TIFA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TIFA_HUMAN
• UniProt AC: Q96CG3
• Protein Name: TRAF-interacting protein with FHA domain-containing protein A
• Gene Name: TIFA
• Organism: Homo sapiens (Human).
• Sequence Length: 184
• Protein Description: Adapter protein which mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, resulting in the downstream activation of NF-kappa-B and AP-1 pathways. Induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism..
• Protein Sequence: MTSFEDADTEETVTCLQMTVYHPGQLQCGIFQSISFNREKLPSSEVVKFGRNSNICHYTFQDKQVSRVQFSLQLFKKFNSSVLSFEIKNMSKKTNLIVDSRELGYLNKMDLPYRCMVRFGEYQFLMEKEDGESLEFFETQFILSPRSLLQENNWPPHRPIPEYGTYSLCSSQSSSPTEMDENES

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	TSFEDADTEETVTCL CCCCCCCHHHEEEEE	37.12	12566447
40	Ubiquitination	SISFNREKLPSSEVV ECCCCCCCCCCCCEE	63.56	29967540
48	Ubiquitination	LPSSEVVKFGRNSNI CCCCCEEEECCCCCC	47.48	21963094
63	Ubiquitination	CHYTFQDKQVSRVQF CEEEECCHHCEEEEE	41.64	21906983
66	Phosphorylation	TFQDKQVSRVQFSLQ EECCHHCEEEEEEHH	25.00	28258704
71	Phosphorylation	QVSRVQFSLQLFKKF HCEEEEEEHHHHHHH	9.71	28258704
77	Ubiquitination	FSLQLFKKFNSSVLS EEHHHHHHHCCCEEE	42.30	29967540
88	Ubiquitination	SVLSFEIKNMSKKTN CEEEEEEEECCCCCC	39.12	29967540
93	Ubiquitination	EIKNMSKKTNLIVDS EEEECCCCCCEEEEH	35.03	29967540
94	Phosphorylation	IKNMSKKTNLIVDSR EEECCCCCCEEEEHH	38.71	27251275
105	Phosphorylation	VDSRELGYLNKMDLP EEHHHHHHHCCCCCC	21.52	-
108	Ubiquitination	RELGYLNKMDLPYRC HHHHHHCCCCCCEEE	31.06	21906983
113	Phosphorylation	LNKMDLPYRCMVRFG HCCCCCCEEEEEEEC	24.60	-
144	Phosphorylation	FETQFILSPRSLLQE EEEEEEECHHHHHHH	17.28	24719451
170	Phosphorylation	YGTYSLCSSQSSSPT CCCEEECCCCCCCCC	36.38	28348404
171	Phosphorylation	GTYSLCSSQSSSPTE CCEEECCCCCCCCCC	32.84	28348404
173	Phosphorylation	YSLCSSQSSSPTEMD EEECCCCCCCCCCCC	34.43	28348404
174	Phosphorylation	SLCSSQSSSPTEMDE EECCCCCCCCCCCCC	32.47	28348404
175	Phosphorylation	LCSSQSSSPTEMDEN ECCCCCCCCCCCCCC	40.88	28348404
177	Phosphorylation	SSQSSSPTEMDENES CCCCCCCCCCCCCCC	45.98	28348404
184	Phosphorylation	TEMDENES------- CCCCCCCC-------	58.04	28348404

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
9	T	Phosphorylation	Kinase	AKT1	P31749	PSP
9	T	Phosphorylation	Kinase	ALPHAK3	Q96QP1	PSP
9	T	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
9	T	Phosphorylation	Phosphorylated at Thr-9 following detection of ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose) by ALPK1.	22566686
9	T	Phosphorylation	Phosphorylation at Thr-9 by ALPK1 leads to the formation of an intermolecular binding between the FHA domain and phosphorylated Thr-9, promoting TIFA oligomerization and TIFA-mediated NF-kappa-B activation.	22566686

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TIFA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF6_HUMAN	TRAF6	physical	12566447
TIFA_HUMAN	TIFA	physical	12566447
IRAK1_HUMAN	IRAK1	physical	12566447
TUT4_HUMAN	ZCCHC11	physical	16643855

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.