FADD
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Official Full Name
Fas (TNFRSF6)-associated via death domain
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Overview
The protein encoded by this gene is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development. [provided by RefSeq, Jul 2008] -
Synonyms
FADD; Fas (TNFRSF6)-associated via death domain; GIG3; MORT1; FAS-associated death domain protein; growth-inhibiting gene 3 protein; mediator of receptor induced toxicity; mediator of receptor-induced toxicity; Fas-associating protein with death domain; Fas-associating death domain-containing protein;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- E.coli
- Escherichia coli (strain K12)
- Human
- Mouse
- E.coli
- HEK293
- HEK293T
- Human
- In Vitro Cell Free System
- Mammalian Cell
- Mammalian cells
- Wheat Germ
- Flag
- GST
- His
- Fc
- Avi
- T7
- Myc
- DDK
- Non
- Involved Pathway
- Protein Function
- Interacting Protein
- Other Resource
FADD involved in several pathways and played different roles in them. We selected most pathways FADD participated on our site, such as Apoptosis, Toll-like receptor signaling pathway, RIG-I-like receptor signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with FADD were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Apoptosis | IRAK3;PRKAR1B;IRF4A;CTNNB1;PRKACB;PKP1;TNFRSF10A;BCL2L11;IL1B |
| Toll-like receptor signaling pathway | MAP2K2;TLR5;MAP2K4B;IFNA14;IFNPHI3;NFKBIAA;IL12B;RAC1A;IFNA16 |
| RIG-I-like receptor signaling pathway | MAPK12;MAVS;IFNA2;DDX3;IKBKB;MAPK13;MAPK10;IFNB;AZI2 |
| TNF signaling pathway | TRAF1;CREB3L2;IL1B;CASP7;MAPK13;ATF4;CXCL3;SOCS3;MAP3K5 |
| Alzheimers disease | SDHC;CALM2;IL1B;NDUFA3;PSEN2;mt-Atp8;APH1C;NDUFS4;NDUFA9 |
| Chagas disease (American trypanosomiasis) | PIK3CA;PLCB2;PLCB1;SMAD2;NFKB1;AKT2;ACE;FASLG;CASP8 |
| Tuberculosis | TLR4;IFNA2;PPP3R1;FCGR2C;MAPK9;PIK3C3;BAX;BCL10;NOS2 |
| Hepatitis B | EGR3;IFNA21;TIRAP;IFNA16;PCNA;PIK3CA;PIK3R3;NFATC4;CCNA2 |
| Herpes simplex infection | SRSF1B;RNASEL;IFNG1-2;SRSF7B;C3A.2;HLA-A;TAF5;HLA-DPA1;IFNA2 |
| Pathways in cancer | TGFB1;WNT11;CSF1R;MAPK9;WNT9B;HRAS;WNT6;HSP90AB1;FGF21 |
FADD has several biochemical functions, for example, caspase binding, death effector domain binding, death receptor binding. Some of the functions are cooperated with other proteins, some of the functions could acted by FADD itself. We selected most functions FADD had, and list some proteins which have the same functions with FADD. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| caspase binding | NOL3;BFAR;FADD;MAGEA3 |
| death effector domain binding | NOL3;CFLAR;CFLARA;FADD;CASP10;CASP8L1;CASP8 |
| death receptor binding | FEM1B;FADD;Casp3;RIPK1;CFLAR;MYD88;TNFSF15;Fasl;FASLG |
| identical protein binding | CCDC91;ATXN3;HJURP;MICU1;KHDC1B;CLDND;SNCA;THG1L;NUDT16 |
| protease binding | RFFL;CD70;OS9;ALPI;TIMP3;LDLR;VWF;THAP5;SEMG2 |
| protein binding | CD1A;MAP4K1;TCF7L1A;BTBD1;DEFA6;THOP1;DACH1;PSPC1;GJB6 |
| protein complex binding | DISC1;CALCA;PTK2B;RBM10;CALY;RXRA;RAP1B;CPD;ERCC8 |
| tumor necrosis factor receptor binding | TNFSF9;TRADD;TNFSF8;TNFSF10;TNFSF14;TNFSF4;TNFSF15;TNFSF13;ERAP1 |
| tumor necrosis factor receptor superfamily binding | TNFSF4;TNFSF11;FADD;TNFSF18;TNFSF9 |
FADD has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with FADD here. Most of them are supplied by our site. Hope this information will be useful for your research of FADD.
FAS
Research Area
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