TIFA
entrez
92610
canonical
uniprot
Q96CG3
canonical
ensembl
ENSG00000145365
resolver
ensp
ENSP00000354911
resolver
ensp
ENSP00000424231
resolver
ensp
ENSP00000516322
resolver
ensp
ENSP00000567989
resolver
ensp
ENSP00000567990
resolver
ensp
ENSP00000619192
resolver
enst
ENST00000361717
resolver
enst
ENST00000500655
resolver
enst
ENST00000610220
resolver
enst
ENST00000897930
resolver
enst
ENST00000897931
resolver
enst
ENST00000949133
resolver
genesymbol
TIFA
resolver
genesymbol_syn
T2BP
resolver
hgnc
HGNC:19075
resolver
uniprot_entry
TIFA_HUMAN
resolver
amino_acid_sequence
MTSFEDADTEETVTCLQMTVYHPGQLQCGIFQSISFNREKLPSSEVVKFGRNSNICHYTFQDKQVSRVQFSLQLFKKFNSSVLSFEIKNMSKKTNLIVDSRELGYLNKMDLPYRCMVRFGEYQFLMEKEDGESLEFFETQFILSPRSLLQENNWPPHRPIPEYGTYSLCSSQSSSPTEMDENES
uniprot
proteins
function
FUNCTION: Adapter molecule that plays a key role in the activation of pro-inflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (PubMed:12566447, PubMed:15492226, PubMed:26068852, PubMed:28222186, PubMed:28877472, PubMed:30111836). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism (PubMed:15492226, PubMed:26068852). TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-Heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of pro-inflammatory NF-kappa-B signaling (PubMed:30111836). {ECO:0000269|PubMed:12566447, ECO:0000269|PubMed:15492226, ECO:0000269|PubMed:26068852, ECO:0000269|PubMed:28222186, ECO:0000269|PubMed:28877472, ECO:0000269|PubMed:30111836}.
uniprot
proteins
mass_dalton
21445
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="T->A: Abolishes phosphorylation by ALPK1 and subsequent TIFA-mediated NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:22566686, ECO:0000269|PubMed:26068852, ECO:0000269|PubMed:28222186, ECO:0000269|PubMed:28877472, ECO:0000269|PubMed:30111836"; MUTAGEN 50; /note="G->E: Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with A-66."; /evidence="ECO:0000269|PubMed:12566447, ECO:0000269|PubMed:26068852"; MUTAGEN 51; /note="R->A: In RKN: Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with 88-A-A-89."; /evidence="ECO:0000269|PubMed:22566686, ECO:0000269|PubMed:28222186"; MUTAGEN 66; /note="S->A: Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with E-50."; /evidence="ECO:0000269|PubMed:12566447, ECO:0000269|PubMed:26068852"; MUTAGEN 88..89; /note="KN->AA: In RKN: Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with A-51."; /evidence="ECO:0000269|PubMed:22566686, ECO:0000269|PubMed:28222186"; MUTAGEN 178; /note="E->A: Loss of binding to TRAF6 and activation of NF-kappa-B and JNK pathways."; /evidence="ECO:0000269|PubMed:12566447, ECO:0000269|PubMed:22566686, ECO:0000269|PubMed:26068852, ECO:0000269|PubMed:28222186
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-9 following detection of ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose) by ALPK1 (PubMed:30111836). 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 (PubMed:22566686, PubMed:26389808, PubMed:30111836). {ECO:0000269|PubMed:22566686, ECO:0000269|PubMed:26389808, ECO:0000269|PubMed:30111836}.
uniprot
proteins
protein_family
TIFA family
uniprot
proteins
pubmed
12566447
uniprot
proteins
pubmed
12761501
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15047173
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492226
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16643855
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22566686
uniprot
proteins
pubmed
26068852
uniprot
proteins
pubmed
26389808
uniprot
proteins
pubmed
28222186
uniprot
proteins
pubmed
28877472
uniprot
proteins
pubmed
30111836
uniprot
proteins
sequence_length
184
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22566686, ECO:0000305|PubMed:26068852}. Note=Colocalizes with lysosomal marker LAMP2 following homooligomerization and subsequent activation. {ECO:0000269|PubMed:26068852}.
uniprot
proteins