FADD

FADD
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3OQ9, 1A1W, 1A1Z, 1E3Y, 1E41, 2GF5, 3EZQ
Identifiers
Aliases	FADD, GIG3, MORT1, Fas associated via death domain
External IDs	OMIM: 602457 MGI: 109324 HomoloGene: 2836 GeneCards: FADD
Gene ontology Molecular function • identical protein binding • tumor necrosis factor receptor superfamily binding • death effector domain binding • death receptor binding • caspase binding • protein binding • protein complex binding • tumor necrosis factor receptor binding • protease binding • receptor serine/threonine kinase binding Cellular component • protein complex • cytosol • membrane raft • ripoptosome • cell body • neuron projection • CD95 death-inducing signaling complex • plasma membrane • death-inducing signaling complex • cytoplasm • nucleus Biological process • TRAIL-activated apoptotic signaling pathway • regulation of extrinsic apoptotic signaling pathway via death domain receptors • positive regulation of apoptotic process • motor neuron apoptotic process • immune system process • necroptotic signaling pathway • activation of cysteine-type endopeptidase activity involved in apoptotic process • negative regulation of necroptotic process • positive regulation of interleukin-8 production • positive regulation of type I interferon-mediated signaling pathway • cell surface receptor signaling pathway • TRIF-dependent toll-like receptor signaling pathway • positive regulation of macrophage differentiation • defense response to virus • activation of cysteine-type endopeptidase activity • activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway • apoptotic signaling pathway • cellular response to mechanical stimulus • extrinsic apoptotic signaling pathway in absence of ligand • positive regulation of transcription from RNA polymerase II promoter • 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 Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8772	14082
Ensembl	ENSG00000168040	ENSMUSG00000031077
UniProt	Q13158	Q61160
RefSeq (mRNA)	NM_003824	NM_010175
RefSeq (protein)	NP_003815	NP_034305.1 NP_034305
Location (UCSC)	Chr 11: 70.2 – 70.21 Mb	Chr 7: 144.58 – 144.58 Mb
PubMed search

3OQ9, 1A1W, 1A1Z, 1E3Y, 1E41, 2GF5, 3EZQ

8772

14082

ENSG00000168040

ENSMUSG00000031077

Q13158

Q61160

NM_003824

NM_010175

NP_003815

NP_034305.1
NP_034305

Fas-Associated protein with Death Domain (FADD), 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 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.

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Wikipedia