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Baculoviral IAP repeat-containing protein 3

May 06, 2024

Baculoviral IAP repeat-containing protein3 (also known as cIAP2) is a protein that in humans is encoded by the BIRC3 gene.[5][6]

BIRC3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBIRC3, AIP1, API2, CIAP2, HAIP1, HIAP1, MALT2, MIHC, RNF49, c-IAP2, baculoviral IAP repeat containing 3, IAP-1
External IDsOMIM: 601721 MGI: 1197007 HomoloGene: 899 GeneCards: BIRC3
Orthologs
SpeciesHumanMouse
Entrez

330

11796

Ensembl

ENSG00000023445

ENSMUSG00000032000

UniProt

Q13489

O08863

RefSeq (mRNA)

NM_001165
NM_182962

NM_007464

RefSeq (protein)

NP_001156
NP_892007

NP_031490

Location (UCSC)Chr 11: 102.32 – 102.34 MbChr 9: 7.85 – 7.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7]

Interactions edit

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

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000023445 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032000 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. Bibcode:1996Natur.379..349L. doi:10.1038/379349a0. PMID 8552191. S2CID 4305853.
  6. ^ 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. S2CID 10694839.
  7. ^ "Entrez Gene: BIRC3 baculoviral IAP repeat-containing 3".
  8. ^ 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.
  9. ^ 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.
  10. ^ a b 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.
  11. ^ a b Li X, Yang Y, Ashwell JD (2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature. 416 (6878): 345–7. Bibcode:2002Natur.416..345L. doi:10.1038/416345a. PMID 11907583. S2CID 4325926.
  12. ^ 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. Bibcode:1996PNAS...93.4974U. doi:10.1073/pnas.93.10.4974. PMC 39390. PMID 8643514.
  13. ^ 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. S2CID 41164520.
  14. ^ 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. S2CID 13619386.

Further reading edit

  • 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. Bibcode:1996PNAS...93.4974U. 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, 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. S2CID 7052915.
  • 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. doi:10.1182/blood.V93.10.3418.410k23_3418_3431. 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. doi:10.1182/blood.V94.9.3270. 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. S2CID 3192775.
  • 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. S2CID 25986338.
  • 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. S2CID 25436077.
  • 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. Bibcode:2002Natur.416..345L. doi:10.1038/416345a. PMID 11907583. S2CID 4325926.
  • 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. S2CID 25809358.
  • 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.

External links edit

  • Human BIRC3 genome location and BIRC3 gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: Q13489 (Baculoviral IAP repeat-containing protein 3) at the PDBe-KB.

May 06, 2024
baculoviral, repeat, containing, protein, baculoviral, repeat, containing, protein3, also, known, ciap2, protein, that, humans, encoded, birc3, gene, birc3available, structurespdbortholog, search, pdbe, rcsblist, codes2uvl, 3eb5, 3eb6, 3m0a, 3m0didentifiersali. Baculoviral IAP repeat containing protein3 also known as cIAP2 is a protein that in humans is encoded by the BIRC3 gene 5 6 BIRC3Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes2UVL 3EB5 3EB6 3M0A 3M0DIdentifiersAliasesBIRC3 AIP1 API2 CIAP2 HAIP1 HIAP1 MALT2 MIHC RNF49 c IAP2 baculoviral IAP repeat containing 3 IAP 1External IDsOMIM 601721 MGI 1197007 HomoloGene 899 GeneCards BIRC3Gene location Human Chr Chromosome 11 human 1 Band11q22 2Start102 317 450 bp 1 End102 339 403 bp 1 Gene location Mouse Chr Chromosome 9 mouse 2 Band9 9 A1Start7 848 700 bp 2 End7 873 187 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inappendixlymph nodespleengallbladderpalpebral conjunctivathymusrectumsuperficial temporal arteryAchilles tendonbody of stomachTop expressed insecondary oocytespleenprostateegg cellthymusbloodleft colonjejunumsubcutaneous adipose tissueright lung lobeMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmetal ion binding cysteine type endopeptidase inhibitor activity involved in apoptotic process protein binding ubiquitin protein transferase activity transferase activity ubiquitin protein ligase activityCellular componentcytoplasm nucleoplasm membrane raft nucleus cytosol protein containing complexBiological processregulation of apoptotic process regulation of nucleotide binding oligomerization domain containing signaling pathway regulation of innate immune response regulation of toll like receptor signaling pathway negative regulation of necroptotic process inhibition of cysteine type endopeptidase activity involved in apoptotic process regulation of cysteine type endopeptidase activity regulation of RIG I signaling pathway regulation of tumor necrosis factor mediated signaling pathway negative regulation of apoptotic process tumor necrosis factor mediated signaling pathway mitotic spindle assembly cell surface receptor signaling pathway NIK NF kappaB signaling spermatogenesis regulation of inflammatory response positive regulation of I kappaB kinase NF kappaB signaling I kappaB kinase NF kappaB signaling positive regulation of protein ubiquitination apoptotic process protein ubiquitination protein deubiquitination regulation of necroptotic process protein heterooligomerization MyD88 independent toll like receptor signaling pathway TRIF dependent toll like receptor signaling pathway negative regulation of cysteine type endopeptidase activity involved in apoptotic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez33011796EnsemblENSG00000023445ENSMUSG00000032000UniProtQ13489O08863RefSeq mRNA NM 001165NM 182962NM 007464RefSeq protein NP 001156NP 892007NP 031490Location UCSC Chr 11 102 32 102 34 MbChr 9 7 85 7 87 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse 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 7 Contents 1 Interactions 2 References 3 Further reading 4 External linksInteractions editBaculoviral IAP repeat containing protein 3 has been shown to interact with CASP9 8 RIPK1 9 TRAF1 10 11 TRAF2 10 11 12 13 and UBE2D2 14 References edit a b c GRCh38 Ensembl release 89 ENSG00000023445 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000032000 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 Bibcode 1996Natur 379 349L doi 10 1038 379349a0 PMID 8552191 S2CID 4305853 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 S2CID 10694839 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 a b 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 a b Li X Yang Y Ashwell JD 2002 TNF RII and c IAP1 mediate ubiquitination and degradation of TRAF2 Nature 416 6878 345 7 Bibcode 2002Natur 416 345L doi 10 1038 416345a PMID 11907583 S2CID 4325926 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 Bibcode 1996PNAS 93 4974U 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 S2CID 41164520 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 S2CID 13619386 Further reading editBertoni 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 Bibcode 1996PNAS 93 4974U 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 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 S2CID 7052915 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 doi 10 1182 blood V93 10 3418 410k23 3418 3431 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 doi 10 1182 blood V94 9 3270 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 S2CID 3192775 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 lt AID GCC1036 gt 3 0 CO 2 I PMID 11066071 S2CID 25986338 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 S2CID 25436077 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 Bibcode 2002Natur 416 345L doi 10 1038 416345a PMID 11907583 S2CID 4325926 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 S2CID 25809358 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 External links editHuman BIRC3 genome location and BIRC3 gene details page in the UCSC Genome Browser Overview of all the structural information available in the PDB for UniProt Q13489 Baculoviral IAP repeat containing protein 3 at the PDBe KB Retrieved from https en wikipedia org w index php title Baculoviral IAP repeat containing protein 3 amp oldid 1142716181, wikipedia, wiki, book, books, library,

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