TNF
entrez
7124
canonical
uniprot
P01375
canonical
ensembl
ENSG00000204490
resolver
ensembl
ENSG00000206439
resolver
ensembl
ENSG00000223952
resolver
ensembl
ENSG00000228321
resolver
ensembl
ENSG00000228849
resolver
ensembl
ENSG00000230108
resolver
ensembl
ENSG00000232810
resolver
ensp
ENSP00000365290
resolver
ensp
ENSP00000372988
resolver
ensp
ENSP00000389490
resolver
ensp
ENSP00000389492
resolver
ensp
ENSP00000392858
resolver
ensp
ENSP00000398698
resolver
ensp
ENSP00000410668
resolver
enst
ENST00000376122
resolver
enst
ENST00000383496
resolver
enst
ENST00000412275
resolver
enst
ENST00000420425
resolver
enst
ENST00000443707
resolver
enst
ENST00000448781
resolver
enst
ENST00000449264
resolver
genesymbol
TNF
resolver
genesymbol_syn
TNFA
resolver
genesymbol_syn
TNFSF2
resolver
genesymbol_syn
TNLG1F
resolver
hgnc
HGNC:11892
resolver
uniprot
E7DB75
resolver
uniprot
O43647
resolver
uniprot
Q5STB3
resolver
uniprot
Q9P1Q2
resolver
uniprot
Q9UIV3
resolver
uniprot_entry
Q5STB3_HUMAN
resolver
uniprot_entry
TNFA_HUMAN
resolver
uniprot_sec
E7DB75
resolver
uniprot_sec
O43647
resolver
uniprot_sec
Q9P1Q2
resolver
uniprot_sec
Q9UIV3
resolver
amino_acid_sequence
MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
uniprot
proteins
disease_involvement
DISEASE: Psoriatic arthritis (PSORAS) [MIM:607507]: An inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy. Five types of psoriatic arthritis have been defined: asymmetrical oligoarthritis characterized by primary involvement of the small joints of the fingers or toes; asymmetrical arthritis which involves the joints of the extremities; symmetrical polyarthritis characterized by a rheumatoid like pattern that can involve hands, wrists, ankles, and feet; arthritis mutilans, which is a rare but deforming and destructive condition; arthritis of the sacroiliac joints and spine (psoriatic spondylitis). {ECO:0000269|PubMed:12746914}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Immunodeficiency 127 (IMD127) [MIM:620977]: An autosomal recessive immunologic disorder characterized by increased susceptibility to pulmonary infection with Mycobacterium tuberculosis. Affected individuals develop recurrent pulmonary tuberculosis, but have no adverse reaction to live BCG vaccination. {ECO:0000269|PubMed:39198650}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Up-regulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line (PubMed:16829952, PubMed:22517918, PubMed:23396208). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (PubMed:12794819). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity). {ECO:0000250|UniProtKB:P06804, ECO:0000269|PubMed:12794819, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:22517918, ECO:0000269|PubMed:23396208}.; FUNCTION: The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. {ECO:0000269|PubMed:16829952}.
uniprot
proteins
mass_dalton
25644
uniprot
proteins
mutagenesis
MUTAGEN 19..20; /note="KK->RR: Abolished myristoylation."; /evidence="ECO:0000269|PubMed:23552949"; MUTAGEN 105; /note="L->S: Low activity."; /evidence="ECO:0000269|PubMed:2009860"; MUTAGEN 108; /note="R->W: Biologically inactive."; /evidence="ECO:0000269|PubMed:2009860"; MUTAGEN 112; /note="L->F: Biologically inactive."; /evidence="ECO:0000269|PubMed:2009860"; MUTAGEN 160; /note="A->V: Biologically inactive."; /evidence="ECO:0000269|PubMed:2009860"; MUTAGEN 162; /note="S->F: Biologically inactive."; /evidence="ECO:0000269|PubMed:2009860"; MUTAGEN 167; /note="V->A,D: Biologically inactive."; /evidence="ECO:0000269|PubMed:2009860"; MUTAGEN 222; /note="E->K: Biologically inactive."; /evidence="ECO:0000269|PubMed:2009860
uniprot
proteins
post_translational_modification
PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space. {ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:9034191}.; PTM: The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1. {ECO:0000269|PubMed:10205166, ECO:0000269|PubMed:8597870}.; PTM: O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid. {ECO:0000269|PubMed:8631363}.; PTM: [Tumor necrosis factor, soluble form]: The soluble form is demyristoylated at Lys-19 and Lys-20 by SIRT6, promoting its secretion. {ECO:0000269|PubMed:23552949}.
uniprot
proteins
protein_family
Tumor necrosis factor family
uniprot
proteins
pubmed
10202016
uniprot
proteins
pubmed
10205166
uniprot
proteins
pubmed
10369255
uniprot
proteins
pubmed
12746914
uniprot
proteins
pubmed
12794819
uniprot
proteins
pubmed
12915457
uniprot
proteins
pubmed
1402651
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16829951
uniprot
proteins
pubmed
16829952
uniprot
proteins
pubmed
1964681
uniprot
proteins
pubmed
2009860
uniprot
proteins
pubmed
22517918
uniprot
proteins
pubmed
23396208
uniprot
proteins
pubmed
23552949
uniprot
proteins
pubmed
2551905
uniprot
proteins
pubmed
2922050
uniprot
proteins
pubmed
2995927
uniprot
proteins
pubmed
3555974
uniprot
proteins
pubmed
3856324
uniprot
proteins
pubmed
3883195
uniprot
proteins
pubmed
39198650
uniprot
proteins
pubmed
3932069
uniprot
proteins
pubmed
6392892
uniprot
proteins
pubmed
8499947
uniprot
proteins
pubmed
8597870
uniprot
proteins
pubmed
8631363
uniprot
proteins
pubmed
9034191
uniprot
proteins
pubmed
9442056
uniprot
proteins
pubmed
9488135
uniprot
proteins
sequence_length
233
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16829952}; Single-pass type II membrane protein {ECO:0000269|PubMed:16829952}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000269|PubMed:23552949}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted.
uniprot
proteins
transmembrane_region
TRANSMEM 36..56; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins