CFLAR

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

3H11, 3H13, 2N5R

Identifiers
AliasesCFLAR, CASH, CASP8AP1, CLARP, Casper, FLAME, FLAME-1, FLAME1, FLIP, I-FLICE, MRIT, c-FLIP, c-FLIPL, c-FLIPR, c-FLIPS, CASP8 and FADD like apoptosis regulator, cFLIP
External IDsOMIM: 603599 MGI: 1336166 HomoloGene: 7652 GeneCards: CFLAR
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for CFLAR
Genomic location for CFLAR
Band2q33.1Start201,116,154 bp[1]
End201,176,687 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for CFLAR
Genomic location for CFLAR
Band1 C1.3|1 29.16 cMStart58,750,667 bp[2]
End58,798,043 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lung

  • upper lobe of left lung

  • left ventricle

  • blood

  • gastrocnemius muscle

  • bone marrow cells

  • monocyte

  • renal medulla

  • spleen

  • lymph node
Top expressed in
  • ascending aorta

  • aortic valve

  • proximal tubule

  • right lung

  • right lung lobe

  • ciliary body

  • thymus

  • lateral recess

  • retinal pigment epithelium

  • left lung
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • cysteine-type peptidase activity
  • protein binding
  • cysteine-type endopeptidase activity involved in execution phase of apoptosis
  • enzyme activator activity
  • cysteine-type endopeptidase activity
  • peptidase activator activity
  • protein heterodimerization activity
  • protease binding
  • death receptor binding
  • protein-containing complex binding
  • cysteine-type endopeptidase activity involved in apoptotic process
Cellular component
  • cytosol
  • CD95 death-inducing signaling complex
  • ripoptosome
  • death-inducing signaling complex
  • membrane raft
  • cytoplasm
Biological process
  • regulation of apoptotic process
  • execution phase of apoptosis
  • negative regulation of apoptotic process
  • proteolysis
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • regulation of necroptotic process
  • regulation of extrinsic apoptotic signaling pathway via death domain receptors
  • viral process
  • apoptotic process
  • positive regulation of catalytic activity
  • response to hypoxia
  • negative regulation of cardiac muscle cell apoptotic process
  • positive regulation of neuron projection development
  • cellular response to insulin stimulus
  • response to testosterone
  • positive regulation of ERK1 and ERK2 cascade
  • cellular response to epidermal growth factor stimulus
  • cellular response to estradiol stimulus
  • cellular response to hypoxia
  • cellular response to dexamethasone stimulus
  • cellular response to nitric oxide
  • positive regulation of glomerular mesangial cell proliferation
  • positive regulation of extracellular matrix organization
  • negative regulation of reactive oxygen species biosynthetic process
  • negative regulation of cellular response to transforming growth factor beta stimulus
  • negative regulation of hepatocyte apoptotic process
  • negative regulation of epithelial cell apoptotic process
  • positive regulation of hepatocyte proliferation
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
  • skeletal muscle tissue development
  • positive regulation of peptidase activity
  • skeletal muscle atrophy
  • regulation of skeletal muscle satellite cell proliferation
  • skeletal myofibril assembly
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • skeletal muscle tissue regeneration
  • positive regulation of NF-kappaB transcription factor activity
  • negative regulation of necroptotic process
  • negative regulation of myoblast fusion
  • negative regulation of extrinsic apoptotic signaling pathway
  • response to bacterium
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8837

12633

Ensembl

ENSG00000003402

ENSMUSG00000026031

UniProt

O15519

O35732

RefSeq (mRNA)
NM_001127183
NM_001127184
NM_001202515
NM_001202516
NM_001202517

NM_001202518
NM_001202519
NM_001308042
NM_001308043
NM_003879
NM_001351590
NM_001351591
NM_001351592
NM_001351593
NM_001351594

NM_001289704
NM_001293804
NM_001293805
NM_009805
NM_207653

NM_001355056

RefSeq (protein)
NP_001120655
NP_001120656
NP_001189444
NP_001189445
NP_001189446

NP_001189447
NP_001189448
NP_001294971
NP_001294972
NP_003870
NP_001338519
NP_001338520
NP_001338521
NP_001338522
NP_001338523

NP_001276633
NP_001280733
NP_001280734
NP_033935
NP_997536

NP_001341985

Location (UCSC)Chr 2: 201.12 – 201.18 MbChr 1: 58.75 – 58.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CASP8 and FADD-like apoptosis regulator is a protein that in humans is encoded by the CFLAR gene.[5][6] Also called c-FLIP (FLICE-like inhibitory protein).

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000003402 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026031 – 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. ^ Shu HB, Halpin DR, Goeddel DV (Jul 1997). "Casper is a FADD- and caspase-related inducer of apoptosis". Immunity. 6 (6): 751–63. doi:10.1016/S1074-7613(00)80450-1. PMID 9208847.
  6. ^ Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, Steiner V, Bodmer JL, Schroter M, Burns K, Mattmann C, Rimoldi D, French LE, Tschopp J (Jul 1997). "Inhibition of death receptor signals by cellular FLIP" (PDF). Nature. 388 (6638): 190–5. doi:10.1038/40657. PMID 9217161. S2CID 4341495.

Further reading

  • Abe K, Kurakin A, Mohseni-Maybodi M, et al. (2001). "The complexity of TNF-related apoptosis-inducing ligand". Ann. N. Y. Acad. Sci. 926 (1): 52–63. doi:10.1111/j.1749-6632.2000.tb05598.x. PMID 11193041. S2CID 45991330.
  • Dutton A, Young LS, Murray PG (2006). "The role of cellular FLICE inhibitory protein (c-FLIP) in the pathogenesis and treatment of cancer". Expert Opin. Ther. Targets. 10 (1): 27–35. doi:10.1517/14728222.10.1.27. PMID 16441226. S2CID 45292123.

External links

  • Human CFLAR genome location and CFLAR gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: O15519 (CASP8 and FADD-like apoptosis regulator) at the PDBe-KB.
  • v
  • t
  • e