activation of cysteine-type endopeptidase activity
apoptotic signaling pathway
cellular response to mechanical stimulus
extrinsic apoptotic signaling pathway in absence of ligand
positive regulation of transcription by RNA polymerase II
extrinsic apoptotic signaling pathway via death domain receptors
regulation of apoptotic process
death-inducing signaling complex assembly
positive regulation of extrinsic apoptotic signaling pathway via death domain receptors
positive regulation of tumor necrosis factor production
positive regulation of I-kappaB kinase/NF-kappaB signaling
signal transduction
positive regulation of proteolysis
viral process
apoptotic process
positive regulation of activated T cell proliferation
extrinsic apoptotic signaling pathway
positive regulation of T cell mediated cytotoxicity
positive regulation of extrinsic apoptotic signaling pathway
thymus development
positive regulation of adaptive immune response
T cell differentiation in thymus
innate immune response
spleen development
negative regulation of activation-induced cell death of T cells
negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
positive regulation of interferon-gamma production
positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation
lymph node development
T cell homeostasis
response to cocaine
response to morphine
behavioral response to cocaine
regulation of necroptotic process
positive regulation of apoptotic process
toll-like receptor 3 signaling pathway
kidney development
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
8772
14082
Ensembl
ENSG00000168040
ENSMUSG00000031077
UniProt
Q13158
Q61160
RefSeq (mRNA)
NM_003824
NM_010175
RefSeq (protein)
NP_003815
NP_034305
Location (UCSC)
Chr 11: 70.2 – 70.21 Mb
n/a
PubMed search
[2]
[3]
Wikidata
View/Edit Human
View/Edit Mouse
FAS-associated death domain protein, also called MORT1, is encoded by the FADD gene on the 11q13.3 region of chromosome 11 in humans.[4]
FADD is an adaptor protein that bridges members of the tumor necrosis factor receptor superfamily, such as the Fas-receptor, to procaspases 8 and 10 to form the death-inducing signaling complex (DISC) during apoptosis. As well as its most well known role in apoptosis, FADD has also been seen to play a role in other processes including proliferation, cell cycle regulation and development.
^ abcGRCh38: Ensembl release 89: ENSG00000168040 – 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.
^Kim, P.K.M., Dutra, A.S., Chandrasekharappa, S.C., PUCK, J.M (1996). "Genomic structure and mapping of human FADD, an intracellular mediator of lymphocyte apoptosis". Journal of Immunology. 157 (12): 5461–5466. doi:10.4049/jimmunol.157.12.5461. PMID 8955195.
protein, also called MORT1, is encoded by the FADD gene on the 11q13.3 region of chromosome 11 in humans. FADD is an adaptor protein that bridges members...
Fadd may refer to: Fadd, Hungary, a village in Hungary FADD, a receptor mediating cellular apoptosis This disambiguation page lists articles associated...
CASP8 and FADD-like apoptosis regulator is a protein that in humans is encoded by the CFLAR gene. Also called c-FLIP (FLICE-like inhibitory protein). GRCh38:...
machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain. FADD also contains a death effector domain (DED)...
A fad diet is a diet that is popular, generally only for a short time, similar to fads in fashion, without being a standard scientific dietary recommendation...
elucidation of the function of this gene in humans. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required...
hearing what would become its backing track, which had been produced by Tony Fadd (real name Anton Matsulevich), a musician from Belarus. The backing track...
receptor-associated death domain (TRADD) and Fas-associated death domain protein (FADD). cIAP1/2 can inhibit TNF-α signaling by binding to TRAF2. FLIP inhibits...
stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected...
molecule Fas-associated death domain (FADD) to bind the death domain (DD) of Fas through its own death domain (DD). FADD also contains a death effector domain...
death signal and induces cell apoptosis. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required...
and adaptor protein FADD/MORT1, and is involved in the Fas-induced cell death pathway. TRADD has been shown to interact with: FADD, Keratin 18 RIPK1, STAT1...
The adaptor protein FADD will recruit (by a Death domain-Death domain interaction) pro-Caspase 8 via the DED domain. This FasR, FADD and pro-Caspase 8 form...
apoptosis cascade such as FAS-associating death domain-containing protein (FADD). FADD recruits procaspase 8 and procaspase 10 into a death induced signaling...
James Lemmo Edited by David Kern Music by Jay Chattaway Production companies Fadd Enterprises Medusa Pictures The Movie House Sales Company Overseas FilmGroup...
vec_res.z = v1.z + v2.z; vec_res.w = v1.w + v2.w; This corresponds to four x86 FADD instructions in the object code. On the other hand, as the following pseudo-code...
receptors require specific adaptor protein such as TRADD, TRAF, RIP and FADD for downstream signalling. TNF receptors are primarily involved in apoptosis...
etc.) then implicitly address the topmost ST(0), while binary operations (FADD, FMUL, FCOM, etc.) implicitly address ST(0) and ST(1). The non-strict stack...
death-induced signaling complex (DISC). The Fas-associated death domain (FADD) translocates with the DISC, allowing recruitment of procaspases 8 and 10...
distinct from apoptosis. Several pro-apoptotic signals, such as TNF, TRAIL, and FADD, also induce autophagy. Additionally, Bcl-2 inhibits Beclin-1-dependent autophagy...
and I 2.1 cell lines. The I 2.1 cell line is functionally defective for FADD and the I 9.2 cell line is functionally defective for caspase-8, both defective...
Global Information
