CASP8AP2

Protein-coding gene in the species Homo sapiens
CASP8AP2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2LR8

Identifiers
AliasesCASP8AP2, CED-4, FLASH, RIP25, caspase 8 associated protein 2
External IDsOMIM: 606880; MGI: 1349399; HomoloGene: 8066; GeneCards: CASP8AP2; OMA:CASP8AP2 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for CASP8AP2
Genomic location for CASP8AP2
Band6q15Start89,829,894 bp[1]
End89,874,436 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for CASP8AP2
Genomic location for CASP8AP2
Band4 A5|4 14.27 cMStart32,615,451 bp[2]
End32,653,265 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • corpus callosum

  • epithelium of colon

  • testicle

  • ventricular zone

  • ganglionic eminence

  • tonsil

  • gonad

  • endometrium

  • lymph node
Top expressed in
  • zygote

  • secondary oocyte

  • primary oocyte

  • genital tubercle

  • tail of embryo

  • cumulus cell

  • primitive streak

  • abdominal wall

  • Gonadal ridge

  • medial ganglionic eminence
More reference expression data
BioGPS
n/a
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
  • nucleoplasm
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
SpeciesHumanMouse
Entrez

9994

26885

Ensembl

ENSG00000118412
ENSG00000288475

ENSMUSG00000028282

UniProt

Q9UKL3

Q9WUF3

RefSeq (mRNA)

NM_012115
NM_001137667
NM_001137668

NM_001122978
NM_011997

RefSeq (protein)

NP_001131139
NP_001131140
NP_036247

NP_001116450
NP_036127

Location (UCSC)Chr 6: 89.83 – 89.87 MbChr 4: 32.62 – 32.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CASP8-associated protein 2 is a protein, that in humans is encoded by the CASP8AP2 gene.[5][6][7][8]

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. Researches 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.[8]

Interactions

CASP8AP2 has been shown to interact with TRAF2.[9]

References

  1. ^ a b c ENSG00000288475 GRCh38: Ensembl release 89: ENSG00000118412, ENSG00000288475 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028282 – 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. ^ 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. Bibcode:1999Natur.398..777I. doi:10.1038/19709. PMID 10235259. S2CID 2792230.
  6. ^ 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.
  7. ^ 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. Bibcode:2006PNAS..10314802B. doi:10.1073/pnas.0604225103. PMC 1578500. PMID 17003126.
  8. ^ a b "Entrez Gene: CASP8AP2 CASP8 associated protein 2".
  9. ^ 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. Bibcode:1999Natur.401Q.662K. doi:10.1038/44317. PMID 10537104. S2CID 4390408.
  • 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. S2CID 12720899.
  • 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. S2CID 41799122.
  • 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. Bibcode:2006PNAS..10314808B. 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. S2CID 25074994.

External links


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