Li X, Yang Y, Ashwell JD |title=TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2 |journal=Nature |volume=416 |issue= 6878 |pages= 345–7 |year= 2002 |pmid= 11907583 |doi= 10.1038/416345a }}
*{{cite journal  | author=Suzuki Y, Imai Y, Nakayama H, ''et al.'' |title=A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 613-21 |year= 2001 |pmid= 11583623 |doi=  }}
*{{cite journal  | vauthors=Gordon GJ, Appasani K, Parcells JP |title=Inhibitor of apoptosis protein-1 promotes tumor cell survival in mesothelioma |journal=Carcinogenesis |volume=23 |issue= 6 |pages= 1017–24 |year= 2002 |pmid= 12082024 |doi=10.1093/carcin/23.6.1017 |display-authors=etal}}
*{{cite journal  | author=Li X, Yang Y, Ashwell JD |title=TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. |journal=Nature |volume=416 |issue= 6878 |pages= 345-7 |year= 2002 |pmid= 11907583 |doi= 10.1038/416345a }}
*{{cite journal  | vauthors=Sharief MK, Noori MA, Zoukos Y |title=Reduced expression of the inhibitor of apoptosis proteins in T cells from patients with multiple sclerosis following interferon-beta therapy |journal=J. Neuroimmunol. |volume=129 |issue= 1–2 |pages= 224–31 |year= 2002 |pmid= 12161039 |doi=10.1016/S0165-5728(02)00185-6  }}
*{{cite journal  | author=Gordon GJ, Appasani K, Parcells JP, ''et al.'' |title=Inhibitor of apoptosis protein-1 promotes tumor cell survival in mesothelioma. |journal=Carcinogenesis |volume=23 |issue= 6 |pages= 1017-24 |year= 2002 |pmid= 12082024 |doi=  }}
*{{cite journal  | vauthors=Ekedahl J, Joseph B, Grigoriev MY |title=Expression of inhibitor of apoptosis proteins in small- and non-small-cell lung carcinoma cells |journal=Exp. Cell Res. |volume=279 |issue= 2 |pages= 277–90 |year= 2002 |pmid= 12243753 |doi=10.1006/excr.2002.5608 |display-authors=etal}}
*{{cite journal  | author=Sharief MK, Noori MA, Zoukos Y |title=Reduced expression of the inhibitor of apoptosis proteins in T cells from patients with multiple sclerosis following interferon-beta therapy. |journal=J. Neuroimmunol. |volume=129 |issue= 1-2 |pages= 224-31 |year= 2002 |pmid= 12161039 |doi=  }}
*{{cite journal  | author=Ekedahl J, Joseph B, Grigoriev MY, ''et al.'' |title=Expression of inhibitor of apoptosis proteins in small- and non-small-cell lung carcinoma cells. |journal=Exp. Cell Res. |volume=279 |issue= 2 |pages= 277-90 |year= 2002 |pmid= 12243753 |doi=  }}
}}
}}
{{refend}}
{{refend}}
==External links==
* {{UCSC gene info|BIRC3}}
{{PDB Gallery|geneid=330}}
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{{protein-stub}}
[[Category:Oncogenes]]
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Revision as of 17:40, 5 December 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

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

  1. 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.
  2. 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.
  3. "Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3".
  4. 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.
  5. 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. 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. 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.
  8. 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.
  9. 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.
  10. 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.

Further reading

External links