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FADD (human)

Overview FADD an adaptor molecule that mediates apoptosis. Recruited through its C-terminal death domain by Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TRAIL-receptor, participating in the death signaling initiated by these receptors. Interaction with the receptors unmasks the N-terminal effector domain of this protein, which recruits caspase-8, and thereby activates the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development. Note: This description may include information from UniProtKB. Protein type: Adaptor/scaffold; Apoptosis Cellular Component: neuron projection; CD95 death-inducing signaling complex; cytosol; lipid raft Molecular Function: identical protein binding; protein binding; protease binding; death receptor binding; tumor necrosis factor receptor superfamily binding; tumor necrosis factor receptor binding Biological Process: caspase activation; positive regulation of interleukin-8 production; positive regulation of I-kappaB kinase/NF-kappaB cascade; induction of apoptosis via death domain receptors; apoptosis; positive regulation of apoptosis; virus-host interaction; innate immune response; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tumor necrosis factor production; defense response to virus Reference #:  Q13158 (UniProtKB) Alt. Names/Synonyms: FADD; Fas (TNFRSF6)-associated via death domain; FAS-associated death domain protein; FAS-associating death domain-containing protein; Fas-associating protein with death domain; GIG3; Growth-inhibiting gene 3 protein; Mediator of receptor induced toxicity; mediator of receptor-induced toxicity; MGC8528; MORT1; Protein FADD Gene Symbols: FADD Molecular weight: 23,279 Da Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states CST Pathways:  Apoptosis  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  Mitochondrial Control of Apoptosis  |  Toll-like Receptors Pathway Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below FADD 1A1W - A=1-83 (human) 1A1Z - A=1-83 (human) 1E3Y - A=93-192 (human) 1E41 - A=93-192 (human) 2GF5 - A=2-191 (human) 3EZQ - H/F/J/N/D/P/L/B=93-208 (human) 3OQ9 - H/J/K/I/L=93-184 (human) 1FAD - A=89-183 (mouse)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1A1W 1A1Z 1E3Y 1E41 2GF5 3EZQ 3OQ9  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
apoptosis, altered: S194‑p apoptosis, induced: S194‑p, S203‑p apoptosis, inhibited: S194‑p carcinogenesis, altered: S194‑p cell cycle regulation: S194‑p intracellular localization: S194‑p phosphorylation: S194‑p protein conformation: S194‑p

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	2		S41-p	RKLERVQsGLDLFSM
0	1		Y133-p	IDSIEDRyPRNLTER
0	1		T157-p	NTEKENAtVAHLVGA
0	1		S190-p	ARDLQNRsGAMsPMS
12	10		S194-p	QNRsGAMsPMSWNSD
1	0		S203-p	MSWNSDAsTSEAS__
0	1		-	gap

	mouse
S41	RKLERVQSGLDLFTV
Y133	MDGIEEKYPRSLSER
S157	NAEKKNASVAGLVKA
S187	AQESVSKSENMsPVL
S191-p	VSKSENMsPVLRDST
S200	VLRDSTVSSSEtP__
T204-p	STVSSSEtP______

	rat
S41	RKLERVQSGLDLFSV
Y133	IDGIEERYPRSLSDR
S157	NVEKENASVAGLVKA
S190	AQGSVSKSDDTSSAL
S194	VSKSDDTSSALRDST
S203	ALRDSTVSFSEtP__
T207-p	STVSFSEtP______

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