Q13158 (FADD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein FADD

Alternative name(s):
FAS-associated death domain protein
FAS-associating death domain-containing protein
Growth-inhibiting gene 3 protein
Mediator of receptor induced toxicity

Gene names

Name:	FADD
Synonyms:	MORT1
ORF Names:	GIG3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling. Ref.16 Ref.22 Ref.23 Ref.24
Subunit structure	Can self-associate. Interacts with CFLAR, PEA15 and MBD4. When phosphorylated, part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with MOCV v-CFLAR protein and LRDD. Interacts (via death domain) with FAS (via death domain). Interacts with CASP8. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.22 Ref.23 Ref.24
Tissue specificity	Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes.
Domain	Contains a death domain involved in the binding of the corresponding domain within Fas receptor. Ref.23 The interaction between the FAS and FADD death domains is crucial for the formation of the death-inducing signaling complex (DISC). Ref.23
Involvement in disease	Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations (IEHDCM) [MIM:613759]: A condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
Sequence similarities	Contains 1 death domain. Contains 1 DED (death effector) domain.

Ontologies

Keywords
Biological process	Apoptosis Host-virus interaction Immunity Innate immunity
Disease	Disease mutation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome activation of cysteine-type endopeptidase activity involved in apoptotic process Traceable author statement. Source: Reactome cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB defense response to virus Inferred from mutant phenotype Ref.16. Source: UniProtKB extrinsic apoptotic signaling pathway via death domain receptors Traceable author statement Ref.1. Source: ProtInc innate immune response Traceable author statement. Source: Reactome necrotic cell death Inferred from mutant phenotype PubMed 11101870. Source: BHF-UCL positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB positive regulation of apoptotic process Inferred from mutant phenotype Ref.24. Source: UniProtKB positive regulation of extrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 21525013. Source: UniProtKB positive regulation of interleukin-8 production Inferred from direct assay Ref.14. Source: BHF-UCL positive regulation of proteolysis Inferred from direct assay PubMed 18387192. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.14. Source: BHF-UCL positive regulation of tumor necrosis factor production Inferred from direct assay Ref.14. Source: BHF-UCL positive regulation of type I interferon-mediated signaling pathway Inferred from mutant phenotype Ref.16. Source: UniProtKB protein heterooligomerization Inferred from electronic annotation. Source: Compara toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CD95 death-inducing signaling complex Inferred from direct assay Ref.24. Source: UniProtKB cell body Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome membrane raft Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara
Molecular_function	death receptor binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-494804,EBI-494804
CASP8	Q14790	30	EBI-494804,EBI-78060
CASP8	Q14790-1	5	EBI-494804,EBI-288309
CASP8	Q14790-5	4	EBI-494804,EBI-288326
FAS	P25445	30	EBI-494804,EBI-494743
Fas	P25446	5	EBI-494804,EBI-296206	From a different organism.
MBD4	O95243	6	EBI-494804,EBI-348011
MYD88	Q99836	3	EBI-494804,EBI-447677
PARK7	Q99497	9	EBI-494804,EBI-1164361
PLK1	P53350	9	EBI-494804,EBI-476768
RIPK1	Q13546	5	EBI-494804,EBI-358507

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 208

208

Protein FADD

PRO_0000191279

Regions

Domain

3 – 81

79

DED

Domain

97 – 181

85

Death

Amino acid modifications

Modified residue

194

1

Phosphoserine Ref.12 Ref.15 Ref.19

Natural variations

Natural variant

105

1

C → W in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS. Ref.16

VAR_065124

Experimental info

Mutagenesis

12

1

S → R: Loss of interaction with CASP8. Ref.22

Mutagenesis

25

1

F → R: Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis. Ref.22

Mutagenesis

33

1

K → E: Loss of self-association. Ref.22

Mutagenesis

38

1

R → A: Loss of interaction with CASP8. Ref.22

Mutagenesis

44

1

D → R: Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS. Ref.22

Mutagenesis

51

1

E → R: Loss of interaction with CASP8. Ref.22

Mutagenesis

117

1

R → E: Loss of interaction with FAS. Ref.24

Mutagenesis

121

1

V → N: Loss of interaction with FAS.

Mutagenesis

123

1

D → R: Strongly decreased interaction with FAS. Ref.24

Mutagenesis

135

1

R → E: Strongly decreased interaction with FAS. Ref.24

Mutagenesis

142

1

R → E: Decreased interaction with FAS. Ref.24

Mutagenesis

172

1

L → A or E: Loss of interaction with FAS. Ref.23 Ref.24

Mutagenesis

172

1

L → K: Strongly decreased interaction with FAS. Ref.23 Ref.24

Mutagenesis

175

1

D → K: Strongly decreased interaction with FAS. Ref.24

Mutagenesis

176

1

L → E: Decreased interaction with FAS. Ref.23

Sequence conflict

32

1

G → V in CAA59197. Ref.2

Secondary structure

1

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208

Helix Strand Turn

Details...

Helix

3 – 13

11

Helix

16 – 30

15

Helix

34 – 38

5

Beta strand

40 – 42

3

Helix

43 – 51

9

Helix

61 – 70

10

Helix

74 – 82

9

Beta strand

88 – 91

4

Helix

94 – 105

12

Beta strand

109 – 111

3

Helix

112 – 118

7

Helix

123 – 132

10

Beta strand

133 – 135

3

Helix

137 – 151

15

Turn

153 – 155

3

Helix

158 – 167

10

Helix

171 – 190

20

Sequences

	Sequence		Length	Mass (Da)
	Q13158 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0E65E2F852E83507	FASTA	208	23,279
	10 20 30 40 50 60 MDPFLVLLHS VSSSLSSSEL TELKFLCLGR VGKRKLERVQ SGLDLFSMLL EQNDLEPGHT 70 80 90 100 110 120 ELLRELLASL RRHDLLRRVD DFEAGAAAGA APGEEDLCAA FNVICDNVGK DWRRLARQLK 130 140 150 160 170 180 VSDTKIDSIE DRYPRNLTER VRESLRIWKN TEKENATVAH LVGALRSCQM NLVADLVQEV 190 200 QQARDLQNRS GAMSPMSWNS DASTSEAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis." Chinnaiyan A.M., O'Rourke K., Tewari M., Dixit V.M. Cell 81:505-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS. Tissue: Umbilical vein endothelial cell.
[2]	"A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain." Boldin M.P., Varfolomeev E.E., Pancer Z., Mett I.L., Camonis J.H., Wallach D. J. Biol. Chem. 270:7795-7798(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Identification of a human growth inhibition gene 3 (GIG3)." Kim J.W. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	NIEHS SNPs program Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[10]	"PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis." Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P., Oriente F., Miele C., Caruso M., Formisano P., Beguinot F. Oncogene 18:4409-4415(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PEA15.
[11]	"LRDD, a novel leucine rich repeat and death domain containing protein." Telliez J.-B., Bean K.M., Lin L.-L. Biochim. Biophys. Acta 1478:280-288(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRDD.
[12]	"FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase activation." Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K., Tschopp J. J. Exp. Med. 192:1165-1174(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HIPK3 AND FAS, PHOSPHORYLATION AT SER-194.
[13]	"Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis." Screaton R.A., Kiessling S., Sansom O.J., Millar C.B., Maddison K., Bird A., Clarke A.R., Frisch S.M. Proc. Natl. Acad. Sci. U.S.A. 100:5211-5216(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MBD4.
[14]	"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction." Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S. Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAVS.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Whole-exome-sequencing-based discovery of human FADD deficiency." Bolze A., Byun M., McDonald D., Morgan N.V., Abhyankar A., Premkumar L., Puel A., Bacon C.M., Rieux-Laucat F., Pang K., Britland A., Abel L., Cant A., Maher E.R., Riedl S.J., Hambleton S., Casanova J.L. Am. J. Hum. Genet. 87:873-881(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN INTERFERON-MEDIATED IMMUNITY, INTERACTION WITH FAS, VARIANT IEHDCM TRP-105, CHARACTERIZATION OF VARIANT IEHDCM TRP-105.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY.
[20]	"NMR structure and mutagenesis of the FADD (Mort1) death-effector domain." Eberstadt M., Huang B., Chen Z., Meadows R.P., Ng S.C., Zheng L., Lenardo M.J., Fesik S.W. Nature 392:941-945(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-83.
[21]	"The three-dimensional solution structure and dynamic properties of the human FADD death domain." Berglund H., Olerenshaw D., Sankar A., Federwisch M., McDonald N.Q., Driscoll P.C. J. Mol. Biol. 302:171-188(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 93-192.
[22]	"The structure of FADD and its mode of interaction with procaspase-8." Carrington P.E., Sandu C., Wei Y., Hill J.M., Morisawa G., Huang T., Gavathiotis E., Wei Y., Werner M.H. Mol. Cell 22:599-610(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-191, FUNCTION, INTERACTION WITH FAS AND CASP8, MUTAGENESIS OF SER-12; PHE-25; LYS-33; ARG-38; ASP-44 AND GLU-51.
[23]	"The Fas-FADD death domain complex structure unravels signalling by receptor clustering." Scott F.L., Stec B., Pop C., Dobaczewska M.K., Lee J.J., Monosov E., Robinson H., Salvesen G.S., Schwarzenbacher R., Riedl S.J. Nature 457:1019-1022(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 93-208 IN COMPLEX WITH FAS, FUNCTION, SUBUNIT, ELECTRON MICROSCOPY, DOMAIN, MUTAGENESIS OF LEU-172 AND LEU-176.
[24]	"The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations." Wang L., Yang J.K., Kabaleeswaran V., Rice A.J., Cruz A.C., Park A.Y., Yin Q., Damko E., Jang S.B., Raunser S., Robinson C.V., Siegel R.M., Walz T., Wu H. Nat. Struct. Mol. Biol. 17:1324-1329(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (6.80 ANGSTROMS) OF 93-184 IN COMPLEX WITH FAS, ELECTRON MICROSCOPY, FUNCTION, MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF ARG-117; ASP-123; ARG-135; ARG-142; LEU-172 AND ASP-175.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U24231 mRNA. Translation: AAA86517.1.
X84709 mRNA. Translation: CAA59197.1.
AY423721 mRNA. Translation: AAS00484.1.
AK291005 mRNA. Translation: BAF83694.1.
BT006927 mRNA. Translation: AAP35573.1.
CR456738 mRNA. Translation: CAG33019.1.
DQ449938 Genomic DNA. Translation: ABD96828.1.
CH471076 Genomic DNA. Translation: EAW74761.1.
BC000334 mRNA. Translation: AAH00334.1.

IPI

IPI00011919.

PIR

A56912.

RefSeq

NP_003815.1. NM_003824.3.

UniGene

Hs.86131.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A1W	NMR	-	A	1-83	[»]
1A1Z	NMR	-	A	1-83	[»]
1E3Y	NMR	-	A	93-192	[»]
1E41	NMR	-	A	93-192	[»]
2GF5	NMR	-	A	2-191	[»]
3EZQ	X-ray	2.73	B/D/F/H/J/L/N/P	93-208	[»]
3OQ9	X-ray	6.80	H/I/J/K/L	93-184	[»]

ProteinModelPortal

Q13158.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-286N.

IntAct

Q13158. 25 interactions.

MINT

MINT-91814.

STRING

9606.ENSP00000301838.

PTM databases

PhosphoSite

Q13158.

Polymorphism databases

DMDM

2498355.

Proteomic databases

PaxDb

Q13158.

PeptideAtlas

Q13158.

PRIDE

Q13158.

Protocols and materials databases

DNASU

8772.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301838; ENSP00000301838; ENSG00000168040.

GeneID

8772.

KEGG

hsa:8772.

UCSC

uc001opm.2. human.

Organism-specific databases

CTD

8772.

GeneCards

GC11P070049.

HGNC

HGNC:3573. FADD.

HPA

CAB010209.
HPA001464.

MIM

602457. gene.
613759. phenotype.

neXtProt

NX_Q13158.

Orphanet

306550. FADD-related immunodeficiency.
99806. Oculootodental syndrome.

PharmGKB

PA27972.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43830.

HOGENOM

HOG000112490.

HOVERGEN

HBG000853.

InParanoid

Q13158.

KO

K02373.

OMA

CQMNLVA.

OrthoDB

EOG4JHCH7.

PhylomeDB

Q13158.

Enzyme and pathway databases

Pathway_Interaction_DB

ceramidepathway. Ceramide signaling pathway.
faspathway. FAS signaling pathway (CD95).
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.

Reactome

REACT_578. Apoptosis.
REACT_6900. Immune System.

SignaLink

Q13158.

Gene expression databases

ArrayExpress

Q13158.

Bgee

Q13158.

CleanEx

HS_FADD.

Genevestigator

Q13158.

GermOnline

ENSG00000168040. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 2 hits.

InterPro

IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001875. DED.
IPR016729. FADD.
[Graphical view]

Pfam

PF00531. Death. 1 hit.
PF01335. DED. 1 hit.
[Graphical view]

PIRSF

PIRSF018586. FADD. 1 hit.

SMART

SM00005. DEATH. 1 hit.
SM00031. DED. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 2 hits.

PROSITE

PS50017. DEATH_DOMAIN. 1 hit.
PS50168. DED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q13158.

GenomeRNAi

8772.

NextBio

32890.

SOURCE

Search...

Entry information

Entry name

FADD_HUMAN

Accession

Primary (citable) accession number: Q13158
Secondary accession number(s): Q14866, Q6IBR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.