Sample Type for Cell Culture Supernates, Cell lysates, Tissue Lysates, Serum, EDTA Plasma, Heparin Plasma

TNFRSF1A

Tumor necrosis factor receptor superfamily member 1A

TNFRSF1A ;
TNFAR ;
TNFR1 ;
Tumor necrosis factor receptor superfamily member 1A ;
Tumor necrosis factor receptor 1 ;
TNF-R1 ;
Tumor necrosis factor receptor type I ;
TNF-RI ;
TNFR-I ;
p55 ;
p60 ;
CD antigen CD120a

disease:Defects in TNFRSF1A are the cause of familial hibernian fever (FHF) [MIM:142680]; also known as tumor necrosis factor receptor-associated periodic syndrome (TRAPS). FHF is a hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases.,domain:Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP.,domain:The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.,function:Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.,online information:Repertory of FMF and hereditary autoinflammatory disorders mutations,PTM:The soluble form is produced from the membrane form by proteolytic processing.,similarity:Contains 1 death domain.,similarity:Contains 4 TNFR-Cys repeats.,subunit:Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with HCV core protein.,

response to molecule of bacterial origin, regulation of transcription, DNA-dependent, regulation of transcription from RNA polymerase II promoter, protein complex assembly, fatty acid metabolic process, icosanoid metabolic process,prostanoid metabolic process, prostaglandin metabolic process, apoptosis, defense response, inflammatory response,immune response, cell death, response to wounding, response to bacterium, defense response, incompatible interaction, defense response to bacterium, incompatible interaction, positive regulation of biosynthetic process,positive regulation of signal transduction, response to organic substance, positive regulation of macromolecule biosynthetic process, positive regulation of macromolecule metabolic process, regulation of protein kinase cascade,positive regulation of gene expression, positive regulation of cell communication, positive regulation of protein kinase cascade, programmed cell death, death, cytokine-mediated signaling pathway, positive regulation of cellular biosynthetic process, positive regulation of defense response, regulation of response to external stimulus, positive regulation of response to external stimulus, response to lipopolysaccharide, unsaturated fatty acid metabolic process,defense response to bacterium, regulation of I-kappaB kinase/NF-kappaB cascade, positive regulation of I-kappaB kinase/NF-kappaB cascade, macromolecular complex subunit organization, innate immune response, regulation of transcription, response to ethanol, regulation of angiogenesis, positive regulation of angiogenesis, positive regulation of transcription, DNA-dependent, positive regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process, positive regulation of transcription, positive regulation of transcription from RNA polymerase II promoter,positive regulation of response to stimulus, regulation of inflammatory response, positive regulation of inflammatory response, positive regulation of developmental process, positive regulation of nitrogen compound metabolic process,regulation of RNA metabolic process, positive regulation of RNA metabolic process, protein oligomerization, protein heterooligomerization, macromolecular complex assembly, protein complex biogenesis,

Cell membrane ; Single-pass type I membrane protein . Golgi apparatus membrane ; Single-pass type I membrane protein . Secreted . A secreted form is produced through proteolytic processing.; [Isoform 4]: Secreted. Lacks a Golgi-retention motif, is not membrane bound and therefore is secreted.