dbPTM

FADD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FADD_HUMAN
UniProt AC	Q13158
Protein Name	FAS-associated death domain protein
Gene Name	FADD
Organism	Homo sapiens (Human).
Sequence Length	208
Subcellular Localization
Protein Description	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..
Protein Sequence	MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDPFLVLL -------CCHHHHHH	15.48	-
10	Phosphorylation	PFLVLLHSVSSSLSS HHHHHHHHHCCCCCC	24.54	20068231
12	Phosphorylation	LVLLHSVSSSLSSSE HHHHHHHCCCCCCCH	19.75	20068231
13	Phosphorylation	VLLHSVSSSLSSSEL HHHHHHCCCCCCCHH	32.89	20068231
14	Phosphorylation	LLHSVSSSLSSSELT HHHHHCCCCCCCHHH	25.43	20068231
16	Phosphorylation	HSVSSSLSSSELTEL HHHCCCCCCCHHHHH	33.49	20068231
17	Phosphorylation	SVSSSLSSSELTELK HHCCCCCCCHHHHHH	32.88	20068231
18	Phosphorylation	VSSSLSSSELTELKF HCCCCCCCHHHHHHH	33.00	20068231
21	Phosphorylation	SLSSSELTELKFLCL CCCCCHHHHHHHHHH	34.91	20068231
41	Phosphorylation	RKLERVQSGLDLFSM HHHHHHHHHHHHHHH	38.17	21082442
47	Phosphorylation	QSGLDLFSMLLEQND HHHHHHHHHHHHCCC	18.80	28464451
69	Phosphorylation	LLRELLASLRRHDLL HHHHHHHHHHHHHHH	23.52	24719451
120	Sumoylation	RRLARQLKVSDTKID HHHHHHCCCCCCCCC	31.21	-
125	Ubiquitination	QLKVSDTKIDSIEDR HCCCCCCCCCCHHHH	49.89	33845483
125	Sumoylation	QLKVSDTKIDSIEDR HCCCCCCCCCCHHHH	49.89	-
128	Phosphorylation	VSDTKIDSIEDRYPR CCCCCCCCHHHHCCC	31.20	25278378
132	Methylation	KIDSIEDRYPRNLTE CCCCHHHHCCCCHHH	30.48	-
133	Phosphorylation	IDSIEDRYPRNLTER CCCHHHHCCCCHHHH	20.90	25278378
138	Phosphorylation	DRYPRNLTERVRESL HHCCCCHHHHHHHHH	25.87	25278378
149	Sumoylation	RESLRIWKNTEKENA HHHHHHHHCCCCCHH	52.17	-
149	Ubiquitination	RESLRIWKNTEKENA HHHHHHHHCCCCCHH	52.17	29967540
153	Ubiquitination	RIWKNTEKENATVAH HHHHCCCCCHHHHHH	54.98	29967540
157	Phosphorylation	NTEKENATVAHLVGA CCCCCHHHHHHHHHH	29.79	-
166	Methylation	AHLVGALRSCQMNLV HHHHHHHHHHHHHHH	34.55	-
167	Phosphorylation	HLVGALRSCQMNLVA HHHHHHHHHHHHHHH	15.00	-
168	Glutathionylation	LVGALRSCQMNLVAD HHHHHHHHHHHHHHH	3.44	22555962
170	Sulfoxidation	GALRSCQMNLVADLV HHHHHHHHHHHHHHH	4.99	28465586
190	Phosphorylation	ARDLQNRSGAMSPMS HHHHHHCCCCCCCCC	38.15	23927012
194	Phosphorylation	QNRSGAMSPMSWNSD HHCCCCCCCCCCCCC	19.54	20201521
197	Phosphorylation	SGAMSPMSWNSDAST CCCCCCCCCCCCCCC	26.87	23927012
200	Phosphorylation	MSPMSWNSDASTSEA CCCCCCCCCCCCCCC	28.44	23403867
203	Phosphorylation	MSWNSDASTSEAS-- CCCCCCCCCCCCC--	37.14	21978935
204	Phosphorylation	SWNSDASTSEAS--- CCCCCCCCCCCC---	32.10	23403867
205	Phosphorylation	WNSDASTSEAS---- CCCCCCCCCCC----	28.77	23403867
208	Phosphorylation	DASTSEAS------- CCCCCCCC-------	36.38	23403867

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
194	S	Phosphorylation	Kinase	HIPK3	Q9H422	PhosphoELM
194	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
194	S	Phosphorylation	Kinase	CK1A	P97633	PSP
194	S	Phosphorylation	Kinase	MAP3K1	Q13233	GPS
194	S	Phosphorylation	Kinase	MAP2K7	O14733	GPS
194	S	Phosphorylation	Kinase	PLK1	P53350	PSP
200	S	Phosphorylation	Kinase	CK2B	P67870	PSP
203	S	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FADD_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of FADD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TR10B_HUMAN	TNFRSF10B	physical	15659383
TNFL6_HUMAN	FASLG	physical	15659383
TNR1A_HUMAN	TNFRSF1A	physical	15659383
MBD4_HUMAN	MBD4	physical	12702765
NACAM_HUMAN	NACA	physical	12684039
NACA_HUMAN	NACA	physical	12684039
ABCA1_HUMAN	ABCA1	physical	12235128
CASPA_HUMAN	CASP10	physical	9045686
CASPA_HUMAN	CASP10	physical	9228018
CFLAR_HUMAN	CFLAR	physical	9228018
CASP8_HUMAN	CASP8	physical	9228018
TNR6_HUMAN	FAS	physical	9325248
CASP8_HUMAN	CASP8	physical	12911633
TRADD_HUMAN	TRADD	physical	12911633
DAPK1_HUMAN	DAPK1	physical	12911633
RT29_HUMAN	DAP3	physical	11376335
PEA15_HUMAN	PEA15	physical	10442631
TNR6_HUMAN	FAS	physical	9082980
KPCZ_HUMAN	PRKCZ	physical	11739185
DEDD_HUMAN	DEDD	physical	11741985
NOL3_HUMAN	NOL3	genetic	9560245
TNR6_HUMAN	FAS	physical	8967952
TNR6_HUMAN	FAS	physical	7538907
TRADD_HUMAN	TRADD	physical	8565075
DEDD_HUMAN	DEDD	physical	9774341
CASP8_HUMAN	CASP8	physical	12107169
TRADD_HUMAN	TRADD	physical	12107169
TNR6_HUMAN	FAS	physical	12107169
EZRI_HUMAN	EZR	physical	21183682
RIPK1_HUMAN	RIPK1	physical	21183682
RO52_HUMAN	TRIM21	physical	21183682
IRF7_HUMAN	IRF7	physical	21183682
CASP8_HUMAN	CASP8	physical	21620750
RIPK1_HUMAN	RIPK1	physical	21620750
KHDR1_HUMAN	KHDRBS1	physical	21620750
CASP8_HUMAN	CASP8	physical	20448643
TNAP3_HUMAN	TNFAIP3	physical	20448643
DAXX_HUMAN	DAXX	physical	17360386
RIPK1_HUMAN	RIPK1	physical	22848449
CLIP3_HUMAN	CLIP3	physical	22297296
RIPK1_HUMAN	RIPK1	physical	21052097
RIPK3_HUMAN	RIPK3	physical	21052097
DAPK1_HUMAN	DAPK1	physical	15048887
FAF1_HUMAN	FAF1	physical	12702723
CASP8_HUMAN	CASP8	physical	12702723
TRADD_HUMAN	TRADD	physical	12796506
RIPK1_HUMAN	RIPK1	physical	21458669
PARK7_HUMAN	PARK7	physical	21785459
CASP8_HUMAN	CASP8	physical	21785459
MKRN1_HUMAN	MKRN1	physical	22864571
RIPK1_HUMAN	RIPK1	physical	22864571
RIPK3_HUMAN	RIPK3	physical	22864571
MYD88_HUMAN	MYD88	physical	21988832
SPOP_HUMAN	SPOP	physical	21988832
RIPK1_HUMAN	RIPK1	physical	23972990
CASP8_HUMAN	CASP8	physical	23972990
TRADD_HUMAN	TRADD	physical	24686082
ATG5_HUMAN	ATG5	physical	15778222
ATG12_HUMAN	ATG12	physical	15778222
CASPA_HUMAN	CASP10	physical	20829884
CASP8_HUMAN	CASP8	physical	20829884
NFH_HUMAN	NEFH	physical	26186194
IL37_HUMAN	IL37	physical	26186194
RIPK1_HUMAN	RIPK1	physical	26186194
P52K_HUMAN	PRKRIR	physical	26186194
NACAM_HUMAN	NACA	physical	24901053
NACA_HUMAN	NACA	physical	24901053
NACAM_MOUSE	Naca	physical	24901053
NACA_MOUSE	Naca	physical	24901053
TNFL6_HUMAN	FASLG	physical	25241761
TNR6_HUMAN	FAS	physical	25241761
DAPK1_HUMAN	DAPK1	physical	25241761
BID_HUMAN	BID	physical	25241761
RHOA_HUMAN	RHOA	physical	25241761
EZRI_HUMAN	EZR	physical	25241761
VFLIP_HHV8P	HHV8GK18_gp80	physical	26865630
RIPK1_HUMAN	RIPK1	physical	26865630
TNAP3_HUMAN	TNFAIP3	physical	26437781
RIPK1_HUMAN	RIPK1	physical	24098568
CFLAR_HUMAN	CFLAR	physical	26972597
CASP8_HUMAN	CASP8	physical	26972597
NLRC4_HUMAN	NLRC4	physical	27974463
CFLAR_HUMAN	CFLAR	physical	27321185
CASP8_HUMAN	CASP8	physical	27321185
FADD_HUMAN	FADD	physical	27321185
CASP8_HUMAN	CASP8	physical	27560715
RIPK1_HUMAN	RIPK1	physical	27560715
RIPK3_HUMAN	RIPK3	physical	27560715
IL37_HUMAN	IL37	physical	28514442
TPPP_HUMAN	TPPP	physical	28514442
P52K_HUMAN	PRKRIR	physical	28514442
PIN1_HUMAN	PIN1	physical	23606538

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613759	Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations (IEHDCM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FADD_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-194 AND SER-197, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-194, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-194 AND SER-197, AND MASS SPECTROMETRY.	19413330 [Abstract]
"FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase thatinduces 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). Cited for: IDENTIFICATION IN A COMPLEX WITH HIPK3 AND FAS, AND PHOSPHORYLATION ATSER-194.	11034606 [Abstract]