Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Study demonstrated that TRAF3, as a novel RIP2 binding partner, was downregulated in glioma tissues and functionally was a negative regulator involved in RIP2induced glioma cell growth.
Data show that TNF receptor-associated factor 3 (TRAF3) autophagy is driven by RAS and results in activation of transcription factor RelB (RELB (show RELB Proteins)).
MicroRNA-214 regulates immunity-related genes in bovine mammary epithelial cells by targeting NFATc3 and TRA
These results indicate that TRAF3 deficiency suffices to metabolically reprogram B cells, a finding that improves our understanding of the role of TRAF3 as a tumor suppressor, and suggests potential therapeutic strategies.
Viral proteins aim to subvert TRAF3 antiviral action.
Mechanistic studies showed that HACE1 (show HACE1 Proteins) exerts its inhibitory role on virus-induced signaling by disrupting the MAVS (show MAVS Proteins)-TRAF3 complex.
An important B cell-sp (show TNFRSF1A Proteins)ecific role for TNFR-associated factor 3 is the (show TNFRSF1A Proteins) inhibition of homeostatic s (show TLR4 Proteins)urvival, directly relevant to the common occurrence of TNFR- (show TNFRSF1A Proteins)associated factor 3 mutations in human B cell malignancies. Review.
The current investigations identified a subset of HPV-positive HNSCCs with mutations in the genes TRAF3 (tumor necrosis factor (show TNF Proteins) receptor-associated factor 3) and CYLD (show CYLD Proteins) (cylindromatosis lysine 63 deubiquitinase). Defects in TRAF3 and CYLD (show CYLD Proteins) correlated with the activation of transcriptional factor nuclear factor kappaB, episomal HPV status of tumors, and improved patient survival.
NDR1 interacts with TRAF3 and interferes with the association of TRAF3 and IL-17R, resulting in increased formation of the activation complex IL-17R-Act1, which is required for the downstream signaling and production of pro-inflammatory factors
Data suggest that UBR5 down-regulates levels of TRAF3, a key component of Toll (show TLR4 Proteins)-like receptor signaling, via the miRNA pathway; p90RSK (show RPS6KA1 Proteins) is an upstream regulator of UBR5; p90RSK (show RPS6KA1 Proteins) phosphorylates UBR5 as required for translational repression of TRAF3 mRNA. (UBR5 = ubiquitin protein ligase E3 component n-recognin 5 protein; TRAF3 = TNF receptor-associated factor 3; p90RSK (show RPS6KA1 Proteins) = 90 kDa ribosomal protein S6 (show RPS6 Proteins) kinase (show RPS6KB1 Proteins))
Depletion of LAP1 during early embryonic myogenesis leads to growth retardation and premature death.
In B lymphocytes, TNFR (show TNFRSF1A Proteins)-associated factor 3 inhibits signaling by TNFR (show TNFRSF1A Proteins) superfamily receptors, Toll (show TLR4 Proteins)-like receptors, and interleukin-6R. In T lymphocytes, TNFR (show TNFRSF1A Proteins)-associated factor 3 is required for normal signaling by the T cell antigen receptor, while inhibiting signaling by the interleukin-2 (show IL2 Proteins) receptor. Cytoplasmic TNFR (show TNFRSF1A Proteins) -associated factor 3 restrains nuclear factor-kappaB2 activation in both T and B cells. Review.
TRAF3 may likely induce apoptosis and resistance to proliferation and may be a new target to inhibit the cyst formation in polycystic kidney disease by regulating the NF-kappaB (show NFKB1 Proteins) signaling pathway Bcl-2 (show BCL2 Proteins) and Bcl-xl (show BCL2L1 Proteins) activity.
this study shows that TRAF3 ubiquitination triggers expulsion of intracellular bacteria by exocyst complex
Data (including data from studies using knockout mice) suggest that RANKL (show TNFSF11 Proteins) enhances TNF (show TNF Proteins)-induced osteoclast formation from precursor spleen cells and enhances bone resorption independently of Traf6 (show TRAF6 Proteins) by degrading Traf3, a known inhibitor of osteoclastogenesis. (RANKL (show TNFSF11 Proteins) = osteoclast differentiation factor (show TNFSF11 Proteins); TNF (show TNF Proteins) = tumor necrosis factor (show TNF Proteins); Traf (show TRAF1 Proteins) = TNF (show TNF Proteins) receptor-associated factor)
Upon stimulation with poly(I:C), malaria parasite-infected red blood cells (iRBCs), or vesicular stomatitis virus (VSV), FOSL1 (show FOSL1 Proteins) "translocated" from the nucleus to the cytoplasm, where it inhibited the interactions between TNF receptor-associated factor 3 (TRAF3), TIR domain-containing adapter inducing IFN-beta (show IFNB1 Proteins) (TRIF (show RNF138 Proteins)), and Tank-binding kinase 1 (TBK1 (show TBK1 Proteins)) via impairing K63-linked polyubiquitination of TRAF3 and TRIF (show RNF138 Proteins).
These findings reveal a novel mechanism that endotoxin tolerance reprograms mitogen-activated protein kinase (show MAPK1 Proteins) signaling by suppressing Pellino 1 (show PELI1 Proteins)-mediated K63-linked ubiquitination of cIAP2 (show BIRC3 Proteins), K48-linked ubiquitination, and degradation of TRAF3.
Findings establish CK1varepsilon as a regulator of antiviral innate immune responses and indicate a novel mechanism of immunoregulation that involves CK1varepsilon-mediated phosphorylation of TRAF3.
The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from, members of the TNF receptor (TNFR) superfamily. This protein participates in the signal transduction of CD40, a TNFR family member important for the activation of the immune response. This protein is found to be a critical component of the lymphotoxin-beta receptor (LTbetaR) signaling complex, which induces NF-kappaB activation and cell death initiated by LTbeta ligation. Epstein-Barr virus encoded latent infection membrane protein-1 (LMP1) can interact with this and several other members of the TRAF family, which may be essential for the oncogenic effects of LMP1. Several alternatively spliced transcript variants encoding three distinct isoforms have been reported.
CD40 associated protein 1
, CD40 binding protein
, CD40 receptor associated factor 1
, LMP1-associated protein 1
, CD40 receptor-associated factor 1
, TNF receptor-associated factor 3