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Currently, seven TRAF proteins have been characterized in mammals: TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, TRAF6 and TRAF7. Except for TRAF7, these proteins share a relatively conserved secondary structure , including a namesake C-terminal TRAF domain that mediates interactions with other signaling components such as the transmembrane TNF receptors ...
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. Three alternatively spliced transcript variants encoding two distinct isoforms have been reported.
The MATH domain, in molecular biology, is a binding domain that was defined originally by a region of homology between otherwise functionally unrelated domains, the intracellular TRAF-C domains of TRAF proteins and a C-terminal region of extracellular meprins A and B.
The TRAF (tumor necrosis factor receptor-associated factor) family of proteins associate with and transduce signals from members of the tumor necrosis factor receptor superfamily. The protein encoded by this gene is found in the cytoplasm and can bind to TRAF1, TRAF2, or TRAF3, thereby inhibiting TRAF function by sequestering the TRAFs in a ...
Adapter protein CIKS is a protein that in humans is encoded by the TRAF3IP2 gene. [5] [6] [7]This gene encodes a protein involved in regulating responses to cytokines by members of the Rel/NF-kappaB transcription factor family.
8717 71609 Ensembl ENSG00000102871 ENSMUSG00000031887 UniProt Q15628 Q3U0V2 RefSeq (mRNA) NM_003789 NM_153425 NM_001323552 NM_001033161 RefSeq (protein) NP_001310481 NP_003780 NP_001028333 Location (UCSC) Chr 16: 67.15 – 67.16 Mb Chr 8: 105.98 – 105.99 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tumor necrosis factor receptor type 1-associated DEATH domain protein is a ...
TICAM1 is primarily active in the spleen and is often regulated when MyD88 is deficient in the liver, indicating organ-specific regulation of signaling pathways. Curiously, there is a lack of redundancy within the TLR4 signaling pathway that leads to microbial evasion of immune response in the host after mutations occur within intermediates of the pathway. [7]
TRAF proteins associate with, and mediate the signal transduction from various receptors of the TNFR superfamily. This protein and TRAF2 form a heterodimeric complex, which is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB.