CASP8AP2

CASP8AP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LR8
Identifiers
Aliases	CASP8AP2, CED-4, FLASH, RIP25, caspase 8 associated protein 2
External IDs	MGI: 1349399 HomoloGene: 8066 GeneCards: CASP8AP2
Gene ontology Molecular function • peptidase activator activity involved in apoptotic process • DNA binding • death receptor binding • transcription corepressor activity • SUMO polymer binding • protein binding • cysteine-type endopeptidase activator activity involved in apoptotic process Cellular component • cytoplasm • PML body • mitochondrion • nucleus Biological process • regulation of transcription, DNA-templated • Fas signaling pathway • transcription, DNA-templated • cellular response to mechanical stimulus • apoptotic signaling pathway • cell cycle • activation of cysteine-type endopeptidase activity involved in apoptotic process • extrinsic apoptotic signaling pathway via death domain receptors • signal transduction • apoptotic process • negative regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9994	26885
Ensembl	ENSG00000118412	ENSMUSG00000028282
UniProt	Q9UKL3	Q9WUF3
RefSeq (mRNA)	NM_012115 NM_001137667 NM_001137668	NM_001122978 NM_011997
RefSeq (protein)	NP_001131139.1 NP_001131140.1 NP_036247.1	NP_001116450.1 NP_036127.2
Location (UCSC)	Chr 6: 89.83 – 89.87 Mb	Chr 4: 32.62 – 32.65 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

CASP8-associated protein 2 is a protein that in humans is encoded by the CASP8AP2 gene.^[3][4][5][6]

Function

This protein is highly similar to FLASH, a mouse apoptotic protein identified by its interaction with the death-effector domain (DED) of caspase 8. Studies of FLASH protein suggested that this protein may be a component of the death-inducing signaling complex that includes Fas receptor, Fas-binding adapter FADD, and caspase 8, and plays a regulatory role in Fas-mediated apoptosis.^[6]

Interactions

CASP8AP2 has been shown to interact with TRAF2.^[7]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Imai Y, Kimura T, Murakami A, Yajima N, Sakamaki K, Yonehara S (Jun 1999). "The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosis". Nature. 398 (6730): 777–85. doi:10.1038/19709. PMID 10235259.
4. Milovic-Holm K, Krieghoff E, Jensen K, Will H, Hofmann TG (Jan 2007). "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies". EMBO J. 26 (2): 391–401. doi:10.1038/sj.emboj.7601504. PMC 1783462. PMID 17245429.
5. Barcaroli D, Dinsdale D, Neale MH, Bongiorno-Borbone L, Ranalli M, Munarriz E, Sayan AE, McWilliam JM, Smith TM, Fava E, Knight RA, Melino G, De Laurenzi V (Oct 2006). "FLASH is an essential component of Cajal bodies". Proc. Natl. Acad. Sci. U.S.A. 103 (40): 14802–7. doi:10.1073/pnas.0604225103. PMC 1578500. PMID 17003126.
6. "Entrez Gene: CASP8AP2 CASP8 associated protein 2".
7. Choi YH, Kim KB, Kim HH, Hong GS, Kwon YK, Chung CW, Park YM, Shen ZJ, Kim BJ, Lee SY, Jung YK (Jul 2001). "FLASH coordinates NF-kappa B activity via TRAF2". J. Biol. Chem. 276 (27): 25073–7. doi:10.1074/jbc.M102941200. PMID 11340079.

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Koonin EV, Aravind L, Hofmann K, Tschopp J, Dixit VM (1999). "Apoptosis. Searching for FLASH domains". Nature. 401 (6754): 662; discussion 662–3. doi:10.1038/44317. PMID 10537104.
• Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
• Choi YH, Kim KB, Kim HH, Hong GS, Kwon YK, Chung CW, Park YM, Shen ZJ, Kim BJ, Lee SY, Jung YK (2001). "FLASH coordinates NF-kappa B activity via TRAF2". J. Biol. Chem. 276 (27): 25073–7. doi:10.1074/jbc.M102941200. PMID 11340079.
• Kino T, Chrousos GP (2003). "Tumor necrosis factor alpha receptor- and Fas-associated FLASH inhibit transcriptional activity of the glucocorticoid receptor by binding to and interfering with its interaction with p160 type nuclear receptor coactivators". J. Biol. Chem. 278 (5): 3023–9. doi:10.1074/jbc.M209234200. PMID 12477726.
• Jun JI, Chung CW, Lee HJ, Pyo JO, Lee KN, Kim NS, Kim YS, Yoo HS, Lee TH, Kim E, Jung YK (2005). "Role of FLASH in caspase-8-mediated activation of NF-kappaB: dominant-negative function of FLASH mutant in NF-kappaB signaling pathway". Oncogene. 24 (4): 688–96. doi:10.1038/sj.onc.1208186. PMID 15592525.
• Kino T, Ichijo T, Chrousos GP (2004). "FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors". J. Steroid Biochem. Mol. Biol. 92 (5): 357–63. doi:10.1016/j.jsbmb.2004.09.003. PMID 15698540.
• Flotho C, Coustan-Smith E, Pei D, Iwamoto S, Song G, Cheng C, Pui CH, Downing JR, Campana D (2006). "Genes contributing to minimal residual disease in childhood acute lymphoblastic leukemia: prognostic significance of CASP8AP2". Blood. 108 (3): 1050–7. doi:10.1182/blood-2006-01-0322. PMC 1895863. PMID 16627760.
• Barcaroli D, Bongiorno-Borbone L, Terrinoni A, Hofmann TG, Rossi M, Knight RA, Matera AG, Melino G, De Laurenzi V (2006). "FLASH is required for histone transcription and S-phase progression". Proc. Natl. Acad. Sci. U.S.A. 103 (40): 14808–12. doi:10.1073/pnas.0604227103. PMC 1578501. PMID 17003125.
• Jeong EG, Lee SH, Lee HW, Soung YH, Yoo NJ, Lee SH (2007). "Immunohistochemical and mutational analysis of FLASH in gastric carcinomas". APMIS. 115 (8): 900–5. doi:10.1111/j.1600-0463.2007.apm_706.x. PMID 17696945.

External links

• CASP8AP2 human gene location in the UCSC Genome Browser.
• CASP8AP2 human gene details in the UCSC Genome Browser.