FADD | ENSG00000168040 | NCBI 8772

Details for: FADD

Gene ID: 8772

Symbol: FADD

Ensembl ID: ENSG00000168040

Description: Fas associated via death domain

Associated with

Apoptosis
(R-HSA-109581)
Casp8 activity is inhibited
(R-HSA-5218900)
Caspase activation via death receptors in the presence of ligand
(R-HSA-140534)
Caspase activation via extrinsic apoptotic signalling pathway
(R-HSA-5357769)
Ddx58/ifih1-mediated induction of interferon-alpha/beta
(R-HSA-168928)
Death receptor signaling
(R-HSA-73887)
Defective ripk1-mediated regulated necrosis
(R-HSA-9693928)
Dimerization of procaspase-8
(R-HSA-69416)
Disease
(R-HSA-1643685)
Diseases of programmed cell death
(R-HSA-9645723)
Fasl/ cd95l signaling
(R-HSA-75157)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Myd88-independent tlr4 cascade
(R-HSA-166166)
Nf-kb activation through fadd/rip-1 pathway mediated by caspase-8 and -10
(R-HSA-933543)
Programmed cell death
(R-HSA-5357801)
Regulated necrosis
(R-HSA-5218859)
Regulation by c-flip
(R-HSA-3371378)
Regulation of necroptotic cell death
(R-HSA-5675482)
Regulation of tnfr1 signaling
(R-HSA-5357905)
Ripk1-mediated regulated necrosis
(R-HSA-5213460)
Signal transduction
(R-HSA-162582)
Tlr3-mediated ticam1-dependent programmed cell death
(R-HSA-9013957)
Tnfr1-induced proapoptotic signaling
(R-HSA-5357786)
Tnf signaling
(R-HSA-75893)
Toll-like receptor cascades
(R-HSA-168898)
Toll like receptor 3 (tlr3) cascade
(R-HSA-168164)
Toll like receptor 4 (tlr4) cascade
(R-HSA-166016)
Trail signaling
(R-HSA-75158)
Trif (ticam1)-mediated tlr4 signaling
(R-HSA-937061)
Trif-mediated programmed cell death
(R-HSA-2562578)
Activation of cysteine-type endopeptidase activity
(GO:0097202)
Apoptotic process
(GO:0006915)
Apoptotic signaling pathway
(GO:0097190)
Behavioral response to cocaine
(GO:0048148)
Caspase binding
(GO:0089720)
Cd95 death-inducing signaling complex
(GO:0031265)
Cell body
(GO:0044297)
Cellular response to mechanical stimulus
(GO:0071260)
Cytoplasm
(GO:0005737)
Cytoplasmic side of plasma membrane
(GO:0009898)
Cytosol
(GO:0005829)
Death-inducing signaling complex
(GO:0031264)
Death-inducing signaling complex assembly
(GO:0071550)
Death effector domain binding
(GO:0035877)
Death receptor binding
(GO:0005123)
Defense response to virus
(GO:0051607)
Extrinsic apoptotic signaling pathway
(GO:0097191)
Extrinsic apoptotic signaling pathway in absence of ligand
(GO:0097192)
Extrinsic apoptotic signaling pathway via death domain receptors
(GO:0008625)
Identical protein binding
(GO:0042802)
Innate immune response
(GO:0045087)
Kidney development
(GO:0001822)
Lymph node development
(GO:0048535)
Motor neuron apoptotic process
(GO:0097049)
Necroptotic signaling pathway
(GO:0097527)
Negative regulation of activation-induced cell death of t cells
(GO:0070236)
Negative regulation of necroptotic process
(GO:0060546)
Plasma membrane
(GO:0005886)
Positive regulation of activated t cell proliferation
(GO:0042104)
Positive regulation of adaptive immune response
(GO:0002821)
Positive regulation of apoptotic process
(GO:0043065)
Positive regulation of canonical nf-kappab signal transduction
(GO:0043123)
Positive regulation of cd8-positive, alpha-beta cytotoxic t cell extravasation
(GO:2000454)
Positive regulation of execution phase of apoptosis
(GO:1900119)
Positive regulation of extrinsic apoptotic signaling pathway
(GO:2001238)
Positive regulation of innate immune response
(GO:0045089)
Positive regulation of interleukin-8 production
(GO:0032757)
Positive regulation of macrophage differentiation
(GO:0045651)
Positive regulation of proteolysis
(GO:0045862)
Positive regulation of t cell mediated cytotoxicity
(GO:0001916)
Positive regulation of transcription by rna polymerase ii
(GO:0045944)
Positive regulation of tumor necrosis factor production
(GO:0032760)
Positive regulation of type ii interferon production
(GO:0032729)
Positive regulation of type i interferon-mediated signaling pathway
(GO:0060340)
Protease binding
(GO:0002020)
Protein-containing complex binding
(GO:0044877)
Protein-macromolecule adaptor activity
(GO:0030674)
Protein binding
(GO:0005515)
Receptor serine/threonine kinase binding
(GO:0033612)
Ripoptosome
(GO:0097342)
Signaling adaptor activity
(GO:0035591)
Spleen development
(GO:0048536)
T cell differentiation in thymus
(GO:0033077)
T cell homeostasis
(GO:0043029)
Thymus development
(GO:0048538)
Trail-activated apoptotic signaling pathway
(GO:0036462)
Tumor necrosis factor receptor binding
(GO:0005164)
Tumor necrosis factor receptor superfamily binding
(GO:0032813)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 88.5916
Cell Significance Index: -13.7800
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 53.0272
Cell Significance Index: -13.4500
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 29.8969
Cell Significance Index: -14.1200
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 27.2753
Cell Significance Index: -14.0300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 11.9834
Cell Significance Index: -14.7800
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 3.8139
Cell Significance Index: -15.0500
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 2.9229
Cell Significance Index: -7.8300
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.5578
Cell Significance Index: 154.1100
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 1.2581
Cell Significance Index: 75.5300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.1145
Cell Significance Index: 121.2200
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.8801
Cell Significance Index: 143.1500
Cell Name: pro-T cell (CL0000827)
Fold Change: 0.7363
Cell Significance Index: 18.8100
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.6960
Cell Significance Index: 628.4400
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 0.6559
Cell Significance Index: 17.5800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.6249
Cell Significance Index: 18.0100
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.5906
Cell Significance Index: 40.8500
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.5059
Cell Significance Index: 13.7700
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 0.4273
Cell Significance Index: 12.5500
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.4140
Cell Significance Index: 8.9700
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.3250
Cell Significance Index: 14.7300
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.2753
Cell Significance Index: 150.3700
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 0.2477
Cell Significance Index: 3.3800
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.2368
Cell Significance Index: 16.7500
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.2354
Cell Significance Index: 104.0800
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.2268
Cell Significance Index: 7.8800
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.2065
Cell Significance Index: 24.3600
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.1997
Cell Significance Index: 27.4300
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.1909
Cell Significance Index: 14.2300
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.1860
Cell Significance Index: 9.6600
Cell Name: lactocyte (CL0002325)
Fold Change: 0.1769
Cell Significance Index: 22.8500
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.1683
Cell Significance Index: 10.8600
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: 0.1596
Cell Significance Index: 3.4000
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.1577
Cell Significance Index: 7.4100
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.1551
Cell Significance Index: 27.9600
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.1513
Cell Significance Index: 4.0400
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.1298
Cell Significance Index: 6.0500
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.1273
Cell Significance Index: 15.6500
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.1175
Cell Significance Index: 2.4600
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.1069
Cell Significance Index: 2.8100
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0953
Cell Significance Index: 3.3500
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 0.0889
Cell Significance Index: 1.0100
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.0665
Cell Significance Index: 2.1300
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.0638
Cell Significance Index: 12.1500
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.0585
Cell Significance Index: 11.6100
Cell Name: odontoblast (CL0000060)
Fold Change: 0.0494
Cell Significance Index: 6.3300
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.0464
Cell Significance Index: 1.1600
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.0364
Cell Significance Index: 7.3100
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0324
Cell Significance Index: 2.0400
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.0017
Cell Significance Index: 0.6100
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0028
Cell Significance Index: -2.1400
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0055
Cell Significance Index: -10.2800
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: -0.0066
Cell Significance Index: -4.5400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.0081
Cell Significance Index: -0.1400
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0109
Cell Significance Index: -7.9900
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0116
Cell Significance Index: -21.3200
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0132
Cell Significance Index: -20.3800
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0149
Cell Significance Index: -20.2400
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0167
Cell Significance Index: -1.7100
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0176
Cell Significance Index: -11.1500
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0177
Cell Significance Index: -13.1300
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.0196
Cell Significance Index: -0.1600
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0197
Cell Significance Index: -5.6700
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0211
Cell Significance Index: -11.9300
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: -0.0214
Cell Significance Index: -0.1800
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0271
Cell Significance Index: -16.9100
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.0282
Cell Significance Index: -3.2300
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0320
Cell Significance Index: -14.5400
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0369
Cell Significance Index: -6.3000
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.0414
Cell Significance Index: -4.8200
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -0.0536
Cell Significance Index: -0.5600
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: -0.0575
Cell Significance Index: -0.6300
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0830
Cell Significance Index: -17.4800
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.0884
Cell Significance Index: -2.4700
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0912
Cell Significance Index: -13.2500
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.1443
Cell Significance Index: -15.0200
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.1501
Cell Significance Index: -11.8900
Cell Name: foveolar cell of stomach (CL0002179)
Fold Change: -0.1549
Cell Significance Index: -1.0100
Cell Name: proerythroblast (CL0000547)
Fold Change: -0.1633
Cell Significance Index: -2.3400
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.1671
Cell Significance Index: -8.7800
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.1708
Cell Significance Index: -13.1100
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.1720
Cell Significance Index: -10.5800
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.1872
Cell Significance Index: -12.5900
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.1926
Cell Significance Index: -11.8100
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.1932
Cell Significance Index: -5.6900
Cell Name: kidney cell (CL1000497)
Fold Change: -0.2067
Cell Significance Index: -1.6500
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.2108
Cell Significance Index: -11.8300
Cell Name: BEST4+ enteroycte (CL4030026)
Fold Change: -0.2110
Cell Significance Index: -3.1800
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.2155
Cell Significance Index: -10.8900
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.2178
Cell Significance Index: -8.9200
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.2280
Cell Significance Index: -6.1000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.2603
Cell Significance Index: -6.6900
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -0.2779
Cell Significance Index: -4.7900
Cell Name: peg cell (CL4033014)
Fold Change: -0.2896
Cell Significance Index: -6.6900
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.2921
Cell Significance Index: -12.9200
Cell Name: helper T cell (CL0000912)
Fold Change: -0.2928
Cell Significance Index: -4.1600
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.3436
Cell Significance Index: -9.8500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.3459
Cell Significance Index: -13.1000
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: -0.3491
Cell Significance Index: -12.2300
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.3558
Cell Significance Index: -7.7900
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -0.3592
Cell Significance Index: -4.6000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** 1. **Death domain**: FADD contains a death domain, a conserved motif that mediates interactions with other proteins involved in apoptosis and immune responses. 2. **Caspase activation**: FADD binds to procaspase-8 and -10, facilitating their activation and subsequent cleavage, leading to apoptosis. 3. **DISC assembly**: FADD is a key component of the death-inducing signaling complex (DISC), which assembles in response to death receptor activation. 4. **Regulation of immune responses**: FADD is involved in the regulation of immune responses, including the activation of T cells and the production of cytokines. 5. **Tissue-specific expression**: FADD is expressed in various cell types, including hematopoietic cells, immune cells, and trophoblasts. **Pathways and Functions** 1. **Apoptosis**: FADD mediates apoptosis through the activation of caspase-8 and -10, leading to the execution of programmed cell death. 2. **Immune responses**: FADD is involved in the regulation of immune responses, including the activation of T cells and the production of cytokines. 3. **Cytokine production**: FADD regulates the production of cytokines, including tumor necrosis factor-alpha (TNF-alpha) and interleukin-8 (IL-8). 4. **Regulation of cell death**: FADD regulates cell death pathways, including the necroptotic pathway and the intrinsic pathway. 5. **Signal transduction**: FADD is involved in signal transduction pathways, including the NF-κB pathway and the MAPK pathway. **Clinical Significance** 1. **Cancer**: Dysregulation of FADD has been implicated in various cancers, including breast cancer, lung cancer, and colon cancer. 2. **Autoimmune disorders**: FADD has been implicated in autoimmune disorders, including rheumatoid arthritis and lupus. 3. **Neurodegenerative diseases**: FADD has been implicated in neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. 4. **Infectious diseases**: FADD is involved in the regulation of immune responses to infectious diseases, including viral and bacterial infections. 5. **Therapeutic targeting**: FADD has been targeted as a potential therapeutic target for the treatment of various diseases, including cancer and autoimmune disorders. In conclusion, FADD plays a critical role in regulating apoptosis, immune responses, and cellular homeostasis. Its dysregulation has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. Further research is needed to fully understand the mechanisms underlying FADD-mediated functions and to explore its potential as a therapeutic target.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

FADD_HUMAN

Genular Protein ID: 2089566895

Symbol: FADD_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q13158 Q14866 Q6IBR4

Database IDs:

Citations:

PubMed ID: 7538907

Title: FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.

PubMed ID: 7538907

DOI: 10.1016/0092-8674(95)90071-3

PubMed ID: 7536190

Title: A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain.

PubMed ID: 7536190

DOI: 10.1074/jbc.270.14.7795

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9184224

Title: FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).

PubMed ID: 9184224

DOI: 10.1093/emboj/16.10.2794

PubMed ID: 10442631

Title: PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis.

PubMed ID: 10442631

DOI: 10.1038/sj.onc.1202831

PubMed ID: 10825539

Title: LRDD, a novel leucine rich repeat and death domain containing protein.

PubMed ID: 10825539

DOI: 10.1016/s0167-4838(00)00029-7

PubMed ID: 11034606

Title: FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase activation.

PubMed ID: 11034606

DOI: 10.1084/jem.192.8.1165

PubMed ID: 11259186

Title: Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein.

PubMed ID: 11259186

DOI: 10.1006/viro.2001.0834

PubMed ID: 12702765

Title: Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis.

PubMed ID: 12702765

DOI: 10.1073/pnas.0431215100

PubMed ID: 16127453

Title: IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction.

PubMed ID: 16127453

DOI: 10.1038/ni1243

PubMed ID: 18846110

Title: Identification of an antiapoptotic protein complex at death receptors.

PubMed ID: 18846110

DOI: 10.1038/cdd.2008.124

PubMed ID: 18632871

Title: The interaction between human papillomavirus type 16 and FADD is mediated by a novel E6 binding domain.

PubMed ID: 18632871

DOI: 10.1128/jvi.00538-08

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 21109225

Title: Whole-exome-sequencing-based discovery of human FADD deficiency.

PubMed ID: 21109225

DOI: 10.1016/j.ajhg.2010.10.028

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23955153

Title: Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains.

PubMed ID: 23955153

DOI: 10.1038/nature12436

PubMed ID: 24025841

Title: A type III effector antagonizes death receptor signalling during bacterial gut infection.

PubMed ID: 24025841

DOI: 10.1038/nature12524

PubMed ID: 28069818

Title: SseK1 and SseK3 type III secretion system effectors inhibit NF-kappaB signaling and necroptotic cell death in salmonella-infected macrophages.

PubMed ID: 28069818

DOI: 10.1128/iai.00010-17

PubMed ID: 28860194

Title: The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD).

PubMed ID: 28860194

DOI: 10.1074/jbc.m117.805036

PubMed ID: 9582077

Title: NMR structure and mutagenesis of the FADD (Mort1) death-effector domain.

PubMed ID: 9582077

DOI: 10.1038/31972

PubMed ID: 10964568

Title: The three-dimensional solution structure and dynamic properties of the human FADD death domain.

PubMed ID: 10964568

DOI: 10.1006/jmbi.2000.4011

PubMed ID: 16762833

Title: The structure of FADD and its mode of interaction with procaspase-8.

PubMed ID: 16762833

DOI: 10.1016/j.molcel.2006.04.018

PubMed ID: 19118384

Title: The Fas-FADD death domain complex structure unravels signalling by receptor clustering.

PubMed ID: 19118384

DOI: 10.1038/nature07606

PubMed ID: 20935634

Title: The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations.

PubMed ID: 20935634

DOI: 10.1038/nsmb.1920

PubMed ID: 30979585

Title: Structural and functional insights into host death domains inactivation by the bacterial arginine GlcNAcyltransferase effector.

PubMed ID: 30979585

DOI: 10.1016/j.molcel.2019.03.028

Sequence Information:

Length: 208
Mass: 23279
Checksum: 0E65E2F852E83507
Sequence:

MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL EQNDLEPGHT 
ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA FNVICDNVGK DWRRLARQLK 
VSDTKIDSIE DRYPRNLTER VRESLRIWKN TEKENATVAH LVGALRSCQM NLVADLVQEV 
QQARDLQNRS GAMSPMSWNS DASTSEAS

Database document:

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Details for: FADD

Associated with

Cells (max top 100)

Other Information

FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. PubMed ID: 7538907

A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. PubMed ID: 7536190

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). PubMed ID: 9184224

PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis. PubMed ID: 10442631

LRDD, a novel leucine rich repeat and death domain containing protein. PubMed ID: 10825539

FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase activation. PubMed ID: 11034606

Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein. PubMed ID: 11259186

Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis. PubMed ID: 12702765

IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. PubMed ID: 16127453

Identification of an antiapoptotic protein complex at death receptors. PubMed ID: 18846110

The interaction between human papillomavirus type 16 and FADD is mediated by a novel E6 binding domain. PubMed ID: 18632871

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Whole-exome-sequencing-based discovery of human FADD deficiency. PubMed ID: 21109225

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains. PubMed ID: 23955153

A type III effector antagonizes death receptor signalling during bacterial gut infection. PubMed ID: 24025841

SseK1 and SseK3 type III secretion system effectors inhibit NF-kappaB signaling and necroptotic cell death in salmonella-infected macrophages. PubMed ID: 28069818

The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD). PubMed ID: 28860194

NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. PubMed ID: 9582077

The three-dimensional solution structure and dynamic properties of the human FADD death domain. PubMed ID: 10964568

The structure of FADD and its mode of interaction with procaspase-8. PubMed ID: 16762833

The Fas-FADD death domain complex structure unravels signalling by receptor clustering. PubMed ID: 19118384

The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. PubMed ID: 20935634

Structural and functional insights into host death domains inactivation by the bacterial arginine GlcNAcyltransferase effector. PubMed ID: 30979585