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Validated All-in-One™ qPCR Primer for TRAF2(NM_021138.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
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 superfamily. This protein directly interacts with TNF receptors, and forms a heterodimeric complex with TRAF1. This protein is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB. The protein complex formed by this protein and TRAF1 interacts with the inhibitor-of-apoptosis proteins (IAPs), and functions as a mediator of the anti-apoptotic signals from TNF receptors. The interaction of this protein with TRADD, a TNF receptor associated apoptotic signal transducer, ensures the recruitment of IAPs for the direct inhibition of caspase activation. BIRC2/c-IAP1, an apoptosis inhibitor possessing ubiquitin ligase activity, can unbiquitinate and induce the degradation of this protein, and thus potentiate TNF-induced apoptosis. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of only one transcript has been determined. [provided by RefSeq].
Gene References into function
- These findings show a role for SphK in the signal transduction by TRAF2 specifically leading to activation of NF-kappa B and antiapoptosis.
- TNF-RII and c-IAP1 mediate its ubiquination
- Lymphotoxin beta receptor induces interleukin 8 gene expression via NF-kappaB and AP-1 activation.(AP-1)
- TRAF2, TRAF3, cIAP1, Smac, and lymphotoxin beta receptor associate and are involved in apoptosis
- TNF signaling leads to oligomerization, ubiquitination, and activation of GCKR and activation of the SAPK pathway in a manner that depends upon TRAF2 polyubiquitination and oligomerization and Ubc13 function
- TRAF2 has a role in TNF-alpha induced IKK phosphorylation of NF-kappaB p65
- stoichiometry of TRAF1-TRAF2 heteromeric complexes ((TRAF2)2-TRAF1 versus TRAF2-(TRAF1)2) determines their capability to mediate CD40 signaling but has no major effect on TNF signaling
- TRAF2 plays an important role as regulator of IAP nucleocytoplasmic localization, by preventing nuclear translocation of cIAP1 and cIAP2.
- AIP1 is a novel transducer in TNF-induced TRAF2-dependent activation of ASK1 that mediates a balance between JNK versus NF-kappaB signaling
- there is a novel association between TRAF2 and TRAF3 that is mediated by unique portions of each protein and that specifically regulates activation of NF-kappaB, but not AP-1
- TNF receptor-associated factor 2 (TRAF2) overexpression does not only block apoptosis induction by CD95 antigen but also converts this death receptor into a mediator of invasiveness in pancreatic adenocarcinoma
- TRAF3 specifically blocked the NF-kappaB activation via TRAF2/5.
- TRAF2 colocalizes with eIF4GI in insoluble stress granules during cellular exposure to stress conditions.
- In contrast with its effects on signaling triggered by other TNF receptors, functional studies reveal that TRAF2 plays a novel inhibitory role in glucocorticoid-induced TNF receptor (GITR)-triggered NF-kappa B activation.
- Results for the first time place tumor necrosis factor receptor-associated factor-2 (TRAF2), previously shown to function in TNF signaling, within the interferon signal transduction pathway
- TRAF2-dependent CD40 signal transduction requires TRAF6 in nonhemopoietic cells
- a single cIAP can direct its E3 ligase activity toward different substrates and can alter the cellular functions of different protein targets, including TRAF2 and SMAC, in accordance with differences in the specificity of individual BIR domains
- A constitutive expression of TRAF1, TRAF2, and TANK/I-TRAF in human gliomas was documented
- These data indicate that vFLIP uses TRAF2 and TRAF3 for signalling to NF-kappaB, which is crucial for KSHV-associated lymphomagenesis
- an LMP1-associated complex containing TRAF6, TAB2, and TAK1 plays an essential role in the activation of JNK
- GSTP1-1 plays an important regulatory role in TNF-alpha-induced signaling by forming ligand-binding interactions with TRAF2, which provides insight for analysing the protective effects of GSTP1-1 in tumor cells.
- the t(11, 18)(q21;q21) translocation creating the c-IAP2.MALT1 fusion protein activates NF-kappaB independently of TRAF1 AND TRAF2 and contributes to human malignancy in the absence of signaling adaptors that might otherwise regulate its activity
- JAB1 regulates ubiquitination of TRAF2
- IHPK2-TRAF2 binding leads to attenuation of TAK1- and NF-kappaB-mediated signaling and is partially responsible for the apoptotic activity of IHPK2.
- TNF-induced TRAF2-RIP1-AIP1-ASK1 complex formation and for the activation of ASK1-JNK/p38 apoptotic signaling.
- These data together uncovers a new signaling pathway regulating APE/Ref-1 nuclear translocation involving CD40-crosslinking, TRAF2 and p38.
- Dominant-negative forms of TRAF2 and TRAF3 inhibited but did not fully block LMP1-mediated transformation.
- These findings demonstrate that Trx, TRAF2, and TRAF6 regulate ASK1 activity by modulating N-terminal homophilic interaction of ASK1.
- LMP2A protein controls the expression of TRAF2 mRNA, which in turn is necessary for signaling by LMP1.
- TNF-R2 mediates TNF-alpha signaling in chromaffin cells via activation of nuclear factor (NF)-kappaB.
- TRAF2 might be involved in activation of NF-kappaB in a subset of ABC-like primary nodal diffuse large B-cell lymphomas indicating a poor outcome.
- place TRAF2 directly in the signaling pathway transduced through the IFNAR1 subunit of the IFN receptor
- These results suggest an important role for Smurf2 binding to TRAF2 in determining specific signalling outputs of TNF-R2.
- TRAF2 expression and subsequent degradation are required for the differentiation of monocytes into fully functional macrophages
- results unveil a new, finely tuned mechanism for TNF-alpha-induced IKK activation modulated by TRAF2 phosphorylation and suggest that TRAF2 phosphorylation contributes to elevated levels of basal NF-kappaB activity in certain human cancers
- TRAF2 plays a critical role in TNF signaling by directing the IKK complex to the membrane, promoting TRAF2 K63-linked ubiquitination, and positioning the IKKalpha and IKKbeta chains with the TAK1/TAB kinase.
